Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O88728
|
IFM5_MOUSE
|
MDTSYPREDPRAPSSRKADAAAHTALSMGTPGPTPRDHMLWSVFSTMYLNLCCLGFLALVHSVKARDQKMAGNLEAARQYGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLSKLAKDSAAFFSTKFDEEDYN
| null | null |
bone mineralization [GO:0030282]; bone morphogenesis [GO:0060349]; in utero embryonic development [GO:0001701]; regulation of bone mineralization [GO:0030500]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]
| null |
PF04505;
| null |
CD225/Dispanin family
|
PTM: Palmitoylated. {ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:24715519}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:18442316}.
| null | null | null | null | null |
FUNCTION: Required for normal bone mineralization. {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:20838829, ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}.
|
Mus musculus (Mouse)
|
O88735
|
MAP7_MOUSE
|
MAEQGAGGDGHRGGDGATHSDPASDGYKVQEKRTAPSRPTSTVSGQTSNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAARETVWLEREERARQHYERHLEARKKKLEDQRLKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPRQKSNRWSWGSPLHGSSSIHSGDPDRRSVSTMNLSKHVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVSRLLTPTHSFLARSKSTAALSGDTASCSPIIMPFKAAHSRNPVDRPKLFVTPPEGSARRRTIHGLASHKREREREHVPFHVSPGARRTLSPSNLKARSPAPARLWLPSKSMPHLPGTPRPASSLPPGSVRAASAQAPSSSPGNIRPFKREVKVEPEKKDPLPAVKSRVPLVKVEEVTVEEGTPVKPPEPAAPASAPIATPAPAPATDPAPVPAPSSTVTVGVVPKTSAGTTDPEEATRLLAEKRRLAREQREKEERERKEKEELERQKIEELARRVAEERSRREEEARRLEEEQAREKEELALRLAEEERERWEREEVERVQKQKEEEARAREEAERARQEREKHFQKEEQERLERKKRLEEIMRRTRRTETADKKTTEQRNGDIAKGVLTGEPEVPALPCMASSGNGESAESPHGVALQQSEVTTESSPDLEKQPNENGMSIQNENFEEVINLPVGSKASRLDVTNENPEIPLKPILAFNDEGTLGPLPQVDGVQTQQTAEVI
| null | null |
cell morphogenesis [GO:0000902]; cell population proliferation [GO:0008283]; fertilization [GO:0009566]; germ cell development [GO:0007281]; glycosphingolipid metabolic process [GO:0006687]; homeostasis of number of cells [GO:0048872]; Leydig cell differentiation [GO:0033327]; microtubule bundle formation [GO:0001578]; microtubule cytoskeleton organization [GO:0000226]; nucleus organization [GO:0006997]; organ growth [GO:0035265]; protein localization to plasma membrane [GO:0072659]; response to osmotic stress [GO:0006970]; response to retinoic acid [GO:0032526]; Sertoli cell development [GO:0060009]; spermatogenesis [GO:0007283]
|
axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
signaling receptor binding [GO:0005102]
|
PF05672;
| null |
MAP7 family
|
PTM: The association with microtubules is regulated by phosphorylation during the cell cycle. During interphase only phosphorylated on serine. Phosphorylated on threonine in mitosis (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:14517216}. Basolateral cell membrane {ECO:0000269|PubMed:14517216}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14517216}. Note=Colocalized on microtubules. An intracellular redistribution is triggered during induction of keratinocyte terminal differentiation from microtubules with a perinuclear localization to cortical microtubules organized in spike-like bundles facing intercellular contacts.
| null | null | null | null | null |
FUNCTION: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269|PubMed:14517216}.
|
Mus musculus (Mouse)
|
O88736
|
DHB7_MOUSE
|
MRKVVLITGASSGIGLALCGRLLAEDDDLHLCLACRNLSKARAVRDTLLASHPSAEVSIVQMDVSSLQSVVRGAEEVKQKFQRLDYLYLNAGILPNPQFNLKAFFCGIFSRNVIHMFTTAEGILTQNDSVTADGLQEVFETNLFGHFILIRELEPLLCHADNPSQLIWTSSRNAKKANFSLEDIQHSKGPEPYSSSKYATDLLNVALNRNFNQKGLYSSVMCPGVVMTNMTYGILPPFIWTLLLPIMWLLRFFVNALTVTPYNGAEALVWLFHQKPESLNPLTKYASATSGFGTNYVTGQKMDIDEDTAEKFYEVLLELEKRVRTTVQKSDHPS
|
1.1.1.210; 1.1.1.270; 1.1.1.62
| null |
androgen metabolic process [GO:0008209]; brain development [GO:0007420]; cell differentiation [GO:0030154]; cholesterol biosynthetic process [GO:0006695]; embryonic organ development [GO:0048568]; embryonic skeletal system development [GO:0048706]; estrogen biosynthetic process [GO:0006703]; nervous system development [GO:0007399]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
3-keto sterol reductase activity [GO:0000253]; 5alpha-androstane-3beta,17beta-diol dehydrogenase activity [GO:0047024]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; prolactin receptor binding [GO:0005148]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family, ERG27 subfamily
|
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q62904}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12829805}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with HMGCR in a wide range of tissues during embryonic development. {ECO:0000269|PubMed:12829805}.
|
CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:9658408}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618; Evidence={ECO:0000305|PubMed:12732193, ECO:0000305|PubMed:9658408}; CATALYTIC ACTIVITY: Reaction=a 3beta-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:34787, ChEBI:CHEBI:15378, ChEBI:CHEBI:36836, ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.270; Evidence={ECO:0000269|PubMed:12829805, ECO:0000269|PubMed:20659585}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34789; Evidence={ECO:0000305|PubMed:12829805, ECO:0000305|PubMed:20659585}; CATALYTIC ACTIVITY: Reaction=3-dehydro-4alpha-methylzymosterol + H(+) + NADPH = 4alpha-methylzymosterol + NADP(+); Xref=Rhea:RHEA:36379, ChEBI:CHEBI:1949, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:136486; EC=1.1.1.270; Evidence={ECO:0000269|PubMed:20659585}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36380; Evidence={ECO:0000305|PubMed:20659585}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + zymosterone = NADP(+) + zymosterol; Xref=Rhea:RHEA:33459, ChEBI:CHEBI:15378, ChEBI:CHEBI:18252, ChEBI:CHEBI:52386, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:12829805}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33460; Evidence={ECO:0000305|PubMed:12829805}; CATALYTIC ACTIVITY: Reaction=4alpha-methyl-5alpha-cholest-8-en-3-one + H(+) + NADPH = 4alpha-methyl-5alpha-cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46832, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87050, ChEBI:CHEBI:87051; Evidence={ECO:0000305|PubMed:20659585}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46833; Evidence={ECO:0000305|PubMed:20659585}; CATALYTIC ACTIVITY: Reaction=4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP(+) = 4alpha-methyl-5alpha-cholest-7-en-3-one + H(+) + NADPH; Xref=Rhea:RHEA:18409, ChEBI:CHEBI:15378, ChEBI:CHEBI:16495, ChEBI:CHEBI:18378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.270; Evidence={ECO:0000250|UniProtKB:Q62904}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18411; Evidence={ECO:0000250|UniProtKB:Q62904}; CATALYTIC ACTIVITY: Reaction=5alpha-cholest-8-en-3-one + H(+) + NADPH = 5alpha-cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46852, ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87056; Evidence={ECO:0000250|UniProtKB:P56937}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46853; Evidence={ECO:0000250|UniProtKB:P56937}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NADP(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:42116, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:12732193}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42118; Evidence={ECO:0000305|PubMed:12732193}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:16297, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.210; Evidence={ECO:0000269|PubMed:12732193}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16299; Evidence={ECO:0000305|PubMed:12732193};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.28 uM for estrone {ECO:0000269|PubMed:9658408}; KM=12.87 uM for 17beta-estradiol {ECO:0000269|PubMed:9658408}; KM=1.19 uM for estrone {ECO:0000269|PubMed:12732193}; Vmax=556 pmol/min/mg enzyme with estrone as substrate {ECO:0000269|PubMed:9658408}; Vmax=616 pmol/min/mg enzyme with 17beta-estradiol as substrate {ECO:0000269|PubMed:9658408};
|
PATHWAY: Steroid biosynthesis; estrogen biosynthesis. {ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:9658408}.; PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6. {ECO:0000269|PubMed:12829805}.
| null | null |
FUNCTION: Bifunctional enzyme involved in steroid-hormone metabolism and cholesterol biosynthesis (PubMed:12732193, PubMed:12829805, PubMed:20659585, PubMed:9658408). Catalyzes the NADP(H)-dependent reduction of estrogens and androgens and regulates the biological potency of these steroids. Converts estrone (E1)to a more potent estrogen, 17beta-estradiol (E2) (PubMed:12732193, PubMed:9658408). Converts moderately dihydrotestosterone (DHT) to their inactive forms 5a-androstane-3beta,17b-diol and 5alpha-androstane-3alpha,17beta-diol (PubMed:12732193). Does not metabolize progesterone (PubMed:12732193). Additionally, participates in the post-squalene cholesterol biosynthesis, as a 3-ketosteroid reductase (PubMed:12829805, PubMed:20659585). {ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:12829805, ECO:0000269|PubMed:20659585, ECO:0000269|PubMed:9658408}.
|
Mus musculus (Mouse)
|
O88737
|
BSN_MOUSE
|
MGNEASLEGGAGEGPLPPGGSGLGPGPGAGKPPSALAGGGQLPVAGAARAAGPPTPGLGPVPGPGPGPGPGSVPRRLDPKEPLGSQRTTSPTPKQASATAPGRESPRETRAQGPSGQEAESPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQIAPLPSSTLCPICKTSDLTSTPSQPNFNTCTQCHNKVCNQCGFNPNPHLTQVKEWLCLNCQMQRALGMDMTTAPRSKSQQQLHSPALSPAHSPAKQPLGKPEQERSPRGPGATQSGPRQAEAARATSVPGPTQATAPPEVGRVSPQPPLSTKPSTAEPRPPAGEAQGKSATTVPSGLGAGEQTQEGLTGKLFGLGASLLTQASTLMSVQPEADTQGQPSPSKGQPKIVFSDASKEAGPRPPGSGPGPGPTPGAKTEPGARMGPGSGPGALAKTGGTASPKHGRAEHQAASKAAAKPKTMPKERASACPLCQAELNMGSRGPANYNTCTACKLQVCNLCGFNPTPHLVEKTEWLCLNCQTKRLLEGSLGEPAPLPLPTPQQPPAGVPHRAAGAAPLKQKGPQGLGQPSGSLPAKASPQATKASPQATKASPQATKASPQTTKASPQAKPLRATEPSKTSSSAQEKKTVTSAKAEPVPKPPPETTVPPGTPKAKSGVKRTDPATPVVKPVPEAPKGGEAEEPVPKPYSQDLSRSPQSLSDTGYSSDGVSSSQSEITGVVQQEVEQLDSAGVTGPRPPSPSELHKVGSSLRPSLEAQAVAPSAEWSKPPRSSSSAVEDQKRRPHSLSITPEAFDSDEELGDILEEDDSLAWGRQREQQDTAESSDDFGSQLRHDYVEDSSEGGLSPLPPQPPARADMTDEEFMRRQILEMSAEEDNLEEDDTAVSGRGLAKHSAQKASARPRPESSQEPKRRLPHNATTGYEELLSEAGPAEPTDSSGALQGGLRRFKTIELNSTGSYGHELDLGQGPDPNLDREPELEMESLTGSPEDRSRGEHSSTLPASTPSYTSGTSPTSLSSLEEDSDSSPSRRQRLEEAKQQRKARHRSHGPLLPTIEDSSEEEELREEEELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKTPPSNLSPIEDASPTEELRQAAEMEELHRSSCSEYSPSPSLDSEAETLDGGPTRLYKSGSEYNLPAFMSLYSPTETPSGSSTTPSSGRPLKSAEEAYEDMMRKAEMLQRQQGQVAGARGPHGGPSQPTGPRSQGSFEYQDTQDHDYGGRASQPVAESTPAGLGAAVYEEILQTSQSIARMRQASSRDLGFTEDKKKEKQFLNAESAYMDPMKQNGGPLTPGTSPTQLAAPVSFSTSTSSDSSGGRVIPDVRVTQHFAKEPQDPLKLHSSPVSSTLTSKEVGMTFSQGPGSPATTASPTRGYMTPTSPAGSERSPSTSSTIHSYGQPPTTANYGSQTEELPHAPSGPPGSGRAPREKPLSGGDSEVGAPQPSRGYSYFTGSSPPLSPSTPSESPTFSPGKLGPRATAEFSTQTPSLTLSSDIPRSPGPPSPMVAQGTQTPHRPSTPRLVWQQSSQEAPIMVITLASDASSQTRMVHASASTSPLCSPTDSQPTSHSYSQTTPPSASQMPSEPAGPPGFPRAPSAGTDGPLALYGWGALPAENISLCRISSVPGTSRVEPGPRPPGTAVVDLRTAVKPTPIILTDQGMDLTSLAVEARKYGLALDPVSGRQSTAVQPLVINLNAQEQTHTFLATATTVSITMASSVLMAQQKQPVVYGDPFQSRLDFGQGSGSPVCLAQVKQVEQAVQTAPYRGGPRGRPREAKFARYNLPNQVTPLARRDILITQMGTAQGVGLKPGPVPEPGAEPHRATPAELRSHAPPGTRKPHTVVVQMGEGTAGTVTTLLPEEPAGALDLTGMRPESQLACCDMVYKFPFGSSCTGTFHPAPSAPDKSVTDTALPGQSSGPFYSPRDPEPPEPLTFRTQGVVGPGPHEEQRPYPQGLPGRLYSSMSDTNLAEAGLNYHAQRLGQLFQGPGRDSAVDLSSLKHSYSLGFADGRYLGQGLQYGSFTDLRHPTDLLSHPLPLRRYSSVSNIYSDHRYGPRGDAVGFQEASLAQYSATTAREISRMCAALNSMDQYGGRHGSGSGGPDLVQYQPQHGPGLSAPQGLAPLRSGLLGNPTYPEGQPSPGNLAQYGPAASQATAVRQLLPSTATVRAADGMIYSTINTPIAATLPITTQPASVLRPMVRGGMYRPYVSGGVTAVPLTSLTRVPMIAPRVPLGPAGLYRYPAPRFPIASSVPPAEGPVYLGKPAAAKASGAGGPPRPELPAGVAREEPFSTTAPAVIKEAPVAPAPGPAPAPPPGQKPAGEAVAGSGSGVLSRPASEKEEASQEDRQRKQQEQLLQLERERVELEKLRQLRLQEELERERVELQRHREEEQLLVQRELQELQTIKQHVLQQQQEERQAQFALQREQLAQQRLQLEQIQQLQQQLQLQLEEQKQRQKAPFPATCEAPSRGPPPAATELAQNGQYWPPLTHAAFIAVAGTEGPGQPREPVLHRGLPSSASDMSLQTEEQWEAGRSGIKKRHSMPRLRDACEPESGPDPSTVRRIADSSVQTDDEEGEGRYLVTRRRRTRRSADCSVQTDDEDNADWEQPVRRRRSRLSRHSDSGSDSKHDATASSSTTAAATARAMSSVGIQTISDCSVQTEPEQLPRVSPAIHITAATDPKVEIVRYISAPEKTGRGESLACQTEPDGQAQGVAGPQLIGPTAISPYLPGIQIVTPGALGRFEKKKPDPLEIGYQAHLPPESLSQLVSRQPPKSPQVLYSPVSPLSPHRLLDTSFASSERLNKAHVSPQKQFIADSTLRQQTLPRPMKTLQRSLSDPKPLSPTAEESAKERFSLYQHQGGLGSQVSALPPNGLVRKVKRTLPSPPPEEAHLPLAGQVPSQLYAASLLQRGLAGPTTVPATKASLLRELDRDLRLVEHESTKLRKKQAELDEEEKEIDAKLKYLELGITQRKESLAKDRGGRDYPPLRGLGEHRDYLSDSELNQLRLQGCTTPAGQYVDYPASAAVPATPSGPTAFQQPRFPPAAPQYTAGSSGPTQNGFPAHQAPTYTGPSTYPAPTYPPGTGYPAEPGLPSQPAFHPTGHYAAPTPMPTTQSAPFPVQADSRAAHQKPRQTSLADLEQKVPTNYEVIGSPAVTMSSAPPETGYSGPAVSGSYEQGKAPEHPRGSDRSSVSQSPAPTYPSDSHYTSLEQNVPRNYVMIDDISELTKDSTPTASESQRLEPLGPGGVSGRPGKDPGEPAVLEGPTLPCCYGRGEEESEEDSYDPRGKSGHHRSMESNGRPSTHYYGDSDYRHGARADKYGPGPMGPKHPSKSLAPAAISSKRSKHRKQGMEQKISKFSPIEEAKDVESDLASYPPPTVSSSLTSRGRKFQDEITYGLKKNVYEQQRYYGVSSRDAAEEDERMYGSSSRSRMASAYSGEKLSSHDYSSRGKGYERERDTAERLQKAGSKPSSLSMAHGRARPPMRSQASEEESPVSPLGRPRPAGGALPPGDTCPQFCSSHSMPDVQEHVKDGPRAHAYKREEGYMLDDSHCVVSDSEAYHLGQEETDWFDKPRDARSDRFRHHGGHTVSSSQKRGPARHSYHDYDEPPEEGLWPHDEGGPGRHTSAKEHRHHSDHGRHSGRHAGEEPGRRAAKPHARDMGRHEARPHPQASPAPAMQKKGQPGYPSSADYSQSSRAPSAYHHASESKKGSRQAHTGPSALQPKADTQAQPQMQGRQAAPGPQQSQPPSSRQTPSGTASRQPQTQQQQQQQQQQQGLGQQAPQQAPSQARLQPQSQPTTRGTAPAASQPAGKPQPGPTTAPGPQPAGPPRAEQASSSKPPAAKAPQQGRAPQAQTTPGPGPAGAKPGARPGGTPGAPASQPGAEGESVFSKILPGGAAEQAGKLTEAVSAFGKKFSSFW
| null | null |
axo-dendritic transport [GO:0008088]; modulation of chemical synaptic transmission [GO:0050804]; presynapse to nucleus signaling pathway [GO:0099526]; presynaptic active zone assembly [GO:1904071]; protein localization to synapse [GO:0035418]; regulation of synaptic vesicle cycle [GO:0098693]; retrograde axonal transport [GO:0008090]; synapse organization [GO:0050808]; synaptic vesicle clustering [GO:0097091]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cell surface [GO:0009986]; cochlear hair cell ribbon synapse [GO:0098683]; cytoskeleton of presynaptic active zone [GO:0048788]; cytosol [GO:0005829]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; extrinsic component of membrane [GO:0019898]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; Golgi-associated vesicle [GO:0005798]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; inhibitory synapse [GO:0060077]; neuron projection terminus [GO:0044306]; neuronal cell body [GO:0043025]; piccolo-bassoon transport vesicle [GO:1990257]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; presynaptic active zone cytoplasmic component [GO:0098831]; ribbon synapse [GO:0097470]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; trans-Golgi network [GO:0005802]
|
dynein light chain binding [GO:0045503]; enzyme inhibitor activity [GO:0004857]; metal ion binding [GO:0046872]; structural constituent of presynaptic active zone [GO:0098882]; transcription corepressor binding [GO:0001222]
|
PF05715;
|
3.30.40.10;
| null |
PTM: Myristoylated. The N-terminal myristoylation is not sufficient for presynaptic localization (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88778}. Presynaptic active zone {ECO:0000269|PubMed:12628168, ECO:0000269|PubMed:12628169}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O88778}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12628169}; Peripheral membrane protein {ECO:0000250|UniProtKB:O88778}. Note=In retina, is localized in the outer plexiform layer at ribbon synapses formed by rods and cones but was absent from basal synaptic contacts formed by cones. In the retinal inner plexiform layer localized to conventional inhibitory GABAergic synapses, made by amacrine cells, but absent from the bipolar cell ribbon synapses (By similarity). {ECO:0000250|UniProtKB:O88778}.
| null | null | null | null | null |
FUNCTION: Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (PubMed:12628168, PubMed:12628169, PubMed:19812333). After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (By similarity). At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity). Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy by associating with ATG5 (By similarity) (PubMed:28231469). Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity). Inhibits the activity of the proportion of DAO enzyme that localizes to the presynaptic active zone, which may modulate synaptic transmission (By similarity). {ECO:0000250|UniProtKB:O35078, ECO:0000250|UniProtKB:O88778, ECO:0000250|UniProtKB:Q9UPA5, ECO:0000269|PubMed:12628168, ECO:0000269|PubMed:12628169, ECO:0000269|PubMed:19812333, ECO:0000269|PubMed:28231469}.
|
Mus musculus (Mouse)
|
O88738
|
BIRC6_MOUSE
|
MVTGCGAAPPGTVTERLPSVIVLSAGRKMAAAAAEASGPSCSSAAAAAGAGAAGVSEWLVLRDGCMRCDADGLHSLSYHPALNAILAVTSRGTIKVIDGTSGATLQASALSAKPGGQVKCQYISAVDKVIFVDDYAVGCRKDLNGILLLDTALQTPVSKQDDVVQLELPVTEAQQLLSACIEKIDVSSTEGYDLFITQLKDGLKNTSHETAANHKVAKWATVTFHLPHHVLKSIASAIVNELKKINQNVAALPVASSVMDRLSYLLPSARPELGVGPGRSVDRALMYSEANRRETFTSWPHVGYRWAQPDPMAQAGFYHQPASSGDDRAMCFTCSVCLVCWEPTDEPWSEHERHSPNCPFVKGEHTQNVPLSVTLATSPAQLPSADGADRIACFGSGSCPQFLAAATKRGKICIWDVSKLMKVHLKFEINAYDPAIVQQLILSGDPSSGVDSRRPTLAWLEDSSSCSDIPKLEGDSDDLLEDSDSEEHSRSDSVTGHTSQKEAMEVSLDITALSILQQPEKLQWEIVANVLEDTVKDLEELGANPSLTNSKSEKTKEKHQEQHNIPFPCLLAGGLLTYKSPATSPISSNSHRSLDGLSRTQGESISEQGSTDNESCTNSELNSPLVRRTLPVLLLYSIKESDEKAGKIFSQMNNIMSKSLHDDGFTVPQIIEMELDNQEQLLLQDPPVTYIQQFADAAASLTSPDSEKWNSVFPKPGALVQCLRLPKFAEEETLCIDSITPCADGIHLLVGLRTCSVESLSAINQVEALNNLNKLNSALCNRRKGDLESNLAVVNGANISVIQHESPADVPEHLLIRPEQRNVVSGGYLVLYKMNYTTRIVTLEEEPVKIQHIKDPQDTITSLILLPPDILDNREDDCEEPAEEMQLASKNGIEREKKSDISTLGHLVVTTQGGYVKVLDLSNFEILAKVEPPKKEGTEEQDTFVSVIYCSGTDRLCACTKGGELHFLQIGGTCDDIDEADILVDGSLSKGIEPALEGSRPLSNPSSPGISGVELLVDQPFTLEILTSLVELTRFETLTPRFSATVPPCWVEVQQEQQQRRHPQHLHQQHHGDAAQHTRTWKLQTDSNSWDEHVFELVLPKACMVGHVDFKFVLNSNITSVPQIQVTLLKNKAPGLGKANALNIEVEHNGNPSLVDLNEEMHHMDVEESQCLRLCPFLEDHKEDILCGPVWLASGLDLSGHAGMLTLTSPKLVKGMAGGKYRSFLIHVKAVSDRGAADEMCSSGLRPVVRLPSLKQQGHKGYSLASLLAKVAAGKEKSSNVKNENAGGTRKSENLRGCDLLQEVSVTIRRFKKTSICKERVQRCAMLQFSEFHEKLLNTLCRRSDDGQVTEHAQSLVLDALCWLAGVHSNGSGSSKEGNECLLSKTRKCLSDIVRVCFFEAGRSIAHKCARFLALCISNGKCEPCQPGFGSVLLKALLDNMCFLPAAATGGSVYWYFVLLNYVKDEDLAGCSTACAALLTAVSRQLQDRLTPLEALLQTRYGLYSSPFDPVLFDLEMSGSSWKTVYSSSTAVQSDEIDLSDVLSGNGRVSSCTAAEGSFTSLTGLLEVEPLHFTCVSTSDGTRIERDDASTFTVSSFGVPPAVGGLSSGTVGEASTALSSAAQVALQSLSHAMASAEQQLQVLQEKQQQLLKLQQQKAKLEAKLHQTTAAAAAAASAAAAAAAGPVHNAVPSNPVAAPGFFIHPSDVIPPTPKTTPLFMTPPLTPPNEAVSVVINAELAQLFPGSVIDPPAVNLAAQNKNSSKSRMNPLGSGLALAISHASHFLQPPPHQSIIIERMHSGARRFVTLDFGRPILLTDVLIPTCGDLASLSIDIWTLGEEVDGRRLVVATDISTHSLILHDLIPPPVCRFMKITVIGRYGSTNARAKIPLGFYYGHSYILPWESELKLMHDPLRGEGESASQPEIDQHLAMMVALQEDIQCRYNLACHRLEALLQSIDLPPLNSANNAQYFLRKPDKAVEEDSRVFSAYQDCIQLQLQLNLAHNAVQRLKVAIGASRKLLNETSGPEDLIQTSSTEQLRTIVRYLLDTLLSLLHSSNGHSVPAVLQSTFHAQACEELFKHLCISGTPKIRLHTGLLLVQLCGGERWWGQFLSNVLQELYNSEQLLIFPQDRVFMLLSCIGQRSLSNSGVLESLLNLLDNLLSPLQPELSMHRRTEGVLDIPMISWVVMLVSRLLDYVATVEDEAAAAKKPLNGKDRERFLTGNQWSFINNNLHTQNLNRSSKGGSSLDRLYSRKIRKQLVHHKQQLNLLKAKQKALVEQMEKEKIQSNKGSSYKLLVEQAKLKQATSKHFKDLIRLRRTAEWSRSNLDTEVTTTKESPEIEPLPFTLAHDRCISVVQKLVLFLLSMDFTCHADLLLFVCKVLARIANATRPTIHLCEIVNEPQLERLLLLLVGTDFNRGDISWGGAWAQYSLTCMLQDILAGELLAPVAAEAMEECTVSEDVGATAGDSDDSLQQSPAQLLETIDEPLTHEIAGTPPLSSLEKDKEIDLELLQDLMEVDIDPLDIDLEKDPLAAKVFKPISSTWYDYWGADYGTYNYNPYIGGLGMPVAKPPSNTEKNGSQTVSVSVSQALDARLEVGLEQQAELMLKMMSTLEADSILQALTNTSPTFSQSPTGTDDSLLGNLQPANQNSQLMIQLSSVPMLNVCFNKLFSMLQVHHVQLESLLQLWLTLSLNSSSSGNKENGADIFLYNANRIPVISLNQASIASFLTVLAWYPNTLLRTWCLVLHSLTLMTNMQLNSGSSSSIGIQETTAHLLVSDPNLIHVLVKFLSGTSPHGTNQHSPQVGPTATQAMQEFLTRLQVHLSSTCPQIFSELLLKLIHILSTERGAFQTGQGPLDAQVKLLEFTLEQNFEVVSVSTISAVIESVTFLVHHYITCSDKVMSRSGSDSSAGARACFGGLFANLIRPGDAKAVCGEMTRDQLMFDLLKLVNILVQLPLSSNREYSARVSVTTNTTDSVSDEEKVSGGKDVNGSSASTPGSPACVADLVLANQQIMSQILSALGLCNSSAMAMIIGASGLHLTKHENFHGGLDAISVGDGLFTILTTLSKKASTVHMMLQPILTYMACGYMGRQGSLATCQLSEPLLWFILRVLDTSDALKAFHDMGGVQLICNNMVTSTRAIVNTARSMVSTIMKFLDSGPNKAVDSTLKTRILASEPDNAEGIHNFAPLGTITSSSPTAQPAEVLLQATPPHRRARSAAWSYIFLPEEAWCDLTIHLPSAVLLKEIHIQPHLASLATCPSSVSVEVSADGVNMLPLSTPVVTSGLTYIKIQLVKAEVASAVCLRLHRPRDASTLGLSQIKLLGLTAFGTTSSATVNNPFLPSEDQVSKTSIGWLRLLHHCLTHISDLEGMMASAAAPTANLLQTCAALLMSPYCGMHSPNIEVVLVKIGLQSTRIGLKLIDILLRNCAASGSDPTDLNSPLLFGRLNGLSSDSTIDILYQLGTTQDPGTKDRIQALLKWVSDSAKMAALKRSGRMNYMCPSSSAVEYGLLMPSPSHLHCVAAILWHSYELLVEYDLPALLDRELFELLFNWSMSLPCNVVLKKAVDSLLCSMCHIHPNYFSLLMGWMGIIPPPVQCHHRLSMTDDSKKQDLSSSLTDDSKNAQAPLSLTESHLATLASSSQSPEAIKQLLDSGLPSLLVRSLASFCFSHISYSESIAQSVDNSQDKLRRHHVPQHCNKMPITADLVAPILRFLTEVGNSHIMKDWLGGSEVNPLWTALLFLLCHSGSTAGGHNLGAQQSSTRSASHSSATTTVLTTQQRTAIENATVAFFLQCISCHPNNQKLMAQVLCELFQTAPQRGSLPTSGNISGFVRRLFLQLMLEDEKVTMFLQSPCPLYKGRINATSHVIQHPMFGAGHKFRTLHLPVSTTLSDVLDRVSDTPSITAKLISEQKDDKEKKNHEEKEKVKAENGFQDNYSVVVASGLKSQSKRAMASTPPRPPSRRGRTIPDKIGSASSSADAASKIITVPVFHLFHRLLAGQPLPAEMTLAQLLTLLYDRKLPQGYRSIDLTVKLGSKVITDPSLSKTDSFKRLHPEKDHGDLVGSCPEDEALTPSDECMDGVLDESLLETCPIQSPLQVFAGMGGLALIAERLPMLYPEVIQQVSAPVIASTTQEKPKDSDQFEWVTIEQSGELVYEAPETIAAEPPPVKSAVQATSPIPAHSLAAFGLFLRLPGYAEVLLKERKHAQCLLRLVLGVTDDGEGSHILQSPSANVLPTLPFHVLRSLFSATPLTTDDGVLLRRMALEIGALHLILVCLSALSHHAPRVPNSSLSQTEPQVSNSHNPTSAEEQQLYWAKGTGFGTGSTASGWDVEQALTKQRLEEEHVTCLLQVLASYINPMSGAVNGEAQASPESRAQNSSALPSVLLELLSQSCLIPAMSSYLRNDSVLDMARHVPLYRALLELLRAIASCTSMVPLLLPLSTENGEEEEDEQSECQTSVGTLLAKMKTCVDTYTNRLRSKRENVKAGVKPDAPDQEPEGLALLVPDIQRTAEIVHAATANLRQANQEKKLGEYSKKVVMKPKPLSVLKSLEEKYVAVMKKLQFDTFEMVSEDDDGKLGFKVNYHYMSQVKNANDANSAARARRLAQEAVTLSTSLPLSSSSSVFVRCDEERLDIMKVLITGPADTPYANGCFEFDVYFPQDYPSSPPLVNLETTGGHSVRFNPNLYNDGKVCLSILNTWHGRPEEKWNPQTSSFLQVLVSVQSLILVAEPYFNEPGYERSRGTPSGTQSSREYDGNIRQATVKWAMLEQIRNPSPCFKEVIHKHFYLKRIELMAQCEEWIADIQQYSSDKRVGRTMSHHAAALKRHTAQLREELLKLPCPEGLDPDIEDASPVCRATAGAEDTLTHDHVNPSSSKDLPSDFQL
|
2.3.2.27
| null |
apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; labyrinthine layer development [GO:0060711]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; placenta development [GO:0001890]; positive regulation of cell population proliferation [GO:0008284]; protein ubiquitination [GO:0016567]; regulation of cell population proliferation [GO:0042127]; regulation of cytokinesis [GO:0032465]; spongiotrophoblast layer development [GO:0060712]
|
centrosome [GO:0005813]; endosome [GO:0005768]; Flemming body [GO:0090543]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle pole [GO:0000922]; trans-Golgi network [GO:0005802]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; ubiquitin conjugating enzyme activity [GO:0061631]
|
PF00653;PF12356;PF00179;
|
3.10.110.10;
|
Ubiquitin-conjugating enzyme family
|
PTM: Ubiquitinated. Ubiquitination is mediated by the RNF41 E3 ligase and leads to proteasomal degradation, impairing inhibition of apoptosis. Deubiquitinated by USP8/UBPY (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NR09}. Endosome {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NR09}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9NR09}. Note=Exhibits cell cycle-dependent localization. Concentrates in a pericentriolar compartment in interphase, moves partially to spindle poles in metaphase, and finally localizes to the spindle midzone and the midbody in telophase and during cytokinesis. On the midbody, localizes to the midbody ring, also called Flemming body. In interphase cells, localizes to the trans-Golgi network membrane and endosomes. During cytokinesis, a fraction moves to the midzone where it specifically arrives at the midbody ring. After abscission completion, travels with the midbody remnant into one daughter cell, and remains bound to it until a new midbody ring is formed during the next cell division. {ECO:0000250|UniProtKB:Q9NR09}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15300255};
| null | null | null | null |
FUNCTION: Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its targets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. Required for normal placenta development. {ECO:0000269|PubMed:15300255, ECO:0000269|PubMed:15485903, ECO:0000269|PubMed:9628897}.
|
Mus musculus (Mouse)
|
O88741
|
GDAP1_MOUSE
|
MARRQDEARAGVPLRVEGPPDKEVHLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSAGEVPVLVHGENIICEATQIIDYLEQTFLDERTPRLMPDEGSMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGNQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGHGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVLGSTLVVGLLVGMGYFAFMLFRRRLGSMILALRPRPNYF
| null | null |
cellular response to vitamin D [GO:0071305]; mitochondrial fission [GO:0000266]; mitochondrial fusion [GO:0008053]; protein targeting to mitochondrion [GO:0006626]; response to retinoic acid [GO:0032526]
|
cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]
| null |
PF13410;PF13417;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily
|
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q8TB36}.
|
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TB36}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TB36}. Cytoplasm {ECO:0000269|PubMed:16172208}.
| null | null | null | null | null |
FUNCTION: Regulates the mitochondrial network by promoting mitochondrial fission. {ECO:0000250, ECO:0000269|PubMed:16172208}.
|
Mus musculus (Mouse)
|
O88746
|
TOM1_MOUSE
|
MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDAFRAVKKRIMGNKNFHEVMLALTVLETCVKNCGHRFHVLVANQDFVENVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETPSRQNSVSSNTSQRGDLSQHATPLPTPAVLPGDSPITPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQVEPADLELLQELNRTCRAMQQRILELIPRISNEQLTEELLMINDNLNNVFLRHERFERFRTGQTAKASSEAELATDLIDMGPDPAATNNLSSQLAGMNLGSRSVRAGLQSLETSGHLEDDFDMFALTRGSSLADQRKGVKYEAPQTTDGLAGALDARQQSTGAIPATQARIMEDIEQWLSTDVGNSAEEPSGVTSEEFDKFLEERAKAADRLPNLASPSAEGPPRPSPGTAPRRKTQEKDDDMLFAL
| null | null |
autophagosome-lysosome fusion [GO:0061909]; endosomal transport [GO:0016197]; positive regulation of autophagosome maturation [GO:1901098]; protein transport [GO:0015031]; regulation of endosome organization [GO:1904978]; signal transduction [GO:0007165]; substrate localization to autophagosome [GO:0061753]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; membrane [GO:0016020]
|
clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; myosin VI binding [GO:0070853]; phosphatidylinositol-5-phosphate binding [GO:0010314]; polyubiquitin modification-dependent protein binding [GO:0031593]; ubiquitin binding [GO:0043130]
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PF03127;PF00790;
|
1.20.58.160;1.25.40.90;
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TOM1 family
|
PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:O60784}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25588840}. Endosome membrane {ECO:0000269|PubMed:25588840}; Peripheral membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:O60784}; Peripheral membrane protein {ECO:0000305}. Note=Localized to endo/exosomal vesicles (PubMed:25588840). Enriched on signaling endosomes (PubMed:25588840). Recruited to early endosomes by TOLLIP and by PtdIns(5)P (By similarity). {ECO:0000250|UniProtKB:O60784, ECO:0000269|PubMed:25588840}.
| null | null | null | null | null |
FUNCTION: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By similarity). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (By similarity). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). Binds to polyubiquitinated proteins via its GAT domain (By similarity). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (By similarity). Mediates clathrin recruitment to early endosomes by ZFYVE16 (By similarity). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition; the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (By similarity). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation (PubMed:25588840). PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation (PubMed:25588840). Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (By similarity). {ECO:0000250|UniProtKB:O60784, ECO:0000269|PubMed:25588840}.
|
Mus musculus (Mouse)
|
O88751
|
CABP1_RAT
|
MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRRLPGPCPDSPATCGDPSSRRPLCRPVPRDEGARGSRRGLPQAHCRPRETLPPARGRDGEERGLAPALSLRGSLRSRGRGDPAPAGTPEADPFLHQLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
| null | null |
modification of postsynaptic actin cytoskeleton [GO:0098885]; negative regulation of cell communication by electrical coupling [GO:0010651]; negative regulation of protein import into nucleus [GO:0042308]; postsynapse to nucleus signaling pathway [GO:0099527]; regulation of postsynapse to nucleus signaling pathway [GO:1905539]; regulation of synaptic plasticity [GO:0048167]; visual perception [GO:0007601]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; protein-containing complex [GO:0032991]; secretory granule [GO:0030141]; subplasmalemmal coating [GO:0044280]
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calcium channel regulator activity [GO:0005246]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; nuclear localization sequence binding [GO:0008139]; protein domain specific binding [GO:0019904]; transmembrane transporter binding [GO:0044325]; type 3 metabotropic glutamate receptor binding [GO:0031800]
|
PF13499;
|
1.10.238.10;
| null |
PTM: Phosphorylated. The phosphorylation regulates the activity (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15095872}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15095872}. Note=Occurs in both the cytoplasmic and cytoskeletal compartment of cell somata and dendrites.
| null | null | null | null | null |
FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling (By similarity). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels (PubMed:11865310). Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function. Suppresses the calcium-dependent inactivation of CACNA1D. Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity). {ECO:0000250|UniProtKB:Q9JLK7, ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:11865310}.
