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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P05327
|
PHR_SYNP6
|
MAAPILFWHRRDLRLSDNIGLAAARAQSAQLIGLFCLDPQILQSADMAPARVAYLQGCLQELQQRYQQAGSRLLLLQGDPQHLIPQLAQQLQAEAVYWNQDIEPYGRDRDGQVAAALKTAGIRAVQLWDQLLHSPDQILSGSGNPYSVYGPFWKNWQAQPKPTPVATPTELVDLSPEQLTAIAPLLLSELPTLKQLGFDWDGGFPVEPGETAAIARLQEFCDRAIADYDPQRNFPAEAGTSGLSPALKFGAIGIRQAWRAASAAHALSRSDEARNSIRVWQQELAWREFYQHALYHFPSLADGPYRSLWQQFPWENREALFTAWTQAQTGYPIVDAAMRQLTETGWMHNRCWMIVASFLTKDLIIDWRRGEQFFMQHLVDGDLAANNGGWQWSASSGMDPKPLRIFNPASQAKKFDATATYIKRWLPELRHVHPKDLISGEITPIGRRGYPAPIVNHNLRQKQFKALYNQLKAAIAEPEAEPDS
|
4.1.99.3
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.; COFACTOR: Name=coenzyme F420-(gamma-Glu)n; Xref=ChEBI:CHEBI:133980; Note=Binds 1 coenzyme F420 non-covalently per subunit.;
|
circadian regulation of gene expression [GO:0032922]; DNA repair [GO:0006281]; entrainment of circadian clock by photoperiod [GO:0043153]
|
cytoplasm [GO:0005737]
|
deoxyribodipyrimidine photo-lyase activity [GO:0003904]; DNA binding [GO:0003677]; FAD binding [GO:0071949]
|
PF00875;PF03441;
|
1.25.40.80;1.10.579.10;3.40.50.620;
|
DNA photolyase class-1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.3;
| null | null | null | null |
FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
|
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
|
P05328
|
TRPG_ASPNG
|
MADSGLVDHSPHHPTKAAQLSTASNVILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPETDAGISSAAIQYFSGKIPIFGVCMGQQCIITCFGGKVDVTGEILHGKTSPLKHDGKGAYEGLPGSLAVTRYHSLAGTHATIPDCLEVSSSVQLADDSNKDVIMGVRHKKLAVEGVQFHPESILTEYGRIMFRNFLKLTAGTWEGNGKHFGEQSSTTKATVPSNPPPKTDKKLSILERIYDHRRAAVAVQKTIPSQRPADLQAAYDLNLAPPQIPFPARLRQSPYPLSLMAEIKRASPSKGMIAENACAPAQARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSLEGMTNRPAILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYKKEGVKAILVGEALMRAADTATFIAELLGGSSQTVSSESRRSPLVKICGTRSEEAARAAIEAGADLIGIIMVQGRTGCVPDDVALPISQVVRSTPKPASQALHTSQEPPAATSVEYFDHSAKILRHPSRALLVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLEWAKLIPVPVIRKFGLDEPAIARRAYHSLPLLDSGVGGTGELLDQSRVQNVLDKDCGLRVILAGGLDPTNVAGIVQKLGESGRKVVGVDVSSGVESDGAQDLNKIRAFVQAVRGL
|
4.1.1.48; 4.1.3.27; 5.3.1.24
| null |
glutamine metabolic process [GO:0006541]; tetrahydrofolate biosynthetic process [GO:0046654]; tryptophan biosynthetic process [GO:0000162]
|
cytosol [GO:0005829]
|
4-amino-4-deoxychorismate synthase activity [GO:0046820]; anthranilate synthase activity [GO:0004049]; indole-3-glycerol-phosphate synthase activity [GO:0004425]; phosphoribosylanthranilate isomerase activity [GO:0004640]
|
PF00117;PF00218;PF00697;
|
3.40.50.880;3.20.20.70;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; CATALYTIC ACTIVITY: Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48; CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27;
| null |
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
| null | null |
FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
|
Aspergillus niger
|
P05341
|
NIFS_AZOVI
|
MADVYLDNNATTRVDDEIVQAMLPFFTEQFGNPSSLHSFGNQVGMALKKARQSVQKLLGAEHDSEILFTSCGTESDSTAILSALKAQPERKTVITTVVEHPAVLSLCDYLASEGYTVHKLPVDKKGRLDLEHYASLLTDDVAVVSVMWANNETGTLFPIEEMARLADDAGIMFHTDAVQAVGKVPIDLKNSSIHMLSLCGHKLHAPKGVGVLYLRRGTRFRPLLRGGHQERGRRAGTENAASIIGLGVAAERALQFMEHENTEVNALRDKLEAGILAVVPHAFVTGDPDNRLPNTANIAFEYIEGEAILLLLNKVGIAASSGSACTSGSLEPSHVMRAMDIPYTAAHGTVRFSLSRYTTEEEIDRVIREVPPIVAQLRNVSPYWSGNGPVEDPGKAFAPVYG
|
2.8.1.7
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:8464885};
|
amino acid metabolic process [GO:0006520]; nitrogen fixation [GO:0009399]
| null |
cysteine desulfurase activity [GO:0031071]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170]
|
PF00266;
|
1.10.260.50;3.90.1150.10;3.40.640.10;
|
Class-V pyridoxal-phosphate-dependent aminotransferase family, NifS/IscS subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000269|PubMed:8464885};
| null | null | null | null |
FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Seems to participate in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for the Fe-S core formation. {ECO:0000269|PubMed:8464885}.
|
Azotobacter vinelandii
|
P05362
|
ICAM1_HUMAN
|
MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP
| null | null |
adhesion of symbiont to host [GO:0044406]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cellular response to amyloid-beta [GO:1904646]; cellular response to glucose stimulus [GO:0071333]; cellular response to leukemia inhibitory factor [GO:1990830]; establishment of endothelial barrier [GO:0061028]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; membrane to membrane docking [GO:0022614]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; positive regulation of cellular extravasation [GO:0002693]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; receptor-mediated virion attachment to host cell [GO:0046813]; regulation of leukocyte mediated cytotoxicity [GO:0001910]; regulation of ruffle assembly [GO:1900027]; T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell [GO:0002291]; T cell antigen processing and presentation [GO:0002457]; T cell extravasation [GO:0072683]
|
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; immunological synapse [GO:0001772]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
integrin binding [GO:0005178]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]; virus receptor activity [GO:0001618]
|
PF21146;PF03921;PF13895;
|
2.60.40.10;
|
Immunoglobulin superfamily, ICAM family
|
PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:17875742}.; FUNCTION: (Microbial infection) Acts as a receptor for major receptor group rhinovirus A-B capsid proteins. {ECO:0000269|PubMed:1968231, ECO:0000269|PubMed:2538243}.; FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus A21 capsid proteins. {ECO:0000269|PubMed:11160747, ECO:0000269|PubMed:16004874, ECO:0000269|PubMed:9539703}.; FUNCTION: (Microbial infection) Upon Kaposi's sarcoma-associated herpesvirus/HHV-8 infection, is degraded by viral E3 ubiquitin ligase MIR2, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes and NK cell. {ECO:0000269|PubMed:11413168}.
|
Homo sapiens (Human)
|
P05364
|
AMPC_ENTCL
|
MMRKSLCCALLLGISCSALATPVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAANKPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQWQGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYANASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWGYRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQGIALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVAEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVEAAYHILEALQ
|
3.5.2.6
| null |
antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677]
|
outer membrane-bounded periplasmic space [GO:0030288]
|
beta-lactamase activity [GO:0008800]
|
PF00144;
|
3.40.710.10;
|
Class-C beta-lactamase family
| null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10102};
| null | null | null | null |
FUNCTION: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
|
Enterobacter cloacae
|
P05369
|
FPPS_RAT
|
MNGDQKLDVHNQEKQNFIQHFSQIVKVLTEDELGHPEKGDAITRIKEVLEYNTVGGKYNRGLTVVQTFQELVEPRKQDAESLQRALTVGWCVELLQAFFLVLDDIMDSSYTRRGQICWYQKPGIGLDAINDALLLEAAIYRLLKFYCREQPYYLNLLELFLQSSYQTEIGQTLDLITAPQGQVDLGRYTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANALKILLEMGEFFQIQDDYLDLFGDPSVTGKVGTDIQDNKCSWLVVQCLLRATPQQRQILEENYGQKDPEKVARVKALYEELDLRSVFFKYEEDSYNRLKSLIEQCSAPLPPSIFLELANKIYKRRK
|
2.5.1.1; 2.5.1.10
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
|
cellular response to fatty acid [GO:0071398]; cholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; male gonad development [GO:0008584]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of cholesterol biosynthetic process [GO:0045542]; response to cholesterol [GO:0070723]; response to peptide hormone [GO:0043434]; response to testosterone [GO:0033574]; response to xenobiotic stimulus [GO:0009410]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; peroxisome [GO:0005777]
|
dimethylallyltranstransferase activity [GO:0004161]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]
|
PF00348;
|
1.10.600.10;
|
FPP/GGPP synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10;
| null |
PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.
| null | null |
FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P05370
|
G6PD_RAT
|
MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKVTPEERPKLEEFFARNSYVAGQYDDPASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQEICMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTDSDDVRDEKVKVLKCISEVETDNVVLGQYVGNPSGEGEATNGYLDDPTVPHGSTTATFAAAVLYVENERWDGVPFILRCGKALNERKAEVRLQFRDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHKIDREKPQPIPYVYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
|
1.1.1.49
| null |
angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure [GO:0001998]; angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0002033]; cellular response to oxidative stress [GO:0034599]; cholesterol biosynthetic process [GO:0006695]; erythrocyte development [GO:0048821]; erythrocyte maturation [GO:0043249]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glutathione metabolic process [GO:0006749]; NADP biosynthetic process [GO:0006741]; NADP metabolic process [GO:0006739]; NADPH regeneration [GO:0006740]; negative regulation of cell growth involved in cardiac muscle cell development [GO:0061052]; negative regulation of protein glutathionylation [GO:0010734]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; pentose biosynthetic process [GO:0019322]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, oxidative branch [GO:0009051]; positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904879]; regulation of multicellular organism growth [GO:0040014]; regulation of neuron apoptotic process [GO:0043523]; response to ethanol [GO:0045471]; response to food [GO:0032094]; response to iron(III) ion [GO:0010041]; response to organic cyclic compound [GO:0014070]; response to oxidative stress [GO:0006979]; ribose phosphate biosynthetic process [GO:0046390]
|
centriolar satellite [GO:0034451]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]
|
carbohydrate binding [GO:0030246]; glucose binding [GO:0005536]; glucose-6-phosphate dehydrogenase activity [GO:0004345]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]
|
PF02781;PF00479;
|
3.40.50.720;
|
Glucose-6-phosphate dehydrogenase family
|
PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity (By similarity). {ECO:0000250|UniProtKB:P11413}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11413}. Membrane {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11413}.
|
CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842; Evidence={ECO:0000250|UniProtKB:P11413};
| null |
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000250|UniProtKB:P11413}.
| null | null |
FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes. {ECO:0000250|UniProtKB:P11413}.