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Rattus norvegicus (Rat)
|
O88763
|
PK3C3_RAT
|
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKPFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGRAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQASVSESLSSSGVSSADIDSSQIITNPLPPVASPPPASKSKEVSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSETGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
|
2.7.1.137
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8NEB9};
|
autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to glucose starvation [GO:0042149]; cellular response to starvation [GO:0009267]; early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; endosome organization [GO:0007032]; macroautophagy [GO:0016236]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; protein localization to phagophore assembly site [GO:0034497]; protein processing [GO:0016485]; regulation of autophagy [GO:0010506]; regulation of cytokinesis [GO:0032465]; regulation of macroautophagy [GO:0016241]; response to leucine [GO:0043201]
|
autolysosome [GO:0044754]; autophagosome [GO:0005776]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; endosome [GO:0005768]; late endosome [GO:0005770]; membrane [GO:0016020]; midbody [GO:0030496]; peroxisome [GO:0005777]; phagocytic vesicle [GO:0045335]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, class III [GO:0035032]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]
|
1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; phosphatidylinositol kinase activity [GO:0052742]; protein kinase activity [GO:0004672]
|
PF00454;PF00792;PF00613;
|
2.60.40.150;1.10.1070.11;1.25.40.70;
|
PI3/PI4-kinase family
|
PTM: Ubiquitinated via 'Lys-29'- and 'Lys-48'-linked ubiquitination by UBE3C, promoting its degradation. Deubiquitination by ZRANB1/TRABID promotes its stabilization, leading to autophagosome maturation. {ECO:0000250|UniProtKB:Q8NEB9}.
|
SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q8NEB9}. Late endosome {ECO:0000250|UniProtKB:Q8NEB9}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8NEB9}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes (By similarity). Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q6PF93, ECO:0000250|UniProtKB:Q8NEB9}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000250|UniProtKB:Q8NEB9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000250|UniProtKB:Q8NEB9};
| null | null | null | null |
FUNCTION: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding. Involved in regulation of degradative endocytic trafficking and required for the abscission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Involved in the transport of lysosomal enzyme precursors to lysosomes (PubMed:11171063). Required for transport from early to late endosomes (PubMed:11171063). {ECO:0000250|UniProtKB:Q8NEB9, ECO:0000269|PubMed:11171063}.
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Rattus norvegicus (Rat)
|
O88764
|
DAPK3_RAT
|
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRVAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:9840928};
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apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to type II interferon [GO:0071346]; chromatin organization [GO:0006325]; intracellular signal transduction [GO:0035556]; negative regulation of translation [GO:0017148]; neuron differentiation [GO:0030182]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; protein autophosphorylation [GO:0046777]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of focal adhesion assembly [GO:0051893]; regulation of mitotic cell cycle [GO:0007346]; regulation of myosin II filament organization [GO:0043519]
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actin filament [GO:0005884]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; membrane raft [GO:0045121]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; PML body [GO:0016605]
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ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; leucine zipper domain binding [GO:0043522]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]
|
PF00069;
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1.10.510.10;
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Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily
|
PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus (By similarity). {ECO:0000250|UniProtKB:O54784}.; PTM: The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm and nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. {ECO:0000250|UniProtKB:O43293}.
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SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10602474, ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9840928}. Nucleus, PML body {ECO:0000269|PubMed:10602474}. Cytoplasm {ECO:0000303|PubMed:10602480}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:14582533}. Chromosome, centromere {ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:14582533}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15096528}. Note=Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments (Probable). Associated with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis. {ECO:0000269|PubMed:14582533, ECO:0000269|PubMed:17953487, ECO:0000303|PubMed:10602474}.
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CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:9840928}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:9840928};
| null | null | null | null |
FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition (By similarity). Phosphorylates STAT3 and enhances its transcriptional activity (By similarity). Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. {ECO:0000250|UniProtKB:O43293, ECO:0000250|UniProtKB:O54784, ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:9840928}.
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Rattus norvegicus (Rat)
|
O88766
|
MMP8_RAT
|
MLHLKTLPFLFFFHTQLATALPVPPEHLEEKNMKTAENYLRKFYHLPSNQFRSARNATMIAEKLKEMQRFFGLPETGKPDAATIEIMEKPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGRGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPVQPTGPSTPTACDPHLRFDAATTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSAYDLQQGYPRDISNYGFPRSVQAIDAAVSYNGKTYFFVNNQCWRYDNQRRSMDPGYPTSIASVFPGINCRIDAVFQQDSFFLFFSGPQYFAFNLVSRRVTRVARSNLWLNCP
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3.4.24.34
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COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
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cellular response to lipopolysaccharide [GO:0071222]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; ossification [GO:0001503]; positive regulation of microglial cell activation [GO:1903980]; positive regulation of neuroinflammatory response [GO:0150078]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tumor necrosis factor-mediated signaling pathway [GO:1903265]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
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extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
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calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; tumor necrosis factor binding [GO:0043120]; zinc ion binding [GO:0008270]
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PF00045;PF00413;PF01471;
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3.40.390.10;2.110.10.10;
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Peptidase M10A family
| null |
SUBCELLULAR LOCATION: Cytoplasmic granule. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Stored in intracellular granules.
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CATALYTIC ACTIVITY: Reaction=Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.; EC=3.4.24.34;
| null | null | null | null |
FUNCTION: Can degrade fibrillar type I, II, and III collagens.
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Rattus norvegicus (Rat)
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O88767
|
PARK7_RAT
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MASKRALVILAKGAEEMETVIPVDIMRRAGIKVTVAGLAGKDPVQCSRDVVICPDTSLEEAKTQGPYDVVVLPGGNLGAQNLSESALVKEILKEQENRKGLIAAICAGPTALLAHEVGFGCKVTSHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALSGKDMANQVKAPLVLKD
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3.1.2.-; 3.5.1.-; 3.5.1.124
|
COFACTOR: Note=Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate. {ECO:0000250|UniProtKB:Q99497};
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adult locomotory behavior [GO:0008344]; autophagy [GO:0006914]; cellular detoxification of aldehyde [GO:0110095]; cellular detoxification of methylglyoxal [GO:0140041]; cellular response to glyoxal [GO:0036471]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to oxidative stress [GO:0034599]; cellular response to reactive oxygen species [GO:0034614]; detection of oxidative stress [GO:0070994]; detoxification of copper ion [GO:0010273]; detoxification of hydrogen peroxide [GO:0061691]; detoxification of mercury ion [GO:0050787]; DNA repair [GO:0006281]; dopamine uptake involved in synaptic transmission [GO:0051583]; fertilization [GO:0009566]; glucose homeostasis [GO:0042593]; glutathione deglycation [GO:0036531]; glycolate biosynthetic process [GO:0046295]; glyoxal metabolic process [GO:1903189]; guanine deglycation [GO:0106044]; guanine deglycation, glyoxal removal [GO:0106046]; guanine deglycation, methylglyoxal removal [GO:0106045]; hydrogen peroxide metabolic process [GO:0042743]; inflammatory response [GO:0006954]; insulin secretion [GO:0030073]; lactate biosynthetic process [GO:0019249]; maternal process involved in female pregnancy [GO:0060135]; membrane depolarization [GO:0051899]; membrane hyperpolarization [GO:0060081]; methylglyoxal catabolic process to lactate [GO:0061727]; methylglyoxal metabolic process [GO:0009438]; mitochondrion organization [GO:0007005]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001268]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of gene expression [GO:0010629]; negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway [GO:1903384]; negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide [GO:1903751]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway [GO:1905259]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903377]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein acetylation [GO:1901984]; negative regulation of protein binding [GO:0032091]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of protein K48-linked deubiquitination [GO:1903094]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein sumoylation [GO:0033234]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of TRAIL-activated apoptotic signaling pathway [GO:1903122]; negative regulation of ubiquitin-specific protease activity [GO:2000157]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; peptidyl-arginine deglycation [GO:0036527]; positive regulation of acute inflammatory response to antigenic stimulus [GO:0002866]; positive regulation of androgen receptor activity [GO:2000825]; positive regulation of dopamine biosynthetic process [GO:1903181]; positive regulation of fertilization [GO:1905516]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of L-dopa biosynthetic process [GO:1903197]; positive regulation of L-dopa decarboxylase activity [GO:1903200]; positive regulation of mitochondrial electron transport, NADH to ubiquinone [GO:1902958]; positive regulation of NAD(P)H oxidase activity [GO:0033864]; positive regulation of oxidative phosphorylation uncoupler activity [GO:2000277]; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of pyrroline-5-carboxylate reductase activity [GO:1903168]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of superoxide dismutase activity [GO:1901671]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tyrosine 3-monooxygenase activity [GO:1903178]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of inflammatory response [GO:0050727]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of neuron apoptotic process [GO:0043523]; regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903376]; response to hydrogen peroxide [GO:0042542]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]; single fertilization [GO:0007338]; spermatogenesis [GO:0007283]; synaptic transmission, dopaminergic [GO:0001963]
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axon [GO:0030424]; cell body [GO:0044297]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane raft [GO:0045121]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; PML body [GO:0016605]; presynapse [GO:0098793]; sperm head [GO:0061827]
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copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; cytokine binding [GO:0019955]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; glyoxalase (glycolic acid-forming) activity [GO:1990422]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-dopa decarboxylase activator activity [GO:0036478]; mercury ion binding [GO:0045340]; mRNA binding [GO:0003729]; nuclear androgen receptor binding [GO:0050681]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684]; oxygen sensor activity [GO:0019826]; peptidase activity [GO:0008233]; peroxiredoxin activity [GO:0051920]; protein deglycase activity [GO:0036524]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; signaling receptor binding [GO:0005102]; small protein activating enzyme binding [GO:0044388]; superoxide dismutase copper chaperone activity [GO:0016532]; transcription coactivator activity [GO:0003713]; tyrosine 3-monooxygenase activator activity [GO:0036470]; ubiquitin-like protein conjugating enzyme binding [GO:0044390]; ubiquitin-specific protease binding [GO:1990381]
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PF01965;
|
3.40.50.880;
|
Peptidase C56 family
|
PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity. {ECO:0000250|UniProtKB:Q99497}.; PTM: Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress. {ECO:0000250|UniProtKB:Q99497}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99LX0}; Lipid-anchor {ECO:0000250|UniProtKB:Q99LX0}. Cytoplasm {ECO:0000269|PubMed:10022524}. Membrane raft {ECO:0000269|PubMed:23847046}. Nucleus {ECO:0000269|PubMed:10022524}. Mitochondrion {ECO:0000269|PubMed:31536960}. Endoplasmic reticulum {ECO:0000269|PubMed:31536960}. Note=Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage (By similarity). Membrane raft localization in astrocytes and neuronal cells requires palmitoylation (PubMed:23847046). {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:23847046}.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000250|UniProtKB:Q99497}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000250|UniProtKB:Q99497};
| null | null | null | null |
FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (By similarity). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (By similarity). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity). {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0}.
|
Rattus norvegicus (Rat)
|
O88775
|
EMB_RAT
|
MRSHTGLRALVAPGCSLLLLYLLAATRPDRAVGDPADSAFTSLPVREEMMAKYANLSLETYNISLTEQTRVSEQNITLERPSHLELECTFTATEDVMSMNVTWKKDDALLETTDGFNTTKMGDTLYSQYRFTVFNSKQMGKYSCFLGEELRGTFNIRVPKVHGKNKPLITYVGDSTVLKCECQNCLPLNWTWYMSNGTAQVPIDVHVNDKFDINGSYANETKLKVKHLLEEDGGSYWCRAAFPLGESEEHIKLVVLSFMVPLKPFLAIIAEVILLVAIILLCEVYTQKKKNDPDDGKEFEQIEQLKSDDSNGIENNVPRYRKTDSGDQ
| null | null |
axon guidance [GO:0007411]; cell adhesion [GO:0007155]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; plasma membrane lactate transport [GO:0035879]
|
axon [GO:0030424]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
cell-cell adhesion mediator activity [GO:0098632]
|
PF07679;
|
2.60.40.10;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:9169423}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20695846, ECO:0000269|PubMed:9169423}; Single-pass type I membrane protein {ECO:0000305|PubMed:19473976, ECO:0000305|PubMed:9169423}. Synapse {ECO:0000250|UniProtKB:P21995}. Note=Localizes to the neuromuscular junctions. {ECO:0000250|UniProtKB:P21995}.
| null | null | null | null | null |
FUNCTION: Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays the retraction of terminal sprouts following re-innervation of denervated endplates (By similarity). Plays a role in targeting the monocarboxylate transporters SLC16A1, SLC16A6 and SLC16A7 to the cell membrane. {ECO:0000250, ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:20695846, ECO:0000269|PubMed:35257743}.
|
Rattus norvegicus (Rat)
|
O88777
|
PSN2_RAT
|
MLTFMASDSEEEVCDERTSLMSAESPTSRSCQDSRPGPEDGENTAQWRSQENEDDCEEDPDHYACSGVPGRPSGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVFKTYNVAMDYPTLFLAVWNFGAVGMVCIHWKGPLVLQQAYLIVISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEAFEAPQPGYPGEEPEEEEERGVKLGLGDFIFYSVLVGKAAATGNGDWSTTLACFIAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI
|
3.4.23.-
| null |
amyloid precursor protein catabolic process [GO:0042987]; amyloid-beta formation [GO:0034205]; amyloid-beta metabolic process [GO:0050435]; apoptotic signaling pathway [GO:0097190]; brain morphogenesis [GO:0048854]; calcium ion transport [GO:0006816]; cardiac muscle contraction [GO:0060048]; cell fate specification [GO:0001708]; dorsal/ventral neural tube patterning [GO:0021904]; embryonic limb morphogenesis [GO:0030326]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; forebrain development [GO:0030900]; hair follicle development [GO:0001942]; hematopoietic progenitor cell differentiation [GO:0002244]; intracellular signal transduction [GO:0035556]; learning or memory [GO:0007611]; locomotion [GO:0040011]; lung alveolus development [GO:0048286]; membrane protein ectodomain proteolysis [GO:0006509]; memory [GO:0007613]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; myeloid leukocyte differentiation [GO:0002573]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; neuroinflammatory response [GO:0150076]; neuron cellular homeostasis [GO:0070050]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of coagulation [GO:0050820]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor recycling [GO:0001921]; protein catabolic process at postsynapse [GO:0140249]; protein maturation [GO:0051604]; protein metabolic process [GO:0019538]; protein processing [GO:0016485]; protein transport [GO:0015031]; regulation of calcium import into the mitochondrion [GO:0110097]; regulation of postsynapse organization [GO:0099175]; regulation of synaptic plasticity [GO:0048167]; response to hypoxia [GO:0001666]; skin morphogenesis [GO:0043589]; somitogenesis [GO:0001756]; T cell activation involved in immune response [GO:0002286]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]
|
apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary rootlet [GO:0035253]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; kinetochore [GO:0000776]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nuclear inner membrane [GO:0005637]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991]; synaptic membrane [GO:0097060]; synaptic vesicle [GO:0008021]; Z disc [GO:0030018]
|
aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175]
|
PF01080;
|
1.10.472.100;
|
Peptidase A22A family
|
PTM: Phosphorylated on serine residues. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis (By similarity). Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria (PubMed:21285369). {ECO:0000250|UniProtKB:P49810, ECO:0000269|PubMed:21285369}.
|
Rattus norvegicus (Rat)
|
O88778
|
BSN_RAT
|
MGNEASLEGGAGEGPLPPGGSGLGPGPGAGKPPSALAGGGQLPVAGAARAAGPPTPGLGLVPGPGPGPGPGSVSRRLDPKEPLGSQRATSPTPKQASATAPGRESPRETRAQGLSGQEAEGPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQIAPLPSSTLCPICKTSDLTSTSSQPNFNTCTQCHNKVCNQCGFNPNPHLTQVKEWLCLNCQMQRALGMDMTTAPRSKSQQQLHSPALSPAHSPAKQPLGKPEQERSRSPGATQSGPRQAEAARATSVPGPTQATAPPEVGRVSPQPPLSTKPSTAEPRPPAGEAQGKSATTVPSGLGAAEQTQGGLTGKLFGLGASLLTQASTLMSVQPEADTQGQPSPSKGPPKIVFSDASKEAGPRPPGSGPGPGPTPGAKTEPGPRTGPGSGPGALAKTGGTPSPKHGRADHQAASKAAAKPKTMPKERAACPLCQAELNVGSRGPANYNTCTACKLRVCTLCGFNPTPHLVEKTEWLCLNCQTKRLLEGSLGEPAPLPLPTPQEPPAGVPQRAAGASPLKQKGPQGPGQPSGSLPPKASPQAAKASPQAAKASPQAKPLRASEPSKTSSSAPEKKTGIPVKAEPVPKPPPETAVPPGTPKAKSGVKRTDPATPVVKPVPEAPKSGEAEEPVPKPYSQDLSRSPQSLSDTGYSSDGVSSSQSEITGVVQQEVEQLDSAGVTGPRPPSPSELHKVGSSMRPSLEAQAVAPSGEWSKPPSGSAVEDQKRRPHSLSIMPEAFDSDEELGDILEEDDSLAMGRQREQQDTAESSDDFGSQLRHDYVEDSSEGGLSPLPPQPPARADMTDEEFMRRQILEMSAEEDNLEEDDTAVSGRGLAKHGAQKASARPRPESSQESVALPKRRLPHNATTGYEELLSEEGPAEPTDGALQGGLRRFKTIGLNSTGRLWSTSLDLGQGSDPNLDREPELEMESLTGSPEDRSRGEHSSTLPASTPSYTSGTSPTSLSSLEEDSDSSPSRRQRLEEAKQQRKARHRSHGPLLPTIEDSSEEEELREEEELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKTPPSNLSPIEDASPTEELRQAAEMEELHRSSCSEYSPSPSLDSEAETLDGGPTRLYKSGSEYNLPAFMSLCSPTETPSGSSTTPSSGRPLKSAEEAYEDMMRKAELLQRQQGQAAGARGPHGGPSQPTGPRSQGSFEYQDTLDHDYGGRASQPAADGTPAGLGATVYEEILQTSQSIARMRQASSRDLAFTEDKKKEKQFLNAESAYMDPMKQNGGPLTPGTSPTQLAAPVSFPTSTSSDSSGGRVIPDVRVTQHFAKEPQEPLKLHSSPASPSLASKEVGMTFSQGPGTPATTAMAPCPASLPRGYMTPAGPERSPSTSSTIHSYGQPPTTANYGSQTEELPHAPSGPAGSGRASREKPLSGGDGEVGPPQPSRGYSYFTGSSPPLSPSTPSESPTFSPSKLGPRATAEFSTQTPSLTPSSDIPRSVGTPSPMVAQGTQTPHRPSTPRLVWQQSSQEAPVMVITLASDASSQTRMVHASASTSPLCSPTDSQPASHSYSQTTPPSASQMPSEPAGPPGFPRAPSAGVDGPLALYGWGALPAENISLCRISSVPGTSRVEPGPRPPGTAVVDLRTAVKPTPIILTDQGMDLTSLAVEARKYGLALDPVPGRQSTAVQPLVINLNAQEQTHTFLATATTVSITMASSVLMAQQKQPVVYGDPFQSRLDFGQGSGSPVCLAQVKQVEQAVQTAPYRGGPRGRPREAKFARYNLPNQVTPLARRDILITQMGTAQSVSLKPGPVPEPGAEPHRATPAELRAHALPGTRKPHTVVVQMGEGAAGTVTTLLPEEPAGALDLTGMRPESRLACCDMAYKFPFGSSCTGTFHPAPSAPDKSVTDAALPGQSSGPFYSPRDPEPPEPLTFRAQGVVGPGPHEEQRPYPQGLPGRLYSSMSDTNLAEAGLNYHAQRIGQLFQGPGRDSAVDLSSLKHSYSLGFADGRYLGQGLQYGSFTDLRHPTDLLSHPLPMRPYSSVSNIYSDHRYGPRGDAVGFQEASLAQYSATTAREISRMCAALNSMDQYGGRHGGGSGGPDLVPYQPQHGPGLNAPQGLASLRSGLLGNPTYPEGQPSPGNLAQYGPAASQGTAVRQLLPSTATVRAADGMIYSTINTPIAATLPITTQPASVLRPMVRGGMYRPYGSGGVTAVPLTSLTRVPMIAPRVPLGPAGLYRYPAPSRFPIASTIPPAEGPVYLGKPAAAKASGAGGPPRPELPAGGAREEPLSTTAPPAVIKEAPVAQAPAPPPGQKPAGDAAAGSGSGVLGRPVMEKEEASQEDRQRKQQEQLLQLERERVELEKLRQLRLQEELERERVELQRHREEEQLLVQRELQELQTIKHHVLQQQQEERQAQFALQREQLAQQRLQLEQIQQLQQQLQQQLEEQKQRQKAPFPATCEAPSRGPPPAATELAQNGQYWPPLTHTAFIAVAGTEGPGQAREPVLHRGLPSSASDMSLQTEEQWEAGRSGIKKRHSMPRLRDACEPESGPDPSTVRRIADSSVQTDDEEGEGRYLLTRRRRTRRSADCSVQTDDEDNAEWEQPVRRRRSRLSRHSDSGSDSKHEASASSSAAAAAARAMSSVGIQTISDCSVQTEPEQLPRVSPAIHITAATDPKVEIVRYISAPEKTGRGESLACQTEPDGQAQGVAGPQLIGPTAISPYLPGIQIVTPGALGRFEKKKPDPLEIGYQAHLPPESLSQLVSRQPPKSPQVLYSPVSPLSPHRLLDTSFASSERLNKAHVSPQKQFIADSTLRQQTLPRPMKTLQRSLSDPKPLSPTAEESAKERFSLYQHQGGLGSQVSALPPNGLVRKVKRTLPSPPPEEAHLPLAGQVPSQLYAASLLQRGLAGPTTVPATKASLLRELDRDLRLVEHESTKLRKKQAELDEEEKEIDAKLKYLELGITQRKESLAKDRVGRDYPPLRGLGEHRDYLSDSELNQLRLQGCTTPAGQYVDYPASAAVPATPSGPTAFQQPRFPPAATQYTAGSSGPTQNGFLAHQAPTYTGPSTYPAPTYPPGTSYPAEPGLPSQPAFHPTGHYAAPTPMPTTQSAPFPVQADSHAAHQKPRQTSLADLEQKVPTNYEVISSPAVTVSSTPSETGYSGPAVSSSYEHGKAPEHPRGGDRSSVSQSPAPTYPSDSHYTSLEQNVPRNYVMIDDISELTKDSTPTASDSQRPEPLGPGGVSGRPGKDPGEPAVLEGPTLPCCYGRGEEESEEDSYDPRGKSGHHRSMESNGRPASTHYYSDSDYRHGARADKYGPGPMGPKHPSKNLAPAAISSKRSKHRKQGMEQKISKFSPIEEAKDVESDLASYPPPTVSSSLTSRSRKFQDEITYGLKKNVYEQQRYYGVSSRDTAEEDDRMYGGSSRSRVASAYSGEKLSSHDFSSRSKGYERERETAQRLQKAGPKPSSLSMAHGRARPPMRSQASEEESPVSPLGRPRPAGGALPPGDTCPQFCSSHSMPDVQEHVKDGPRAHAYKREEGYILDDSHCVVSDSEAYHLGQEETDWFDKPRDARSDRFRHHGGHTVSSSQKRGPARHSYHDYDEPPEEGLWPHDEGGPGRHTSAKEHRHHGDHGRHSGRHAGEEPGRRAARPHARDMGRHETRPHPQASPAPAMQKKGQPGYPSSADYSQPSRAPSAYHHASDSKKGSRQAHSGPTVLQPKPEAQAQPQMQGRQAVPGPQQSQPPSSRQTPSGTASRQPQTQQQQQQQQQQQQQQQQQQQQQQQQGLGQQAPQQAPSQARLQQQSQPTTRSTAPAASHPAGKPQPGPTTAPGPQPAGLPRAEQAGSSKPAAKAPQQGRAPQAQSAPGPAGAKTGARPGGTPGAPAGQPAAEGESVFSKILPGGAAEQAGKLTEAVSAFGKKFSSFW
| null | null |
axo-dendritic transport [GO:0008088]; cytoskeleton organization [GO:0007010]; maintenance of presynaptic active zone structure [GO:0048790]; modulation of chemical synaptic transmission [GO:0050804]; presynapse to nucleus signaling pathway [GO:0099526]; presynaptic active zone assembly [GO:1904071]; protein localization to synapse [GO:0035418]; regulation of synaptic vesicle cycle [GO:0098693]; regulation of ubiquitin protein ligase activity [GO:1904666]; retrograde axonal transport [GO:0008090]; synapse organization [GO:0050808]; synaptic vesicle clustering [GO:0097091]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cell surface [GO:0009986]; cochlear hair cell ribbon synapse [GO:0098683]; cytoskeleton of presynaptic active zone [GO:0048788]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; Golgi-associated vesicle [GO:0005798]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; inhibitory synapse [GO:0060077]; neuron projection terminus [GO:0044306]; neuronal cell body [GO:0043025]; piccolo-bassoon transport vesicle [GO:1990257]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; presynaptic active zone cytoplasmic component [GO:0098831]; ribbon synapse [GO:0097470]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; trans-Golgi network [GO:0005802]
|
dynein light chain binding [GO:0045503]; enzyme inhibitor activity [GO:0004857]; metal ion binding [GO:0046872]; structural constituent of presynaptic active zone [GO:0098882]; transcription corepressor binding [GO:0001222]
|
PF05715;
|
3.30.40.10;
| null |
PTM: Myristoylated. The N-terminal myristoylation is not sufficient for presynaptic localization. {ECO:0000269|PubMed:12812759}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10564375}. Presynaptic active zone {ECO:0000269|PubMed:10564375, ECO:0000269|PubMed:12812759, ECO:0000269|PubMed:26212709}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10564375}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:26212709, ECO:0000269|PubMed:29150638}; Peripheral membrane protein {ECO:0000269|PubMed:26212709, ECO:0000269|PubMed:29150638}. Note=In retina, is localized in the outer plexiform layer at ribbon synapses formed by rods and cones but was absent from basal synaptic contacts formed by cones. In the retinal inner plexiform layer localized to conventional inhibitory GABAergic synapses, made by amacrine cells, but absent from the bipolar cell ribbon synapses (PubMed:10564375). {ECO:0000269|PubMed:10564375, ECO:0000269|PubMed:12812759, ECO:0000269|PubMed:26212709}.
| null | null | null | null | null |
FUNCTION: Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (PubMed:22875941). After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (PubMed:22875941). At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (PubMed:27907191). Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy by associating with ATG5 (PubMed:23403927, PubMed:27907191). Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (PubMed:25652077). Inhibits the activity of the proportion of DAO enzyme that localizes to the presynaptic active zone, which may modulate synaptic transmission (PubMed:21700703). {ECO:0000269|PubMed:21700703, ECO:0000269|PubMed:22875941, ECO:0000269|PubMed:23403927, ECO:0000269|PubMed:25652077, ECO:0000269|PubMed:27907191}.
|
Rattus norvegicus (Rat)
|
O88780
|
KLK8_RAT
|
MGRPPPCAIQTWILLFLLMGAWAGLTRAQGSKILEGQECKPHSQPWQTALFQGERLVCGGVLVGDRWVLTAAHCKKDKYSVRLGDHSLQKRDEPEQEIQVARSIQHPCFNSSNPEDHSHDIMLIRLQNSANLGDKVKPIELANLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCERAYPGKITEGMVCAGSSNGADTCQGDSGGPLVCNGVLQGITTWGSDPCGKPEKPGVYTKICRYTNWIKKTMGKRD
|
3.4.21.118
| null |
keratinocyte proliferation [GO:0043616]; memory [GO:0007613]; neuron projection morphogenesis [GO:0048812]; proteolysis [GO:0006508]; regulation of synapse organization [GO:0050807]; response to wounding [GO:0009611]; synapse organization [GO:0050808]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; secretory granule [GO:0030141]; serine protease inhibitor complex [GO:0097180]
|
peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shows a cytoplasmic distribution in the keratinocytes. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.; EC=3.4.21.118;
| null | null | null | null |
FUNCTION: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88783
|
FA5_MOUSE
|
MLLVCPCFFLLVVLGTRWAGWGSHQAEAAQLRQFYVAAQGILWNYHPEPTDPSLNSIPSFKKIVYREYEQYFKKEKPRSSNSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFNSGLIGPLLICKKGTLTEDGTQKMFDKQHVLLFAVFDESKSRSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDIKNCPKKTRSPKTLTREQRRYMKRWEYFIAAEEVIWNYAPVIPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPSIKQSGILGPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGSHTTIRPVQPGETFTYKWNILEFDEPTENDAQCLTRPYYSDVDVTRDIASGLIGLLLICKSRSLDQRGVQRVADIEQQAVFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHFTGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPKRRNLRLRFRDVKCNRDYDNEDSYEIYEPPAPTSMTTRRIHDSLENEFGIDNEDDDYQYLLASSLGIRSFKNSSLNPEENEFNLTALALENSSEFISPSTDRVVDSNSSRILSKIINNNLKDFQRTLPGSGATVAGTLLRNLIGLDENFVLNSSTEHRSSSYHENDMENPQSNITMVYLLPLGPKGSGNREQDKPKTIKTGRPHMMKHRFSWMKAPAGKTGRHSNPKNSYSGMKSEEDIPSELIPLKQKITSKFLNRRWRVASEKGSYEIIAANGEDTDVDKLTNSPQNQNITVPRGESTSHTNTTRKPSDLPTFSGVGHKSPHVRQEEENSGFQKRQLFIRTRKKKKNKKLALHSPLSPRGFDPLRGHNHSPFPDRRLLNHSLLLHKSNETALSPDLNQTSPSMSTDRSLPDYNQYSKNDTEQMSSSLDLYQSVPAEEHSPTFPAQDPDQTHSTTDPSYRSSPPELSQGLDYDLSHDFYPDDIGLTSFFPDQSQKSSFSSDDDQAIPSSDLSLFTISPELDQTIIYPDLDQLLLSPEDNQKTSSPDLGQVPLSPDDNQKTSSPDLGQVSLSPDDNQKTSSPDLGQVPLSLDDNQKTTSPDLGQVPLSPDDNQMITSPDLGQVPLSSDNQKTSSPDLGQVPLFPEDNQNYFLDLSQVPLSSDQNQETSSTDLLTLSPDFGQTVLSPDLDQLPLPSDNSQVTVSPDLSLLTLSPDFNEIILAPDLGQVTLSPDLIQTNPALNHGHKASSADPDQASYPPDSGQASSLPELNRTLPHPDLTHIPPPSPSPTLNNTSLSRKFNPLVVVGLSRVDGDDVEIVPSEEPERIDEDYAEDDFVTYNDPYRTDTRTDVNSSRNPDTIAAWYLRGHGGHKKFYYIAAEEITWNYAEFAQSEMDHEDTGHTPKDTTYKKVVFRKYLDSTFTSRDPRAEYEEHLGILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVNVERDIHSGLIGPLLICRKGTLHMERNLPMDMREFVLLFMVFDEKKSWYYEKSKGSRRIESPEEKNAHKFYAINGMIYNLPGLRMYEQEWVRLHLLNMGGSRDIHVVHFHGQTLLDNRTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLIIDKECKMPMGLSTGVISDSQIKASEYLTYWEPRLARLNNAGSYNAWSIEKTALDFPIKPWIQVDMQKEVVVTGIQTQGAKHYLKSCFTTEFQVAYSSDQTNWQIFRGKSGKSVMYFTGNSDGSTIKENRLDPPIVARYIRIHPTKSYNRPTLRLELQGCEVNGCSTPLGLEDGRIQDKQITASSFKKSWWGDYWEPSLARLNAQGRVNAWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSLSSEMYVKSYSIQYSDQGVAWKPYRQKSSMVDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFGCDIY
| null | null |
blood circulation [GO:0008015]; blood coagulation [GO:0007596]; response to vitamin K [GO:0032571]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule [GO:0031091]
|
copper ion binding [GO:0005507]; signaling receptor activity [GO:0038023]
|
PF07732;PF00754;
|
2.60.40.420;2.60.120.260;
|
Multicopper oxidase family
|
PTM: Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus). {ECO:0000250}.; PTM: Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity. {ECO:0000250}.; PTM: Activated protein C inactivates factor V and factor Va by proteolytic degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
|
Mus musculus (Mouse)
|
O88786
|
I13R2_MOUSE
|
MAFVHIRCLCFILLCTITGYSLEIKVNPPQDFEILDPGLLGYLYLQWKPPVVIEKFKGCTLEYELKYRNVDSDSWKTIITRNLIYKDGFDLNKGIEGKIRTHLSEHCTNGSEVQSPWIEASYGISDEGSLETKIQDMKCIYYNWQYLVCSWKPGKTVYSDTNYTMFFWYEGLDHALQCADYLQHDEKNVGCKLSNLDSSDYKDFFICVNGSSKLEPIRSSYTVFQLQNIVKPLPPEFLHISVENSIDIRMKWSTPGGPIPPRCYTYEIVIREDDISWESATDKNDMKLKRRANESEDLCFFVRCKVNIYCADDGIWSEWSEEECWEGYTGPDSKIIFIVPVCLFFIFLLLLLCLIVEKEEPEPTLSLHVDLNKEVCAYEDTLC
| null | null |
cytokine-mediated signaling pathway [GO:0019221]; immunoglobulin mediated immune response [GO:0016064]; negative regulation of immunoglobulin production [GO:0002638]; negative regulation of mast cell degranulation [GO:0043305]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; receptor complex [GO:0043235]
|
cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]
|
PF09240;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 5 subfamily
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
| null | null | null | null | null |
FUNCTION: Binds as a monomer with high affinity to interleukin-13 (IL13). {ECO:0000269|PubMed:9725226}.