|
Rattus norvegicus (Rat)
|
P05371
|
CLUS_RAT
|
MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME
| null | null |
cell morphogenesis [GO:0000902]; cellular response to growth factor stimulus [GO:0071363]; central nervous system myelin maintenance [GO:0032286]; chaperone-mediated protein complex assembly [GO:0051131]; chaperone-mediated protein folding [GO:0061077]; endocrine pancreas development [GO:0031018]; estrous cycle [GO:0044849]; immune complex clearance [GO:0002434]; intrinsic apoptotic signaling pathway [GO:0097193]; microglial cell activation [GO:0001774]; microglial cell proliferation [GO:0061518]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of apoptotic process [GO:0043066]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of response to endoplasmic reticulum stress [GO:1903573]; neuron projection morphogenesis [GO:0048812]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of neurofibrillary tangle assembly [GO:1902998]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; protein import [GO:0017038]; protein stabilization [GO:0050821]; protein targeting to lysosome involved in chaperone-mediated autophagy [GO:0061740]; regulation of amyloid-beta clearance [GO:1900221]; regulation of apoptotic process [GO:0042981]; regulation of cell population proliferation [GO:0042127]; regulation of neuronal signal transduction [GO:1902847]; response to light stimulus [GO:0009416]; response to misfolded protein [GO:0051788]; response to potassium ion [GO:0035864]; response to virus [GO:0009615]; spermatogenesis [GO:0007283]
|
aggresome [GO:0016235]; apical dendrite [GO:0097440]; cell surface [GO:0009986]; chromaffin granule [GO:0042583]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; growth cone [GO:0030426]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; neurofibrillary tangle [GO:0097418]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum lumen [GO:0099020]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]; spherical high-density lipoprotein particle [GO:0034366]; synapse [GO:0045202]
|
amyloid-beta binding [GO:0001540]; low-density lipoprotein particle receptor binding [GO:0050750]; misfolded protein binding [GO:0051787]; protein carrier chaperone [GO:0140597]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; tau protein binding [GO:0048156]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]
|
PF01093;
| null |
Clusterin family
|
PTM: Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen (PubMed:3415696, PubMed:3651384). Proteolytic cleavage is not necessary for its chaperone activity. All non-secreted forms are not proteolytically cleaved. Chaperone activity of uncleaved forms is dependent on a non-reducing environment (By similarity). {ECO:0000250|UniProtKB:P10909, ECO:0000269|PubMed:3415696, ECO:0000269|PubMed:3651384}.; PTM: Polyubiquitinated, leading to proteasomal degradation. Under cellular stress, the intracellular level of cleaved form is reduced due to proteasomal degradation. {ECO:0000250|UniProtKB:P10909}.; PTM: Extensively glycosylated with sulfated N-linked carbohydrates (PubMed:3651384). About 30% of the protein mass is comprised of complex N-linked carbohydrate. Endoplasmic reticulum (ER) stress induces changes in glycosylation status and increases level of hypoglycosylated forms. Core carbohydrates are essential for chaperone activity. Non-secreted forms are hypoglycosylated or unglycosylated (By similarity). {ECO:0000250|UniProtKB:P10909, ECO:0000269|PubMed:3651384}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3415696, ECO:0000269|PubMed:3651384}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000269|PubMed:16038898}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16038898}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
| null | null | null | null | null |
FUNCTION: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (PubMed:16038898). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890, ECO:0000269|PubMed:16038898}.
|
Rattus norvegicus (Rat)
|
P05373
|
HEM2_YEAST
|
MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDNPDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDPVGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDGTINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAHKTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALERDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAAEKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDEEN
|
4.2.1.24
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10386874}; Note=Binds 1 zinc ion per monomer. {ECO:0000269|PubMed:10386874};
|
heme biosynthetic process [GO:0006783]; protoporphyrinogen IX biosynthetic process [GO:0006782]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
porphobilinogen synthase activity [GO:0004655]; zinc ion binding [GO:0008270]
|
PF00490;
|
3.20.20.70;
|
ALAD family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
| null |
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
| null | null |
FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05374
|
CHO2_YEAST
|
MSSCKTTLSEMVGSVTKDRGTINVEARTRSSNVTFKPPVTHDMVRSLFDPTLKKSLLEKCIALAIISNFFICYWVFQRFGLQFTKYFFLVQYLFWRIAYNLGIGLVLHYQSHYETLTNCAKTHAIFSKIPQNKDANSNFSTNSNSFSEKFWNFIRKFCQYEIRSKMPKEYDLFAYPEEINVWLIFRQFVDLILMQDFVTYIIYVYLSIPYSWVQIFNWRSLLGVILILFNIWVKLDAHRVVKDYAWYWGDFFFLEESELIFDGVFNISPHPMYSIGYLGYYGLSLICNDYKVLLVSVFGHYSQFLFLKYVENPHIERTYGDGTDSDSQMNSRIDDLISKENYDYSRPLINMGLSFNNFNKLRFTDYFTIGTVAALMLGTIMNARFINLNYLFITVFVTKLVSWLFISTILYKQSQSKWFTRLFLENGYTQVYSYEQWQFIYNYYLVLTYTLMIIHTGLQIWSNFSNINNSQLIFGLILVALQTWCDKETRLAISDFGWFYGDFFLSNYISTRKLTSQGIYRYLNHPEAVLGVVGVWGTVLMTNFAVTNIILAVLWTLTNFILVKFIETPHVNKIYGKTKRVSGVGKTLLGLKPLRQVSDIVNRIENIIIKSLVDESKNSNGGAELLPKNYQDNKEWNILIQEAMDSVATRLSPYCELKIENEQVETNFVLPTPVTLNWKMPIELYNGDDWIGLYKVIDTRADREKTRVGSGGHWSATSKDSYMNHGLRHKESVTEIKATEKYVQGKVTFDTSLLYFENGIYEFRYHSGNSHKVLLISTPFEISLPVLNTTTPELFEKDLTEFLTKVNVLKDGKFRPLGNKFFGMDSLKQLIKNSIGVELSSEYMRRVNGDAHVISHRAWDIKQTLDSLA
|
2.1.1.17
| null |
methylation [GO:0032259]; phosphatidylcholine biosynthetic process [GO:0006656]
|
cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
phosphatidylethanolamine N-methyltransferase activity [GO:0004608]
|
PF04191;
|
1.20.120.1630;2.60.40.2840;
|
Class VI-like SAM-binding methyltransferase superfamily, CHO2 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03217}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:2684666}; KM=110 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:2198947}; KM=57 uM for phosphatidylethanolamine (PE) {ECO:0000269|PubMed:2198947};