|
Mus musculus (Mouse)
|
O88792
|
JAM1_MOUSE
|
MGTEGKAGRKLLFLFTSMILGSLVQGKGSVYTAQSDVQVPENESIKLTCTYSGFSSPRVEWKFVQGSTTALVCYNSQITAPYADRVTFSSSGITFSSVTRKDNGEYTCMVSEEGGQNYGEVSIHLTVLVPPSKPTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTAMRSEAAHMDAVELNVGGIVAAVLVTLILLGLLIFGVWFAYSRGYFERTKKGTAPGKKVIYSQPSTRSEGEFKQTSSFLV
| null | null |
actomyosin structure organization [GO:0031032]; cell adhesion [GO:0007155]; cellular response to mechanical stimulus [GO:0071260]; epithelial cell differentiation [GO:0030855]; establishment of endothelial intestinal barrier [GO:0090557]; intestinal absorption [GO:0050892]; leukocyte cell-cell adhesion [GO:0007159]; memory T cell extravasation [GO:0035683]; negative regulation of stress fiber assembly [GO:0051497]; positive regulation of blood pressure [GO:0045777]; positive regulation of establishment of endothelial barrier [GO:1903142]; positive regulation of platelet aggregation [GO:1901731]; positive regulation of Rho protein signal transduction [GO:0035025]; protein localization to bicellular tight junction [GO:1902396]; protein localization to plasma membrane [GO:0072659]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of cell shape [GO:0008360]; regulation of cytokine production [GO:0001817]; regulation of membrane permeability [GO:0090559]
|
bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; slit diaphragm [GO:0036057]
|
integrin binding [GO:0005178]; PDZ domain binding [GO:0030165]; protein homodimerization activity [GO:0042803]
|
PF13927;PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily
| null |
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11036763}. Cell membrane {ECO:0000269|PubMed:11036763}; Single-pass type I membrane protein {ECO:0000269|PubMed:11036763}. Note=Localized at tight junctions of both epithelial and endothelial cells.
| null | null | null | null | null |
FUNCTION: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11447115). The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (PubMed:11447115). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (PubMed:9660867). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (By similarity). Involved in platelet activation (By similarity). {ECO:0000250|UniProtKB:Q9Y624, ECO:0000269|PubMed:11447115, ECO:0000269|PubMed:9660867}.
|
Mus musculus (Mouse)
|
O88797
|
DAB2_RAT
|
MSNEVETSTTNGQPDQQAAPKAPSKKEKKKGSEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEEKKKVEEANKAEENGSEALMTLDDQANKLKLGVDQMDLFGDMSTPPDLNNPTESRDILLVDLNSEIDTNQNSLRENPFLTNGVTSCSLPRPKPQASFLPESAFSANLNFFPTPNPDPFRDDPFAQPDQSAPSSFHSLTSADQKKANPGSLSTPQSKGPLNGDTDYFGQQFDQISNRTGKQEAQGGPWPYPSSQTQQAVRTQNGVSEKEQNGFHIKSSPNPFVGSPPKGLSVPNGVKQDLESSVQSSAHDSIAIIPPPQSTKPGRGRRTAKSSANDLLASDIFASEPPGQMSPTGQPAVPQANFMDLFKTSAPAPMGSGPLVGLGTVPVTPPQAGPWTPVVFTPSTTVVPGAIISGQPSGFGQPLVFGTTPAVQVWNQPSSFATAASPPPPAVWCPTTSVAPNTWSSTSPLGNPFQSSNIFPPSTISTQSFPQPMMSSVLVTPPQPPPRNGPLKDTLSDAFTGLDPLGDKEVKEVKEMFKDFQLRQPPLVPSRKGETPSSGTSSAFSSYFNNKVGIPQEHVDHDDFDANQLLNKINEPPKPAPRQGVLSGTKSADNSLENPFSKGFSSTNPSVVSQPASSDAHRSPFGNPFA
| null | null |
cell morphogenesis [GO:0000902]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to transforming growth factor beta stimulus [GO:0071560]; clathrin coat assembly [GO:0048268]; extrinsic apoptotic signaling pathway [GO:0097191]; hematopoietic stem cell proliferation [GO:0071425]; in utero embryonic development [GO:0001701]; leading edge cell differentiation [GO:0035026]; myeloid cell differentiation [GO:0030099]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth [GO:0030308]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of neuron projection development [GO:0010977]; negative regulation of protein localization to plasma membrane [GO:1903077]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of aldosterone biosynthetic process [GO:0032349]; positive regulation of aldosterone secretion [GO:2000860]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of clathrin-dependent endocytosis [GO:2000370]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of endocytosis [GO:0045807]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; positive regulation of JNK cascade [GO:0046330]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor internalization [GO:0002092]; positive regulation of receptor recycling [GO:0001921]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; renal protein absorption [GO:0097017]; response to salt [GO:1902074]; response to steroid hormone [GO:0048545]; transforming growth factor beta receptor signaling pathway [GO:0007179]; Wnt signaling pathway [GO:0016055]
|
apical plasma membrane [GO:0016324]; clathrin coat of coated pit [GO:0030132]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
AP-2 adaptor complex binding [GO:0035612]; cargo receptor activity [GO:0038024]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; integrin binding [GO:0005178]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; SMAD binding [GO:0046332]
|
PF21792;PF00640;
|
2.30.29.30;
| null |
PTM: Phosphorylated. Phosphorylation during mitosis is leading to membrane displacement. There is some ambiguity for the mitotic phosphosite Ser-326/328. {ECO:0000269|PubMed:21097498}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and translocated to the cytoplasm (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269|PubMed:12473651, ECO:0000269|PubMed:19000037}.
|
Rattus norvegicus (Rat)
|
O88799
|
ZAN_MOUSE
|
MALPVWTLMLLVGAAWGQEQVPAWRPNSPDLGPMVHTSREDSILSKCDFEDNSRPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQGPLCVHFAFHMFGLSWGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDIPSWLMFEGMRGNTAYLDISLDGLSIQRGTCNQVCMSQMCTFDTLNDLCGWSWVPTATGAKWTQKKGPTGKQGVGPAEDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSHSRGCMTLSFHYIMHGQGHEEGLFVYATFLGNIRKYTLFSGHPGPDWQAVSVNYTGQGQIQFMVVGMFGNIPEPAIAVDAISIAPCGESFPQCDFEDRVHPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKLSQEGQSARLVSPPFCAPGGICVEFAYHMYGLGKGTTLKLLLGSPAGSSPIPLWNRVGSQSSGWMNSSVTIPKGYQQPMQLFIEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTVPTEVPIVLIEATASPTGEITLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTPTEVTTTPPEETTIPAEVTTVPPASIPPEETASLTEVTTTPPEETTTPTEVTTVPPEKTTIPTEVTTVPPASIFPEETTVPPEETTIASEETTVSTQETTLLTEQSAVTQTSIACRPPCPSPPLMPIGPLLSKPPGVSMFSLAPTTGVSTTESCPPNAHIELCACPASCESPKPSCQPPCIPGCVCNPGFLFSNNQCINESSCNCPYNNKHYKPGEEWFTPNCTERCRCLPGSLMECQISQCGTHTVCQLKSDQYQCEPYGKATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVSCLDKVVISLPETTVTMISGRHTLIGDQEVTLPAILSDDTYVGLSGRFVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGMMTHDEEELRLSWQVEEDEDKDWVSSRCQKKKNPPSCDAALGSTMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCARMSAMTATCQDAGYPVKPWREPQFCPLVCPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILSGSECVPSSQCGCTSFQGRYFKLQEQWFNPDCKEICTCESHNHILCKPWKCKAQEACSYKNGVLGCHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSQENNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNLRADMKPAGNSLLLGAAWKILEASDPGCFLAGGKPSRCADSDMDDVWTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTFCHSLQAYASLCAQAGQVTTWRNSTFCPMRCPPRSSYNPCANSCPATCLTLSTPRDCPTLPCVEGCECQSGHILSGTTCVPLRQCGCSDQDGSYHLLGESWYTEKTCTTLCTCSAHSNITCSPTACKANHVCLRQEGLLRCAAEMGECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNMPFFMISAKTDINTNGKNKTFGVYQLYIDIFNFHITLQKDHLVLISLINDSIVTLPTTTHIPGVSVMTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSGELAEDEQEFMNSWKDKSMDPNCQKIEGQNLQVEQQEIMNGKCRPIDFEKAQANCQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCPLECPAHSHYTNCLPSCPPSCLDPDSRCEGSGHKVPATCREGCICQPDYVLLNDKCVLRSHCGCKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNSNDGSSNCVKISLQCPAHSKFTDCLPPCHPSCSDPDGHCEGISTNAHSNCKEGCVCQPGYVLRNDKCVLRIECGCQHTQGGFIPAGKNWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIEDGTSNCANITLQCPAHSSFTNCLPPCQPSCSDPEGHCGGSTTKAPSACQEGCVCEPDYVVLNNKCVPRIECGCKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDIKDDASNCTEIILQCPDHSLYTHCLPSCLLSCSDPDGLCRGTSPEAPSTCKEGCVCDPDYVLSNDKCVLRIECGCKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDMEDGNSNCTSIPLQCPAHSHYTNCLPTCQPSCSDPDGHCEGSSTKAPSACKEGCVCEPDYVMLNNKCVPRIECGCKDTQGVLIPADKTWINRGCTQSCTCRGGAIQCQKYHCSSGTYCKDMEDDSSSCATITLQCPAHSHFTNCLPPCQPSCLDSEGHCEGSTTKAPSACQEGCVCEPDYVVLNNKCVPRIECGCKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIEDGNSNCTRISLQCPANSNFTSCLPSCQPSCSNTDVHCEGSSPNTLSSCREGCVCQSGYVLHNDKCILRNQCGCKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDLKDGSSNCTNIPLQCPAHSRYTNCLPSCPPLCLDPEGLCEGTSPKVPSTCREGCICQPGYLMHKNKCVLRIFCGCKNTQGAFISADKTWISRGCTQSCTCPAGAIHCRNFKCPSGTYCKNGDNGSSNCTEITLQCPTNSQFTDCLPSCVPSCSNRCEVTSPSVPSSCREGCLCNHGFVFSEDKCVPRTQCGCKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSEGSSTCTKITLQCPAHTQYTSCLPSCLPSCLDPEGLCKDISPKVPSTCKEGCVCQSGYVLNSDKCVLRAECDCKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNEDGNSNCAKITLQCPAHSLFTNCLPPCLPSCLDPDGLCKGASPKVPSTCKEGCICQSGYVLSNNKCLLRNRCGCKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSSQCPPGAYCKDNEDGSSNCARIPPQCPANSHYTDCFPPCPPSCSDPEGHCEASGPRVLSTCREGCLCNPGFVLDRDKCVPRVECGCKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNEDGNSNCAKITLQCPTHSNYTDCLPFCLPSCLDPSALCGGTSPKGPSTCKEGCVCQPGYVLDKDKCILKIECGCRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYCNHNNNCAKIPLQCPAHSHFTSCLPSCPPSCANLDGSCEQTSPKVPSTCKEGCLCQPGYFLNNGKCVLQTHCDCKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSGDGSSNCTKIHKGAMGDGVLMAGGIRALQCPAHSHFTSCLPSCPPSCSNLDGSCVESNFKAPSVCKKGCICQPGYLLNNDKCVLRIQCGCKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSRTCAKIPLQCPAHSHYTNCLPACSRSCTDLDGHCEGTSPKVPSPCKEGCLCQPGYVVHNHKCVLQIHCGCKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSSCSKITVQCPAHSQYTTCLPSCLPSCFDPEGLCGGASPRAPSTCREGCVCEADYVLREDKCVLRTQCGCKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDSVDGGSNCTKIALQCPAHSHHTYCLPSCIPSCSNVNDRCESTSLQRPSTCIEGCLCHSGFVFSKDKCVPRTQCGCKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIEDGNSNCVEITVQCPAHSHYSKCLPPCQPSCSDPDGHCEGTSPEAPSTCEEGCVCEPDYVLSNDKCVPSSECGCKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNEGNSNCVTYALKCPAHSLYTNCLPSCLPSCSDPEGLCGGTSPEVPSTCKEGCICQSGYVLHKNKCMLRIHCDCKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESEDGSSNCVSSTMKCPANSLYTHCLPTCLPSCSNPDGRCEGTSHKAPSTCREGCVCQPGYLLNKDTCVHKNQCGCKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNEDGSSDCAANKLERCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRGIEPLIMEGRNKISPKGSSTLHEVTTIVYGYKIQLQEELVVLVNDEKVAVPYNPNEHLRVMLRAQRLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGVLTSNVHVFGNSWEVKAQHAFFRFPRALPEDEERDEEPDLLQSECSQEQTALISSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTGWKTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCAMTCPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDTQSLPVTHCGCTADGIYYKLGDSFVTNDCSQHCTCASQGILLCEPYGCRAGESCMVANFTRGCFQDSPCLQNPCHNDGRCEEQGATFICHCDFGYGGEFCTEPQDITTRKKIEASSLVAILPGVLVMVLVPVLLPRVYVYMATRTTMGRRRMKRKEKKLLRQSRLRLEDADVPEPTFKATEF
| null | null |
binding of sperm to zona pellucida [GO:0007339]; cell adhesion [GO:0007155]; regulation of binding of sperm to zona pellucida [GO:2000359]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
extracellular matrix binding [GO:0050840]
|
PF00629;PF01826;PF12714;PF00094;
|
2.60.120.200;2.10.70.10;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Exclusively on the apical region of the sperm head.
| null | null | null | null | null |
FUNCTION: Binds in a species-specific manner to the zona pellucida of the egg. May be involved in gamete recognition and/or signaling.
|
Mus musculus (Mouse)
|
O88801
|
HOME2_RAT
|
MGEQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRANTVFGLGFSSEQQLTKFAEKFQEVREAARLARDKSQEKIETSSNHSQESGCETPSSTQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKLGTDN
| null | null |
behavioral response to cocaine [GO:0048148]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; G protein-coupled glutamate receptor signaling pathway [GO:0007216]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of interleukin-2 production [GO:0032703]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of store-operated calcium entry [GO:2001256]; sensory perception of sound [GO:0007605]
|
apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; intracellular organelle [GO:0043229]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; stereocilium tip [GO:0032426]
|
actin binding [GO:0003779]; G protein-coupled glutamate receptor binding [GO:0035256]; glutamate receptor binding [GO:0035254]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; synaptic receptor adaptor activity [GO:0030160]
|
PF00568;
|
1.20.5.1700;2.30.29.30;
|
Homer family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17584991}. Cell membrane {ECO:0000269|PubMed:17584991}. Postsynaptic density. Synapse. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q9QWW1}. Note=Postsynaptic density of neuronal cells. The stabilization and clustering of the metabotropic glutamate receptors appears to be mediated by isoform 1 and isoform 2 at the cell surface.
| null | null | null | null | null |
FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. Required for normal hearing (By similarity). Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA (By similarity). {ECO:0000250|UniProtKB:Q9NSB8}.
|
Rattus norvegicus (Rat)
|
O88807
|
PADI4_RAT
|
MAQGAVIHVAPEEPTHAVCVVGTATPLDIRGSAPRGSTSFSITASPEVVVDVIHGPPSKKSTTGASKWPLDPKLEVTLQMKAASSRIDDQKVRISYYGPKTSSTQALLYLTGVELSLSADVTRTGKAKPAPAGKDQSTWTWGPDGHGAILLVNCDKEDPKSSGMDFEDDKVLDNKDLQDMSPMTLSTKTPKDFFDKYQLVLQVPKAKMNKVRVFRATRGKLPSRYKVVLGPQQFSHRLELLGGQHSTDFYVEGLAFPDADFKGLIPLTISLLDKSNPELPEALVFQDTVMFRVAPWIMTPNTQPPQEVYVCRFSDNEDFLKSLATFTKKAKCKLTVCPEEENQDDQWMQDEMEIGYIQAPHKTLPVVFDSPRDRGLKDFPVKRVMGPNFGYVTRGLYRAEVTGLDAFGNLEVSPPVTVRGKEYPLGRILIGSSGYSSSESRDMHQILQDFLGAQQVQAPVRLFSDWLFVGHVDEFLSFVPARGKQGFRLLLSSPRACYQMFQELQTEGHGEASLFEGLKRKRQTISDILSSQKLRDQNAYVESCIDWNREVLKRELGLTEGDIIDIPQLFRIVGNSRGNPKAEAFFPNMVNMLVLGKHLGIPKPFGPIINGRCCLEEKVCSLLEPLGLHCTFINDFYSYHMYHGEVHCGTNVRRKPFAFKWWHMVP
|
3.5.3.15
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9UM07}; Note=Binds 5 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UM07};
|
chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; innate immune response [GO:0045087]; nucleosome assembly [GO:0006334]; post-translational protein modification [GO:0043687]; stem cell population maintenance [GO:0019827]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
calcium ion binding [GO:0005509]; histone arginine deiminase activity [GO:0140794]; histone H3R17 arginine deiminase activity [GO:0140797]; histone H3R2 arginine deiminase activity [GO:0140795]; histone H3R26 arginine deiminase activity [GO:0140798]; histone H3R8 arginine deiminase activity [GO:0140796]; identical protein binding [GO:0042802]; protein-arginine deiminase activity [GO:0004668]
|
PF03068;PF08527;PF08526;
|
2.60.40.1700;2.60.40.1860;
|
Protein arginine deiminase family
|
PTM: Autocitrullination at Arg-372 and Arg-374 inactivates the enzyme. {ECO:0000250|UniProtKB:Q9UM07}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UM07}. Nucleus {ECO:0000250|UniProtKB:Q9UM07}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9UM07}. Note=Cytoplasmic granules of eosinophils and neutrophils. {ECO:0000250|UniProtKB:Q9UM07}.
|
CATALYTIC ACTIVITY: Reaction=H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+); Xref=Rhea:RHEA:18089, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:10588, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29965, ChEBI:CHEBI:83397; EC=3.5.3.15; Evidence={ECO:0000250|UniProtKB:Q9UM07};
| null | null | null | null |
FUNCTION: Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci (By similarity). Required for the formation of neutrophil extracellular traps (NETs); NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1 (By similarity). {ECO:0000250|UniProtKB:Q9UM07, ECO:0000250|UniProtKB:Q9Z183}.
|
Rattus norvegicus (Rat)
|
O88808
|
TUB_RAT
|
MTSKPHSDWIPYSVLDDEGSNLRQQKLDRQRALLEQKQKKKRQEPLMVQANADGRPRSRRARQSEEQAPLVESYLSSSGSTSYQVQEADSLASVQPGATRPPAPASAKKTKGAAASGGQGGAPRKEKKGKHKGTSGPATLAEDKSEAQGPVQILTVGQSDHAKDAGETAAGGGAQPSGQDLRATMQRKGISSSMSFDEEEDEDENSSSSSQLNSNTRPSSATSRKSTREAASAPSPAAPEPPVDIEVQDLEEFALRPAPQGITIKCRITRDKKGMDRGMYPTYFLHLDREDGKKVFLLAGRKRKKSKTSNYLISVDPTDLSRGGDSYIGKLRSNLMGTKFTVYDNGVNPQKASSSTLESGTLRQELAAVCYETNVLGFKGPRKMSVIVPGMNMVHERVCIRPRNEHETLLARWQNKNTESIIELQNKTPVWNDDTQSYVLNFHGRVTQASVKNFQIIHGNDPDYIVMQFGRVAEDVFTMDYNYPLCALQAFAIALSSFDSKLACE
| null | null |
intraciliary transport [GO:0042073]; phagocytosis, recognition [GO:0006910]; photoreceptor cell maintenance [GO:0045494]; positive regulation of phagocytosis [GO:0050766]; protein localization to cilium [GO:0061512]; protein localization to photoreceptor outer segment [GO:1903546]; receptor localization to non-motile cilium [GO:0097500]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to cocaine [GO:0042220]; response to hormone [GO:0009725]; retina development in camera-type eye [GO:0060041]; sensory perception of sound [GO:0007605]
|
cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
G protein-coupled receptor binding [GO:0001664]; intraciliary transport particle A binding [GO:0120160]; protein-containing complex binding [GO:0044877]
|
PF01167;PF16322;
| null |
TUB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19695251}. Nucleus {ECO:0000250}. Secreted {ECO:0000269|PubMed:19695251}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Binds phospholipid and is anchored to the plasma membrane through binding phosphatidylinositol 4,5-bisphosphate. Is released upon activation of phospholipase C. Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha. Does not have a cleavable signal peptide and is secreted by a non-conventional pathway (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight (By similarity). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88809
|
DCX_MOUSE
|
MELDFGHFDERDKASRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNSAQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSAAAGPKASPTPQKTSAKSPGPMRRSKSPADSGNDQDANGTSSSQLSTPKSKQSPISTPTSPGSLRKHKVDLYLPLSLDDSDSLGDSM
| null | null |
axon extension [GO:0048675]; axoneme assembly [GO:0035082]; brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; dendrite morphogenesis [GO:0048813]; hippocampus development [GO:0021766]; intracellular signal transduction [GO:0035556]; layer formation in cerebral cortex [GO:0021819]; neuron migration [GO:0001764]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of endocytosis [GO:0045807]; pyramidal neuron development [GO:0021860]; retina development in camera-type eye [GO:0060041]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; growth cone [GO:0030426]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]
|
microtubule binding [GO:0008017]
|
PF03607;
|
3.10.20.230;
| null |
PTM: Phosphorylation by MARK1, MARK2 and PKA regulates its ability to bind microtubules (By similarity). Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21 (PubMed:15099191, PubMed:22807455). {ECO:0000250|UniProtKB:Q9ESI7, ECO:0000269|PubMed:15099191, ECO:0000269|PubMed:22807455}.; PTM: Ubiquitinated by MDM2, leading to its degradation by the proteasome (PubMed:25088421). Ubiquitinated by MDM2 and subsequent degradation leads to reduce the dendritic spine density of olfactory bulb granule cells (PubMed:25088421). {ECO:0000269|PubMed:25088421}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9ESI7}. Note=Localizes at neurite tips. {ECO:0000250|UniProtKB:Q9ESI7}.
| null | null | null | null | null |
FUNCTION: Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May participate along with PAFAH1B1/LIS-1 in a distinct overlapping signaling pathway that promotes neuronal migration. {ECO:0000250|UniProtKB:Q9ESI7}.
|
Mus musculus (Mouse)
|
O88811
|
STAM2_MOUSE
|
MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDRVGSTPSGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRSVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGVTFPSAGSQTVAAAAKNGTSLNKNKEDEDIAKAIELSLQEQKQQYTETKALYPPAESQLNNKAARRVRALYDFEAVEDNELTFKHGELITVLDDSDANWWQGENHRGTGLFPSNFVTTDLSTEVETATVDKLNVIDDDVEEIKKSEPEPVYIDEGKMDRALQILQSIDPKESKPDSQDLLDLEDVCQQMGPMIDEKLEEIDRKHSELSELNVKVLEALDLYNKLVNEAPVYSVYSKLHPAHYPPAAAGVPVQTYPVQSHGGNYLGHGIHQVSVAQNYNLGPDPMGSLRSLPPNMNSVTAHTVQPPYLSTGQDTVSNPSYMNQSSRLQAAAGTAAYTQPVGMSTDVSSFQNTASGLPQLAGFPVAVPAPVAAQPQASYHQQPLL
| null | null |
protein transport [GO:0015031]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; nucleoplasm [GO:0005654]
|
phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]
|
PF00018;PF02809;PF00790;
|
1.20.5.1940;1.25.40.90;2.30.30.40;
|
STAM family
|
PTM: Phosphorylated in response to IL-2, GM-CSF, EGF and PDGF. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10651905, ECO:0000269|PubMed:12551915}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as a sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). {ECO:0000250, ECO:0000269|PubMed:12972556}.
|
Mus musculus (Mouse)
|
O88813
|
ACSL5_RAT
|
MLFIFNFLFSPLPTPALICLLTFGTAIFLWLINRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYEVFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMLIENVEKDLTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKENFKKPMPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVRNGIIRRNSLWDKLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLPSFAAKIGVKGSFEELCQNQCVKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE
|
6.2.1.15; 6.2.1.3
| null |
cellular response to insulin stimulus [GO:0032869]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of long-chain fatty acid import across plasma membrane [GO:0010747]; positive regulation of triglyceride biosynthetic process [GO:0010867]; response to cholesterol [GO:0070723]; response to glucose [GO:0009749]; response to nutrient [GO:0007584]; response to sucrose [GO:0009744]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; oleoyl-CoA ligase activity [GO:0090434]
|
PF00501;
|
3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16263710}. Endoplasmic reticulum {ECO:0000269|PubMed:16263710}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q9ULC5}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52016, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84024, ChEBI:CHEBI:136117, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52012, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:76625, ChEBI:CHEBI:136115, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q9ULC5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000250|UniProtKB:Q9ULC5}; CATALYTIC ACTIVITY: Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526, ChEBI:CHEBI:72745, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q9ULC5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; Evidence={ECO:0000250|UniProtKB:Q9ULC5}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000305|PubMed:28209804};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=666 uM for ATP {ECO:0000269|PubMed:15683247}; KM=2.4 uM for CoA {ECO:0000269|PubMed:15683247}; KM=8.6 uM for palmitate {ECO:0000269|PubMed:15683247}; KM=6.5 uM for palmitate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=4.4 uM for stearate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=6.3 uM for oleate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=5.8 uM for linoleate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=1.8 uM for arachidonate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=5053 nmol/min/mg enzyme with palmitate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=2164 nmol/min/mg enzyme with stearate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=3726 nmol/min/mg enzyme with oleate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=1351 nmol/min/mg enzyme with linoleate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=1880 nmol/min/mg enzyme with arachidonate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=130 nmol/min/mg enzyme with palmitate as substrate {ECO:0000269|PubMed:15683247};
| null | null | null |
FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:28209804). ACSL5 may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL at the villus tip of the crypt-villus axis of the small intestine (By similarity). May have a role in the survival of glioma cells (By similarity). May activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. It was suggested that it may also stimulate fatty acid oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids. {ECO:0000250, ECO:0000269|PubMed:16263710, ECO:0000269|PubMed:17761945, ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:9722683}.
|
Rattus norvegicus (Rat)
|
O88816
|
SNAT_MOUSE
|
MLNINSLKPEALHLPLGTSEFLGCQRRHTLPASEFRCLTPEDATSAFEIEREAFISVSGTCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLTQESLTLHRPGGRTAHLHVLAVHRTFRQQGKGSVLLWRYLHHLGSQPAVRRAVLMCEDALVPFYEKFGFQAVGPCAITVGSLTFTELQCSLRCHAFLRRNSGC
|
2.3.1.87
| null |
cellular response to cAMP [GO:0071320]; circadian rhythm [GO:0007623]; melatonin biosynthetic process [GO:0030187]; N-terminal protein amino acid acetylation [GO:0006474]; photoperiodism [GO:0009648]; response to calcium ion [GO:0051592]; response to copper ion [GO:0046688]; response to corticosterone [GO:0051412]; response to cytokine [GO:0034097]; response to insulin [GO:0032868]; response to light stimulus [GO:0009416]; response to organic cyclic compound [GO:0014070]; response to prostaglandin E [GO:0034695]; response to zinc ion [GO:0010043]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]
|
14-3-3 protein binding [GO:0071889]; aralkylamine N-acetyltransferase activity [GO:0004059]; arylamine N-acetyltransferase activity [GO:0004060]
|
PF00583;
|
3.40.630.30;
|
Acetyltransferase family, AANAT subfamily
|
PTM: cAMP-dependent phosphorylation on both N-terminal Thr-29 and C-terminal Ser-203 regulates AANAT activity by promoting interaction with 14-3-3 proteins. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}.
|
CATALYTIC ACTIVITY: Reaction=a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine + CoA + H(+); Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378, ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:77827; EC=2.3.1.87; Evidence={ECO:0000250|UniProtKB:Q29495};
| null |
PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.
| null | null |
FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. {ECO:0000250|UniProtKB:Q29495}.
|
Mus musculus (Mouse)
|
O88819
|
FUT9_MOUSE
|
MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWVFSPMESASSVLKMKNFFSTKTDYFNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNLPQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVFEVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDFNSPSELAKYLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
|
2.4.1.152
| null |
fucosylation [GO:0036065]; glycosphingolipid biosynthetic process [GO:0006688]; Lewis x epitope biosynthetic process [GO:0106402]; N-glycan fucosylation [GO:0036071]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; neuronal stem cell division [GO:0036445]; oligosaccharide biosynthetic process [GO:0009312]; polysaccharide biosynthetic process [GO:0000271]; positive regulation of neuron projection development [GO:0010976]; protein glycosylation [GO:0006486]; protein N-linked glycosylation [GO:0006487]; protein O-linked glycosylation [GO:0006493]; regulation of leukocyte cell-cell adhesion [GO:1903037]; regulation of leukocyte tethering or rolling [GO:1903236]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
|
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity [GO:0017083]; alpha-(1->3)-fucosyltransferase activity [GO:0046920]; protein homodimerization activity [GO:0042803]
|
PF17039;PF00852;
|
3.40.50.11660;
|
Glycosyltransferase 10 family
|
PTM: N-glycosylated with complex-type N-glycans. {ECO:0000250|UniProtKB:Q9Y231}.
|
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y231}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6P4F1}. Golgi apparatus membrane {ECO:0000269|PubMed:12626397}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941; EC=2.4.1.152; Evidence={ECO:0000269|PubMed:12626397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258; Evidence={ECO:0000269|PubMed:12626397, ECO:0000269|PubMed:15121843, ECO:0000269|PubMed:16973732, ECO:0000269|PubMed:22645129, ECO:0000269|PubMed:9756916}; CATALYTIC ACTIVITY: Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:68044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:145343, ChEBI:CHEBI:176900; Evidence={ECO:0000250|UniProtKB:Q9Y231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68045; Evidence={ECO:0000250|UniProtKB:Q9Y231}; CATALYTIC ACTIVITY: Reaction=alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP-beta-L-fucose = alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48388, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90383, ChEBI:CHEBI:90384; Evidence={ECO:0000269|PubMed:12626397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48389; Evidence={ECO:0000269|PubMed:12626397}; CATALYTIC ACTIVITY: Reaction=alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP-beta-L-fucose = a neolactoside IV(3)-alpha-Gal,III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48380, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90380, ChEBI:CHEBI:90381; Evidence={ECO:0000269|PubMed:12626397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48381; Evidence={ECO:0000269|PubMed:12626397, ECO:0000269|PubMed:16973732}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48376, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90376, ChEBI:CHEBI:90379; Evidence={ECO:0000269|PubMed:12626397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377; Evidence={ECO:0000269|PubMed:12626397, ECO:0000269|PubMed:16973732}; CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:136545, ChEBI:CHEBI:139509; Evidence={ECO:0000250|UniProtKB:Q9Y231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077; Evidence={ECO:0000250|UniProtKB:Q9Y231}; CATALYTIC ACTIVITY: Reaction=beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose = beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP + H(+); Xref=Rhea:RHEA:77187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60239, ChEBI:CHEBI:61352; Evidence={ECO:0000250|UniProtKB:Q9Y231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77188; Evidence={ECO:0000250|UniProtKB:Q9Y231}; CATALYTIC ACTIVITY: Reaction=an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:77191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133510, ChEBI:CHEBI:195560; Evidence={ECO:0000250|UniProtKB:Q9Y231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77192; Evidence={ECO:0000250|UniProtKB:Q9Y231};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:22645129}.; PATHWAY: Glycolipid biosynthesis. {ECO:0000269|PubMed:12626397, ECO:0000269|PubMed:16973732}.
| null | null |
FUNCTION: Catalyzes alpha(1->3) linkage of fucosyl moiety transferred from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2 lactosamine (LacNAc, beta-D-Gal-(1->4)-beta-D-GlcNAc-) glycan attached to glycolipids and N- or O-linked glycoproteins. Fucosylates distal type 2 LacNAc and its fucosylated (H-type 2 LacNAc) and sialylated (sialyl-type 2 LacNAc) derivatives to form Lewis x (Lex) (CD15) and Lewis y (Ley) antigenic epitopes involved in cell adhesion and differentiation (By similarity) (PubMed:12626397, PubMed:15121843, PubMed:16973732, PubMed:22645129, PubMed:9756916). Generates Lex epitopes in the brain, presumably playing a role in the maintenance of neuronal stemness and neurite outgrowth in progenitor neural cells (By similarity) (PubMed:16973732, PubMed:22645129). Fucosylates the internal type 2 LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE (By similarity). Can also modify milk oligosaccharides in particular type 2 tetrasaccharide LNnT (By similarity) (PubMed:9756916). {ECO:0000250|UniProtKB:Q9Y231, ECO:0000269|PubMed:12626397, ECO:0000269|PubMed:15121843, ECO:0000269|PubMed:16973732, ECO:0000269|PubMed:22645129, ECO:0000269|PubMed:9756916}.
|
Mus musculus (Mouse)
|
O88824
|
JTB_MOUSE
|
MLAGAGRRGLPRAGHLCWLLCAFTLKLCEAEAPVREEKLSVSTSTSPCWLAEEFVVTEECTPCSNFQIKTTPECGSTGYVEKITCSSSKRNEFKSCRSALLEQHLFWKFEGVVVAVALVFACLVIVRQRQLDRKALEKVRKQIESI
| null | null |
apoptotic mitochondrial changes [GO:0008637]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; positive regulation of protein kinase activity [GO:0045860]; regulation of cell population proliferation [GO:0042127]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrion [GO:0005739]; spindle [GO:0005819]
|
protein kinase binding [GO:0019901]
|
PF05439;
|
3.30.720.220;
|
JTB family
|
PTM: Undergoes N-terminal proteolytic processing, removing a peptide of about 1 kDa from the N-terminus of the protein. {ECO:0000269|PubMed:17369841}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:17369841}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected at the centrosome and along spindle fibers during prophase and metaphase. Detected at the midbody during telophase (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity (By similarity). Inhibits apoptosis induced by TGFB1. Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential. {ECO:0000250, ECO:0000269|PubMed:17369841}.
|
Mus musculus (Mouse)
|
O88828
|
RPAB2_RAT
|
MSDNEDNFDGDDFDDVEEDEGLDDLENAEEEGQENVEILPSGERPQANQKRITTPYMTKYERARVLGTRALQIAMCAPVMVELEGETDPLLIAMKELKARKIPIIIRRYLPDGSYEDWGVDELIISD
| null | null |
transcription by RNA polymerase I [GO:0006360]; transcription by RNA polymerase II [GO:0006366]; transcription by RNA polymerase III [GO:0006383]; tRNA transcription by RNA polymerase III [GO:0042797]
|
fibrillar center [GO:0001650]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]; RNA polymerase II, core complex [GO:0005665]; RNA polymerase III complex [GO:0005666]
|
DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; RNA polymerase I activity [GO:0001054]; RNA polymerase II activity [GO:0001055]; RNA polymerase III activity [GO:0001056]
|
PF01192;
|
3.90.940.10;
|
Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61218}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P61218}.
| null | null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPABC2 is part of the clamp element and together with parts of POLR2A/RPB1 and POLR2B/RPB2 forms a pocket to which the POLR2D/RPB4-POLR2G/RPB7 subcomplex binds. {ECO:0000250|UniProtKB:P20435, ECO:0000250|UniProtKB:P61218}.
|
Rattus norvegicus (Rat)
|
O88829
|
SIAT9_MOUSE
|
MHTEAVGGAARRPQKLRSQAAAPACRAMPSEFTSAKLRSDCSRTSLQWYTRTQHKMRRPSLLIKDICKCTLVAFGVWLLYILILNYTAEECDMKRMHYVDPDRIKRAQSYAQEVLQKECRPRYAKTAMALLFEDRYSINLEPFVQKVPTASEAELKYDPPFGFRKFSSKVQSLLDMLPEHDFPEHLRAKACKRCVVVGNGGILHGLELGHALNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDVEYYANDLFVTVLFKSVDFKWLQAMVKNESLPFWVRLFFWKQVAEKVPLQPKHFRILNPVIIKETAFDILQYSEPQSRFWGHDKNIPTIGVIAVVLATHLCDEVSLAGFGYDLSQPRTPLHYFDSQCMGAMHWQVMHNVTTETKFLLKLLKEGVVEDLSGGIH
|
2.4.3.9
| null |
lipid metabolic process [GO:0006629]; protein glycosylation [GO:0006486]
|
Golgi membrane [GO:0000139]
|
lactosylceramide alpha-2,3-sialyltransferase activity [GO:0047291]
|
PF00777;
|
3.90.1480.20;
|
Glycosyltransferase 29 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GM3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:18417, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377; EC=2.4.3.9; Evidence={ECO:0000269|PubMed:10092602, ECO:0000269|PubMed:12629211, ECO:0000269|PubMed:9875239}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18418; Evidence={ECO:0000305|PubMed:10092602, ECO:0000305|PubMed:12629211, ECO:0000305|PubMed:9875239}; CATALYTIC ACTIVITY: Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA2 (d18:1(4E)/18:0) = CMP + ganglioside GM2 (d18:1(4E)/18:0) + H(+); Xref=Rhea:RHEA:41776, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78485, ChEBI:CHEBI:78486; Evidence={ECO:0000250|UniProtKB:Q9UNP4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41777; Evidence={ECO:0000250|UniProtKB:Q9UNP4}; CATALYTIC ACTIVITY: Reaction=beta-D-Gal-(1<->1')-Cer + CMP-N-acetyl-beta-neuraminate = CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1<->1')-ceramide; Xref=Rhea:RHEA:41780, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82643, ChEBI:CHEBI:143593; Evidence={ECO:0000250|UniProtKB:Q9UNP4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41781; Evidence={ECO:0000250|UniProtKB:Q9UNP4}; CATALYTIC ACTIVITY: Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 (d18:1(4E)/18:0) = CMP + ganglioside GM1 (d18:1(4E)/18:0) + H(+); Xref=Rhea:RHEA:41784, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:78484; Evidence={ECO:0000250|UniProtKB:Q9UNP4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41785; Evidence={ECO:0000250|UniProtKB:Q9UNP4};
| null | null | null | null |
FUNCTION: (Microbial infection) Gangliosides GD1b and GT1b (derived from GM3) may serve as receptors for some C.botulinum neurotoxins (minimally types BoNT/A, B, C) (PubMed:16115873). {ECO:0000305|PubMed:16115873}.; FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, embryogenesis, development, and oncogenesis) (PubMed:10092602, PubMed:12629211, PubMed:9875239). Mainly involved in the biosynthesis of ganglioside GM3 but can also use different glycolipids as substrate acceptors such as D-galactosylceramide (GalCer), asialo-GM2 (GA2) and asialo-GM1 (GA1), although less preferentially than beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer (LacCer) (By similarity). {ECO:0000250|UniProtKB:Q9UNP4, ECO:0000269|PubMed:10092602, ECO:0000269|PubMed:12629211, ECO:0000269|PubMed:9875239}.
|
Mus musculus (Mouse)
|
O88831
|
KKCC2_RAT
|
MSSCVSSQPTSDRAAPQDELGSGGVSRESQKPCEALRGLSSLSIHLGMESFIVVTECEPGRGVDLSLARDQPLEADGQELPLDASEPESRSLLSGGKMSLQERSQGGPASSSSLDMNGRCICPSLSYSPASSPQSSPRMPRRPTVESHHVSITGLQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRASPCGGGGSALVKGGPCVESCGAPAPGSPPRTPPQQPEEAMEPE
|
2.7.11.17
| null |
CAMKK-AMPK signaling cascade [GO:0061762]; positive regulation of protein phosphorylation [GO:0001934]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]
|
cytosol [GO:0005829]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]
|
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein kinase activator activity [GO:0030295]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Phosphorylated by PKA (By similarity). Each isoform may show a different pattern of phosphorylation (By similarity). Autophosphorylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96RR4}. Cytoplasm {ECO:0000250|UniProtKB:Q96RR4}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q96RR4}. Note=Predominantly nuclear in unstimulated cells, relocalizes into cytoplasm and neurites after forskolin induction. {ECO:0000250|UniProtKB:Q96RR4}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.17;
| null | null | null | null |
FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1 and CAMK4. Phosphorylates CAMK1D (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals. May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching. {ECO:0000250, ECO:0000269|PubMed:21807092, ECO:0000269|PubMed:21957496, ECO:0000269|PubMed:8631893, ECO:0000269|PubMed:9822657}.
|
Rattus norvegicus (Rat)
|
O88833
|
CP4AA_MOUSE
|
MSVSALSPTRFADSLSGFLQVASVLGLLLLLVKAVQFYLHRQWLLKAFQQFPSPPFHWFFGHEKFKGDQELQEIVSCIENFPSAFPRWFWGSKAYLTVYDPDYMKVILGRSDPKANGAYRLLAPWIGYGLLLLNGQPWFQHRRMLTPAFHYDILKPYVKNMADSIRLMLDKWERLADQDSSIEIFQHISLMTLDTVMKCAFSHKGSVQVDGNYRTYLQAIGDLNNLFHSRVRNIFHQNDTIYKLSSNGRLAKQACQLAHDHTDGVIKLRKDQLQDEGELEKIKKKRRLDFLDILLFARMENGDSMSDKDLRAEVDTFMFEGHDTTASGVSWIFYALATHPDHQQRCREEVQSLLGDGSSITWDHLDQIPYTTMCIKEALRLYPPVPGIVRELSTSVTFPDGRSLPKGVQVTLSIYGLHHNPKVWPNPEVFDPSRFAPDSPRHSHSFLPFSGGARNCIGKQFAMSELKVIVALTLLRFELLPDPTRVPMPLARLVLKSKNGIYLHLKKLH
|
1.14.14.80
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P08516};
|
arachidonic acid metabolic process [GO:0019369]; fatty acid metabolic process [GO:0006631]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651]
|
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; long-chain fatty acid omega-hydroxylase activity [GO:0102033]; monooxygenase activity [GO:0004497]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08516}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:P08516}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991, ChEBI:CHEBI:140992; EC=1.14.14.80; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56749; Evidence={ECO:0000250|UniProtKB:P08516}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:36204, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38948; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76628; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 14-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40203, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77033; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40204; Evidence={ECO:0000250|UniProtKB:P08516}; CATALYTIC ACTIVITY: Reaction=hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40199, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:55329, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.80; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40200; Evidence={ECO:0000250|UniProtKB:P08516}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41728, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78424; EC=1.14.14.80; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41729; Evidence={ECO:0000250|UniProtKB:P08516}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60580, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132029; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60581; Evidence={ECO:0000250|UniProtKB:P08516}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 17-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60932, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144041; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60933; Evidence={ECO:0000250|UniProtKB:P08516}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76624; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756; Evidence={ECO:0000250|UniProtKB:P08516}; CATALYTIC ACTIVITY: Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53572, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84025, ChEBI:CHEBI:137474; Evidence={ECO:0000250|UniProtKB:P08516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573; Evidence={ECO:0000250|UniProtKB:P08516};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for dodecanoate {ECO:0000269|PubMed:17112342}; Vmax=55 nmol/min/nmol enzyme toward dodecanoate {ECO:0000269|PubMed:17112342};
| null | null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long-chain fatty acids (By similarity). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (By similarity) (PubMed:17112342). In kidney, may play an important role in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (By similarity). Also participates in the formation of anti-inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) in kidney by converting 8,9-epoxyeicosatrienoic acid (EET) to 20,8,9-HEET, an activator of PPARA. Displays substantially lower fatty acid omega-1 hydroxylase activity (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). {ECO:0000250|UniProtKB:P08516, ECO:0000269|PubMed:17112342}.
|
Mus musculus (Mouse)
|
O88838
|
SPSB2_MOUSE
|
MGQTALARGSSSTPTSQALYSDFSPPEGLEELLSAPPPDLVAQRHHGWNPKDCSENIDVKEGGLCFERRPVAQSTDGVRGKRGYSRGLHAWEISWPLEQRGTHAVVGVATALAPLQADHYAALLGSNSESWGWDIGRGKLYHQSKGLEAPQYPAGPQGEQLVVPERLLVVLDMEEGTLGYSIGGTYLGPAFRGLKGRTLYPSVSAVWGQCQVRIRYMGERRVEEPQSLLHLSRLCVRHALGDTRLGQISTLPLPPAMKRYLLYK
| null | null |
intracellular signal transduction [GO:0035556]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytosol [GO:0005829]; SCF ubiquitin ligase complex [GO:0019005]
|
ubiquitin ligase-substrate adaptor activity [GO:1990756]
|
PF07525;PF00622;
|
2.60.120.920;1.10.750.20;
|
SPSB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99619}. Note=Exhibits a diffuse cytosolic localization. {ECO:0000250|UniProtKB:Q99619}.
| null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20603330). Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2 (PubMed:20603330). Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity). {ECO:0000250|UniProtKB:Q99619, ECO:0000269|PubMed:20603330}.
|
Mus musculus (Mouse)
|
O88839
|
ADA15_MOUSE
|
MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTLSGSMESRVVQDSPPMSLADVLQTGLPEALRISLELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLSPERGYTLELGPGDLQRPVISRIQDHLLLGHTCAPSWHASVPTRAGPDLLLEQHHAHRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPGPAPAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFERQPSLAPMSSLCGNMFVDPGEQCDCGFPDECTDPCCDHFTCQLRPGAQCASDGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSDIRLGDGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPGGSYMPCAPRDVMCGQLQCQWGRSQPLLGSVQDRLSEVLEANGTQLNCSWVDLDLGNDVAQPLLALPGTACGPGLVCIGHRCQPVDLLGAQECRRKCHGHGVCDSSGHCRCEEGWAPPDCMTQLKATSSLTTGLLLSLLLLLVLVLLGASYWHRARLHQRLCQLKGSSCQYRAPQSCPPERPGPPQRAQQMTGTKQASVVSFPVPPSRPLPPNPVPKKLQAALADRSNPPTRPLPADPVVRRPKSQGPTKPPPPRKPLPANPQGQHPPGDLPGPGDGSLPLVVPSRPAPPPPAASSLYL
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion per subunit. {ECO:0000305};
|
angiogenesis [GO:0001525]; cardiac epithelial to mesenchymal transition [GO:0060317]; cell adhesion [GO:0007155]; cellular response to phorbol 13-acetate 12-myristate [GO:1904628]; collagen catabolic process [GO:0030574]; immune response to tumor cell [GO:0002418]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; male gonad development [GO:0008584]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cell-matrix adhesion [GO:0001953]; proteolysis [GO:0006508]; response to hypobaric hypoxia [GO:1990910]; tissue regeneration [GO:0042246]
|
acrosomal vesicle [GO:0001669]; adherens junction [GO:0005912]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; motile cilium [GO:0031514]
|
integrin binding [GO:0005178]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; SH3 domain binding [GO:0017124]
|
PF08516;PF00200;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;2.60.120.260;
| null |
PTM: The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site. {ECO:0000269|PubMed:9748307}.; PTM: May be partially sialylated.; PTM: Phosphorylation increases association with PTKs. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:18390692}; Single-pass type I membrane protein {ECO:0000269|PubMed:18390692}. Cell junction, adherens junction {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:18390692}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:18390692}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed.
| null | null | null | null | null |
FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration (By similarity). Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg. {ECO:0000250, ECO:0000269|PubMed:11882657, ECO:0000269|PubMed:12897135, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:18390692}.
|
Mus musculus (Mouse)
|
O88844
|
IDHC_MOUSE
|
MSRKIQGGSVVEMQGDEMTRIIWELIKEKLILPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKYNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVTGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPKDGTQKVTYMVHDFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKKYKSQFEAQKICYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLICPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWSRGLAHRAKLDNNTELSFFAKALEDVCIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKAKLAQAKL
|
1.1.1.42
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:29923039}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:29923039}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000305|PubMed:29923039};
|
2-oxoglutarate metabolic process [GO:0006103]; female gonad development [GO:0008585]; glutathione metabolic process [GO:0006749]; glyoxylate cycle [GO:0006097]; isocitrate metabolic process [GO:0006102]; NADP metabolic process [GO:0006739]; regulation of phospholipid biosynthetic process [GO:0071071]; regulation of phospholipid catabolic process [GO:0060696]; response to organic cyclic compound [GO:0014070]; response to oxidative stress [GO:0006979]; response to steroid hormone [GO:0048545]; tricarboxylic acid cycle [GO:0006099]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]
|
isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]
|
PF00180;
|
3.40.718.10;
|
Isocitrate and isopropylmalate dehydrogenases family
|
PTM: Acetylation at Lys-374 dramatically reduces catalytic activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12031902}.
|
CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; Evidence={ECO:0000269|PubMed:12031902, ECO:0000269|PubMed:29923039}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19630; Evidence={ECO:0000305|PubMed:12031902, ECO:0000305|PubMed:29923039};
| null | null | null | null |
FUNCTION: Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:12031902, PubMed:29923039). Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways (PubMed:12031902). May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity). {ECO:0000250|UniProtKB:Q9XSG3, ECO:0000269|PubMed:12031902, ECO:0000269|PubMed:29923039, ECO:0000303|PubMed:12031902}.
|
Mus musculus (Mouse)
|
O88845
|
AKA10_MOUSE
|
MRGAGPSPRHSPRALRPDPGPAMSFFRRKVKGKEQEKTLDVKSTKASVAVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLRDTVVLPYFLQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKRHETPASSVTEALDRRLGDSSSAPLLVTQSEGTDLSSRTQNPQNHLLLSQEGHSARSLHREVARTGSHQIPTDSQDSSSRLAVGSRNSCSSPLRELSEKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIAKICGEDGQVDPNCFVLAQAVVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLAAHGSVCLPEESHSGGSDGSTAQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMSFGRVSDLGQFIRESEPEPDVKKSKGFMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDVMQQAHHDQPLEKSTKL
| null | null |
protein localization [GO:0008104]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
protein kinase A binding [GO:0051018]
|
PF00615;
|
1.10.167.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11248059}. Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but also membrane associated and cytoplasmic.
| null | null | null | null | null |
FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase.
|
Mus musculus (Mouse)
|
O88846
|
RNF4_RAT
|
MSTRNPQRKRRGGAVNSRQTQKRTRETTSTPEISLEAEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSKDKDVYVTTHTPRSTKDEGTTGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI
|
2.3.2.27
| null |
cellular response to arsenic-containing substance [GO:0071243]; cellular response to cytokine stimulus [GO:0071345]; cellular response to gamma radiation [GO:0071480]; cellular response to hydroxyurea [GO:0072711]; cellular response to testosterone stimulus [GO:0071394]; male gonad development [GO:0008584]; negative regulation of protein localization to chromatin [GO:0120186]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein K6-linked ubiquitination [GO:0085020]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; regulation of kinetochore assembly [GO:0090234]; regulation of spindle assembly [GO:0090169]; response to arsenic-containing substance [GO:0046685]; response to estradiol [GO:0032355]; response to human chorionic gonadotropin [GO:0044752]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
DNA binding [GO:0003677]; identical protein binding [GO:0042802]; nuclear androgen receptor binding [GO:0050681]; nuclear estrogen receptor binding [GO:0030331]; nucleosome binding [GO:0031491]; SUMO polymer binding [GO:0032184]; TBP-class protein binding [GO:0017025]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF13639;
|
3.30.40.10;
| null |
PTM: Sumoylated; conjugated by one or two SUMO1 moieties. {ECO:0000269|PubMed:15707587}.; PTM: Autoubiquitinated. {ECO:0000269|PubMed:14987998}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78317}. Nucleus {ECO:0000269|PubMed:11319220, ECO:0000269|PubMed:9710597}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20943951}. Nucleus, PML body {ECO:0000269|PubMed:20943951}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18408734};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18408734}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation (PubMed:14987998, PubMed:15707587, PubMed:18408734). Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (PubMed:15707587, PubMed:20943951). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (By similarity). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (By similarity). Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation (PubMed:11319220, PubMed:9710597). Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (By similarity). {ECO:0000250|UniProtKB:P78317, ECO:0000269|PubMed:11319220, ECO:0000269|PubMed:14987998, ECO:0000269|PubMed:15707587, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:20943951, ECO:0000269|PubMed:9710597}.
|
Rattus norvegicus (Rat)
|
O88848
|
ARL6_MOUSE
|
MGLLDRLSGLLGLKKKEVHVLCLGLDNSGKTTIINKLKPSNAQSQDIVPTIGFSIEKFKSSSLSFTVFDMSGQGRYRNLWEHYYKDGQAIIFVIDSSDKLRMVVAKEELDTLLNHPDIKHRRIPILFFANKMDLRDSVTSVKVSQLLCLESIKDKPWHICASDAIKGEGLQEGVDWLQDQIQAVKT
| null | null |
brain development [GO:0007420]; cilium assembly [GO:0060271]; fat cell differentiation [GO:0045444]; intracellular protein transport [GO:0006886]; protein localization to cilium [GO:0061512]; protein localization to non-motile cilium [GO:0097499]; protein polymerization [GO:0051258]; protein targeting to membrane [GO:0006612]; protein transport from ciliary membrane to plasma membrane [GO:1903445]; Ras protein signal transduction [GO:0007265]; regulation of smoothened signaling pathway [GO:0008589]; retina layer formation [GO:0010842]; vesicle-mediated transport [GO:0016192]
|
axonemal microtubule [GO:0005879]; axoneme [GO:0005930]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; membrane coat [GO:0030117]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; phospholipid binding [GO:0005543]
|
PF00025;
|
3.40.50.300;
|
Small GTPase superfamily, Arf family
| null |
SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in membrane protein trafficking at the base of the ciliary organelle (By similarity). Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). Together with BBS1, is necessary for correct trafficking of PKD1 to primary cilia (PubMed:24939912). Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation (By similarity). May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade (By similarity). Isoform 2 may be required for proper retinal function and organization (PubMed:20333246). {ECO:0000250|UniProtKB:Q9H0F7, ECO:0000269|PubMed:20333246, ECO:0000269|PubMed:24939912}.
|
Mus musculus (Mouse)
|
O88850
|
HIPK3_RAT
|
MASQVLVYPPYVYQTQSSAFCSVKKLKVEPSGCVFQERACPQIHVNGRHFGNPLPSTKGSAFQTKIPFSKPRGHSFSLQAGAIVVKDTAGATKVIAAQAQQAGVEAPRAVVWRNRLHFLGGPQRCGLKRKSEELDNHSGAMQIVDELSILPAMLQTNMGNPVTVVTATTGSKQNCTSGEGDYQLVQHEVLCSVKNTYEVLDFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTENADEYNFVRAYECFQHRNHTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPVLQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKSTRFFCRETDMSHSGWRLKTLEEHEAETGMKSKEARKYIFNSLDDIVHVNTVMDLEGSDLLAEKADRREFVSLLKKMLLIDADLRITPIETLNHPFVSMKHLLDFPHSSHVKSCFHIMDICKSPSSCETNNHSKMSLLRPVASNGTAALAANFTKVGTLRSQALTTSAHSVVHHGIPLQAGTAQFGCGDAFHQTLIICPPAIQGIPAAHGKPTSYSIRVDNTVPLVTQAPAVQPLQIRPGVLSQTWSGRTQQMLIPAWQQVTPMAPAAATLTSEGMAGSQRLGDWGKMIPHSNHYNSVMPPPLLTNQITLSAPQPISVGIAHVVWPQPATTKKNKLCQNRSNSLQNTNVPHSAFISPKIISGKEVEEVSCVETQDNHTSEGEARTCHEASVRQDSSVSDKQRQTIIIADSPSPAVSVITISSDTDDEETSPRPSLRECKGSLDCEACQSTLNIDRMCSLSSPDSTLSTSSSGQSSPSPCKRPNSMSDDEQESGCETVDGSPTSDSSGHDSPFAESSFVEDTPQNPELGTCAGTEAKPALSTAVEPPVGTERGLNVDAHMANTDSTCQPLTKGQPAPGKLNQPSASAARQQKPTSAFQQQHLNLSQVQHFGTGHQEWNGNFGHRRQQAYIPTSVTSNPFTLSHGSPNHTAVHAHLAGSAHLGGQPTLLPYPPSTALSSAAPVAHLLASPCTSRPMLQHPTYNISHPSGIVHQVPVGINPRLLPSPTIHQTQYKPIFPPHSYIAASPAYTGFPLSPTKLSQYPYM
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; mRNA transcription [GO:0009299]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; PML body [GO:0016605]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, HIPK subfamily
|
PTM: Autophosphorylated. Autophosphorylation is not required for catalytic activity.; PTM: May be sumoylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9725910}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. {ECO:0000269|PubMed:9725910}.
|
Rattus norvegicus (Rat)
|
O88856
|
TPST2_MOUSE
|
MRLSVRKVLLAAGCALALVLAVQLGQQVLECRAVLGGTRNPRRMRPEQEELVMLGADHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWTKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLARLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGRDKCLPVYYEQLVLHPRRSLKRILDFLGIAWSDTVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPRDVVRDMAQIAPMLARLGYDPYANPPNYGNPDPIVINNTHRVLKGDYKTPANLKGYFQVNQNSTSPHLGSS
|
2.8.2.20
| null |
fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; peptidyl-tyrosine sulfation [GO:0006478]; prevention of polyspermy [GO:0060468]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
protein-tyrosine sulfotransferase activity [GO:0008476]
|
PF13469;
|
3.40.50.300;
|
Protein sulfotransferase family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60704}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60704}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60704}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]; Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20; Evidence={ECO:0000269|PubMed:9733778};
| null | null | null | null |
FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:9733778}.
|
Mus musculus (Mouse)
|
O88867
|
KMO_RAT
|
MASSDTEGKRVVVIGGGLVGALNACFLAKRNFQVDVYEAREDIRVANFMRGRSINLALSYRGRQALKAVGLEDQIVSKGVPMKARMIHSLSGKKSAIPYGNKSQYILSISREKLNKDLLTAVESYPNAKVHFGHKLSKCCPEEGILTMLGPNKVPRDITCDLIVGCDGAYSTVRAHLMKKPRFDYSQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFTCTLFMSFEEFEKLPTHSDVLDFFQKNFPDAIPLMGEQALMRDFFLLPAQPMISVKCSPFHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNNDLSVCLPEFSRFRIPDDHAISDLSMYNYIEMRAHVNSRWFLFQRLLDKFLHALMPSTFIPLYTMVAFTRIRYHEAVLRWHWQKKVINRGLFVLGSLVAIGSAYILVHHLSPRPLELLRSAWTGTSGHWNRSADISPRVPWSH
|
1.14.13.9
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O15229, ECO:0000255|HAMAP-Rule:MF_03018};
|
'de novo' NAD biosynthetic process from tryptophan [GO:0034354]; anthranilate metabolic process [GO:0043420]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; kynurenic acid biosynthetic process [GO:0034276]; kynurenine metabolic process [GO:0070189]; L-kynurenine metabolic process [GO:0097052]; NAD metabolic process [GO:0019674]; positive regulation of glutamate secretion [GO:0014049]; positive regulation of glutamate secretion, neurotransmission [GO:1903296]; quinolinate biosynthetic process [GO:0019805]; response to lipopolysaccharide [GO:0032496]; response to salt stress [GO:0009651]; tryptophan catabolic process [GO:0006569]
|
extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741]
|
FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; kynurenine 3-monooxygenase activity [GO:0004502]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]
|
PF01494;
|
3.50.50.60;
|
Aromatic-ring hydroxylase family, KMO subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:1332540}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:1332540}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349; EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:1332540};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=258 uM for L-kynurenine {ECO:0000269|PubMed:26752518}; KM=11.3 uM for NADPH {ECO:0000269|PubMed:1332540}; KM=316 uM for NADH {ECO:0000269|PubMed:1332540};
|
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}.
| null | null |
FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract. {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:26752518, ECO:0000269|PubMed:28398044}.
|
Rattus norvegicus (Rat)
|
O88869
|
RASF9_RAT
|
MAPFGRNLLKTRHKNRSPTKDMDPEEKEIVVWVCQEEKIVCGLTKRTTSIDVIQALLEEHEATFGEKRFLLGKASDYCIVEKWRGSERALPPLTRILKLWKAWGDEQPNMQFVLVKTDAFLPVPLWRTAETKLVQNNEKPWELSPANYMKTLPPDKQKRIVRKTFRKLAKIRQDTGSHDRDNMECLVHLIISQDHTIHQQVQRMKELDMEIEKCEAKIHLDRIGNDGADYVQEAYLMPRSSEEEQKLDFQSEDNQTLEDLNDGEGVSQLEEQLQYYRALIDKLSAEIEREVKGAGTDGSEDMEGAAACELENSDLESVKCDLEKSMKAGLKIHSHLSGIQREIKYSDSLLQMKAREYELLAKEFSSLHISSKDGCQGKENRGKEAEASSSNGEIPPLTQRVFNTYTNDTDSDTGISSNHSQDSETTLGDVLLLAT
| null | null |
endosomal transport [GO:0016197]; intracellular transport [GO:0046907]; protein targeting [GO:0006605]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; endosome [GO:0005768]; recycling endosome [GO:0055037]; trans-Golgi network transport vesicle membrane [GO:0012510]
|
enzyme binding [GO:0019899]; protein domain specific binding [GO:0019904]
| null | null | null | null |
SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:9837933}. Note=Accumulates on perinuclear endosomes.
| null | null | null | null | null |
FUNCTION: May play a role in regulating vesicuar trafficking in cells. {ECO:0000269|PubMed:9837933}.
|
Rattus norvegicus (Rat)
|
O88870
|
BEST1_MOUSE
|
MTITYTNKVANARLGSFSSLLLCWRGSIYKLLYGEFLVFIFLYYSIRGLYRMVLSSDQQLLFEKLALYCDSYIQLIPISFVLGFYVTLVVSRWWSQYENLPWPDRLMIQVSSFVEGKDEEGRLLRRTLIRYAILGQVLILRSISTSVYKRFPTLHHLVLAGFMTHGEHKQLQKLGLPHNTFWVPWVWFANLSMKAYLGGRIRDTVLLQSLMNEVCTLRTQCGQLYAYDWISIPLVYTQVVTVAVYSFFLACLIGRQFLNPNKDYPGHEMDLVVPVFTILQFLFYMGWLKVAEQLINPFGEDDDDFETNWIIDRNLQVSLLSVDGMHQNLPPMERDMYWNEAAPQPPYTAASARSRRHSFMGSTFNISLKKEDLELWSKEEADTDKKESGYSSTIGCFLGLQPKNYHLPLKDLKTKLLCSKNPLLEGQCKDANQKNQKDVWKFKGLDFLKCVPRFKRRGSHCGPQAPSSHPTEQSAPSSSDTGDGPSTDYQEICHMKKKTVEFNLNIPESPTEHLQQRRLDQMSTNIQALMKEHAESYPYRDEAGTKPVLYE
| null | null |
chloride transport [GO:0006821]; detection of light stimulus involved in visual perception [GO:0050908]; gamma-aminobutyric acid secretion, neurotransmission [GO:0061534]; glutamate secretion [GO:0014047]; protein complex oligomerization [GO:0051259]; regulation of calcium ion transport [GO:0051924]; regulation of synaptic plasticity [GO:0048167]; transepithelial chloride transport [GO:0030321]
|
basolateral plasma membrane [GO:0016323]; chloride channel complex [GO:0034707]; membrane microdomain [GO:0098857]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
bicarbonate channel activity [GO:0160133]; chloride channel activity [GO:0005254]; identical protein binding [GO:0042802]; intracellular calcium activated chloride channel activity [GO:0005229]; ligand-gated channel activity [GO:0022834]
|
PF01062;
| null |
Anion channel-forming bestrophin (TC 1.A.46) family, Calcium-sensitive chloride channel subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23021213, ECO:0000269|PubMed:29121962}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76090}. Basolateral cell membrane {ECO:0000250|UniProtKB:O76090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76090}. Note=Localized at the surface membrane of microdomains adjacent to glutamatergic synapses. {ECO:0000269|PubMed:23021213}.
|
CATALYTIC ACTIVITY: Reaction=4-aminobutanoate(in) = 4-aminobutanoate(out); Xref=Rhea:RHEA:35035, ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:20929730}; CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:23021213, ECO:0000269|PubMed:29121962}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:O76090}; CATALYTIC ACTIVITY: Reaction=hydrogencarbonate(in) = hydrogencarbonate(out); Xref=Rhea:RHEA:28695, ChEBI:CHEBI:17544; Evidence={ECO:0000250|UniProtKB:O76090}; CATALYTIC ACTIVITY: Reaction=D-serine(in) = D-serine(out); Xref=Rhea:RHEA:29455, ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:34952697};
| null | null | null | null |
FUNCTION: Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (By similarity). Allows the movement of chloride and hydrogencarbonate (By similarity). Found in a partially open conformation leading to significantly smaller chloride movement (By similarity). Upon F2R/PAR-1 activation, the sequestered calcium is released into the cytosol of astrocytes, leading to the (Ca2+)-dependent release of L-glutamate into the synaptic cleft that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (PubMed:23021213, PubMed:25645137, PubMed:29121962). Upon activation of the norepinephrine-alpha-1 adrenergic receptor signaling pathway, transports as well D-serine than L-glutamate in a (Ca2+)-dependent manner, leading to activation of adjacent NMDAR receptors and therefore regulates the heterosynaptic long-term depression and metaplasticity during initial memory acquisition (PubMed:34952697). Releases the 4-aminobutanoate neurotransmitter in a (Ca2+)-dependent manner, and participates in its tonic release from cerebellar glial cells (PubMed:20929730). {ECO:0000250|UniProtKB:O76090, ECO:0000269|PubMed:20929730, ECO:0000269|PubMed:23021213, ECO:0000269|PubMed:25645137, ECO:0000269|PubMed:29121962, ECO:0000269|PubMed:34952697}.
|
Mus musculus (Mouse)
|
O88871
|
GABR2_RAT
|
MASPPSSGQPRPPPPPPPPARLLLPLLLSLLLWLAPGAWGWTRGAPRPPPSSPPLSIMGLMPLTKEVAKGSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHFRWRRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFSNDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAFEESMFGSKYQWIIPGWYEPAWWEQVHVEANSSRCLRRSLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQFEREYNSKRSGVGPSKFHGYAYDGIWVIAKTLQRAMETLHASSRHQRIQDFNYTDHTLGKIILNAMNETNFFGVTGQVVFRNGERMGTIKFTQFQDSREVKVGEYNAVADTLEIINDTIRFQGSEPPKDKTIILEQLRKISLPLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWILTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVERYSMEPDPAGRDISIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNVQFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRRFQFTQNQKKEDSKTSTSVTSVNQASTSRLEGLQSENHRLRMKITELDKDLEEVTMQLQDTPEKTTYIKQNHYQELNDILSLGNFTESTDGGKAILKNHLDQNPQLQWNTTEPSRTCKDPIEDINSPEHIQRRLSLQLPILHHAYLPSIGGVDASCVSPCVSPTASPRHRHVPPSFRVMVSGL
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; gamma-aminobutyric acid signaling pathway [GO:0007214]; neuron-glial cell signaling [GO:0150099]; synaptic transmission, GABAergic [GO:0051932]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; G protein-coupled GABA receptor complex [GO:1902712]; G protein-coupled receptor heterodimeric complex [GO:0038039]; GABA receptor complex [GO:1902710]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]
|
G protein-coupled GABA receptor activity [GO:0004965]; protein heterodimerization activity [GO:0046982]
|
PF00003;PF01094;PF18455;
|
3.40.50.2300;
|
G-protein coupled receptor 3 family, GABA-B receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872317, ECO:0000305|PubMed:10457184}; Multi-pass membrane protein {ECO:0000269|PubMed:9872317}. Postsynaptic cell membrane {ECO:0000269|PubMed:9872317}; Multi-pass membrane protein {ECO:0000269|PubMed:9872317}. Perikaryon {ECO:0000269|PubMed:14718537}. Cell projection, dendrite {ECO:0000269|PubMed:10457184}. Note=Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane (PubMed:10457184). In contrast, GABBR2 does not depend on GABBR1 for transport to the cell membrane. {ECO:0000305|PubMed:10457184}.
| null | null | null | null | null |
FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:9872315, PubMed:9872317, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:10658574, PubMed:9872317). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10924501, PubMed:9872315, PubMed:9872317, PubMed:9872744, Ref.4). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10457184, PubMed:10924501, PubMed:9872315, PubMed:9872317, PubMed:9872744). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:10457184, PubMed:9872317, PubMed:9872744). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10924501, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (By similarity). {ECO:0000250|UniProtKB:O75899, ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10457184, ECO:0000269|PubMed:10658574, ECO:0000269|PubMed:10924501, ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872317, ECO:0000269|PubMed:9872744, ECO:0000269|Ref.4}.