|
PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000305|PubMed:2445736, ECO:0000305|PubMed:3066687}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.9. {ECO:0000269|PubMed:2684666};
| null |
FUNCTION: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). Preferentially converts di-C16:1 substrates. {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:15258140, ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666, ECO:0000269|PubMed:3066687, ECO:0000269|PubMed:6759124, ECO:0000269|PubMed:6988218}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05375
|
PLMT_YEAST
|
MKESVQEIIQQLIHSVDLQSSKFQLAIVCTMFNPIFWNIVARMEYHKHSLTKMCGGARKGCYMLAATIFSLGIVRDMVYESALREQPTCSLITGENWTKLGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYFMYKIALRWEEPFTAMIYANRDKAKKNM
|
2.1.1.17; 2.1.1.71
| null |
methylation [GO:0032259]; phosphatidylcholine biosynthetic process [GO:0006656]
|
cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]
|
phosphatidyl-N-dimethylethanolamine N-methyltransferase activity [GO:0080101]; phosphatidyl-N-methylethanolamine N-methyltransferase activity [GO:0000773]; phosphatidylethanolamine N-methyltransferase activity [GO:0004608]
|
PF04191;
|
1.20.120.1630;
|
Class VI-like SAM-binding methyltransferase superfamily, PEMT/PEM2 methyltransferase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17; Evidence={ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; EC=2.1.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=180 uM for S-adenosyl-L-methionine (in presence of phosphatidylethanolamine (PE) as substrate) {ECO:0000269|PubMed:2684666}; KM=190 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-methylethanolamine (PMME) as substrate) {ECO:0000269|PubMed:2684666}; KM=240 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-dimethylethanolamine (PDME) as substrate) {ECO:0000269|PubMed:2684666}; KM=270 uM for phosphatidyl-N-methylethanolamine (PMME) {ECO:0000269|PubMed:2684666}; KM=110 uM for phosphatidyl-N-dimethylethanolamine (PDME) {ECO:0000269|PubMed:2684666}; KM=54 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-methylethanolamine (PMME) as substrate) {ECO:0000269|PubMed:2198947}; KM=59 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-dimethylethanolamine (PDME) as substrate) {ECO:0000269|PubMed:2198947}; KM=380 uM for phosphatidyl-N-methylethanolamine (PMME) {ECO:0000269|PubMed:2198947}; KM=180 uM for phosphatidyl-N-dimethylethanolamine (PDME) {ECO:0000269|PubMed:2198947};
|
PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000305|PubMed:6337128}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1. {ECO:0000269|PubMed:2684666};
| null |
FUNCTION: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC). Can also catalyze the first methylation reaction of PE to PMME in the absence of PE methyltransferase CHO2. {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2670666, ECO:0000269|PubMed:2684666, ECO:0000269|PubMed:6337128, ECO:0000269|PubMed:6759124, ECO:0000269|PubMed:7047296}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05383
|
KAPCB_PIG
|
MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCGKEFCEF
|
2.7.11.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
negative regulation of TORC1 signaling [GO:1904262]; protein kinase A signaling [GO:0010737]; protein phosphorylation [GO:0006468]
|
cAMP-dependent protein kinase complex [GO:0005952]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily
|
PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form. {ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:9521123}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22694}. Cell membrane {ECO:0000250|UniProtKB:P22694}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250|UniProtKB:P05131}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. {ECO:0000250|UniProtKB:P05131}.
|
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=2.7.11.11; 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=2.7.11.11;
| null | null | null | null |
FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA. Acts as a negative regulator of mTORC1 by mediating phosphorylation of RPTOR. {ECO:0000250|UniProtKB:P22694}.
|
Sus scrofa (Pig)
|
P05386
|
RLA1_HUMAN
|
MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD
| null | null |
cytoplasmic translation [GO:0002181]; translation [GO:0006412]; translational elongation [GO:0006414]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; focal adhesion [GO:0005925]
|
protein kinase activator activity [GO:0030295]; ribonucleoprotein complex binding [GO:0043021]; structural constituent of ribosome [GO:0003735]
|
PF00428;
|
1.10.10.1410;
|
Eukaryotic ribosomal protein P1/P2 family
|
PTM: Ubiquitinated at Lys-92 and Lys-93 by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling). {ECO:0000269|PubMed:36638793}.
| null | null | null | null | null | null |
FUNCTION: Plays an important role in the elongation step of protein synthesis.
|
Homo sapiens (Human)
|
P05387
|
RLA2_HUMAN
|
MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD
| null | null |
cytoplasmic translation [GO:0002181]; cytoplasmic translational elongation [GO:0002182]; translation [GO:0006412]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]
|
structural constituent of ribosome [GO:0003735]
|
PF00428;
|
1.10.10.1410;
|
Eukaryotic ribosomal protein P1/P2 family
| null | null | null | null | null | null | null |
FUNCTION: Plays an important role in the elongation step of protein synthesis.
|
Homo sapiens (Human)
|
P05388
|
RLA0_HUMAN
|
MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD
| null | null |
cytoplasmic translation [GO:0002181]; ribosome biogenesis [GO:0042254]; translation [GO:0006412]
|
cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; ribonucleoprotein complex [GO:1990904]
|
large ribosomal subunit rRNA binding [GO:0070180]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF00428;PF00466;PF17777;
|
3.30.70.1730;3.90.105.20;
|
Universal ribosomal protein uL10 family
|
PTM: Ubiquitinated at Lys-264 by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling). {ECO:0000269|PubMed:36638793}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19188445}. Cytoplasm {ECO:0000269|PubMed:19188445}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661, PubMed:19188445). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19188445}.