|
Rattus norvegicus (Rat)
|
O88873
|
GMEB2_RAT
|
MATPDVSVHMEEVVVVTTPDTAVDGSGVEEVKTVLVTTNLAPHGGDLTEDNMETENAAAAACAFTASSQLKEAVLVKMAEEGENLEAEIVYPITCGDSRANLIWRKFVCPGINVKCVQYDEHVISPKEFVHLAGKSTLKDWKRAIRMNGIMLRKIMDSGELDFYQHDKVCSNTCRSTKIDLSGARVSLSSPTSTEYIPLTPAAADVNGSPATITIETCEDPGDWTTTIGDDTFAFWRGLKDAGLLDEVIQEFQQELEETMKGLQQRVQDPPLQLRDAVLLNNIVQNFGMLDLVKKVLASHKCQMDRSREQYARDLAALEQQCDEHRRRAKELKHKSQHLSNVLMTLTPVSLPSPMKRPRLARATSGPAAMASQVLTQSAQIALGPGMPMSQLTSVPLGKVVSTLPSTVLGKGSPQAAPASSPASPLLGGYTVLASSGSTFPSTVEIHPDTSSLTVLSTAAMQDGTTVLKVVSPLQLLTLPGLGPTLQNVAQASPAGSTIVTMPTAAATGPEEHTATIEVAAVAEDHEQK
| null | null |
positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF01342;
|
3.10.390.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
| null | null | null | null | null |
FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88874
|
CCNK_MOUSE
|
MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQGPQSQPSQGSEAAQPPQKDSQQSAQQQQQQAQQPKKPSPQPSPPRQAKRAVVVSPKEENKATEPPPPPKIPKLEATHPPLPPAHPPPDRKPPLAPALGEAEATGPVETSDLPKVQIPPPAHPAPVHQPPPLPHRPPPPPPSSYMTGMSTTSSYMSGEGYQSLQSMMKTEGPSYGALPPASFPPPTIPPPTPGYPPPPPTYNPNFPPPPPRLPPTHAVPPHPPPGLGLPPASYPPPAVPPGGQPPVPPPIPPPGMPPVGGLGRAAWMR
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response [GO:0006974]; in utero embryonic development [GO:0001701]; negative regulation of stem cell differentiation [GO:2000737]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of signal transduction [GO:0009966]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cyclin K-CDK12 complex [GO:0002944]; cyclin K-CDK13 complex [GO:0002945]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nucleus [GO:0005634]
|
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase binding [GO:0019901]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]
|
PF00134;PF21797;
|
1.10.472.10;
|
Cyclin family, Cyclin C subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:22012619}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:22012619}.
|
Mus musculus (Mouse)
|
O88875
|
BY55_MOUSE
|
MQRILMAPGQSCCALAILLAIVNFQHGGCIHVTSSASQKGGRLDLTCTLWHKKDEAEGLILFWCKDNPWNCSPETNLEQLRVKRDPETDGITEKSSQLVFTIEQATPSDSGTYQCCARSQKPEIYIHGHFLSVLVTGNHTEIRQRQRSHPDFSHINGTLSSGFLQVKAWGMLVTSLVALQALYTL
| null | null |
adaptive immune response [GO:0002250]; defense response to Gram-negative bacterium [GO:0050829]; innate immune response [GO:0045087]; mucosal immune response [GO:0002385]; negative regulation of adaptive immune memory response [GO:1905675]; negative regulation of angiogenesis [GO:0016525]; negative regulation of CD4-positive, alpha-beta T cell costimulation [GO:1900280]; negative regulation of T cell receptor signaling pathway [GO:0050860]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of natural killer cell cytokine production [GO:0002729]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated immune response to tumor cell [GO:0002857]; positive regulation of type II interferon production [GO:0032729]; T cell costimulation [GO:0031295]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
activating MHC class I receptor activity [GO:0032397]; kinase binding [GO:0019900]; MHC class I protein complex binding [GO:0023024]; MHC class Ib receptor activity [GO:0032394]; signaling receptor binding [GO:0005102]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: [CD160 antigen]: Cell membrane {ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O95971}.; SUBCELLULAR LOCATION: [CD160 antigen, soluble form]: Secreted {ECO:0000250|UniProtKB:O95971, ECO:0000305|PubMed:16177084}. Note=Released from the cell membrane by GPI cleavage. {ECO:0000250|UniProtKB:O95971, ECO:0000305|PubMed:16177084}.
| null | null | null | null | null |
FUNCTION: [CD160 antigen]: Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in activated T cells (By similarity). Receptor for both classical and non-classical MHC class I molecules (PubMed:16177084). Receptor or ligand for TNF superfamily member TNFRSF14, participating in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to NK cells enhancing IFNG production and anti-tumor immune response (PubMed:25711213). On activated CD4+ T cells, interacts with TNFRSF14 and down-regulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (By similarity). In the context of bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells, triggering the production of antimicrobial proteins and pro-inflammatory cytokines (PubMed:22801499). {ECO:0000250|UniProtKB:O95971, ECO:0000269|PubMed:16177084, ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}.; FUNCTION: [CD160 antigen, soluble form]: The soluble GPI-cleaved form, usually released by activated lymphocytes, might play an immune regulatory role by limiting lymphocyte effector functions. {ECO:0000250|UniProtKB:O95971}.
|
Mus musculus (Mouse)
|
O88876
|
DHRS3_MOUSE
|
MVWKWLGALVVFPLQMIYLVTKAAVGMVLPPKLRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAALEEIHRFSGTYTCMNTFKGRT
|
1.1.1.300
| null |
bone morphogenesis [GO:0060349]; cardiac septum morphogenesis [GO:0060411]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; outflow tract morphogenesis [GO:0003151]; regulation of ossification [GO:0030278]; regulation of retinoic acid receptor signaling pathway [GO:0048385]; retinoid metabolic process [GO:0001523]; roof of mouth development [GO:0060021]
|
lipid droplet [GO:0005811]; membrane [GO:0016020]
|
NAD-retinol dehydrogenase activity [GO:0004745]; NADP-retinol dehydrogenase activity [GO:0052650]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.300; Evidence={ECO:0000250|UniProtKB:O75911};
| null | null | null | null |
FUNCTION: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH. {ECO:0000250|UniProtKB:O75911}.
|
Mus musculus (Mouse)
|
O88878
|
ZFAN5_MOUSE
|
MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADAGLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSSSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI
| null | null |
face development [GO:0060324]; fibroblast migration [GO:0010761]; in utero embryonic development [GO:0001701]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; respiratory system process [GO:0003016]; skeletal system morphogenesis [GO:0048705]; smooth muscle tissue development [GO:0048745]; vasculature development [GO:0001944]
|
cytoplasm [GO:0005737]
|
DNA binding [GO:0003677]; zinc ion binding [GO:0008270]
|
PF01754;PF01428;
|
1.20.5.4770;4.10.1110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. {ECO:0000269|PubMed:16194934, ECO:0000269|PubMed:16424905}.
|
Mus musculus (Mouse)
|
O88879
|
APAF_MOUSE
|
MDAKARNCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAALLQSGLPLVSSSSGKDTDGGITSFVRTVLCEGGVPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSGGVHWVSIGKQDKSGLLMKLQNLCMRLDQEESFSQRLPLNIEEAKDRLRVLMLRKHPRSLLILDDVWDPWVLKAFDNQCQILLTTRDKSVTDSVMGPKHVVPVESGLGREKGLEILSLFVNMKKEDLPAEAHSIIKECKGSPLVVSLIGALLRDFPNRWAYYLRQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCVLWDLETEEVEDILQEFVNKSLLFCNRNGKSFCYYLHDLQVDFLTEKNRSQLQDLHRKMVTQFQRYYQPHTLSPDQEDCMYWYNFLAYHMASANMHKELCALMFSLDWIKAKTELVGPAHLIHEFVAYRHILDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYRQAKLQAKQEGDTGRLYLEWINKKTIKNLSRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQVNCCHFTNKSNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSINVKRFFLSSEDPPEDVEVIVKCCSWSADGDKIIVAAKNKVLLFDIHTSGLLAEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETKKVCKNSAIVLKQEIDVVFQENETMVLAVDNIRGLQLIAGKTGQIDYLPEAQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVFLQAHQETVKDFRLLQDSRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCAPISVEEGTATHGGWVTDVCFSPDSKTLVSAGGYLKWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQVLE
| null | null |
brain development [GO:0007420]; cardiac muscle cell apoptotic process [GO:0010659]; cell differentiation [GO:0030154]; cellular response to transforming growth factor beta stimulus [GO:0071560]; forebrain development [GO:0030900]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; neural tube closure [GO:0001843]; neuron apoptotic process [GO:0051402]; positive regulation of apoptotic signaling pathway [GO:2001235]; regulation of apoptotic DNA fragmentation [GO:1902510]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584]
|
apoptosome [GO:0043293]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ADP binding [GO:0043531]; ATP binding [GO:0005524]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]
|
PF21296;PF17908;PF00619;PF00931;PF00400;
|
1.25.40.370;1.10.533.10;1.10.8.430;3.40.50.300;1.10.10.10;2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O88881
|
BEGIN_RAT
|
MWTGGRRPGRLRRAASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQQRVSLHMEKHGCSLPSPLCHPSYADSVPTCVIAKVLEKPDPGSLSSRMSDASARDLAYRDGVENPGPRPPYKGDIYCSDTALYCPDERDHDRRPSVDTPVTDVGFLRAQNSTDSLAEEEEAEAAAFPEAYRREAFQGYAASLPTSSSYSSFSATSEEKEHAQASTLTASQQAIYLNSREELFSRKPPSATYGSSPRYAKAAATLGSPLEAQVAPGFARTVSPYPAEPYRYPASQQALMPPNLWSLRAKPSGNRLAAREDIRGQWRPLSVEDVGAYSYQAGAAGRAASPCNFSERFYGGGGGGGSPGKNAEGRASPLYASYKADSFSEGDDLSQGHLAEPCFLRAGGDLSLSPSRSADPLPGYATSDGDGDRLGVQLCGPGSSPEPEHGSRDSLEPSSMEASPEMHPPTRLSPQQAFPRTGGSGLSRKDSLTKAQLYGTLLN
| null | null |
evoked excitatory postsynaptic potential [GO:0098817]
|
cytosol [GO:0005829]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; postsynapse [GO:0098794]; presynapse [GO:0098793]; synapse [GO:0045202]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
| null | null | null | null | null |
FUNCTION: May sustain the structure of the postsynaptic density (PSD).
|
Rattus norvegicus (Rat)
|
O88884
|
AKAP1_RAT
|
MAIQFRSLFPLALPGMLALLGWWWFFSRKKDRLSSNGKQVGTLKVGPAIEDRLPTEEACPGVLSVTPSVTQPPGKEEQRSMDRPLSDPPALPRTRQVRRRSESSGNLPSIVDTRLQAGQCSDENSKVVLSLMGDEAKSIPLGRPLFPKDLSFPYEAVEGCKQESALGRTPGRGWLSQCAASGENARETGGAEGTGDAVLGESVLEEGLLPQECVSEVEKSEFPILAPGGGGGEKVRSGPPQVDELLKKEEYIVGKLPSSFVGPVHSELVKDEGALVPQVKGSQDRSLARELDKDKTLPEKDQIEQTAFQIISQVILEATEEIRATTVGKTVAQVHPTPGTQPQGQEESCVPASQETSLGQEIPDPASTRTGATASPSAGAPPPKTYVSCLSSPLSGPTKDQKPKNSAHHISLAPCPPPVTPQRQSLDGASNPRGDDTFVTCTSNNSQSVLSVTSLGLCSDPVSTSRLEDSCTETISSSGDKAVTPPLPDSTEPFSNGVLKEELSDLGTEDGWTMDTEADHSGGSDGNSMDSVDSCCGLTKPDSPQTVQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQNIQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVVPLSDDDHFSPEADAAMSEMTGNTALLAQVTSYSATGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSCYASL
| null | null |
antiviral innate immune response [GO:0140374]; apoptotic process [GO:0006915]; cellular response to cAMP [GO:0071320]; cellular response to peptide hormone stimulus [GO:0071375]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of protein dephosphorylation [GO:0035308]; negative regulation of protein import into nucleus [GO:0042308]; regulation of protein kinase A signaling [GO:0010738]
|
lipid droplet [GO:0005811]; membrane [GO:0016020]; mitochondrial crista [GO:0030061]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; postsynaptic membrane [GO:0045211]; postsynaptic specialization, intracellular component [GO:0099091]
|
beta-tubulin binding [GO:0048487]; microtubule binding [GO:0008017]; molecular adaptor activity [GO:0060090]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein phosphatase 2B binding [GO:0030346]; protein phosphatase binding [GO:0019903]; RNA binding [GO:0003723]
|
PF00013;PF10522;PF00567;
|
2.30.30.140;2.40.50.90;3.30.1370.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O08715}. Mitochondrion {ECO:0000250|UniProtKB:O08715}.
| null | null | null | null | null |
FUNCTION: Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity (By similarity). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (By similarity). {ECO:0000250|UniProtKB:O08715, ECO:0000250|UniProtKB:Q92667}.
|
Rattus norvegicus (Rat)
|
O88890
|
SH21A_MOUSE
|
MDAVTVYHGKISRETGEKLLLATGLDGSYLLRDSESVPGVYCLCVLYQGYIYTYRVSQTETGSWSAETAPGVHKRFFRKVKNLISAFQKPDQGIVTPLQYPVEKSSGRGPQAPTGRRDSDICLNAP
| null | null |
adaptive immune response [GO:0002250]; cell-cell signaling [GO:0007267]; cellular defense response [GO:0006968]; humoral immune response [GO:0006959]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]
|
cytoplasm [GO:0005737]
| null |
PF00017;
|
3.30.505.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with SH2D1B/EAT-2. Initially it has been proposed that association with SLAMF1 prevents SLAMF1 binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2. However, by simultaneous interactions, recruits FYN which subsequently phosphorylates and activates SLAMF1 (By similarity). Positively regulates CD244/2B4- and CD84-mediated natural killer (NK) cell functions (PubMed:22683124). Can also promote CD48-, SLAMF6 -, LY9-, and SLAMF7-mediated NK cell activation (PubMed:19648922). In the context of NK cell-mediated cytotoxicity enhances conjugate formation with target cells (PubMed:22683124). May also regulate the activity of the neurotrophin receptors NTRK1, NTRK2 and NTRK3. {ECO:0000250|UniProtKB:B2RZ59, ECO:0000250|UniProtKB:O60880, ECO:0000269|PubMed:16223723, ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:22683124, ECO:0000305|PubMed:21219180}.
|
Mus musculus (Mouse)
|
O88895
|
HDAC3_MOUSE
|
MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVISQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI
|
3.5.1.-; 3.5.1.98
| null |
cellular response to fluid shear stress [GO:0071498]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; cornified envelope assembly [GO:1903575]; DNA repair-dependent chromatin remodeling [GO:0140861]; epidermis development [GO:0008544]; establishment of mitotic spindle orientation [GO:0000132]; establishment of skin barrier [GO:0061436]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of interleukin-1 production [GO:0032692]; negative regulation of JNK cascade [GO:0046329]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of TOR signaling [GO:0032008]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type B pancreatic cell apoptotic process [GO:2000676]; protein modification process [GO:0036211]; regulation of circadian rhythm [GO:0042752]; regulation of mitotic cell cycle [GO:0007346]; regulation of multicellular organism growth [GO:0040014]; regulation of protein stability [GO:0031647]; spindle assembly [GO:0051225]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; histone deacetylase complex [GO:0000118]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Rpd3L-Expanded complex [GO:0070210]; transcription repressor complex [GO:0017053]
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chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cyclin binding [GO:0030332]; deacetylase activity [GO:0019213]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; GTPase binding [GO:0051020]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; histone decrotonylase activity [GO:0160009]; NF-kappaB binding [GO:0051059]; protein de-2-hydroxyisobutyrylase activity [GO:0160010]; protein lysine deacetylase activity [GO:0033558]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222]; ubiquitin-specific protease binding [GO:1990381]
|
PF00850;
|
3.40.800.20;
|
Histone deacetylase family, HD type 1 subfamily
|
PTM: Sumoylated in vitro. {ECO:0000269|PubMed:19204783}.; PTM: Deubiquitinated on 'Lys-63'-linked ubiquitin chains by USP38; leading to a decreased level of histone acetylation. {ECO:0000250|UniProtKB:O15379}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26776516}. Cytoplasm {ECO:0000269|PubMed:26776516}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15379}. Note=Colocalizes with XBP1 and AKT1 in the cytoplasm. Predominantly expressed in the nucleus in the presence of CCAR2 (By similarity). {ECO:0000250|UniProtKB:O15379}.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000305|PubMed:23911289, ECO:0000305|PubMed:30279482}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; Evidence={ECO:0000305|PubMed:23911289, ECO:0000305|PubMed:30279482}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-[protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:O15379}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109; Evidence={ECO:0000250|UniProtKB:O15379}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; Evidence={ECO:0000269|PubMed:30279482}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173; Evidence={ECO:0000269|PubMed:30279482}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] = 2-hydroxy-2-methylpropanoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69176, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15377, ChEBI:CHEBI:19641, ChEBI:CHEBI:29969, ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:O15379}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69177; Evidence={ECO:0000250|UniProtKB:O15379};
| null | null | null | null |
FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates (PubMed:23911289, PubMed:30279482). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:23911289). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:23911289). Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression (PubMed:23911289). Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (PubMed:19204783). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (By similarity). Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner (PubMed:26776516). During the activation phase, promotes the accumulation of ubiquitinated BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and BMAL1 (PubMed:26776516). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene BMAL1 and the genes involved in lipid metabolism in the liver (PubMed:19037247). Also functions as deacetylase for non-histone targets, such as KAT5, MEF2D, MAPK14, RARA and STAT3 (By similarity). Serves as a corepressor of RARA, mediating its deacetylation and repression, leading to inhibition of RARE DNA element binding (By similarity). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (By similarity). In addition to protein deacetylase activity, also acts as protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation and de-2-hydroxyisobutyrylation, respectively (PubMed:30279482). Catalyzes decrotonylation of MAPRE1/EB1 (By similarity). {ECO:0000250|UniProtKB:O15379, ECO:0000269|PubMed:19037247, ECO:0000269|PubMed:19204783, ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:26776516, ECO:0000269|PubMed:30279482}.
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Mus musculus (Mouse)
|
O88898
|
P63_MOUSE
|
MNFETSRCATLQYCPDPYIQRFIETPAHFSWKESYYRSAMSQSTQTSEFLSPEVFQHIWDFLEQPICSVQPIELNFVDEPSENGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSAKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSMQSQSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTMPEGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHDFSSPPHLLRTPSGASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDSRRNKQQRIKEEGE
| null |
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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anatomical structure formation involved in morphogenesis [GO:0048646]; animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; cellular senescence [GO:0090398]; chromatin remodeling [GO:0006338]; cloacal septation [GO:0060197]; cranial skeletal system development [GO:1904888]; determination of adult lifespan [GO:0008340]; ectoderm and mesoderm interaction [GO:0007499]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic limb morphogenesis [GO:0030326]; epidermal cell differentiation [GO:0009913]; epidermal cell division [GO:0010481]; epidermis development [GO:0008544]; epithelial cell development [GO:0002064]; epithelial cell differentiation [GO:0030855]; establishment of planar polarity [GO:0001736]; establishment of skin barrier [GO:0061436]; female genitalia morphogenesis [GO:0048807]; hair follicle development [GO:0001942]; hair follicle morphogenesis [GO:0031069]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; keratinocyte differentiation [GO:0030216]; keratinocyte proliferation [GO:0043616]; morphogenesis of a polarized epithelium [GO:0001738]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of keratinocyte differentiation [GO:0045617]; negative regulation of mesoderm development [GO:2000381]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron apoptotic process [GO:0051402]; Notch signaling pathway [GO:0007219]; odontogenesis of dentin-containing tooth [GO:0042475]; pattern specification process [GO:0007389]; polarized epithelial cell differentiation [GO:0030859]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of keratinocyte proliferation [GO:0010838]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of somatic stem cell population maintenance [GO:1904674]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-anal tail morphogenesis [GO:0036342]; prostate gland development [GO:0030850]; prostatic bud formation [GO:0060513]; protein tetramerization [GO:0051262]; proximal/distal pattern formation [GO:0009954]; regulation of epidermal cell division [GO:0010482]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal system development [GO:0001501]; skin epidermis development [GO:0098773]; skin morphogenesis [GO:0043589]; spermatogenesis [GO:0007283]; squamous basal epithelial stem cell differentiation involved in prostate gland acinus development [GO:0060529]; stem cell differentiation [GO:0048863]; stem cell proliferation [GO:0072089]; sympathetic nervous system development [GO:0048485]; transcription by RNA polymerase II [GO:0006366]
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chromatin [GO:0000785]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
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chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; MDM2/MDM4 family protein binding [GO:0097371]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; promoter-specific chromatin binding [GO:1990841]; protein domain specific binding [GO:0019904]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; WW domain binding [GO:0050699]
|
PF00870;PF07710;PF07647;
|
2.60.40.720;4.10.170.10;1.10.150.50;
|
P53 family
|
PTM: May be sumoylated. {ECO:0000250}.; PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein. {ECO:0000269|PubMed:18806757}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14729569}.
| null | null | null | null | null |
FUNCTION: Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Activates transcription of the p21 promoter (By similarity). Activates RIPK4 transcription. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. {ECO:0000250, ECO:0000269|PubMed:10227293, ECO:0000269|PubMed:10227294, ECO:0000269|PubMed:11932750, ECO:0000269|PubMed:14729569, ECO:0000269|PubMed:22197488}.
|
Mus musculus (Mouse)
|
O88900
|
GRB14_RAT
|
MTTSLQDGQSAAGRAGAQDSPLAVQVCRVAQGKGDAQDPAQVPGLHALSPASDATRRGAMDRRKAKDLEVQETPSIPNPFPELCCSPLTSVLSAGLFPRSNSRKKQVIKVYSEDETSRALEVPSDVTARDVCQLLILKNHYVDDNSWTLFEHLSHTGVERTVEDHELLTEVLSHWVMEEDNKLYLRKNYAKYEFFKNPMYFFPEHMVSFATEMNGDRSLTQIPQVFLSSNTYPEIHGFLHAKEQGKKSWKKAYFFLRRSGLYFSTKGTSKEPRHLQFFSEFSTSNVYMSLAGKKKHGAPTPYGFCFKPTKAGGPRDLKMLCAEEDQSRMCWVTAIRLLKYGMQLYQNYMHPSQARSACSSQSVSPMRSVSENSLVAMDFSGQKTRVIDNPTEALSVAVEEGLAWRKKGCLRLGNHGSPTAPSQSSAVNMALHRSQPWFHHRISRDEAQQLITRQGPVDGVFLVRDSQSNPRTFVLSMSHGQKIKHFQIIPVEDDGEVFHTLDDGHTKFTDLIQLVEFYQLNKGVLPCKLKHYCARMAV
| null | null |
cellular response to insulin stimulus [GO:0032869]; insulin receptor signaling pathway [GO:0008286]; intracellular signal transduction [GO:0035556]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904145]
|
cytoplasm [GO:0005737]; endosome [GO:0005768]; endosome membrane [GO:0010008]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
|
molecular adaptor activity [GO:0060090]; phosphoprotein binding [GO:0051219]; protein-macromolecule adaptor activity [GO:0030674]; receptor tyrosine kinase binding [GO:0030971]
|
PF08947;PF00169;PF00788;PF00017;
|
2.30.29.30;3.30.505.10;
|
GRB7/10/14 family
|
PTM: Phosphorylated on serine residues. Phosphorylated on tyrosine residues by TEK/TIE2 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14449}. Endosome membrane {ECO:0000250|UniProtKB:Q14449}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14449}. Note=Upon insulin stimulation, translocates to the plasma membrane. {ECO:0000250|UniProtKB:Q14449}.
| null | null | null | null | null |
FUNCTION: Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88902
|
PTN23_RAT
|
LNVNLMLGQAQECLLEKSMLDNRKSFLVARISAQVVDYYKEACRALENPDTASLLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQSALDKLNEAIKLAKGQPDTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPTDPAVTGPDIFAKLVPMAAHEASSLYSEEKAKLLREMLAKIEDKNEVLDQFMDSMQLDPDTVDNLDAYNHIPPQLMEKCAALSVRPDTVKNLVQSMQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPGPSVTKAELGEVRREWAKYTEVHEKASFTNSELHRAMNLHVGNLRLLSGPLDQVRAALPTPALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSEMKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYADLESKVAALLERAQSLCRAQEAARQQLLDRELKKKAPPPRPTAPKPLLSRREEGEAAEAGDQPEELRSLPPDMMAGPRLPDPFLGTAAPLHFSPGPFPGSTGPATHYLSGPLPPGTYSGPTQLMQPRAAVPMAPGPVLYPAPVYTSELGLVPRSSPQHGIVSSPYAGVGPPQPIVGLPSAPPPQFSGPELAMDVRPATTTVDSVQAPISSHMALRPGPAPAPPQPCFPVPQPVPQSVPQPQPLPTPYTYSIGTKQHLTGPLPQHHFPPGIPTSFPAPRIGPQPPPQLQPQPQPQPQPQPPPQPQPQPQPQPQPQPQPQPQRPVFGPQPTQQPLPFQHPHLFPSQAPGILTPPPPYPFTPQPGVLGQPPPTRHTQLYPGPPPDTLPPHSGALPFPSPGPPHPHPTLAYGPAPSPRPLGPQATPVSIRGPPPANQPAPSPHLVPSPAPSPGPGPVPSRPPTAEPPPCLRRGAAAADLLSSSPESQHGGTQPPGGGQPLLQPTKVDAAERPTAQALRLIEQDPYEHPERLQKLQQELESFRGQLGDAGALDAVWRELQEAQEHDARGRSIAIARCYSLKNRHQDVMPYDSNRVVLRSGKDDYINASCVEGLSPYCPPLVATQRPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPIERGQPMVHGALSVALSSVRTTDTHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGSRIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALVRHVEQVLQRHGVPPPGKPVASMSVSQKSHLPQDSQDLVLGGDVPISSIQATIAKLSIRPLGGLDSPAASLPSLVEPPGLPPASLPEPTPAPPSSPPPPSSPLPEPPQPEEEPSVPEAPSLGPPSSSLELLASLTPEAFSLDSSLRGKQRMSKQNFLQAHNGQGLRAAQPTDDPLSLLDPLWTLNKT
|
3.1.3.48
| null |
cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; early endosome to late endosome transport [GO:0045022]; endocytic recycling [GO:0032456]; negative regulation of epithelial cell migration [GO:0010633]; positive regulation of adherens junction organization [GO:1903393]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of homophilic cell adhesion [GO:1903387]; positive regulation of Wnt protein secretion [GO:0061357]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]
|
ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome [GO:0005768]; nucleus [GO:0005634]
|
protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]
|
PF13949;PF03097;PF00102;
|
1.20.120.560;1.20.140.50;1.25.40.280;3.90.190.10;
|
Protein-tyrosine phosphatase family, Non-receptor class subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000269|PubMed:9694860}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044};
| null | null | null | null |
FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:9694860}.
|
Rattus norvegicus (Rat)
|
O88904
|
HIPK1_MOUSE
|
MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQASSSHQVANFNLPAYDQGLLLPAPAVEHIVVTAADSSGSAATATFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVESNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDPNLGYPLWRLKTPEEHELETGIKSKEARKYIFNCLDDMAQVNMSTDLEGTDMLAEKADRREYIDLLKKMLTIDADKRITPLKTLNHQFVTMSHLLDFPHSSHVKSCFQNMEICKRRVHMYDTVSQIKSPFTTHVAPNTSTNLTMSFSNQLNTVHNQASVLASSSTAAAATLSLANSDVSLLNYQSALYPSSAAPVPGVAQQGVSLQPGTTQICTQTDPFQQTFIVCPPAFQTGLQATTKHSGFPVRMDNAVPIVPQAPAAQPLQIQSGVLTQGSCTPLMVATLHPQVATITPQYAVPFTLSCAAGRPALVEQTAAVLQAWPGGTQQILLPSAWQQLPGVALHNSVQPAAVIPEAMGSSQQLADWRNAHSHGNQYSTIMQQPSLLTNHVTLATAQPLNVGVAHVVRQQQSSSLPSKKNKQSAPVSSKSSLEVLPSQVYSLVGSSPLRTTSSYNSLVPVQDQHQPIIIPDTPSPPVSVITIRSDTDEEEDNKYKPNSSSLKARSNVISYVTVNDSPDSDSSLSSPHPTDTLSALRGNSGTLLEGPGRPAADGIGTRTIIVPPLKTQLGDCTVATQASGLLSSKTKPVASVSGQSSGCCITPTGYRAQRGGASAVQPLNLSQNQQSSSASTSQERSSNPAPRRQQAFVAPLSQAPYAFQHGSPLHSTGHPHLAPAPAHLPSQPHLYTYAAPTSAAALGSTSSIAHLFSPQGSSRHAAAYTTHPSTLVHQVPVSVGPSLLTSASVAPAQYQHQFATQSYIGSSRGSTIYTGYPLSPTKISQYSYL
|
2.7.11.1
| null |
adherens junction assembly [GO:0034333]; anterior/posterior pattern specification [GO:0009952]; cell population proliferation [GO:0008283]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; endothelial cell apoptotic process [GO:0072577]; extrinsic apoptotic signaling pathway [GO:0097191]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; iris morphogenesis [GO:0061072]; lens induction in camera-type eye [GO:0060235]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA binding [GO:0043388]; protein phosphorylation [GO:0006468]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; retina layer formation [GO:0010842]; smoothened signaling pathway [GO:0007224]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; PML body [GO:0016605]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; transcription corepressor activity [GO:0003714]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, HIPK subfamily
|
PTM: Phosphorylated and activated by JNK1 (By similarity). Autophosphorylated. {ECO:0000250}.; PTM: Sumoylated. When conjugated it is directed to nuclear speckles. SENP1-mediated desumoylation is mediated by TNF in response to stress stimuli, triggering transient translocation from nucleus to cytoplasm. {ECO:0000269|PubMed:18219322}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:18219322, ECO:0000269|PubMed:20579985}. Cytoplasm {ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:18219322, ECO:0000269|PubMed:20579985}. Nucleus speckle {ECO:0000269|PubMed:12529400}. Note=Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation. {ECO:0000269|PubMed:18219322}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation. Phosphorylates PAGE4 at 'Thr-51' which is critical for the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (By similarity). {ECO:0000250|UniProtKB:Q86Z02, ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:20231426, ECO:0000269|PubMed:20579985}.
|
Mus musculus (Mouse)
|
O88907
|
PIAS1_MOUSE
|
MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPPTLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRTYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGSWAPMRSKKEVQEVTASYNGVDGCLSSTLEHQVASHNQSSNKNKKVEVIDLTIDSSSDEEEEEPPAKRTCPSLSPTSPLSNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPATNGSSSGSNSSLVSSNSLRESHGHGVASRSSADTASIFGIIPDIISLD
|
2.3.2.27
| null |
fat cell differentiation [GO:0045444]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of apoptotic process [GO:0043066]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein localization to cell periphery [GO:1904377]; positive regulation of protein sumoylation [GO:0033235]; positive regulation of smooth muscle cell differentiation [GO:0051152]; protein sumoylation [GO:0016925]; protein-DNA complex assembly [GO:0065004]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]; visual learning [GO:0008542]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nuclear periphery [GO:0034399]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
DNA-binding transcription factor binding [GO:0140297]; protein domain specific binding [GO:0019904]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF14324;PF02891;
|
2.60.120.780;1.10.720.30;3.30.40.10;
|
PIAS family
|
PTM: Sumoylated. {ECO:0000250|UniProtKB:O75925}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16600910}. Nucleus speckle {ECO:0000250|UniProtKB:O75925}. Nucleus, PML body {ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:22406621}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O75925}. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton (By similarity). Interaction with MSX1 is required for localization to the nuclear periphery (PubMed:16600910). {ECO:0000250|UniProtKB:O75925, ECO:0000269|PubMed:16600910}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null |
PATHWAY: Protein modification; protein sumoylation.
| null | null |
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor (PubMed:24061474). Catalyzes sumoylation of various proteins, such as CEBPB, MRE11, MTA1, PTK2 and PML (PubMed:24061474). Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway (By similarity). In vitro, binds A/T-rich DNA (By similarity). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context (By similarity). Mediates sumoylation of MRE11, stabilizing MRE11 on chromatin during end resection (By similarity). Sumoylates PML (at 'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation (PubMed:22406621). PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (PubMed:22406621). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (By similarity). Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (PubMed:24061474). Mediates the nuclear mobility and localization of MSX1 to the nuclear periphery, whereby MSX1 is brought into the proximity of target myoblast differentiation factor genes (PubMed:16600910). Also required for the binding of MSX1 to the core enhancer region in target gene promoter regions, independent of its sumoylation activity (PubMed:16600910). Capable of binding to the core enhancer region TAAT box in the MYOD1 gene promoter (PubMed:16600910). {ECO:0000250|UniProtKB:O75925, ECO:0000269|PubMed:16600910, ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:24061474}.
|
Mus musculus (Mouse)
|
O88908
|
SOAT2_MOUSE
|
MQPKVPQLRRREGLGEEQEKGARGGEGNARTHGTPDLVQWTRHMEAVKTQFLEQAQRELAELLDRALWEAMQAYPKQDRPLPSAAPDSTSKTQELHPGKRKVFITRKSLIDELMEVQHFRTIYHMFIAGLCVLIISTLAIDFIDEGRLMLEFDLLLFSFGQLPLALMTWVPMFLSTLLVPYQTLWLWARPRAGGAWMLGASLGCVLLAAHAVVLCVLPVHVSVRHELPPASRCVLVFEQVRLLMKSYSFLRETVPGIFCVRGGKGISPPSFSSYLYFLFCPTLIYRETYPRTPSIRWNYVAKNFAQVLGCLLYACFILGRLCVPVFANMSREPFSTRALLLSILHATGPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLWLLGRRARGVAMLGVFLVSAVVHEYIFCFVLGFFYPVMLMLFLVFGGLLNFTMNDRHTGPAWNILMWTFLFMGQGIQVSLYCQEWYARRHCPLPQTTFWGMVTPRSWSCHP
|
2.3.1.26
| null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; very-low-density lipoprotein particle assembly [GO:0034379]
|
brush border [GO:0005903]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]
|
PF03062;
| null |
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
|
PTM: Polyubiquitinated by AMFR/gp78 at Cys-280, leading to its degradation when the lipid levels are low. Association with AMFR/gp78 is mediated via interaction with INSIG1. High concentration of cholesterol and fatty acid results in Cys-280 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization. {ECO:0000250|UniProtKB:O75908}.; PTM: Oxidized at Cys-280: high concentration of cholesterol and fatty acid induce reactive oxygen species, which oxidizes Cys-280, preventing ubiquitination at the same site, and resulting in protein stabilization. {ECO:0000250|UniProtKB:O75908}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11071899}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA; Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + cholesterol = (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-cholesterol + CoA; Xref=Rhea:RHEA:46612, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:73862, ChEBI:CHEBI:84969; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46613; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-cholesterol + CoA; Xref=Rhea:RHEA:46620, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:84341; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46621; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA; Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:82751; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817; Evidence={ECO:0000250|UniProtKB:O75908};
| null | null | null | null |
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa. {ECO:0000250|UniProtKB:O75908}.
|
Mus musculus (Mouse)
|
O88909
|
S22A8_MOUSE
|
MTFSEILDRVGSMGPFQYLHVTLLALPILGIANHNLLQIFTATTPDHHCRPPPNASLEPWVLPLGPNGKPEKCLRFVHLPNASLPNDTQGATEPCLDGWIYNSTRDTIVTEWDLVCGSNKLKEMAQSVFMAGILVGGPVFGELSDRFGRKPILTWSYLLLAASGSSAAFSPSLTVYMIFRFLCGCSISGISLSTIILNVEWVPTSTRAISSTTIGYCYTIGQFILPGLAYAVPQWRWLQLSVSAAFFIFSLLSWWVPESIRWLVLSGKFSKALKTLQRVATFNGKKEEGEKLTVEELKFNLQKDITSAKVKYGLSDLFRVSILRRVTFCLSLAWFATGFAYYSLAMGVEEFGVNIYILQIIFGGVDIPAKFITILSISYLGRRITQGFLLILAGVAILALIFVSSEMQLLRTALAVFGKGCLSGSFSCLFLYTSELYPTVLRQTGMGISNIWARVGSMIAPLVKITGELQPFIPNVIFGTMTLLGGSAAFFLLETLNRPLPETIEDIQDWYQQTKKTKQEPEAEKASQTIPLKTGGP
| null | null |
glutathione transport [GO:0034635]; monoatomic ion transport [GO:0006811]; prostaglandin transport [GO:0015732]; quaternary ammonium group transport [GO:0015697]; response to toxic substance [GO:0009636]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]
|
antiporter activity [GO:0015297]; organic anion transmembrane transporter activity [GO:0008514]; prostaglandin transmembrane transporter activity [GO:0015132]; protein kinase C binding [GO:0005080]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; solute:inorganic anion antiporter activity [GO:0005452]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
| null |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:15944205, ECO:0000269|PubMed:17220594, ECO:0000269|PubMed:23389457}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the basolateral side of all renal epithelia except the glomerulus (PubMed:15944205). Localizes on the brush border membrane of the choroid epithelial cells. Localizes to the basolateral membrane of the proximal tubular cells. Localizes on the abluminal and possibly, luminal membrane of the brain capillary endothelial cells (BCEC) (By similarity). {ECO:0000250, ECO:0000269|PubMed:15944205}.
|
CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) + glutarate(in) = estrone 3-sulfate(in) + glutarate(out); Xref=Rhea:RHEA:72151, ChEBI:CHEBI:30921, ChEBI:CHEBI:60050; Evidence={ECO:0000269|PubMed:17220594, ECO:0000305|PubMed:12011098, ECO:0000305|PubMed:15075193, ECO:0000305|PubMed:21325432}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(out) + estrone 3-sulfate(in) = 2-oxoglutarate(in) + estrone 3-sulfate(out); Xref=Rhea:RHEA:72399, ChEBI:CHEBI:16810, ChEBI:CHEBI:60050; Evidence={ECO:0000305|PubMed:17220594}; CATALYTIC ACTIVITY: Reaction=glutarate(in) + taurocholate(out) = glutarate(out) + taurocholate(in); Xref=Rhea:RHEA:72159, ChEBI:CHEBI:30921, ChEBI:CHEBI:36257; Evidence={ECO:0000305|PubMed:12011098}; CATALYTIC ACTIVITY: Reaction=dehydroepiandrosterone 3-sulfate(out) + glutarate(in) = dehydroepiandrosterone 3-sulfate(in) + glutarate(out); Xref=Rhea:RHEA:72355, ChEBI:CHEBI:30921, ChEBI:CHEBI:57905; Evidence={ECO:0000305|PubMed:21325432}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(out) + glutarate(in) = 2-oxoglutarate(in) + glutarate(out); Xref=Rhea:RHEA:71751, ChEBI:CHEBI:16810, ChEBI:CHEBI:30921; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(out) + urate(in) = 2-oxoglutarate(in) + urate(out); Xref=Rhea:RHEA:72403, ChEBI:CHEBI:16810, ChEBI:CHEBI:17775; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=glutarate(in) + prostaglandin F2alpha(out) = glutarate(out) + prostaglandin F2alpha(in); Xref=Rhea:RHEA:72503, ChEBI:CHEBI:30921, ChEBI:CHEBI:57404; Evidence={ECO:0000305|PubMed:15100168}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(in) + prostaglandin F2alpha(out) = 2-oxoglutarate(out) + prostaglandin F2alpha(in); Xref=Rhea:RHEA:72507, ChEBI:CHEBI:16810, ChEBI:CHEBI:57404; Evidence={ECO:0000305|PubMed:15100168}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + 2-oxoglutarate(in) = (R)-carnitine(in) + 2-oxoglutarate(out); Xref=Rhea:RHEA:72511, ChEBI:CHEBI:16347, ChEBI:CHEBI:16810; Evidence={ECO:0000305|PubMed:15100168}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + glutarate(in) = (R)-carnitine(in) + glutarate(out); Xref=Rhea:RHEA:72515, ChEBI:CHEBI:16347, ChEBI:CHEBI:30921; Evidence={ECO:0000305|PubMed:15100168}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(in) + prostaglandin E2(out) = 2-oxoglutarate(out) + prostaglandin E2(in); Xref=Rhea:RHEA:72499, ChEBI:CHEBI:16810, ChEBI:CHEBI:606564; Evidence={ECO:0000305|PubMed:15100168}; CATALYTIC ACTIVITY: Reaction=glutarate(in) + prostaglandin E2(out) = glutarate(out) + prostaglandin E2(in); Xref=Rhea:RHEA:72495, ChEBI:CHEBI:30921, ChEBI:CHEBI:606564; Evidence={ECO:0000305|PubMed:15100168}; CATALYTIC ACTIVITY: Reaction=glutarate(out) + urate(in) = glutarate(in) + urate(out); Xref=Rhea:RHEA:72551, ChEBI:CHEBI:17775, ChEBI:CHEBI:30921; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(in) + taurocholate(out) = 2-oxoglutarate(out) + taurocholate(in); Xref=Rhea:RHEA:72547, ChEBI:CHEBI:16810, ChEBI:CHEBI:36257; Evidence={ECO:0000305|PubMed:12011098}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(in) + dehydroepiandrosterone 3-sulfate(out) = 2-oxoglutarate(out) + dehydroepiandrosterone 3-sulfate(in); Xref=Rhea:RHEA:72543, ChEBI:CHEBI:16810, ChEBI:CHEBI:57905; Evidence={ECO:0000305|PubMed:21325432}; CATALYTIC ACTIVITY: Reaction=a dicarboxylate(in) + kynurenate(out) = a dicarboxylate(out) + kynurenate(in); Xref=Rhea:RHEA:76087, ChEBI:CHEBI:28965, ChEBI:CHEBI:58454; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=(indol-3-yl)acetate(out) + a dicarboxylate(in) = (indol-3-yl)acetate(in) + a dicarboxylate(out); Xref=Rhea:RHEA:75983, ChEBI:CHEBI:28965, ChEBI:CHEBI:30854; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=a dicarboxylate(in) + indoxyl sulfate(out) = a dicarboxylate(out) + indoxyl sulfate(in); Xref=Rhea:RHEA:75987, ChEBI:CHEBI:28965, ChEBI:CHEBI:144643; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=a dicarboxylate(in) + N-benzoylglycine(out) = a dicarboxylate(out) + N-benzoylglycine(in); Xref=Rhea:RHEA:75991, ChEBI:CHEBI:28965, ChEBI:CHEBI:606565; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=3-carboxy-4-methyl-5-propyl-2-furanpropanoate(out) + a dicarboxylate(in) = 3-carboxy-4-methyl-5-propyl-2-furanpropanoate(in) + a dicarboxylate(out); Xref=Rhea:RHEA:75995, ChEBI:CHEBI:28965, ChEBI:CHEBI:194524; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(out) + a dicarboxylate(in) = (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(in) + a dicarboxylate(out); Xref=Rhea:RHEA:76071, ChEBI:CHEBI:28965, ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=a dicarboxylate(in) + L-erythro-7,8-dihydrobiopterin(out) = a dicarboxylate(out) + L-erythro-7,8-dihydrobiopterin(in); Xref=Rhea:RHEA:76075, ChEBI:CHEBI:28965, ChEBI:CHEBI:43029; Evidence={ECO:0000250|UniProtKB:Q8TCC7}; CATALYTIC ACTIVITY: Reaction=a dicarboxylate(in) + L-sepiapterin(out) = a dicarboxylate(out) + L-sepiapterin(in); Xref=Rhea:RHEA:76079, ChEBI:CHEBI:28965, ChEBI:CHEBI:194527; Evidence={ECO:0000250|UniProtKB:Q8TCC7};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=61.9 nM for L-carnitine {ECO:0000269|PubMed:15100168}; KM=4.01 uM for 6-mercaptopurine {ECO:0000269|PubMed:15100168}; KM=53.9 nM for 5-fluorouracil {ECO:0000269|PubMed:15100168}; KM=1.48 uM for prostaglandin E(2) {ECO:0000269|PubMed:17220594};
| null | null | null |
FUNCTION: Functions as an organic anion/dicarboxylate exchanger that couples organic anion uptake indirectly to the sodium gradient (By similarity). Transports organic anions such as estrone 3-sulfate (E1S) and urate in exchange for dicarboxylates such as glutarate or ketoglutarate (2-oxoglutarate) (PubMed:17220594). Plays an important role in the excretion of endogenous and exogenous organic anions, especially from the kidney and the brain (PubMed:12011098, PubMed:15075193, PubMed:17220594, PubMed:21325432). E1S transport is pH- and chloride-dependent and may also involve E1S/cGMP exchange. Responsible for the transport of prostaglandin E2 (PGE2) and prostaglandin F2(alpha) (PGF2(alpha)) in the basolateral side of the renal tubule. Involved in the transport of neuroactive tryptophan metabolites kynurenate and xanthurenate. Functions as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins (By similarity). May be involved in the basolateral transport of steviol, a metabolite of the popular sugar substitute stevioside (By similarity). May participate in the detoxification/ renal excretion of drugs and xenobiotics, such as the histamine H(2)-receptor antagonists fexofenadine and cimetidine, the antibiotic benzylpenicillin (PCG), the anionic herbicide 2,4-dichloro-phenoxyacetate (2,4-D), the diagnostic agent p-aminohippurate (PAH), the antiviral acyclovir (ACV), and the mycotoxin ochratoxin (OTA), by transporting these exogenous organic anions across the cell membrane in exchange for dicarboxylates such as 2-oxoglutarate (By similarity). May contribute to the release of cortisol in the adrenals (By similarity). Involved in one of the detoxification systems on the choroid plexus (CP), removes substrates such as E1S or taurocholate (TC), PCG, 2,4-D and PAH, from the cerebrospinal fluid (CSF) to the blood for eventual excretion in urine and bile (PubMed:12011098). Also contributes to the uptake of several other organic compounds such as the prostanoids prostaglandin E(2) and prostaglandin F(2-alpha), L-carnitine, and the therapeutic drugs allopurinol, 6-mercaptopurine (6-MP) and 5-fluorouracil (5-FU) (PubMed:15100168, PubMed:17220594). Mediates the transport of PAH, PCG, and the statins pravastatin and pitavastatin, from the cerebrum into the blood circulation across the blood-brain barrier (BBB) (By similarity). Contributes to the renal uptake of potent uremic toxins (indoxyl sulfate (IS), indole acetate (IA), hippurate/N-benzoylglycine (HA) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF)), pravastatin, PCG, E1S and dehydroepiandrosterone sulfate (DHEAS), and is partly involved in the renal uptake of temocaprilat (an angiotensin-converting enzyme (ACE) inhibitor) (By similarity). In summary, plays a role in the efflux of drugs and xenobiotics, helping reduce their undesired toxicological effects on the body (By similarity). {ECO:0000250|UniProtKB:Q8TCC7, ECO:0000250|UniProtKB:Q9R1U7, ECO:0000269|PubMed:12011098, ECO:0000269|PubMed:15075193, ECO:0000269|PubMed:15100168, ECO:0000269|PubMed:17220594, ECO:0000269|PubMed:21325432}.
|
Mus musculus (Mouse)
|
O88910
|
MPP3_MOUSE
|
MPVLSEDSGLHETLALLTSQLRPDSNHREEMGFLRDVFSEKSLSYLMKIHEKLRYYERQSPTPVLHSAMALAEDVMEELQAASVHSDERELLQLLSTPHLRAVLMVHDTVAQKNFDPVLPPLPDNIDEDFEEESVKIVRLVKNKEPLGATIRRDEHSGAVVVARIMRGGAADRSGLVHVGDELREVNGIAVLHKRPDEISQILAQSQGSITLKIIPATQEEDRFKDSKVFMRALFHYDPREDRAIPCQEAGLPFQRRQVLEVVSQDDPTWWQAKRVGDTNLRAGLIPSKQFQERRLSYRRTTGTLPSPQNFKKPPYDQPCDKETCDCDGYFKGHYVAGLRRSFRLGCRERLGGSQEAKVPTGAESQVLLTYEEVARYQHQPGERPRLVVLIGSLGAHLHELKQRVVAEDPQQFAVAVPHTTRPRKSHERDGVEYHFVSKQAFEADVHHNKFLEHGEYKENLYGTSLEAIQAVMAKNKVCLVDVEPEALRHLRTPEFKPYVIFVKPAIQERRKTPPVSPDSEDIASSLDEQQQEMAASAAFIDQHYGHLIDTVLVRQDLQEPAASSELS
| null | null | null |
adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cell-cell junction [GO:0005911]; plasma membrane [GO:0005886]
|
PDZ domain binding [GO:0030165]
|
PF00625;PF02828;PF00595;PF07653;
|
2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40;
|
MAGUK family
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:23658188, ECO:0000269|PubMed:23893895}. Cell membrane {ECO:0000250|UniProtKB:Q13368}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q13368}. Note=Localized in apical villi of Mueller glia cells (PubMed:23893895). Localized at the apical membrane in the developing cortex and colocalized with apical proteins and adherens junction proteins (PubMed:23658188). Localized at the outer limiting membrane (OLM), and outer plexiform (OPL) of retina (By similarity). {ECO:0000250|UniProtKB:Q13368, ECO:0000269|PubMed:23658188, ECO:0000269|PubMed:23893895}.
| null | null | null | null | null |
FUNCTION: Participates in cell spreading through the phosphoinositide-3-kinase (PI3K) pathway by connecting CADM1 to DLG1 and the regulatory subunit of phosphoinositide-3-kinase (PI3K) (By similarity). Stabilizes HTR2C at the plasma membrane and prevents its desensitization (PubMed:16914526). May participates in the maintenance of adherens junctions (PubMed:23658188, PubMed:23893895). {ECO:0000250|UniProtKB:Q13368, ECO:0000269|PubMed:16914526, ECO:0000269|PubMed:23658188, ECO:0000269|PubMed:23893895}.
|
Mus musculus (Mouse)
|
O88917
|
AGRL1_RAT
|
MARLAAALWSLCVTTVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLAFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKQNVVLEVTVLSTEGQVQELVFPQEYASESSIQLSANTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGTGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEAKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEVACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGAHGSLKTSAMRSNTRYYTGTQVPGQGRHIHQVSLGPRGRSALPESQKDPGGQSGPGDPLTFGLCPSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGASGGAKGPPPEPPVPPVPGVSEDEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPNEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPSLEGPGPDGDGQMQLVTSL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell surface receptor signaling pathway [GO:0007166]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synapse maturation [GO:0090129]
|
axon [GO:0030424]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synapse [GO:0045202]
|
carbohydrate binding [GO:0030246]; cell adhesion molecule binding [GO:0050839]; G protein-coupled receptor activity [GO:0004930]; latrotoxin receptor activity [GO:0016524]; toxic substance binding [GO:0015643]
|
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
|
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. {ECO:0000269|PubMed:9208860}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:22333914}; Multi-pass membrane protein {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:22333914}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane. Cell projection, axon. Cell projection, growth cone. Synapse. Presynaptic cell membrane. Synapse, synaptosome. Note=Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts.
| null | null | null | null | null |
FUNCTION: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000269|PubMed:9208860, ECO:0000269|PubMed:9830014}.; FUNCTION: [Isoform 2]: Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization.
|
Rattus norvegicus (Rat)
|
O88923
|
AGRL2_RAT
|
MVSSGCRMRSLWFIMIISFSPNTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCVVVTGSDVFPDPCPGTYKYLEVQYECVPYMEQKVFVCPGTLKAIVDSPSIYEAEQKAGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETTYDKRAASNAFMICGVLYVVRSVYQDNESEAGKNVIDYIYNTRLSRGEHVDVPFPNQYQYIAAVDYNPRDNQLYVWNNNFILRYSLEFGPPDPAQVPTTAVTITSSAELFKTTVSTTSSTSQRGPVSSTVAGPQEGSRGTKPPPAVSTTKIPPVTNIFPLPERFCEALEMKGIKWPQTQRGMMVERPCPKGTRGTASYLCMASTGTWNPKGPDLSNCTSHWVNQLAQKIRSGENAASLANELAKHTKGTVFAGDVSSSVRLMEQLVDILDAQLQELKPSEKDSAGRSYNKLQKREKTCRAYLKAIVDTVDNLLRAETLDCWKHMNSSEQAHTATMLLDTLEEGAFVLADNLLEPTRVSMPTDNIVLEVAVLSTEGQVQDFTFHLGFKGAFSSIQLSANTVKQNSRNGLAKVVFIIYRSLGPFLSTENATVKLGADLLGRNSTIAVNSHVLSVSINKESSRVYLTDPVLFSMPHIDSDNYFNANCSFWNYSERTMMGYWSTQGCKLVDTNKTRTTCACSHLTNFAILMAHREIVYKDGVHKLLLTVITWVGIVVSLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTQYTIACPVFAGLLHFFFLAAFSWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDSKSYGTLEACWLHVDNYFIWSFIGPVTFIILLNIIFLVITLCKMVKHSNTLKPDSSRLENINNYRVCDGYYNTDLPGYEDNKPFIKSWVLGAFALLCLLGLTWSFGLLFVNEETVVMAYLFTAFNAFQGLFIFIFHCALQKKVRKEYAKCFRHWYCCGGLPTESPHSSVKASTSRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLRPHGTNNPYNTLLAETVVCNAPSAPVFNSPGHSLNNTRDTSAMDTLPLNGNFNNSYSLRKADYHDGVQVVDCGLSLNDTAFEKMIISELVHNNLRGSNKTHNLELKLPVKPVIGGSSSEDDAIVADASSLMHGDNPGLEFRHKELEAPLIPQRTHSLLYQPQKKVKPEATDSYVSQLTAEADEHLQSPNRDSLYTSMPNLRDSPYPESSPDMAEDLSPSRRSENEDIYYKSMPNLGAGRQLQMCYQISRGNSDGYIIPINKEGCIPEGDVREGQMQLVTSL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; positive regulation of synapse assembly [GO:0051965]; response to bacterium [GO:0009617]; synapse organization [GO:0050808]
|
glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]
|
carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930]; PDZ domain binding [GO:0030165]
|
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
|
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:O88917}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000269|PubMed:10026162}.
|
Rattus norvegicus (Rat)
|
O88935
|
SYN1_MOUSE
|
MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPSAASPGATPGSATASAERASTAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMTQALPRQPQRDASPGRGSHSQSSSPGALTLGRQTSQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPPPQGQQHLSGLGPPAGSPLPQRLPSPTAAPQQSASQATPVTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGAPQATRQASISGPAPTKASGAPPGGQQRQGPPQKPPGPAGPTRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPAKPQLAQKPSQDVPPPITAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD
| null | null |
neuron development [GO:0048666]; neurotransmitter secretion [GO:0007269]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; regulation of synaptic vesicle cycle [GO:0098693]; regulation of synaptic vesicle exocytosis [GO:2000300]; synapse organization [GO:0050808]; synaptic vesicle clustering [GO:0097091]; synaptic vesicle cycle [GO:0099504]
|
axon [GO:0030424]; cell body [GO:0044297]; clathrin-sculpted glutamate transport vesicle membrane [GO:0060203]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; extrinsic component of synaptic vesicle membrane [GO:0098850]; Golgi apparatus [GO:0005794]; myelin sheath [GO:0043209]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; synaptonemal complex [GO:0000795]
|
actin binding [GO:0003779]; ATP binding [GO:0005524]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]
|
PF02078;PF02750;PF10581;
|
3.40.50.20;3.30.1490.20;3.30.470.20;
|
Synapsin family
|
PTM: Substrate of different protein kinases. Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover. {ECO:0000250|UniProtKB:P09951}.
|
SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:11571277}. Golgi apparatus {ECO:0000269|PubMed:11571277}. Presynapse {ECO:0000250|UniProtKB:P09951}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P09951}. Note=Dissociates from synaptic vesicles and redistributes into the axon during action potential firing, in a step that precedes fusion of vesicles with the plasma membrane. Reclusters to presynapses after the cessation of synaptic activity. {ECO:0000250|UniProtKB:P09951}.
| null | null | null | null | null |
FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (By similarity). Also involved in the regulation of axon outgrowth and synaptogenesis (PubMed:7568107). The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxide functions at a presynaptic level (By similarity). {ECO:0000250|UniProtKB:P09951, ECO:0000269|PubMed:7568107}.
|
Mus musculus (Mouse)
|
O88939
|
ZBT7A_MOUSE
|
MAGGVDGPIGIPFPDHSSDILSGLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEIDFVSAEALTALMDFAYTATLTVSTANVGDILSAARLLEIPAVSHVCADLLERQILAADDVGDASQPDGAGPTDQRNLLRAKEYLEFFRSNPMNSLPPTAFPWSGFGAPDDDLDATKEAVAAAVAAVAAGDCNGLDFYGPGPPADRPPAGDGDEGDSTPGLWPERDEDAPPGGLFPPPTAPPATTQNGHYGRAGAGTGEEEAAALSEAAPEPGDSPGFLSGAAEGEDGDAADVDGLAASTLLQQMMSSVGRAGDSDEESRTDDKGVMDYYLKYFSGAHEGDVYPAWSQKGEKKIRAKAFQKCPICEKVIQGAGKLPRHIRTHTGEKPYECNICKVRFTRQDKLKVHMRKHTGEKPYLCQQCGAAFAHNYDLKNHMRVHTGLRPYQCDSCCKTFVRSDHLHRHLKKDGCNGVPSRRGRKPRVRGVPPDVPAGAGAPPGLPDAPRNGQEKHFKDEEEDEEEASPDGSGRLNVAGSGGDDGAGGPAVATAEGNFAT
| null | null |
B cell differentiation [GO:0030183]; cartilage development [GO:0051216]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA-templated transcription [GO:0006351]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; erythrocyte maturation [GO:0043249]; fat cell differentiation [GO:0045444]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein localization to nucleus [GO:0034504]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of apoptotic process [GO:0042981]; regulation of DNA-binding transcription factor activity [GO:0051090]; regulation of DNA-templated transcription [GO:0006355]; regulation of glycolytic process [GO:0006110]; regulation of osteoclast differentiation [GO:0045670]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transcription regulatory region DNA binding [GO:2000677]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone acetyltransferase binding [GO:0035035]; metal ion binding [GO:0046872]; nuclear androgen receptor binding [GO:0050681]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; SMAD binding [GO:0046332]; transcription corepressor binding [GO:0001222]
|
PF00651;PF00096;
|
3.30.160.60;
| null |
PTM: Sumoylated. Undergoes sumoylation with SUMO1 that may regulate its transcriptional activity. {ECO:0000250|UniProtKB:O95365}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:9927193}. Note=Recruited to double-strand break sites of damaged DNA. {ECO:0000269|PubMed:26446488}.
| null | null | null | null | null |
FUNCTION: Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation (PubMed:15337766, PubMed:15662416, PubMed:17495164, PubMed:26816381, PubMed:29813070). Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating the organization of chromatin and through the direct recruitment of transcription factors to gene regulatory regions (PubMed:15337766, PubMed:15662416, PubMed:26816381, PubMed:29813070). Negatively regulates SMAD4 transcriptional activity in the TGF-beta signaling pathway through these two mechanisms (By similarity). That is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the recruitment of the transcriptional activators CREBBP and EP300 (By similarity). Collaborates with transcription factors like RELA to modify the accessibility of gene transcription regulatory regions to secondary transcription factors (PubMed:29813070). Also directly interacts with transcription factors like SP1 to prevent their binding to DNA (By similarity). Functions as an androgen receptor/AR transcriptional corepressor by recruiting NCOR1 and NCOR2 to the androgen response elements/ARE on target genes (By similarity). Thereby, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (By similarity). Involved in the switch between fetal and adult globin expression during erythroid cells maturation (PubMed:26816381). Through its interaction with the NuRD complex regulates chromatin at the fetal globin genes to repress their transcription (PubMed:26816381). Specifically represses the transcription of the tumor suppressor ARF isoform from the CDKN2A gene (PubMed:15662416). Efficiently abrogates E2F1-dependent CDKN2A transactivation (PubMed:15662416). Regulates chondrogenesis through the transcriptional repression of specific genes via a mechanism that also requires histone deacetylation (PubMed:15337766). Regulates cell proliferation through the transcriptional regulation of genes involved in glycolysis (By similarity). Involved in adipogenesis through the regulation of genes involved in adipocyte differentiation (By similarity). Plays a key role in the differentiation of lymphoid progenitors into B and T lineages (PubMed:17495164). Promotes differentiation towards the B lineage by inhibiting the T-cell instructive Notch signaling pathway through the specific transcriptional repression of Notch downstream target genes (PubMed:17495164). Also regulates osteoclast differentiation (By similarity). May also play a role, independently of its transcriptional activity, in double-strand break repair via classical non-homologous end joining/cNHEJ (PubMed:26446488). Recruited to double-strand break sites on damage DNA, interacts with the DNA-dependent protein kinase complex and directly regulates its stability and activity in DNA repair (PubMed:26446488). May also modulate the splicing activity of KHDRBS1 toward BCL2L1 in a mechanism which is histone deacetylase-dependent and thereby negatively regulates the pro-apoptotic effect of KHDRBS1 (By similarity). {ECO:0000250|UniProtKB:O95365, ECO:0000250|UniProtKB:Q9QZ48, ECO:0000269|PubMed:15337766, ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:17495164, ECO:0000269|PubMed:26446488, ECO:0000269|PubMed:26816381, ECO:0000269|PubMed:29813070}.
|
Mus musculus (Mouse)
|
O88940
|
MUSC_MOUSE
|
MSTGSVSDPEDSEMRGLQRVYPAPASKRPPLLRMERGYGSPSDISSAEEEDGEEEPGSLGAAGGCKRKRLRGADAGGAGGRAGGAGKKPLPPKGSAAECKQSQRNAANARERARMRVLSKAFSRLKTSLPWVPPDTKLSKLDTLRLASSYIAHLRQLLQEDRYEDSYVHPVNLTWPFVVSGRPDSDSKDVSAANRLCGTSA
| null | null |
branchiomeric skeletal muscle development [GO:0014707]; cellular response to leukemia inhibitory factor [GO:1990830]; diaphragm development [GO:0060539]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]; skeletal muscle tissue development [GO:0007519]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcription repressor that blocks myogenesis and activation of E-box dependent muscle genes.
|
Mus musculus (Mouse)
|
O88942
|
NFAC1_MOUSE
|
MPNTSFPVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAEEEHYSYVSPSVTSTLPLPTAHSALPAACHDLQTSTPGISAVPSANHPPSYGGAVDSGPSGYFLSSGNTRPNGAPTLESPRIEITSYLGLHHGSGQFFHDVEVEDVLPSCKRSPSTATLHLPSLEAYRDPSCLSPASSLSSRSCNSEASSYESNYSYPYASPQTSPWQSPCVSPKTTDPEEGFPRSLGACHLLGSPRHSPSTSPRASITEESWLGARGSRPTSPCNKRKYSLNGRQPSCSPHHSPTPSPHGSPRVSVTEDTWLGNTTQYTSSAIVAAINALTTDSTLDLGDGVPIKSRKTALEHAPSVALKVEPAGEDLGTTPPTSDFPPEEYTFQHLRKGAFCEQYLSVPQASYQWAKPKSLSPTSYMSPSLPALDWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRTLSLQVASNPIECSQRSAQELPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPAQVSFYVCNGKRKRSQYQRFTYLPANGNSVFLTLSSESELRGGFY
| null | null |
aortic valve development [GO:0003176]; aortic valve morphogenesis [GO:0003180]; B-1a B cell differentiation [GO:0002337]; branching involved in lymph vessel morphogenesis [GO:0060854]; calcineurin-NFAT signaling cascade [GO:0033173]; calcium ion transport [GO:0006816]; cellular response to calcium ion [GO:0071277]; endocardial cushion development [GO:0003197]; epithelial to mesenchymal transition [GO:0001837]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; heart development [GO:0007507]; heart trabecula morphogenesis [GO:0061384]; heart valve development [GO:0003170]; heart valve morphogenesis [GO:0003179]; intracellular signal transduction [GO:0035556]; keratinocyte proliferation [GO:0043616]; lymphangiogenesis [GO:0001946]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of stem cell proliferation [GO:2000647]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoclast differentiation [GO:0030316]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; pulmonary valve development [GO:0003177]; pulmonary valve morphogenesis [GO:0003184]; regulation of hair cycle [GO:0042634]; regulation of transcription by RNA polymerase II [GO:0006357]; semi-lunar valve development [GO:1905314]; stem cell proliferation [GO:0072089]; transcription by RNA polymerase II [GO:0006366]; transition between fast and slow fiber [GO:0014883]; ventricular septum morphogenesis [GO:0060412]; wound healing [GO:0042060]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasm [GO:0016528]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; mitogen-activated protein kinase p38 binding [GO:0048273]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; transcription coactivator binding [GO:0001223]
|
PF16179;PF00554;
|
2.60.40.10;2.60.40.340;
| null |
PTM: Phosphorylated by NFATC-kinase and GSK3B; phosphorylation induces NFATC1 nuclear exit and dephosphorylation by calcineurin promotes nuclear import. Phosphorylation by PKA and DYRK2 negatively modulates nuclear accumulation, and promotes subsequent phosphorylation by GSK3B or casein kinase 1 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19626032, ECO:0000269|PubMed:24970700, ECO:0000269|PubMed:28341745, ECO:0000269|PubMed:32741026}. Nucleus {ECO:0000269|PubMed:19626032, ECO:0000269|PubMed:21514407, ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563, ECO:0000269|PubMed:28341745, ECO:0000269|PubMed:32741026}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. Translocation to the nucleus is increased in the presence of calcium in pre-osteoblasts (PubMed:21514407). The subcellular localization of NFATC plays a key role in the regulation of gene transcription (By similarity). Nuclear translocation of NFATC1 is enhanced in the presence of TNFSF11 (PubMed:26644563). Nuclear translocation is decreased in the presence of FBN1 which can bind and sequester TNFSF11 (PubMed:24039232). {ECO:0000250|UniProtKB:O95644, ECO:0000269|PubMed:21514407, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563}.
| null | null | null | null | null |
FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription (PubMed:9388475). Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells (By similarity). Required for osteoclastogenesis and regulates many genes important for osteoclast differentiation and function (PubMed:23990468, PubMed:26644563). {ECO:0000250|UniProtKB:O95644, ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:9388475, ECO:0000303|PubMed:26644563}.
|
Mus musculus (Mouse)
|
O88943
|
KCNQ2_RAT
|
MVQKSRNGGVYPGTSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSVLSKPRTGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMISSQTQTYGASRLIPPLNQLEMLRNLKSKSGLTFRKEPQPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLDDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVEDNKSCNCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPTITDKDRTKGPAETELPEDPSMMGRLGKVEKQVLSMEKKLDFLVSIYTQRMGIPPAETEAYFGAKEPEPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRKYAAPPVMPPAECPPSTSWQQSHQRHGTSPVGDHGSLVRIPPPPAHERSLSAYSGGNRASTEFLRLEGTPACRPSEAALRDSDTSISIPSVDHEELERSFSGFSISQSKENLNALASCYAAVAPCAKVRPYIAEGESDTDSDLCTPCGPPPRSATGEGPFGDVAWAGPRK
| null | null |
action potential [GO:0001508]; action potential initiation [GO:0099610]; apoptosome assembly [GO:0097314]; brain development [GO:0007420]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; cognition [GO:0050890]; dentate gyrus development [GO:0021542]; determination of adult lifespan [GO:0008340]; endocytosis [GO:0006897]; establishment of cell polarity [GO:0030010]; excitatory chemical synaptic transmission [GO:0098976]; exocytosis [GO:0006887]; exploration behavior [GO:0035640]; gene expression [GO:0010467]; grooming behavior [GO:0007625]; hippocampal pyramidal neuron differentiation [GO:0097432]; hippocampus development [GO:0021766]; inhibitory chemical synaptic transmission [GO:0098977]; learning [GO:0007612]; membrane hyperpolarization [GO:0060081]; memory [GO:0007613]; mitochondrial depolarization [GO:0051882]; monoatomic ion transmembrane transport [GO:0034220]; motor behavior [GO:0061744]; nerve development [GO:0021675]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; neuron remodeling [GO:0016322]; neuronal action potential [GO:0019228]; potassium ion transmembrane transport [GO:0071805]; protein import into nucleus [GO:0006606]; protein transport [GO:0015031]; psychomotor behavior [GO:0036343]; regulation of action potential firing threshold [GO:0099611]; regulation of membrane potential [GO:0042391]; regulation of synaptic plasticity [GO:0048167]; response to auditory stimulus [GO:0010996]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; response to temperature stimulus [GO:0009266]; response to xenobiotic stimulus [GO:0009410]; sensory perception of sound [GO:0007605]; social behavior [GO:0035176]; sodium ion transmembrane transport [GO:0035725]; substantia propria of cornea development [GO:1903701]; transmission of nerve impulse [GO:0019226]
|
axon initial segment [GO:0043194]; cell surface [GO:0009986]; mitochondrion [GO:0005739]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076]
|
ankyrin binding [GO:0030506]; calmodulin binding [GO:0005516]; potassium channel activity [GO:0005267]; voltage-gated monoatomic ion channel activity [GO:0005244]; voltage-gated potassium channel activity [GO:0005249]
|
PF00520;PF16642;PF03520;PF11956;
|
1.10.287.70;6.10.140.1910;
|
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.2/KCNQ2 sub-subfamily
|
PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region. {ECO:0000250|UniProtKB:O43526}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43526}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11038262, ECO:0000269|PubMed:11230508}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2 current is blocked by barium and tetraethylammonium whereas 4-aminopyridine and charybdotoxin have no effect on KCNQ2 current. Tyrosine kinase inhibitors genistein or herbimycin a markedly down-regulate KCNQ2 current. As the native M-channel, the potassium channel composed of KCNQ2 and KCNQ3 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1 (PubMed:11038262, PubMed:11230508). KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (By similarity). {ECO:0000250|UniProtKB:O43526, ECO:0000269|PubMed:11038262, ECO:0000269|PubMed:11230508}.