| null | null | null | null | null |
FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
|
Homo sapiens (Human)
|
P05408
|
7B2_HUMAN
|
MVSRMVSTMLSGLLFWLASGWTPAFAYSPRTPDRVSEADIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPVGKTADDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGERRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE
| null | null |
intracellular protein transport [GO:0006886]; neuropeptide signaling pathway [GO:0007218]; peptide hormone processing [GO:0016486]; regulation of hormone secretion [GO:0046883]
|
extracellular region [GO:0005576]; nucleus [GO:0005634]; secretory granule [GO:0030141]
|
enzyme inhibitor activity [GO:0004857]; enzyme regulator activity [GO:0030234]; GTP binding [GO:0005525]; unfolded protein binding [GO:0051082]
|
PF05281;
| null |
7B2 family
|
PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides. {ECO:0000250|UniProtKB:P12961}.; PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P12961}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01165}. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000250|UniProtKB:P01165}.
| null | null | null | null | null |
FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro. {ECO:0000269|PubMed:7913882}.
|
Homo sapiens (Human)
|
P05412
|
JUN_HUMAN
|
MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; integrated stress response signaling [GO:0140467]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of DNA binding [GO:0043392]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of DNA-templated transcription initiation [GO:2000144]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; release from viral latency [GO:0019046]; response to endoplasmic reticulum stress [GO:0034976]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
chromatin [GO:0000785]; euchromatin [GO:0000791]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]
|
cAMP response element binding [GO:0035497]; 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 repressor activity, RNA polymerase II-specific [GO:0001227]; enzyme binding [GO:0019899]; general transcription initiation factor binding [GO:0140296]; GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; R-SMAD binding [GO:0070412]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-like protein ligase binding [GO:0044389]
|
PF00170;PF03957;
|
1.20.5.170;
|
BZIP family, Jun subfamily
|
PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation (PubMed:14739463, PubMed:27458189). Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7 (PubMed:14739463). {ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:27458189}.; PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-243; this primes the protein for subsequent phosphorylation by GSK3B at Thr-239. Phosphorylated at Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity. Phosphorylated by VRK1 (PubMed:31527692). {ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:17804415, ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:18650425, ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:31527692, ECO:0000269|PubMed:8464713, ECO:0000269|PubMed:8855261}.; PTM: Acetylated at Lys-271 by EP300. {ECO:0000269|PubMed:11689449}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in colorectal cancer (CRC) cells (PubMed:24623306). {ECO:0000250|UniProtKB:P05627, ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:12618758, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:22083952, ECO:0000269|PubMed:24623306}.; FUNCTION: (Microbial infection) Upon Epstein-Barr virus (EBV) infection, binds to viral BZLF1 Z promoter and activates viral BZLF1 expression. {ECO:0000269|PubMed:31341047}.
|
Homo sapiens (Human)
|
P05413
|
FABPH_HUMAN
|
MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA
| null | null |
brown fat cell differentiation [GO:0050873]; cholesterol homeostasis [GO:0042632]; intracellular lipid transport [GO:0032365]; long-chain fatty acid transport [GO:0015909]; negative regulation of cell population proliferation [GO:0008285]; phospholipid homeostasis [GO:0055091]; positive regulation of long-chain fatty acid import into cell [GO:0140214]; positive regulation of phospholipid biosynthetic process [GO:0071073]; regulation of fatty acid oxidation [GO:0046320]; regulation of phosphatidylcholine biosynthetic process [GO:2001245]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
cytoskeletal protein binding [GO:0008092]; long-chain fatty acid binding [GO:0036041]; oleic acid binding [GO:0070538]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
|
Homo sapiens (Human)
|
P05414
|
GOX_SPIOL
|
MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWDGPSSRAVARL
|
1.1.3.15
|
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:2644287, ECO:0000269|PubMed:2681790, ECO:0000269|PubMed:7705356, ECO:0000269|PubMed:9144771}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:2681790};
|
fatty acid alpha-oxidation [GO:0001561]; lactate oxidation [GO:0019516]; oxidative photosynthetic carbon pathway [GO:0009854]; response to other organism [GO:0051707]
|
peroxisome [GO:0005777]; plasma membrane [GO:0005886]
|
(S)-2-hydroxy-acid oxidase activity [GO:0003973]; FMN binding [GO:0010181]; L-lactate dehydrogenase activity [GO:0004459]
|
PF01070;
|
3.20.20.70;
|
FMN-dependent alpha-hydroxy acid dehydrogenase family
| null |
SUBCELLULAR LOCATION: Peroxisome.
|
CATALYTIC ACTIVITY: Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655; EC=1.1.3.15; Evidence={ECO:0000269|PubMed:1324737, ECO:0000269|PubMed:7705356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312; Evidence={ECO:0000305|PubMed:7705356}; CATALYTIC ACTIVITY: Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2; Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15; Evidence={ECO:0000269|PubMed:7705356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790; Evidence={ECO:0000305|PubMed:7705356};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for glycolate (at 25 degrees Celsius) {ECO:0000269|PubMed:1324737}; KM=1 mM for glycolate {ECO:0000269|PubMed:7705356}; KM=11.5 mM for L-lactate {ECO:0000269|PubMed:7705356}; KM=0.21 mM for O2 {ECO:0000269|PubMed:7705356}; KM=3 mM for L-2-hydroxbyutanoate {ECO:0000269|PubMed:7705356}; KM=58 mM for L-mandelate {ECO:0000269|PubMed:7705356}; Note=kcat is 20 sec(-1) with glycolate as substrate. kcat is 11 sec(-1) with L-lactate as substrate. kcat is 13.2 sec(-1) with L-2-hydroxbyutanoate as substrate. kcat is 0.09 sec(-1) with L-mandelate as substrate. {ECO:0000269|PubMed:7705356};
|
PATHWAY: Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3. {ECO:0000305|PubMed:2644287}.