|
Rattus norvegicus (Rat)
|
O88944
|
KCNQ3_RAT
|
MGLKARRAAGAAGGGGGEGGGGGGGAANPAGGDSAVAGDEERKVGLAPGDVEQVTLALGTGADKDGTLLLEGGGREEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEMDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRLDLVATWRFYESVVSFPFFRKEQLEAAASQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMTEDRGYGNDFLIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTYPSQQSPRNEPYVARAATSETEDQSMMGKFVKVERQVHDMGKKLDFLVDMHMQHMERLQVHVTEYYPTKGASSPAEGEKKEDNRYSDLKTIICNYSESGPPDPPYSFHQVPIDRVGPYGFFAHDPVKLTRGGPSSTKAQANLPSSGSTYAERPTVLPILTLLDSCVSYHSQTELQGPYSDHISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPSGGSSWMREKRYLAEGETDTDTDPFTPSGSMPMSSTGDGISDSIWTPSNKPT
| null | null |
action potential initiation [GO:0099610]; apoptosome assembly [GO:0097314]; cellular response to ammonium ion [GO:0071242]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; endocytosis [GO:0006897]; establishment of localization in cell [GO:0051649]; excitatory chemical synaptic transmission [GO:0098976]; exocytosis [GO:0006887]; ganglion development [GO:0061548]; gene expression [GO:0010467]; inhibitory chemical synaptic transmission [GO:0098977]; membrane hyperpolarization [GO:0060081]; mitochondrial depolarization [GO:0051882]; monoatomic ion transmembrane transport [GO:0034220]; nerve development [GO:0021675]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; neuron remodeling [GO:0016322]; neuronal action potential [GO:0019228]; oligodendrocyte development [GO:0014003]; potassium ion transmembrane transport [GO:0071805]; protein import into nucleus [GO:0006606]; protein targeting [GO:0006605]; protein transport [GO:0015031]; protein-containing complex assembly [GO:0065003]; psychomotor behavior [GO:0036343]; regulation of action potential firing threshold [GO:0099611]; regulation of synaptic plasticity [GO:0048167]; response to auditory stimulus [GO:0010996]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; sensory perception of sound [GO:0007605]; substantia propria of cornea development [GO:1903701]
|
axon initial segment [GO:0043194]; cell surface [GO:0009986]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; somatodendritic compartment [GO:0036477]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076]
|
calmodulin binding [GO:0005516]; potassium channel activity [GO:0005267]; protein kinase binding [GO:0019901]; transmembrane transporter binding [GO:0044325]; ubiquitin protein ligase binding [GO:0031625]; voltage-gated monoatomic ion channel activity [GO:0005244]; voltage-gated potassium channel activity [GO:0005249]
|
PF00520;PF03520;PF11956;
|
1.10.287.70;6.10.140.1910;
|
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.3/KCNQ3 sub-subfamily
|
PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43525}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9836639}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability (PubMed:9836639). KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (By similarity). {ECO:0000250|UniProtKB:O43525, ECO:0000269|PubMed:9836639}.
|
Rattus norvegicus (Rat)
|
O88947
|
FA10_MOUSE
|
MGSPVQLSLLCVVLASLLLPGKGVFINRERANNVLARTRRANSFFEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYKDGDQCESSPCQNQGACRDGIGGYTCTCSEGFEGKNCELFVRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSCISTAPFPCGKITTGRRKRSVALNTSDSELDLEDALLDEDFLSPTENPIELLNLNETQPERSSDDLVRIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDWAESTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCKLSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDRSMKARVGPTAETPRTAGPPN
|
3.4.21.6
| null |
blood coagulation [GO:0007596]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF14670;PF00594;PF00089;
|
4.10.740.10;2.10.25.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (By similarity). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity). {ECO:0000250|UniProtKB:P00742, ECO:0000250|UniProtKB:P00743}.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6;
| null | null | null | null |
FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
|
Mus musculus (Mouse)
|
O88951
|
LIN7B_MOUSE
|
MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEVRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHHSYTSLESRG
| null | null |
exocytosis [GO:0006887]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; neurotransmitter secretion [GO:0007269]; protein localization to basolateral plasma membrane [GO:1903361]; protein transport [GO:0015031]
|
basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; MPP7-DLG1-LIN7 complex [GO:0097025]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; synapse [GO:0045202]; transport vesicle membrane [GO:0030658]
|
L27 domain binding [GO:0097016]; PDZ domain binding [GO:0030165]; protein kinase binding [GO:0019901]
|
PF02828;PF00595;
|
2.30.42.10;1.10.287.650;
|
Lin-7 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction {ECO:0000269|PubMed:15494546}. Postsynaptic density membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction, tight junction {ECO:0000269|PubMed:15494546}. Note=Mainly basolateral in renal epithelial cells.
| null | null | null | null | null |
FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (PubMed:10846156). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface. {ECO:0000269|PubMed:10846156, ECO:0000269|PubMed:15317815}.
|
Mus musculus (Mouse)
|
O88952
|
LIN7C_MOUSE
|
MAALGEPVRLERDICRAIELLEKLQRSGEVPPQKLQALQRVLQSEFCNAVREVYEHVYETVDISSSPEVRANATAKATVAAFAASEGHSHPRVVELPKTEEGLGFNIMGGKEQNSPIYISRIIPGGIADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGKVKLVVRYTPKVLEEMESRFEKMRSAKRRQQT
| null | null |
exocytosis [GO:0006887]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; morphogenesis of an epithelial sheet [GO:0002011]; neurotransmitter secretion [GO:0007269]; protein localization to basolateral plasma membrane [GO:1903361]; protein transport [GO:0015031]
|
basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; glutamatergic synapse [GO:0098978]; MPP7-DLG1-LIN7 complex [GO:0097025]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; synapse [GO:0045202]; transport vesicle membrane [GO:0030658]
|
cytoskeletal protein binding [GO:0008092]; L27 domain binding [GO:0097016]; PDZ domain binding [GO:0030165]
|
PF02828;PF00595;
|
2.30.42.10;1.10.287.650;
|
Lin-7 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Basolateral cell membrane; Peripheral membrane protein. Cell junction. Postsynaptic density membrane; Peripheral membrane protein. Cell junction, tight junction. Note=Mainly basolateral in renal epithelial cells.
| null | null | null | null | null |
FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (PubMed:10846156). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. {ECO:0000269|PubMed:10846156}.
|
Mus musculus (Mouse)
|
O88956
|
PLPP1_CAVPO
|
MFDKARLPYVALDVLCVVLAGLPFAILTSRHTPFQRGIFCNDESIKYPYKEDTIPYALLGGIMIPFSIVVMIIGETLSVYCNLLHSNSFIRNNYIATIYKSIGTFLFGAAASQSLTDIAKYSIGRLRPHFLSVCDPDWSKVNCSDGYIEYYVCRGNAEKVKEGRLSFYSGHSSFSMYCMVFVALYLQARMKGDWARLLRPTLQFGLVAASIYVGLSRISDYKHHWSDVLTGLIQGAIVAILVAVYVSDFFKARNSPFQERKEEDSHTTLHETPTAGNHYRSNHQP
|
3.1.3.-; 3.1.3.106; 3.1.3.4; 3.6.1.75
| null |
ceramide metabolic process [GO:0006672]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]; sphingosine metabolic process [GO:0006670]
|
apical plasma membrane [GO:0016324]; caveola [GO:0005901]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
ceramide-1-phosphate phosphatase activity [GO:0106235]; diacylglycerol diphosphate phosphatase activity [GO:0000810]; lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]; sphingosine-1-phosphate phosphatase activity [GO:0042392]
|
PF01569;
|
1.20.144.10;
|
PA-phosphatase related phosphoesterase family
|
PTM: N-glycosylated. N-linked sugars are of the complex type. N-glycosylation is not required for the phosphatase activity. {ECO:0000250|UniProtKB:Q61469}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q61469}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000269|PubMed:18215144}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000305|PubMed:18215144}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683; EC=3.1.3.106; Evidence={ECO:0000250|UniProtKB:Q61469}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156; Evidence={ECO:0000250|UniProtKB:Q61469}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:Q61469}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836; Evidence={ECO:0000250|UniProtKB:Q61469}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75; Evidence={ECO:0000250|UniProtKB:Q61469}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450; Evidence={ECO:0000250|UniProtKB:Q61469}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466; Evidence={ECO:0000250|UniProtKB:O08564}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256; Evidence={ECO:0000250|UniProtKB:O08564};
| null |
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:18215144}.
| null | null |
FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:18215144). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (By similarity). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (By similarity). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (By similarity). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (By similarity). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (By similarity). {ECO:0000250|UniProtKB:O08564, ECO:0000250|UniProtKB:O14494, ECO:0000269|PubMed:18215144}.
|
Cavia porcellus (Guinea pig)
|
O88958
|
GNPI1_MOUSE
|
MKLIILEHYSQASEWAAKYIRNRIIQFNPGPDKYFTLGLPTGSTPLGCYQKLIEYYKNGDLSFQYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAADLQAECDAFEEKIQAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGDLAKVPTMALTVGVGTVMDAKEVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCDEDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKEIQKSQSAKKPYSD
|
3.5.99.6
| null |
acrosome reaction [GO:0007340]; fructose 6-phosphate metabolic process [GO:0006002]; fructose biosynthetic process [GO:0046370]; generation of precursor metabolites and energy [GO:0006091]; glucosamine catabolic process [GO:0006043]; glucosamine metabolic process [GO:0006041]; N-acetylglucosamine catabolic process [GO:0006046]; N-acetylneuraminate catabolic process [GO:0019262]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]
|
cytoplasm [GO:0005737]
|
glucosamine-6-phosphate deaminase activity [GO:0004342]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853]
|
PF01182;
|
3.40.50.1360;
|
Glucosamine/galactosamine-6-phosphate isomerase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10481053}.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; Evidence={ECO:0000250|UniProtKB:P46926}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173; Evidence={ECO:0000250|UniProtKB:P46926}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174; Evidence={ECO:0000250|UniProtKB:P46926};
| null |
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P46926}.
| null | null |
FUNCTION: Catalyzes the reversible conversion of alpha-D-glucosamine 6-phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and ammonium ion, a regulatory reaction step in de novo uridine diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via hexosamine pathway. Deamination is coupled to aldo-keto isomerization mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high ammonium level can drive amination and isomerization of Fru-6P toward hexosamines and UDP-GlcNAc synthesis (By similarity). Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and their effects on hyaluronan synthesis that occur during tissue remodeling (By similarity). Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity). {ECO:0000250|UniProtKB:P46926, ECO:0000250|UniProtKB:Q64422}.
|
Mus musculus (Mouse)
|
O88962
|
CP8B1_MOUSE
|
MTLWCTVLGALLTVVGCLCLSLLLRHRRPWEPPLDKGFVPWLGHSMAFRKNMFEFLKGMRAKHGDVFTVQLGGQYFTFVMDPLSFGPIIKNTEKALDFQSYAKELVLKVFGYQSVDGDHRMIHLASTKHLMGQGLEELNQAMLDSLSLVMLGPKGSSLGASSWCEDGLFHFCYRILFKAGFLSLFGYTKDKQQDLDEADELFRKFRRFDFLFPRFVYSLLGPREWVEVSQLQRLFHQRLSVEQNLEKDGISCWLGYMLQFLREQGIASSMQDKFNFMMLWASQGNTGPTCFWVLLFLLKHQDAMKAVREEATRVMGKARLEAKKSFTFTPSALKHTPVLDSVMEESLRLCATPTLLRVVQEDYVLKMASGQEYQIRRGDKVALFPYLSVHMDPDIHPEPTAFKYDRFLNPDGTRKVDFYKSGKKIHHYSMPWGSGVSKCPGRFFALSEMKTFVLLMIMYFDFKLVDPDIPVPPIDPRRWGFGTSQPSHEVRFLYRLKPVQ
|
1.14.14.139
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:O02766};
|
bile acid biosynthetic process [GO:0006699]; positive regulation of intestinal cholesterol absorption [GO:0045797]
|
endoplasmic reticulum membrane [GO:0005789]
|
5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase activity [GO:0033779]; 7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase activity [GO:0033778]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; sterol 12-alpha-hydroxylase activity [GO:0008397]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=7alpha-hydroxycholest-4-en-3-one + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46752, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17899, ChEBI:CHEBI:28477, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.139; Evidence={ECO:0000250|UniProtKB:O02766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46753; Evidence={ECO:0000250|UniProtKB:O02766}; CATALYTIC ACTIVITY: Reaction=5beta-cholestane-3alpha,7alpha-diol + O2 + reduced [NADPH--hemoprotein reductase] = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:15261, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16496, ChEBI:CHEBI:28047, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.139; Evidence={ECO:0000250|UniProtKB:O02766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15262; Evidence={ECO:0000250|UniProtKB:O02766}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholate + O2 + reduced [NADPH--hemoprotein reductase] = cholate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65700, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29747, ChEBI:CHEBI:36234, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.139; Evidence={ECO:0000250|UniProtKB:O02766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65701; Evidence={ECO:0000250|UniProtKB:O02766};
| null |
PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000269|PubMed:12393855, ECO:0000269|PubMed:28377401}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis (By similarity). Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating the intestinal absorption of dietary lipids (PubMed:12393855, PubMed:28377401). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase) (By similarity). {ECO:0000250|UniProtKB:O02766, ECO:0000250|UniProtKB:Q9UNU6, ECO:0000269|PubMed:12393855, ECO:0000269|PubMed:28377401}.
|
Mus musculus (Mouse)
|
O88967
|
YMEL1_MOUSE
|
MFSLSSTVQPQVTIPLSHLINAFHSPKNISVSVNTPVSQKQHRDTVPEHEAPSSEPVLNLRDLGLSELKIGQIDKMVENLLPGFYKDKRVSSCWHTSHISAQSFFENKYGHLDMFSTLRSSSLYRQHPKTLRSICSDLQYFPVFIQSRGFKTLKSRTRRLQSTSERLVEAQNIAPSFVKGFLLRDRGTDLESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTVLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDKSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRESYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR
|
3.4.24.-; 3.6.-.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96TA2}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q96TA2};
|
cell population proliferation [GO:0008283]; mitochondrial protein catabolic process [GO:0035694]; mitochondrial protein processing [GO:0034982]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; protein hexamerization [GO:0034214]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF00004;PF17862;PF01434;
|
1.10.8.60;3.40.50.300;1.20.58.760;
|
AAA ATPase family; Peptidase M41 family
|
PTM: Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. Degraded in an OMA1-dependent manner in response to oxidative stress. {ECO:0000250|UniProtKB:Q96TA2}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96TA2}. Mitochondrion {ECO:0000250|UniProtKB:Q96TA2}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q96TA2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q96TA2};
| null | null | null | null |
FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:17709429, PubMed:24616225, PubMed:24703695, PubMed:26785494, PubMed:27495975, PubMed:33237841). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (PubMed:17709429, PubMed:24616225, PubMed:24703695, PubMed:26785494, PubMed:27495975, PubMed:33237841). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (By similarity). Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (By similarity). Involved in the mitochondrial adaptation in response to various signals, such as stress or developmental cues, by mediating degradation of mitochondrial proteins to rewire the mitochondrial proteome (PubMed:35172139). Catalyzes degradation of mitochondrial proteins, such as translocases, lipid transfer proteins and metabolic enzymes in response to nutrient starvation in order to limit mitochondrial biogenesis: mechanistically, YME1L is activated by decreased phosphatidylethanolamine levels caused by LPIN1 activity in response to mTORC1 inhibition (By similarity). Acts as a regulator of adult neural stem cell self-renewal by promoting mitochondrial proteome rewiring, preserving neural stem and progenitor cells self-renewal (PubMed:35172139). Required for normal, constitutive degradation of PRELID1 (PubMed:26785494). Catalyzes the degradation of OMA1 in response to membrane depolarization (By similarity). Mediates degradation of TIMM17A downstream of the integrated stress response (ISR) (By similarity). {ECO:0000250|UniProtKB:Q96TA2, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:24703695, ECO:0000269|PubMed:26785494, ECO:0000269|PubMed:27495975, ECO:0000269|PubMed:33237841, ECO:0000269|PubMed:35172139}.
|
Mus musculus (Mouse)
|
O88974
|
SETB1_MOUSE
|
MSSLPGCMSLAAAPAAADSAEIAELQQAVVEELGISMEELRQYIDEELEKMDCIQQRKKQLAELETWVLQKESEVAYVDRLFDDASREVTNCESLVKDFYSKLGLQYHDSSSEDEASRPTEIIEIPDEDDDVLSIDSGDAGSRTPKDQKLREAMAALRKSAQDVQKFMDAVNKKSSSQDLHKGTLGQVSGELSKDGDLIVSMRILGKKRTKTWHKGTLIAIQTVGLGKKYKVKFDNKGKSLLSGNHIAYDYHPPADKLFVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFDDGYASYVTQSELYPICRPLKKTWEDIEDSSCRDFIEEYITAYPNRPMVLLKSGQLIKTEWEGTWWKSRVEEVDGSLVRILFLDDKRCEWIYRGSTRLEPMFSMKTSSASAMEKKQGGQLRTRPNMGAVRSKGPVVQYTQDLTGTGIQFKPMEPLQPIAPPAPLPIPPLSPQAADTDLESQLAQSRKQVAKKSTSFRPGSVGSGHSSPTSSTLSENVSAGKLGINQTYRSPLASVTSTPASAAPPVPPVPPGPPTPPGPPAPPGPLAPPAFHGMLERAPAEPSYRAPMEKLFYLPHVCSYTCLSRIRPMRNEQYRGKNPLLVPLLYDFRRMTARRRVNRKMGFHVIYKTPCGLCLRTMQEIERYLFETGCDFLFLEMFCLDPYVLVDRKFQPFKPFYYILDITYGKEDVPLSCVNEIDTTPPPQVAYSKERIPGKGVFINTGPEFLVGCDCKDGCRDKSKCACHQLTIQATACTPGGQVNPNSGYQYKRLEECLPTGVYECNKRCNCDPNMCTNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGSFVCIYAGKILTDDFADKEGLEMGDEYFANLDHIESVENFKEGYESDVPTSSDSSGVDMKDQEDGNSGSEDPEESNDDSSDDNFCKDEDFSTSSVWRSYATRRQTRGQKENELSEMTSKDSRPPDLGPPHVPIPSSVSVGGCNPPSSEETPKNKVASWLSCNSVSEGGFADSDSRSSFKTSEGGDGRAGGGRGEAERASTSGLSFKDEGDNKQPKKEDPENRNKMPVVTEGSQNHGHNPPMKSEGLRRPASKMSVLQSQRVVTSTQSNPDDILTLSSSTESEGESGTSRKPTAGHTSATAVDSDDIQTISSGSDGDDFEDKKNLSGPTKRQVAVKSTRGFALKSTHGIAIKSTNMASVDKGESAPVRKNTRQFYDGEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIRAGTELTWDYNYEVGSVEGKELLCCCGAIECRGRLL
|
2.1.1.366
| null |
bone development [GO:0060348]; heterochromatin organization [GO:0070828]; inner cell mass cell proliferation [GO:0001833]; methylation [GO:0032259]; negative regulation of gene expression [GO:0010629]; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045869]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA methylation-dependent heterochromatin formation [GO:0090309]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 monomethyltransferase activity [GO:0140948]; histone H3K9me2 methyltransferase activity [GO:0140947]; promoter-specific chromatin binding [GO:1990841]; zinc ion binding [GO:0008270]
|
PF18300;PF01429;PF05033;PF00856;PF18358;PF18359;
|
2.30.30.140;2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily
|
PTM: Degraded by the proteasome, shielded by interaction with ATF7IP. {ECO:0000250|UniProtKB:Q15047}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29728365}. Chromosome {ECO:0000269|PubMed:29728365}. Note=Associated with non-pericentromeric regions of chromatin. {ECO:0000250|UniProtKB:Q15047}.
|
CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60288, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15541, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; EC=2.1.1.366; Evidence={ECO:0000255|PROSITE-ProRule:PRU00906, ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:22939622}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60289; Evidence={ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:22939622};
| null | null | null | null |
FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (PubMed:11791185, PubMed:22939622). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (By similarity). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (By similarity). In ESCs, in collaboration with TRIM28, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (PubMed:20164836, PubMed:29728365). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (By similarity). {ECO:0000250|UniProtKB:Q15047, ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:20164836, ECO:0000269|PubMed:22939622, ECO:0000269|PubMed:29728365}.
|
Mus musculus (Mouse)
|
O88978
|
DAA11_MOUSE
|
MGRITEDLIRRNAEHNDCVIFSLEELSLHQQEIERLEHIDKWCRDLKILYLQNNLIGKIENVSKLKKLEYLNLALNNIERIENLEGCEWLTKLDLTVNFIGELSSVKTLTHNIHLKELFLMGNPCADFDGYRQFVVVTLQQLKWLDGKEIERSERIQALQNYTSVEQQIREQEKAYCLRRAKEKEEAQRKLEEENESEDKKKSSTGFDGHWYTDIHTACPSATENQDYPQVPETQEEQHNTKESDDIEDDLAFWNKPSLFTPESRLETLRHMEKQRKAQDKLSEKKKKAKPPRTLITEDGKVLNVNEAKLDFSLKDDEKHNQIILDLAVYRYMDTSLIEVDVQPTYVRVMVKGKPFQLALSTEVQPDRSSAKRSQTTGHLLICMPKVGEMITGGQRTPTSVKTTSTSSREQTNPRKKQIERLEVDPSKHSCPDVSTIVQEKRHRPKRMESQPRDEPSEEDPDFEDNPEVPPLI
| null | null |
axonemal dynein complex assembly [GO:0070286]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; flagellated sperm motility [GO:0030317]; inner dynein arm assembly [GO:0036159]; male gonad development [GO:0008584]; motile cilium assembly [GO:0044458]; outer dynein arm assembly [GO:0036158]; protein localization to cilium [GO:0061512]; protein localization to motile cilium [GO:0120229]
|
apical cytoplasm [GO:0090651]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynein axonemal particle [GO:0120293]; extracellular region [GO:0005576]; motile cilium [GO:0031514]
| null |
PF14580;
|
3.80.10.10;
|
TilB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10775177, ECO:0000269|PubMed:27353389}. Cell projection, cilium {ECO:0000250|UniProtKB:Q86X45}. Dynein axonemal particle {ECO:0000305|PubMed:27353389}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q86X45}.
| null | null | null | null | null |
FUNCTION: Involved in dynein arm assembly, is important for expression and transporting outer dynein arm (ODA) proteins from the cytoplasm to the cilia (PubMed:27353389). Acts as a crucial component in the formation and motility of spermatozoal flagella (By similarity). {ECO:0000250|UniProtKB:Q86X45, ECO:0000269|PubMed:27353389}.
|
Mus musculus (Mouse)
|
O88983
|
STX8_MOUSE
|
MAPDPWFSTYDSTCQIAQEIAEKIQERNQCERRGEKTPKLTLTIRTLLKNLKVKIDLLKDLLLRAVSTRQITQLEGDRRQNLLDDLVTRERLLLASFKNEGAEPDLIRSSLMSEEAKRGTPNPWLCEEPEETRGLGFDEIRQQQQKIIQEQDAGLDALSSIISRQKQMGQEIGNELDEQNEIIDDLANLVENTDEKLRTEARRVTLVDRKSTSCGMIMVILLLLVAIVVVAVWPTN
| null | null |
cellular response to type II interferon [GO:0071346]; early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; regulation of protein localization to plasma membrane [GO:1903076]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]
|
early endosome [GO:0005769]; endomembrane system [GO:0012505]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; recycling endosome [GO:0055037]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
|
chloride channel inhibitor activity [GO:0019869]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]; ubiquitin protein ligase binding [GO:0031625]
|
PF05739;
|
1.20.5.110;
|
Syntaxin family
|
PTM: Ubiquitinated by HECTD3. {ECO:0000269|PubMed:18821010}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Preferentially associated with the early endosome. To a lesser extent, also present in late endosome, the plasma membrane and coated pits (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O88984
|
NXF1_RAT
|
MADEGKSYNEHDDRVSFPQRRKKGRGPFRWKCGVGNRRSGRGGSGIRSSRFEEDDGDVAMNDPQDGPRVRFNPYTTRPNRRRDTWHDRDRIHVTVRRDRAPQERGGAGTSQDGTTKNWFKITIPYGKKYDKMWLLSMIQSKCSVPFNPIEFHYENTRAHFFVENATTASALKAVNYKIQDRENGRISIIINSSAPPYIVQNELKPEQVEQLKLIMSKRYDGSQQALDLKGLRSDPDLVAQNIDVVLNRRGCMAAALRIIEENIPELLSLNLSNNRLYKLDDMSSIVQKAPNLKILNLSGNELKSEWELDKIKGLKLEELWLDRNPMCDTFLDQSTYISTIRERFPKLLRLDGHELPPPIAFDVEAPTMLPPCKGSYFGTENLKSLVLHFLQQYYAIYDSGDRQGLLDAYHDGACCSLSTPSNPQNPVRHNLAKYFNDSRNVKKIKDTTTRFRLLKHTRLNVVAFLNELPKTHHDVNSFVVDISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASPEEIQRAFAMPAPTPSSSPVPTLSQEQQDMLQAFSTQSGMNLEWSQKCLQDNNWDYTRSAQAFTHLKAKGEIPEVAFMK
| null | null |
mRNA export from nucleus [GO:0006406]; poly(A)+ mRNA export from nucleus [GO:0016973]; protein transport [GO:0015031]; RNA export from nucleus [GO:0006405]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nuclear inclusion body [GO:0042405]; nuclear pore [GO:0005643]; nuclear RNA export factor complex [GO:0042272]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; transcription export complex [GO:0000346]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]
|
PF02136;PF09162;PF03943;
|
3.10.450.50;3.30.70.330;1.10.8.10;3.80.10.10;
|
NXF family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UBU9}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles. Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q9UBU9}.
| null | null | null | null | null |
FUNCTION: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export. Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export. {ECO:0000250|UniProtKB:Q9UBU9}.
|
Rattus norvegicus (Rat)
|
O88987
|
AKAP3_MOUSE
|
MADRVDWLQSQSGVCKVGVYSPGDNQHQDWKMDTSTDPVRVLSWLRKDLEKSTAGFQDSRFKPGESSFVEEVAYPVDQRKGFCVDYYNTTNKGSPGRLHFEMSHKENPSQGLISHVGNGGSIDEVSFYANRLTNLVIAMARKEINEKIHGAENKCVHQSLYMGDEPTPHKSLSTVASELVNETVTACSKNISSDKAPGSGDRASGSSQAPGLRYTSTLKIKESTKEGKCPDDKPGTKKSFFYKEVFESRNAGDAKEGGRSLPGDQKLFRTSPDNRPDDFSNSISQGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLMKHAKEVVSDLIDSFMKNLHGVTGSLMTDTDFVSAVKRSFFSHGSQKATDIMDAMLGKLYNVMFAKKFPENIRRARDKSESYSLISTKSRAGDPKLSNLNFAMKSESKLKENLFSTCKLEKEKTCAETLGEHIIKEGLHMWHKSQQKSPGLERAAKLGNAPQEVSFECPDPCEANPPHQPQPPENFANFMCDSDSWAKDLIVSALLLIQYHLAQGGKMDAQSFLEAAASTNFPTNKPPPPSPVVQDECKLKSPPHKICDQEQTEKKDLMSVIFNFIRNLLSETIFKSSRNCESNVHEQNTQEEEIHPCERPKTPCERPITPPAPKFCEDEEATGGALSGLTKMVANQLDNCMNGQMVEHLMDSVMKLCLIIAKSCDSPLSELGEEKCGDASRPNSAFPDNLYECLPVKGTGTAEALLQNAYLTIHNELRGLSGQPPEGCEIPKVIVSNHNLADTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSATAVEKGRSVGEVLQSVLRYEKERQLDEAVGNVTRLQLLDWLMANL
| null | null |
blastocyst hatching [GO:0001835]; protein localization [GO:0008104]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]
|
acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; motile cilium [GO:0031514]; sperm fibrous sheath [GO:0035686]; sperm midpiece [GO:0097225]; sperm principal piece [GO:0097228]
|
protein kinase A binding [GO:0051018]
|
PF05716;
| null |
AKAP110 family
|
PTM: Phosphorylated on tyrosine. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11278869}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:37709195}. Note=Dorsal margin of the acrosomal segment (PubMed:11278869). Ribs of the fibrous sheath in the principal piece of the sperm tail (PubMed:11278869, PubMed:37709195). {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:37709195}.
| null | null | null | null | null |
FUNCTION: Has a role in the maintenance of acrosome structure. May function as a regulator of both spermatozoa motility and head-associated functions such as capacitation and the acrosome reaction. {ECO:0000250|UniProtKB:O75969}.
|
Mus musculus (Mouse)
|
O88989
|
MDHC_RAT
|
MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLQDVIATDKEEVAFKDLDVAVLVGSMPRREGMERKDLLKANVKIFKSQGAALEKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKSQIALKLGVTADDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAISDHIRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKETAFEFLSSA
|
1.1.1.37; 1.1.1.96
| null |
malate metabolic process [GO:0006108]; NAD metabolic process [GO:0019674]; NADH metabolic process [GO:0006734]; NADP metabolic process [GO:0006739]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
hydroxyphenylpyruvate reductase activity [GO:0047995]; L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase activity [GO:0016615]; NAD binding [GO:0051287]
|
PF02866;PF00056;
|
3.90.110.10;3.40.50.720;
|
LDH/MDH superfamily, MDH type 2 family
|
PTM: ISGylated. {ECO:0000250|UniProtKB:P40925}.; PTM: Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation. {ECO:0000250|UniProtKB:P40925}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P40925}.
|
CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000250|UniProtKB:P40925}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21433; Evidence={ECO:0000250|UniProtKB:P40925}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21434; Evidence={ECO:0000250|UniProtKB:P40925}; CATALYTIC ACTIVITY: Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:10780, ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.96; Evidence={ECO:0000250|UniProtKB:P40925}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10782; Evidence={ECO:0000250|UniProtKB:P40925}; CATALYTIC ACTIVITY: Reaction=(S)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH; Xref=Rhea:RHEA:57172, ChEBI:CHEBI:15378, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P40925}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57174; Evidence={ECO:0000250|UniProtKB:P40925};
| null | null | null | null |
FUNCTION: Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation. Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading to elevated reactive oxygen species (ROS). {ECO:0000250|UniProtKB:P40925}.
|
Rattus norvegicus (Rat)
|
O88990
|
ACTN3_MOUSE
|
MMMVMQPEGLGAGEGPFSGGGGGEYMEQEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENEKLMEEYEKLASELLEWIRRTVPWLENRVGEPSMSAMQRKLEDFRDYRRLHKPPRVQEKCQLEINFNTLQTKLRLSHRPAFMPSEGKLVSDIANAWRGLEQVEKGYEDWLLSEIRRLQRLQHLAEKFQQKASLHEAWTRGKEEMLNQHDYESASLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERMEKLLETIDQLQLEFARRAAPFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQFKATLPEADRERGAILGIQGEIQKICQTYGLRPKSGNPYITLSSQDINNKWDTVRKLVPSRDQTLQEELARQQVNERLRRQFAAQANAIGPWIQGKVEEVGRLAAGLAGSLEEQMAGLRQQEQNIINYKSNIDRLEGDHQLLQESLVFDNKHTVYSMEHIRVGWEQLLTSIARTINEVENQVLTRDAKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETDTAEQVVASFKILAGDKNYITPEELRRELPAEQAEYCIRRMAPYKGSGAPSGALDYVAFSSALYGESDL
| null | null |
actin cytoskeleton organization [GO:0030036]; bone morphogenesis [GO:0060349]; focal adhesion assembly [GO:0048041]; muscle cell development [GO:0055001]; muscle contraction [GO:0006936]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of glycolytic process [GO:0045820]; negative regulation of oxidative phosphorylation [GO:0090324]; negative regulation of relaxation of muscle [GO:1901078]; positive regulation of bone mineralization involved in bone maturation [GO:1900159]; positive regulation of fast-twitch skeletal muscle fiber contraction [GO:0031448]; positive regulation of glucose catabolic process to lactate via pyruvate [GO:1904025]; positive regulation of skeletal muscle fiber development [GO:0048743]; positive regulation of skeletal muscle tissue growth [GO:0048633]; regulation of aerobic respiration [GO:1903715]; regulation of muscle system process [GO:0090257]; regulation of the force of skeletal muscle contraction [GO:0014728]; response to denervation involved in regulation of muscle adaptation [GO:0014894]; skeletal muscle atrophy [GO:0014732]; transition between fast and slow fiber [GO:0014883]
|
brush border [GO:0005903]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; sarcomere [GO:0030017]; striated muscle thin filament [GO:0005865]; Z disc [GO:0030018]
|
actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; transmembrane transporter binding [GO:0044325]
|
PF00307;PF08726;PF00435;
|
1.20.58.60;1.10.418.10;1.10.238.10;
|
Alpha-actinin family
| null | null | null | null | null | null | null |
FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O88992
|
C1QRF_MOUSE
|
MLLVLVVLIPVLVSSGGPDGHYEMLGTCRMVCDPYPARGPGAGARSDGGDALSEQSGAPPPSTLVQGPQGKPGRTGKPGPPGPPGDRGPPGPVGPPGEKGEPGKPGPPGLPGSGGSGAISTATYTTVPRVAFYAGLKNPHEGYEVLKFDDVVTNLGNNYDAASGKFTCNIPGTYFFTYHVLMRGGDGTSMWADLCKNGQVRASAIAQDADQNYDYASNSVILHLDAGDEVFIKLDGGKAHGGNSNKYSTFSGFIIYSD
| null | null |
maintenance of synapse structure [GO:0099558]; motor learning [GO:0061743]; neuron remodeling [GO:0016322]; regulation of synapse pruning [GO:1905806]
|
cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; climbing fiber [GO:0044301]; collagen trimer [GO:0005581]; cytoplasm [GO:0005737]; presynapse [GO:0098793]; synaptic cleft [GO:0043083]
|
signaling receptor binding [GO:0005102]
|
PF00386;PF01391;
|
2.60.120.40;1.20.5.320;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. {ECO:0000269|PubMed:21262840}.
|
Mus musculus (Mouse)
|
O88998
|
NOE1_MOUSE
|
MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAASGGTLDRSTGVLPTNPEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISDPVTVKTSGSRFGSWMTDPLAPEGDNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGSIYFNKFQSHIIIRFDLKTEAILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPVSLQILQTWNTSYPKRSAGEAFIICGTLYVTNGYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGHQTLYNVTLFHVIRSDEL
| null | null |
atrioventricular valve formation [GO:0003190]; cardiac epithelial to mesenchymal transition [GO:0060317]; negative regulation of gene expression [GO:0010629]; neuronal signal transduction [GO:0023041]; positive regulation of apoptotic process [GO:0043065]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of gene expression [GO:0010628]; regulation of axon extension [GO:0030516]; signal transduction [GO:0007165]
|
AMPA glutamate receptor complex [GO:0032281]; axon [GO:0030424]; axonal growth cone [GO:0044295]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; extrinsic component of synaptic membrane [GO:0099243]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; synaptic membrane [GO:0097060]
| null |
PF12308;PF02191;
| null | null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22923615, ECO:0000305|PubMed:22632720}. Synapse {ECO:0000305|PubMed:22632720}. Endoplasmic reticulum {ECO:0000269|PubMed:22923615}. Cell projection, axon {ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}. Perikaryon {ECO:0000269|PubMed:22923615}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:9473566, ECO:0000305|PubMed:25903135}.