| null | null |
FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 (PubMed:1324737, PubMed:7705356). Is a key enzyme in photorespiration in green plants (Probable). To a lesser extent, is also able to use L-lactate and 2-hydroxbyutanoate as substrate in vitro, but shows almost no activity with L-mandelate (PubMed:7705356). {ECO:0000269|PubMed:1324737, ECO:0000269|PubMed:7705356, ECO:0000305|PubMed:2644287}.
|
Spinacia oleracea (Spinach)
|
P05423
|
RPC4_HUMAN
|
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTPNIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKKGNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQLPLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAARKTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVLIKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQELVSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
| null | null |
defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-beta production [GO:0032728]; tRNA transcription by RNA polymerase III [GO:0042797]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; RNA polymerase III complex [GO:0005666]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]
|
PF05132;
| null |
Eukaryotic RPC4/POLR3D RNA polymerase subunit family
|
PTM: Sumoylation on Lys-141 can serve as a signal to mark misfolded Pol III for proteasomal degradation. {ECO:0000269|PubMed:33558764}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104}.
| null | null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:12391170, PubMed:20413673, PubMed:33558764, PubMed:34675218, PubMed:35637192). Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci. Assembles with POLR3E/RPC5 forming a subcomplex that binds the Pol III core. Enables recruitment of Pol III at transcription initiation site and drives transcription initiation from both type 2 and type 3 DNA promoters. Required for efficient transcription termination and reinitiation (By similarity) (PubMed:12391170, PubMed:20413673, PubMed:35637192). Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through the RIG-I pathway (PubMed:19609254, PubMed:19631370). {ECO:0000250|UniProtKB:P25441, ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218, ECO:0000269|PubMed:35637192}.
|
Homo sapiens (Human)
|
P05425
|
COPB_ENTHA
|
MNNGIDPENETNKKGAIGKNPEEKITVEQTNTKNNLQEHGKMENMDQHHTHGHMERHQQMDHGHMSGMDHSHMDHEDMSGMNHSHMGHENMSGMDHSMHMGNFKQKFWLSLILAIPIILFSPMMGMSFPFQVTFPGSNWVVLVLATILFIYGGQPFLSGAKMELKQKSPAMMTLIAMGITVAYVYSVYSFIANLINPHTHVMDFFWELATLIVIMLLGHWIEMNAVSNASDALQKLAELLPESVKRLKKDGTEETVSLKEVHEGDRLIVRAGDKMPTDGTIDKGHTIVDESAVTGESKGVKKQVGDSVIGGSINGDGTIEITVTGTGENGYLAKVMEMVRKAQGEKSKLEFLSDKVAKWLFYVALVVGIIAFIAWLFLANLPDALERMVTVFIIACPHALGLAIPLVVARSTSIAAKNGLLLKNRNAMEQANDLDVIMLDKTGTLTQGKFTVTGIEILDEAYQEEEILKYIGALEAHANHPLAIGIMNYLKEKKITPYQAQEQKNLAGVGLEATVEDKDVKIINEKEAKRLGLKIDPERLKNYEAQGNTVSFLVVSDKLVAVIALGDVIKPEAKEFIQAIKEKNIIPVMLTGDNPKAAQAVAEYLGINEYYGGLLPDDKEAIVQRYLDQGKKVIMVGDGINDAPSLARATIGMAIGAGTDIAIDSADVVLTNSDPKDILHFLELAKETRRKMIQNLWWGAGYNIIAIPLAAGILAPIGLILSPAVGAVLMSLSTVVVALNALTLK
|
7.2.2.8
| null |
copper ion homeostasis [GO:0055070]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; P-type divalent copper transporter activity [GO:0043682]; P-type monovalent copper transporter activity [GO:0140581]
|
PF00122;PF00702;
|
3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552, ChEBI:CHEBI:456216; EC=7.2.2.8; Evidence={ECO:0000269|PubMed:7721839};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:7721839};
| null |
FUNCTION: Involved in copper export. Can also export silver. {ECO:0000269|PubMed:7721839, ECO:0000269|PubMed:8037745, ECO:0000269|PubMed:8048974}.
|
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R)
|
P05426
|
RL7_RAT
|
MEAVPEKKKKVAAALGTLKKKKVPAVPETLKKKRRNFAELKVKRLRKKFALKTLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASVNMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNSLVARSLGKFGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN
| null | null |
liver regeneration [GO:0097421]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]
|
A band [GO:0031672]; cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; postsynaptic density [GO:0014069]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840]; synapse [GO:0045202]
|
5S rRNA binding [GO:0008097]; DNA binding [GO:0003677]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF00327;PF08079;
|
3.30.1390.20;
|
Universal ribosomal protein uL30 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P18124}.
| null | null | null | null | null |
FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs. {ECO:0000250|UniProtKB:P18124}.
|
Rattus norvegicus (Rat)
|
P05431
|
FMM1_NEIMB
|
MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLNHGEWPGNNTSAGVATSSEIKGKYVKSVEVKNGVVTAQMASSNVNNEIKGKKLSLWAKRQNGSVKWFCGQPVTRDKAKAANDDVTAAAAANGKKIDTKHLPSTCRDASDAS
| null | null |
cell adhesion [GO:0007155]
|
membrane [GO:0016020]; pilus [GO:0009289]
| null |
PF07963;PF00114;
|
3.30.700.10;
|
N-Me-Phe pilin family
|
PTM: O-linked glycan has been reported to consist either of the Gal(alpha1-3) GlcNAc disaccharide, or the Gal(beta 1-4) Gal(alpha 1-3) 2,4-diacetamido-2,4,6-trideoxyhexose trisaccharide. {ECO:0000269|PubMed:7934852, ECO:0000269|PubMed:9515697}.
|
SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Major component of the type IV pilus (T4P) that plays a role in cellular adherence, microcolony formation as well as twitching motility. {ECO:0000269|PubMed:17121595, ECO:0000269|PubMed:27698424, ECO:0000269|PubMed:7934852}.
|
Neisseria meningitidis serogroup B (strain MC58)
|
P05432
|
ERRFI_RAT
|
MSTAGVAAQDIRVPLKTGFLHNGQALGNMKTCWGSRNEFEKNFLNIDPITMAYNLNSPAPEHLTTLGCASPSAPGSGHFFAERGPSPKSSLPPLVIPPSESSGQREEDQVLCGFKKLSVNGVCASTPPLTPIQSCSSPFPCAAPCDRSSRPLPPLPISEDPSLDEADCEVEFLTSADTDFLLEDCVPSDFKYDVPGRRSFRGCGQINYAYFDSPTVSVADLSCASDQNRVVPDPNPPPPQSHRRLRRSHSGPAGSFNKPAIRISSCTHRASPSSDEDKPEIPPRVPIPPRPAKPDYRRWSAEVTSNTYSDEDRPPKVPPREPLSRSNSRTPSPKSLPSYLNGVMPPTQSFAPDPKYVSSKALQRQSSEGSAKAPCILPIIENGKKVSSTHYYLLPERPPYLDKYEKYFREAEEANPSTQIQPLPAACGMVSATDKLASRMKMDVGGHGKRKHLSYVVSP
| null | null |
apoptotic process [GO:0006915]; bile acid biosynthetic process [GO:0006699]; cartilage development [GO:0051216]; cell migration [GO:0016477]; cellular hyperosmotic response [GO:0071474]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to insulin stimulus [GO:0032869]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chondrocyte proliferation [GO:0035988]; embryo implantation [GO:0007566]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation [GO:0050673]; epithelium development [GO:0060429]; fat pad development [GO:0060613]; gene expression [GO:0010467]; glucose metabolic process [GO:0006006]; limb joint morphogenesis [GO:0036022]; lipid metabolic process [GO:0006629]; liver development [GO:0001889]; lung alveolus development [GO:0048286]; lung epithelium development [GO:0060428]; lung vasculature development [GO:0060426]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of collagen biosynthetic process [GO:0032966]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of epidermal growth factor-activated receptor activity [GO:0007175]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of tumor necrosis factor production [GO:0032720]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; progesterone receptor signaling pathway [GO:0050847]; protein localization to plasma membrane [GO:0072659]; regulation of keratinocyte differentiation [GO:0045616]; regulation of type B pancreatic cell proliferation [GO:0061469]; response to 1-oleoyl-sn-glycerol 3-phosphate [GO:1904565]; response to estradiol [GO:0032355]; response to insulin [GO:0032868]; response to progesterone [GO:0032570]; response to steroid hormone [GO:0048545]; response to xenobiotic stimulus [GO:0009410]; skeletal system development [GO:0001501]; skin development [GO:0043588]; skin morphogenesis [GO:0043589]; tissue homeostasis [GO:0001894]; uterine epithelium development [GO:0035847]; uterus development [GO:0060065]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
kinase binding [GO:0019900]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; small GTPase binding [GO:0031267]
|
PF09027;PF11555;
| null |
MIG6 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity). {ECO:0000250, ECO:0000269|PubMed:11003669, ECO:0000269|PubMed:17599051}.
|
Rattus norvegicus (Rat)
|
P05451
|
REG1A_HUMAN
|
MAQTSSYFMLISCLMFLSQSQGQEAQTELPQARISCPEGTNAYRSYCYYFNEDRETWVDADLYCQNMNSGNLVSVLTQAEGAFVASLIKESGTDDFNVWIGLHDPKKNRRWHWSSGSLVSYKSWGIGAPSSVNPGYCVSLTSSTGFQKWKDVPCEDKFSFVCKFKN
| null | null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; disruption of cell wall in another organism [GO:0044278]; positive regulation of cell population proliferation [GO:0008284]; response to peptide hormone [GO:0043434]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; molecular function inhibitor activity [GO:0140678]; oligosaccharide binding [GO:0070492]; peptidoglycan binding [GO:0042834]; signaling receptor activity [GO:0038023]
|
PF00059;
|
3.10.100.10;
| null |
PTM: The composition of the O-linked carbohydrate on Thr-27 is complex and varied. In the crystallographic structure, the attached sugar appears to be N-acetylglucosamine, typical of an intracellular protein, rather than N-acetylgalactosamine. {ECO:0000269|PubMed:2493268}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.
|
Homo sapiens (Human)
|
P05452
|
TETN_HUMAN
|
MELWGAYLLLCLFSLLTQVTTEPPTQKPKKIVNAKKDVVNTKMFEELKSRLDTLAQEVALLKEQQALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLGTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV
| null | null |
bone mineralization [GO:0030282]; cellular response to organic substance [GO:0071310]; cellular response to transforming growth factor beta stimulus [GO:0071560]; ossification [GO:0001503]; positive regulation of plasminogen activation [GO:0010756]
|
collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; granular component [GO:0001652]; platelet dense granule lumen [GO:0031089]
|
calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; heparin binding [GO:0008201]; kringle domain binding [GO:0036143]
|
PF00059;
|
3.10.100.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis. Plays a role in retinal function (PubMed:35331648). {ECO:0000269|PubMed:35331648}.