| null | null | null | null | null |
FUNCTION: Contributes to the regulation of axonal growth in the embryonic and adult central nervous system by inhibiting interactions between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone collapse (PubMed:22923615). May play an important role in regulating the production of neural crest cells by the neural tube (By similarity). May be required for normal responses to olfactory stimuli (PubMed:26107991). {ECO:0000250|UniProtKB:Q9IAK4, ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}.
|
Mus musculus (Mouse)
|
O89000
|
DPYD_RAT
|
MAGVLSRDAPDIESILALNPRIQAHATLRSTMAKKLDKKHWKRNTDKNCFICEKLENNFDDIKHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHATEEGPINIGGLQQFATEVFKAMNIPQIRSPLLPPPEHMPEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSISTDEMTLSTLKENGYKAAFIGIGLPEPKKDHIFQGLTQVQGFYTSKDFLPLVAKGSKPGMCACHSPLPSVRGAVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEEMELAKEEKCEFLPFLSPRKVIVKDGKIVGMQFVRTEQDETGNWVEDEEQIVRLKADVVISPFGSVLDDPKVIEALSPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHEYIQAQYGALVPSQPTLPLFYTPVDLVDISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPLYGPGQSSFLNIELISEKTAAYWCHSVTELKADFPDNILIASIMCSYNKNDWMELSKMAEASGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADGSPWPSVGSGKRTTYGGVSGTTIRPIALRAVTAIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELSDWDGQSPPTMSHQKGKPVPHIAELMGQKLPSFGPYLERRKKILAASKIRENDQNRACSPLQRKHFNSQKPIPAIKDVIGKSLQYLGTFGELNIMEQVVALIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTVSDTCTGCTLCLSVCPIMDCIRMVSRATPYEPKRGLPLAVKPVC
|
1.3.1.2
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q28943}; Note=Binds 2 FAD. {ECO:0000250|UniProtKB:Q28943}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q28943}; Note=Binds 2 FMN. {ECO:0000250|UniProtKB:Q28943}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q28943}; Note=Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms per subunit. {ECO:0000250|UniProtKB:Q28943};
|
beta-alanine biosynthetic process [GO:0019483]; circadian rhythm [GO:0007623]; CMP catabolic process [GO:0006248]; dCMP catabolic process [GO:0006249]; dUMP catabolic process [GO:0046079]; purine nucleobase catabolic process [GO:0006145]; pyrimidine nucleobase catabolic process [GO:0006208]; response to glucocorticoid [GO:0051384]; response to nutrient [GO:0007584]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; thymidine catabolic process [GO:0006214]; thymine catabolic process [GO:0006210]; UMP catabolic process [GO:0046050]; uracil catabolic process [GO:0006212]; uracil metabolic process [GO:0019860]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; dihydropyrimidine dehydrogenase (NADP+) activity [GO:0017113]; FAD binding [GO:0071949]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]; uracil binding [GO:0002058]
|
PF01180;PF14691;PF14697;PF07992;
|
3.30.70.20;3.20.20.70;1.10.1060.10;3.50.50.60;
|
Dihydropyrimidine dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12882}.
|
CATALYTIC ACTIVITY: Reaction=5,6-dihydrouracil + NADP(+) = H(+) + NADPH + uracil; Xref=Rhea:RHEA:18093, ChEBI:CHEBI:15378, ChEBI:CHEBI:15901, ChEBI:CHEBI:17568, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.2; Evidence={ECO:0000250|UniProtKB:Q12882}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18095; Evidence={ECO:0000250|UniProtKB:Q12882}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrothymine + NADP(+) = H(+) + NADPH + thymine; Xref=Rhea:RHEA:58284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17821, ChEBI:CHEBI:27468, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.2; Evidence={ECO:0000250|UniProtKB:Q12882}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58286; Evidence={ECO:0000250|UniProtKB:Q12882};
| null |
PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis. {ECO:0000250|UniProtKB:Q12882}.
| null | null |
FUNCTION: Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil. {ECO:0000250|UniProtKB:Q12882}.
|
Rattus norvegicus (Rat)
|
O89001
|
CBPD_MOUSE
|
MASGRDERPPWRLGRLRLLPPPPLLLLLLLLRSSAQAAHIKKAEATTTTVGGSEAAEGQFDHYYHEAALGEALEAAAAAGPPGLARLFSIGSSVEGRPLWVLRLTAGLGPPPTAAAGLDAAGPLLPGRPQVKLVGNMHGDETVSRQVLVYLARELASGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGLGDSGPPGTSGRDNSRGRDLNRSFPDQFSTGEPPSLDEVPEVRALIDWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKTTGLYSKTSDDEVFRYLAKAYASNHPIMKTGEPHCPGDEDETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGIKGFVKDSVTGSGLENATISVAGINHNITTGRFGDFHRLLVPGTYNLTALSTGYMPLTINNIMVKEGPATEMDFSLRPTVMSVMPGSTEAVTTPGTVAVPNIPPGTPSSHQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVRSTRIHLMPSMNPDGYEKSQEGDSISVVGRNNSNNFDLNRNFPDQFVPITEPTQPETIAVMSWVKAYPFVLSANLHGGSLVVNYPYDDNEQGVATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKDMYLNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPFENELPKYWEQNRRSLIQFMKQVHQGVKGFVLDATDGRGILNATLSVAEINHPVTTYKAGDYWRLLVPGTYKITASARGYNPVTKNVTVRSEGAVQVNFTLVRSSADANNESKKGRGHSTSTDDTSDPTSKEFEALIKHLSAENGLEGFMLSSSSDLALYRYHSYKDLSEFLRGLVMNYPHITNLTTLGQSVEYRHIWSLEISNKPNISEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKRNPVVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKTGHTNAHGKDLDTDFTSNASQPETKAIIENLIQKQDFSLSIALDGGSVLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNNSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAAQLPALWAENKKSLLSMLVEVHKGVHGLVKDKAGKPISKAVIVLNEGIKVYTKEGGYFHVLLAPGVHNINAIADGYQQQHTQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH
|
3.4.17.22
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q90240}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q90240};
|
peptide metabolic process [GO:0006518]; protein processing [GO:0016485]
|
extracellular space [GO:0005615]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
metallocarboxypeptidase activity [GO:0004181]; protein phosphatase 2A binding [GO:0051721]; protein-containing complex binding [GO:0044877]; zinc ion binding [GO:0008270]
|
PF13620;PF00246;
|
2.60.40.1120;3.40.630.10;
|
Peptidase M14 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Releases C-terminal Arg and Lys from polypeptides.; EC=3.4.17.22;
| null | null | null | null | null |
Mus musculus (Mouse)
|
O89016
|
ABCD4_MOUSE
|
MAVPGPTARAGARPRLDLQLVQRFVRIQKVFFPSWSSQNVLMFMTLLCVTLLEQLVIYQVGLIPSQYYGVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYYTYQCFQSTGWLGPVSIFGYFIVGTMVNKTLMGPIVTKLVQQEKLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPTELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDMSRKSQDCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPHGVLFLPQKPFFTDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSWELTRIKLE
|
7.6.2.8
| null |
cellular response to leukemia inhibitory factor [GO:1990830]; cobalamin metabolic process [GO:0009235]; cobalamin transport [GO:0015889]; fatty acid beta-oxidation [GO:0006635]; long-chain fatty acid import into peroxisome [GO:0015910]; peroxisome organization [GO:0007031]; very long-chain fatty acid catabolic process [GO:0042760]
|
endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; peroxisomal membrane [GO:0005778]
|
ABC-type vitamin B12 transporter activity [GO:0015420]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; identical protein binding [GO:0042802]; long-chain fatty acid transporter activity [GO:0005324]
|
PF06472;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCD family, Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14678}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14678}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate; Xref=Rhea:RHEA:17873, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:140785, ChEBI:CHEBI:456216; EC=7.6.2.8; Evidence={ECO:0000250|UniProtKB:O14678}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17874; Evidence={ECO:0000250|UniProtKB:O14678};
| null | null | null | null |
FUNCTION: Lysosomal membrane protein that transports cobalamin (Vitamin B12) from the lysosomal lumen to the cytosol in an ATP-dependent manner. Targeted by LMBRD1 lysosomal chaperone from the endoplasmic reticulum to the lysosomal membrane. Then forms a complex with lysosomal chaperone LMBRD1 and cytosolic MMACHC to transport cobalamin across the lysosomal membrane. {ECO:0000250|UniProtKB:O14678}.
|
Mus musculus (Mouse)
|
O89017
|
LGMN_MOUSE
|
MTWRVAVLLSLVLGAGAVPVGVDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDVTPENFLAVLRGDAEAVKGKGSGKVLKSGPRDHVFIYFTDHGATGILVFPNDDLHVKDLNKTIRYMYEHKMYQKMVFYIEACESGSMMNHLPDDINVYATTAANPKESSYACYYDEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKSISTMKVMQFQGMKHRASSPISLPPVTHLDLTPSPDVPLTILKRKLLRTNDVKESQNLIGQIQQFLDARHVIEKSVHKIVSLLAGFGETAERHLSERTMLTAHDCYQEAVTHFRTHCFNWHSVTYEHALRYLYVLANLCEAPYPIDRIEMAMDKVCLSHY
|
3.4.22.34
| null |
antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; associative learning [GO:0008306]; cellular response to amyloid-beta [GO:1904646]; cellular response to calcium ion [GO:0071277]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; dendritic spine organization [GO:0097061]; memory [GO:0007613]; negative regulation of ERBB signaling pathway [GO:1901185]; negative regulation of gene expression [GO:0010629]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell chemotaxis [GO:2001028]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of monocyte chemotaxis [GO:0090026]; protein maturation [GO:0051604]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; receptor catabolic process [GO:0032801]; renal system process [GO:0003014]; response to acidic pH [GO:0010447]; self proteolysis [GO:0097264]; vacuolar protein processing [GO:0006624]
|
apical part of cell [GO:0045177]; extracellular region [GO:0005576]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]
|
cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activator activity [GO:0061133]; peptidase activity [GO:0008233]
|
PF20985;PF01650;
|
1.10.132.130;3.40.50.1460;
|
Peptidase C13 family
|
PTM: Glycosylated. {ECO:0000305|PubMed:24407422}.; PTM: Activated by autocatalytic processing at pH 4. {ECO:0000250|UniProtKB:Q99538}.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:9742219}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.; EC=3.4.22.34; Evidence={ECO:0000269|PubMed:24407422, ECO:0000269|PubMed:9742219, ECO:0000269|PubMed:9891971};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:9742219};
| null |
FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds (PubMed:24407422, PubMed:9742219, PubMed:9891971). Can also cleave aspartyl bonds slowly, especially under acidic conditions (PubMed:24407422, PubMed:9742219, PubMed:9891971). Involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system (By similarity). Also involved in MHC class I antigen presentation in cross-presenting dendritic cells by mediating cleavage and maturation of Perforin-2 (MPEG1), thereby promoting antigen translocation in the cytosol (PubMed:37347855). Required for normal lysosomal protein degradation in renal proximal tubules (PubMed:17350006, PubMed:21292981). Required for normal degradation of internalized EGFR (PubMed:21292981). Plays a role in the regulation of cell proliferation via its role in EGFR degradation (PubMed:21292981). {ECO:0000250|UniProtKB:Q99538, ECO:0000269|PubMed:17350006, ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:24407422, ECO:0000269|PubMed:37347855, ECO:0000269|PubMed:9742219, ECO:0000269|PubMed:9891971}.
|
Mus musculus (Mouse)
|
O89019
|
INVS_MOUSE
|
MNISEDVLSTGSSLASQVHAAAVNGDKGALQRLIVGNSALRDKEDRFGRTPLMYCVLADRVDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDPSAVHTVRCILDAAPTESLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTIPSDSQGATPLHYAAQSNFAETVKVFLQHPSVKDDSDLEGRTSFMWAAGKGNDDVLRTMLSLKSDIDINMSDKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAFKIQAVYKGYKVRKAFRDRKNLLMKHEQLRKDAAAKKREEENKRKEAEQQKGQLDTDPPRSHCSSSAPVLPCPPSPQNEGSKQDATPSKQPPASHTVQSPDPEHSRLPGRCPGRASQGDSSIDLQGTASRKPSETPIEHCRGPSACVHPRSWEGGNSSKNQGTSSVEKRRGETNGKHRRCEEGPSSARQPLCTGSGRPAEKGEDSSPAVASASQQDHPRKPNKRQDRAARPRGASQKRRTHQLRDRCSPAGSSRPGSAKGEVACADQSSLHRHTPRSKVTQDKLIGGVSSGLPLSTEASRSGCKQLYEDICASPETGVAHGPPPGQCMNIHLLPVEQRLLIIQRERSRKELFRRKNKAAAVIQRAWRSYQLRKHLSRLLHLKQLGAREVLRCTQVCTALLLQVWRKELELKFPKSISVSRTSKSPSKGSSATKYARHSVLRQIYGCSQEGKGHHPIKSSKAPAVLHLSSVNSLQSIHLDNSGRSKKFSYNLQPSSQSKNKPKL
| null | null |
animal organ development [GO:0048513]; embryonic heart tube left/right pattern formation [GO:0060971]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; kidney development [GO:0001822]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; pancreas development [GO:0031016]; post-embryonic development [GO:0009791]; protein localization to ciliary inversin compartment [GO:1904108]; Wnt signaling pathway [GO:0016055]
|
ciliary base [GO:0097546]; ciliary inversin compartment [GO:0097543]; extracellular region [GO:0005576]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]
|
calmodulin binding [GO:0005516]
|
PF00023;PF12796;PF00612;
|
1.25.40.20;
| null |
PTM: May be ubiquitinated via its interaction with APC2.; PTM: Hydroxylated at Asn-75, most probably by HIF1AN. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle. Note=Associates with several components of the cytoskeleton including ciliary, random and polarized microtubules. During mitosis, it is recruited to mitotic spindle (By similarity). Membrane localization is dependent upon cell-cell contacts and is redistributed when cell adhesion is disrupted after incubation of the cell monolayer with low-calcium/EGTA medium. Also nuclear and perinuclear. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin-proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8. Does not seem to be strictly required for ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:9744276, ECO:0000269|PubMed:9771707}.
|
Mus musculus (Mouse)
|
O89020
|
AFAM_MOUSE
|
MRHLKLTGFIFFLLPLTESLALPTKPQDVDHFNATQKFIDENTTYLAIIAFSQYVQEASFDEVETLVKVMLDYRDRCWADNTLPECSKTANDAIQDMLCDMEGLPQKHNFSHCCGKAGFPRRLCFFYNKKANVGFLPPFPTLDPEEKCQAYKNNSESFLHLYMYEVARRNPFVFAPVLLAVAAWFEEAATTCCEQQQKATCFQAKAAPITQYLKASSSYQRNVCGALIKFGPKVLNSINVAVFSKKFPKIGFKDLTTLLEDVSSMYEGCCEGDVVHCIRSQSQVVNHICSKQDSISSKIKVCCEKKTLEREACIINANKDDRPEGLSLREAKFTESENVCQERDSDPDKFFAEFIYEYSRRHPDLSTPELLRITKVYMDFLEDCCSRENPAGCYRHVEDKFNETTQRSLAMVQQECKQFQELGKDTLQRHFLVKFTKAAPQLPMEELVSLSKEMVAALTTCCTLSDEFACVDNLADLVLGELCGVNTNRTINPAVDHCCKTDFAFRRHCFEHLKADTTYELPSVSALVSALHTDWCQPRKEDLQNKKHRFLVNLVKWMPGITDEEWLCLFTKFTAAREECSEVQEPESCFSPESSKTGDESQATEKQR
| null | null |
protein stabilization [GO:0050821]; protein transport within extracellular region [GO:0071693]; vitamin transport [GO:0051180]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
vitamin E binding [GO:0008431]
|
PF00273;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: N-glycosylated; more than 90% of the glycans are sialylated. {ECO:0000250|UniProtKB:P43652}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P43652}.
| null | null | null | null | null |
FUNCTION: Functions as a carrier for hydrophobic molecules in body fluids. Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B. Binds vitamin E. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the transport of vitamin E across the blood-brain barrier. {ECO:0000250|UniProtKB:P43652}.
|
Mus musculus (Mouse)
|
O89023
|
TPP1_MOUSE
|
MGLQARLLGLLALVIAGKCTYNPEPDQRWMLPPGWVSLGRVDPEEELSLTFALKQRNLERLSELVQAVSDPSSPQYGKYLTLEDVAELVQPSPLTLLTVQKWLSAAGARNCDSVTTQDFLTCWLSVRQAELLLPGAEFHRYVGGPTKTHVIRSPHPYQLPQALAPHVDFVGGLHRFPPSSPRQRPEPQQVGTVSLHLGVTPSVLRQRYNLTAKDVGSGTTNNSQACAQFLEQYFHNSDLTEFMRLFGGSFTHQASVAKVVGKQGRGRAGIEASLDVEYLMSAGANISTWVYSSPGRHEAQEPFLQWLLLLSNESSLPHVHTVSYGDDEDSLSSIYIQRVNTEFMKAAARGLTLLFASGDTGAGCWSVSGRHKFRPSFPASSPYVTTVGGTSFKNPFLITDEVVDYISGGGFSNVFPRPPYQEEAVAQFLKSSSHLPPSSYFNASGRAYPDVAALSDGYWVVSNMVPIPWVSGTSASTPVFGGILSLINEHRILNGRPPLGFLNPRLYQQHGTGLFDVTHGCHESCLNEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP
|
3.4.14.9
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O14773}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:O14773};
|
bone resorption [GO:0045453]; central nervous system development [GO:0007417]; epithelial cell differentiation [GO:0030855]; lysosomal protein catabolic process [GO:1905146]; lysosome organization [GO:0007040]; nervous system development [GO:0007399]; neuromuscular process controlling balance [GO:0050885]; peptide catabolic process [GO:0043171]; protein catabolic process [GO:0030163]; protein localization to chromosome, telomeric region [GO:0070198]; proteolysis [GO:0006508]
|
Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; recycling endosome [GO:0055037]
|
endopeptidase activity [GO:0004175]; lysophosphatidic acid binding [GO:0035727]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; sulfatide binding [GO:0120146]; tripeptidyl-peptidase activity [GO:0008240]
|
PF00082;PF09286;
|
3.40.50.200;
| null |
PTM: Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity (By similarity). {ECO:0000250|UniProtKB:O14773}.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}. Melanosome {ECO:0000250|UniProtKB:O14773}.
|
CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.; EC=3.4.14.9; Evidence={ECO:0000269|PubMed:28464005};
| null | null | null | null |
FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:28464005). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (By similarity). Requires substrates with an unsubstituted N-terminus (By similarity). {ECO:0000250|UniProtKB:O14773, ECO:0000269|PubMed:28464005}.
|
Mus musculus (Mouse)
|
O89026
|
ROBO1_MOUSE
|
MIAEPAHFYLFGLICLCSGSRLRQEDFPPRIVEHPSDLIVSKGEPATLNCKAEGRPTPTIEWYKGGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRKSRPDEGVYICVARNYLGEAVSHNASLEVAILRDDFRQNPSDVMVAVGEPAVMECQPPRGHPEPTISWKKDGSPLDDKDERITIRGGKLMITYTRKSDAGKYVCVGTNMVGERESEVAELTVLERPSFVKRPSNLAVTVDDSAEFKCEARGDPVPTVRWRKDDGELPKSRYEIRDDHTLKIRKVTAGDMGSYTCVAENMVGKAEASATLTVQEPPHFVVKPRDQVVALGRTVTFQCEATGNPQPAIFWRREGSQNLLFSYQPPQSSSRFSVSQTGDLTITNVQRSDVGYYICQTLNVAGSIITKAYLEVTDVIADRPPPVIRQGPVNQTVAVDGTLILSCVATGSPAPTILWRKDGVLVSTQDSRIKQLESGVLQIRYAKLGDTGRYTCTASTPSGEATWSAYIEVQEFGVPVQPPRPTDPNLIPSAPSKPEVTDVSKNTVTLSWQPNLNSGATPTSYIIEAFSHASGSSWQTAAENVKTETFAIKGLKPNAIYLFLVRAANAYGISDPSQISDPVKTQDVPPTSQGVDHKQVQRELGNVVLHLHNPTILSSSSVEVHWTVDQQSQYIQGYKILYRPSGASHGESEWLVFEVRTPTKNSVVIPDLRKGVNYEIKARPFFNEFQGADSEIKFAKTLEEAPSAPPRSVTVSKNDGNGTAILVTWQPPPEDTQNGMVQEYKVWCLGNETKYHINKTVDGSTFSVVIPSLVPGIRYSVEVAASTGAGPGVKSEPQFIQLDSHGNPVSPEDQVSLAQQISDVVRQPAFIAGIGAACWIILMVFSIWLYRHRKKRNGLTSTYAGIRKVPSFTFTPTVTYQRGGEAVSSGGRPGLLNISEPATQPWLADTWPNTGNNHNDCSINCCTAGNGNSDSNLTTYSRPADCIANYNNQLDNKQTNLMLPESTVYGDVDLSNKINEMKTFNSPNLKDGRFVNPSGQPTPYATTQLIQANLSNNMNNGAGDSSEKHWKPPGQQKPEVAPIQYNIMEQNKLNKDYRANDTIPPTIPYNQSYDQNTGGSYNSSDRGSSTSGSQGHKKGARTPKAPKQGGMNWADLLPPPPAHPPPHSNSEEYNMSVDESYDQEMPCPVPPAPMYLQQDELQEEEDERGPTPPVRGAASSPAAVSYSHQSTATLTPSPQEELQPMLQDCPEDLGHMPHPPDRRRQPVSPPPPPRPISPPHTYGYISGPLVSDMDTDAPEEEEDEADMEVAKMQTRRLLLRGLEQTPASSVGDLESSVTGSMINGWGSASEEDNISSGRSSVSSSDGSFFTDADFAQAVAAAAEYAGLKVARRQMQDAAGRRHFHASQCPRPTSPVSTDSNMSAVVIQKARPAKKQKHQPGHLRREAYADDLPPPPVPPPAIKSPTVQSKAQLEVRPVMVPKLASIEARTDRSSDRKGGSYKGREALDGRQVTDLRTNPSDPREAQEQPNDGKGRGTRQPKRDLPPAKTHLGQEDILPYCRPTFPTSNNPRDPSSSSSMSSRGSGSRQREQANVGRRNMAEMQVLGGFERGDENNEELEETES
| null | null |
aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; chemotaxis [GO:0006935]; coronary vasculature development [GO:0060976]; endocardial cushion formation [GO:0003272]; heart development [GO:0007507]; heart induction [GO:0003129]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; kidney development [GO:0001822]; mammary duct terminal end bud growth [GO:0060763]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of gene expression [GO:0010629]; negative regulation of synapse assembly [GO:0051964]; neuron projection extension [GO:1990138]; olfactory bulb interneuron development [GO:0021891]; outflow tract septum morphogenesis [GO:0003148]; positive regulation of gene expression [GO:0010628]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of Rho protein signal transduction [GO:0035025]; pulmonary valve morphogenesis [GO:0003184]; regulation of dendrite morphogenesis [GO:0048814]; Roundabout signaling pathway [GO:0035385]; synapse organization [GO:0050808]; ventricular septum development [GO:0003281]; ventricular septum morphogenesis [GO:0060412]
|
axolemma [GO:0030673]; axon [GO:0030424]; dendrite [GO:0030425]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
axon guidance receptor activity [GO:0008046]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
|
Immunoglobulin superfamily, ROBO family
|
PTM: Ubiquitinated. May be deubiquitinated by USP33. {ECO:0000269|PubMed:19684588}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24560577}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:24560577}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:O55005}; Single-pass membrane protein {ECO:0000250|UniProtKB:O55005}. Note=Detected at growth cones in thalamus neurons (PubMed:24560577). PRRG4 prevents cell surface location and both colocalize in the Endoplasmic reticulum/Golgi adjacent to the cell nucleus (By similarity). {ECO:0000250|UniProtKB:O55005, ECO:0000269|PubMed:24560577}.
| null | null | null | null | null |
FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10433822, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (PubMed:11734623). {ECO:0000250|UniProtKB:Q9Y6N7, ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:11734623, ECO:0000269|PubMed:15091338, ECO:0000269|PubMed:24560577}.
|
Mus musculus (Mouse)
|
O89032
|
SPD2A_MOUSE
|
MLAYCVQDATVVDVEKRRSPSKHYVYIINVTWSDSTSQTIYRRYSKFFDLQMQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDVNPPKEDYGSSKRKSVWLSSWAESPKKDVTGADTNAEPMILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNGTRDDSDINTSKTGEVSKRRKAHLRRLDRRWTLGGMVNRQHSREEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYLKKAKDDLPTRKKNLAGPVEIIGNIMEISNLLNKKASGDKEAPAEGEGSEAPITKKEISLPILCNASNGSALAIPERTTSKLAQGSPAVARIAPQRAQISSPNLRTRPPPRRESSLGFQLPKPPEPPSVEVEYYTIAEFQSCISDGISFRGGQKAEVIDKNSGGWWYVQIGEKEGWAPASYIDKRKKPNLSRRTSTLTRPKVPPPAPPSKPKEAEENPVGACESQGSPLKVKYEEPEYDVPAFGFDSEPEMNEEPSGDRGSGDKHPAQPRRISPASSLQRAHFKVGESSEDVALEEETIYENEGFRPYTEDTLSARGSSGDSDSPGSSSLSLAVKNSPKSDSPKSSSLLKLKAEKNAQAELGKNQSNISFSSSVTISTTCSSSSSSSSLSKNNGDLKPRSASDAGIRDTPKVGTKKDPDVKAGLASCARAKPSVRPKPVLNRAESQSQEKMDISSLRRQLRPTGQLRGGLKGSRSEDSELPPQMASEGSRRGSADIIPLTATTPPCVPKKEWEGQGATYVTCSAYQKVQDSEISFPEGAEVHVLEKAESGWWYVRFGELEGWAPSHYLVAEENQQPDTASKEGDTGKSSQNEGKSDSLEKIEKRVQALNTVNQSKRATPPIPSKPPGGFGKTSGTVAVKMRNGVRQVAVRPQSVFVSPPPKDNNLSCALRRNESLTATDSLRGVRRNSSFSTARSAAAEAKGRLAERAASQGSESPLLPTQRKGIPVSPVRPKPIEKSQFIHNNLKDVYISIADYEGDEETAGFQEGVSMEVLEKNPNGWWYCQILDEVKPFKGWVPSNYLEKKN
| null | null |
in utero embryonic development [GO:0001701]; osteoclast fusion [GO:0072675]; reactive oxygen species metabolic process [GO:0072593]; superoxide anion generation [GO:0042554]
|
anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; mating projection tip [GO:0043332]; podosome [GO:0002102]
|
phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; protease binding [GO:0002020]; protein-macromolecule adaptor activity [GO:0030674]; superoxide-generating NADPH oxidase activator activity [GO:0016176]
|
PF00787;PF00018;PF07653;
|
3.30.1520.10;2.30.30.40;
|
SH3PXD2 family
|
PTM: Tyrosine phosphorylated by SRC. Phosphorylation plays a regulatory role in the protein localization. The intramolecular interaction of the PX domain with the third SH3 domain maintains the protein in the cytoplasm and phosphorylation disrupts this interaction, resulting in the redistribution of the protein from cytoplasm to the perimembrane region. Phosphorylated on serine upon DNA damage, probably by ATM or ATR (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome {ECO:0000250}. Note=Cytoplasmic in normal cells and localizes to podosomes in Src-transformed cells. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide (By similarity). {ECO:0000250, ECO:0000269|PubMed:18417249, ECO:0000269|PubMed:19755709}.
|
Mus musculus (Mouse)
|
O89033
|
CDC6_MOUSE
|
MPQTRSQTQATIGFPKKKLSNTLKKPNSRDCEVKLRNVQPVPTTPCVDVKLLPLSPRKRLGDDNLCNTPRLSPCSPPKLGKKENGPPRSHTWKGCRLVFDDEPTFKASPPKEQDRVRQHQIRSSSAQRSPESKADPEQKCPPEKESVCIRLFKQEGTCYQQAKLVLNTAVPDRLPAREQEMGVIRNFLKEHICGKKAGSLYLSGAPGTGKTACLSRILQDFKKEVKGFKSILLNCMSLRSAQAVFPAIAQEIGREELCRPAGKDLMRKLEKHLTAEKGPMIVLVLDEMDQLDSKGQDVLYTLFEWPWLSNSRLVLIGIANTLDLTDRILPRLEARENCKPQLLNFPPYTRNQIAAILQDRLSQVSKDQVLDSAAIQFCARKVSAVSGDIRKALDVCRRAIEIVESDVRSQTVLKPLSECKSPSESPVPKRVGLAHISQVISEVDGNRVTLSQENTQDSLPLQQKILVCSLLLLTRRLKIKEVTLGKLYEAYSSICRKQQVTAVDQSECLSLSGLLESRGLVGLKKNKESRLTKVSLKIEEKEIEHVLNGKAFTGNILAAGLP
| null | null |
cell division [GO:0051301]; DNA replication initiation [GO:0006270]; mitotic DNA replication checkpoint signaling [GO:0033314]; positive regulation of fibroblast proliferation [GO:0048146]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle [GO:0005819]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]
|
PF13401;PF17872;PF09079;
|
1.10.8.60;3.40.50.300;1.10.10.10;
|
CDC6/cdc18 family
|
PTM: Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase complex. {ECO:0000250|UniProtKB:Q99741}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99741}. Cytoplasm {ECO:0000250|UniProtKB:Q99741}. Note=The protein is nuclear in G1 and cytoplasmic in S-phase cells. {ECO:0000250|UniProtKB:Q99741}.
| null | null | null | null | null |
FUNCTION: Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated.
|
Mus musculus (Mouse)
|
O89035
|
DIC_RAT
|
MAEARTSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALQVVRTDGFLALYNGLSASLCRQMTYSLTRFAIYETMRDYMTKDSQGPLPFYSKVLLGGISGLTGGFVGTPADLVNVRMQNDMKLPLSQRRNYSHALDGLYRVAREEGLKKLFSGATMASSRGALVTVGQLSCYDQAKQLVLSTGYLSDNIFTHFLSSFIAGGCATFLCQPLDVLKTRLMNSKGEYQGVFHCAVETAKLGPQAFFKGLVPAGVRLVPHTVLTFMFLEQLRKHFGIKVAT
| null | null |
glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; lipid transport [GO:0006869]; malate transmembrane transport [GO:0071423]; malate transport [GO:0015743]; oxaloacetate transport [GO:0015729]; phosphate ion transmembrane transport [GO:0035435]; phosphate ion transport [GO:0006817]; succinate transmembrane transport [GO:0071422]; succinate transport [GO:0015744]; sulfate transport [GO:0008272]; thiosulfate transport [GO:0015709]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
antiporter activity [GO:0015297]; dicarboxylic acid transmembrane transporter activity [GO:0005310]; malate transmembrane transporter activity [GO:0015140]; oxaloacetate transmembrane transporter activity [GO:0015131]; phosphate ion transmembrane transporter activity [GO:0015114]; secondary active transmembrane transporter activity [GO:0015291]; succinate transmembrane transporter activity [GO:0015141]; sulfate transmembrane transporter activity [GO:0015116]; thiosulfate transmembrane transporter activity [GO:0015117]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:3355813}; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + phosphate(out) = (S)-malate(out) + phosphate(in); Xref=Rhea:RHEA:71607, ChEBI:CHEBI:15589, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:29211846, ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + malonate(out) = (S)-malate(out) + malonate(in); Xref=Rhea:RHEA:71611, ChEBI:CHEBI:15589, ChEBI:CHEBI:15792; Evidence={ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in); Xref=Rhea:RHEA:29327, ChEBI:CHEBI:15589, ChEBI:CHEBI:30031; Evidence={ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + sulfate(out) = (S)-malate(out) + sulfate(in); Xref=Rhea:RHEA:71615, ChEBI:CHEBI:15589, ChEBI:CHEBI:16189; Evidence={ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=malonate(out) + phosphate(in) = malonate(in) + phosphate(out); Xref=Rhea:RHEA:71623, ChEBI:CHEBI:15792, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=phosphate(in) + succinate(out) = phosphate(out) + succinate(in); Xref=Rhea:RHEA:71627, ChEBI:CHEBI:30031, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=phosphate(in) + sulfate(out) = phosphate(out) + sulfate(in); Xref=Rhea:RHEA:71631, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=malonate(out) + succinate(in) = malonate(in) + succinate(out); Xref=Rhea:RHEA:71667, ChEBI:CHEBI:15792, ChEBI:CHEBI:30031; Evidence={ECO:0000250|UniProtKB:Q9QZD8};
| null | null | null | null |
FUNCTION: Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane (PubMed:29211846, PubMed:3355813, PubMed:9733776). Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, particularly in liver, by supplying the substrates for the different metabolic processes (PubMed:9733776). Regulates fatty acid release from adipocytes, and contributes to systemic insulin sensitivity (By similarity). {ECO:0000250|UniProtKB:Q9QZD8, ECO:0000269|PubMed:29211846, ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}.
|
Rattus norvegicus (Rat)
|
O89038
|
MEF2D_RAT
|
MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSSVPAPNFAMPVTVPVSNQSSMQFSNPSSSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGRDLNSANGACPNPVGNGYVSARASPGLLPVANGNGLNKVIPAKSPPPPTHNTQLGAPSRKPDLRVITSQGGKGLMHHLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFSSMPTAYNTDYQLPSAELSSLPAFSSPAGLALGNVTAWQQPQQPQQPQPPQPPQSQPQPPQPQPQQPPQQQPHLVPVSLSNLIPGSPLPHVGAALTVTTHPHISIKSEPVSPSRERSPAPPPPAVFPAARPEPGEGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK
| null | null |
adult heart development [GO:0007512]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; chondrocyte differentiation [GO:0002062]; endochondral ossification [GO:0001958]; nervous system development [GO:0007399]; osteoblast differentiation [GO:0001649]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; regulation of DNA-templated transcription [GO:0006355]; skeletal muscle cell differentiation [GO:0035914]
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cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF12347;PF00319;
|
3.40.1810.10;
| null |
PTM: Phosphorylated on Ser-430 by CDK5 is required for Lys-425 sumoylation and inhibits transcriptional activity. In neurons, enhanced CDK5 activity induced by neurotoxins promotes caspase 3-mediated cleavage leading to neuron apoptosis. Phosphorylation on Ser-180 can be enhanced by EGF. Phosphorylated and activated by CaMK4 (By similarity). {ECO:0000250}.; PTM: Acetylated on Lys-425 by CREBBP. Acetylated by EP300. Deacetylated by SIRT1 and HDAC3 (By similarity). {ECO:0000250|UniProtKB:Q14814}.; PTM: Sumoylated on Lys-425 with SUMO2 but not SUMO1; which inhibits transcriptional activity and myogenic activity. Desumoylated by SENP3 (By similarity). {ECO:0000250}.
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SUBCELLULAR LOCATION: Nucleus. Note=Translocated by HDAC4 to nuclear dots. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
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