|
Homo sapiens (Human)
|
P05453
|
ERF3_YEAST
|
MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDVVFMPVSGYSGANLKDHVDPKECPWYTGPTLLEYLDTMNHVDRHINAPFMLPIAAKMKDLGTIVEGKIESGHIKKGQSTLLMPNKTAVEIQNIYNETENEVDMAMCGEQVKLRIKGVEEEDISPGFVLTSPKNPIKSVTKFVAQIAIVELKSIIAAGFSCVMHVHTAIEEVHIVKLLHKLEKGTNRKSKKPPAFAKKGMKVIAVLETEAPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIAE
|
3.6.5.-
| null |
nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; translation [GO:0006412]; translational termination [GO:0006415]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; translation release factor complex [GO:0018444]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; translation release factor activity [GO:0003747]
|
PF00009;PF03144;PF03143;
|
3.40.50.300;2.40.30.10;
|
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, ERF3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:34413231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:34413231};
| null | null | null | null |
FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:34413231, PubMed:7556078). SUP35/eRF3 mediates SUP45/eRF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:34413231, PubMed:7556078). GTP hydrolysis by SUP35/eRF3 induces a conformational change that leads to its dissociation, permitting SUP45/eRF1 to accommodate fully in the A-site (PubMed:34413231, PubMed:7556078). Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs (PubMed:12923185, PubMed:15337765). Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening (PubMed:12923185, PubMed:15337765). {ECO:0000269|PubMed:12923185, ECO:0000269|PubMed:15337765, ECO:0000269|PubMed:34413231, ECO:0000269|PubMed:7556078}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05455
|
LA_HUMAN
|
MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ
| null | null |
histone mRNA metabolic process [GO:0008334]; IRES-dependent viral translational initiation [GO:0075522]; nuclear histone mRNA catabolic process [GO:0071045]; positive regulation of translation [GO:0045727]; protein localization to cytoplasmic stress granule [GO:1903608]; tRNA 3'-end processing [GO:0042780]; tRNA 5'-leader removal [GO:0001682]; tRNA export from nucleus [GO:0006409]; tRNA modification [GO:0006400]; tRNA processing [GO:0008033]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
mRNA binding [GO:0003729]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]; sequence-specific mRNA binding [GO:1990825]; tRNA binding [GO:0000049]
|
PF05383;PF00076;PF08777;
|
3.30.70.330;1.10.10.10;
| null |
PTM: Phosphorylated. The phosphorylation sites are at the C-terminal part of the protein. {ECO:0000269|PubMed:9054510}.; PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation (PubMed:2470590, PubMed:3192525). In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:12384597). {ECO:0000269|PubMed:12384597, ECO:0000269|PubMed:2470590, ECO:0000269|PubMed:3192525}.
|
Homo sapiens (Human)
|
P05458
|
PTRA_ECOLI
|
MPRSTWFKALLLLVALWAPLSQAETGWQPIQETIRKSDKDNRQYQAIRLDNGMVVLLVSDPQAVKSLSALVVPVGSLEDPEAYQGLAHYLEHMSLMGSKKYPQADSLAEYLKMHGGSHNASTAPYRTAFYLEVENDALPGAVDRLADAIAEPLLDKKYAERERNAVNAELTMARTRDGMRMAQVSAETINPAHPGSKFSGGNLETLSDKPGNPVQQALKDFHEKYYSANLMKAVIYSNKPLPELAKMAADTFGRVPNKESKKPEITVPVVTDAQKGIIIHYVPALPRKVLRVEFRIDNNSAKFRSKTDELITYLIGNRSPGTLSDWLQKQGLVEGISANSDPIVNGNSGVLAISASLTDKGLANRDQVVAAIFSYLNLLREKGIDKQYFDELANVLDIDFRYPSITRDMDYVEWLADTMIRVPVEHTLDAVNIADRYDAKAVKERLAMMTPQNARIWYISPKEPHNKTAYFVDAPYQVDKISAQTFADWQKKAADIALSLPELNPYIPDDFSLIKSEKKYDHPELIVDESNLRVVYAPSRYFASEPKADVSLILRNPKAMDSARNQVMFALNDYLAGLALDQLSNQASVGGISFSTNANNGLMVNANGYTQRLPQLFQALLEGYFSYTATEDQLEQAKSWYNQMMDSAEKGKAFEQAIMPAQMLSQVPYFSRDERRKILPSITLKEVLAYRDALKSGARPEFMVIGNMTEAQATTLARDVQKQLGADGSEWCRNKDVVVDKKQSVIFEKAGNSTDSALAAVFVPTGYDEYTSSAYSSLLGQIVQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDKQPSFLWERYKAFFPTAEAKLRAMKPDEFAQIQQAVITQMLQAPQTLGEEASKLSKDFDRGNMRFDSRDKIVAQIKLLTPQKLADFFHQAVVEPQGMAILSQISGSQNGKAEYVHPEGWKVWENVSALQQTMPLMSEKNE
|
3.4.24.55
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
amyloid-beta metabolic process [GO:0050435]; hormone catabolic process [GO:0042447]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; outer membrane-bounded periplasmic space [GO:0030288]; peroxisomal matrix [GO:0005782]
|
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00675;PF05193;PF16187;
|
3.30.830.10;
|
Peptidase M16 family
| null |
SUBCELLULAR LOCATION: Periplasm.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon.; EC=3.4.24.55; Evidence={ECO:0000255|PROSITE-ProRule:PRU10096};
| null | null | null | null |
FUNCTION: Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin.
|
Escherichia coli (strain K12)
|
P05480
|
SRC_MOUSE
|
MGSNKSKPKDASQRRRSLEPSENVHGAGGAFPASQTPSKPASADGHRGPSAAFVPPAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKGETGKYLRLPQLVDMSAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
|
2.7.10.2
| null |
adherens junction organization [GO:0034332]; angiotensin-activated signaling pathway [GO:0038166]; bone resorption [GO:0045453]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cellular response to fatty acid [GO:0071398]; cellular response to fluid shear stress [GO:0071498]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to progesterone stimulus [GO:0071393]; cellular response to prolactin [GO:1990646]; cellular response to reactive oxygen species [GO:0034614]; cellular response to transforming growth factor beta stimulus [GO:0071560]; DNA biosynthetic process [GO:0071897]; epidermal growth factor receptor signaling pathway [GO:0007173]; focal adhesion assembly [GO:0048041]; forebrain development [GO:0030900]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; interleukin-6-mediated signaling pathway [GO:0070102]; intestinal epithelial cell development [GO:0060576]; intracellular signal transduction [GO:0035556]; learning or memory [GO:0007611]; myoblast proliferation [GO:0051450]; negative regulation of anoikis [GO:2000811]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of gene expression [GO:0010629]; negative regulation of hippo signaling [GO:0035331]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of mitochondrial depolarization [GO:0051902]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of telomere maintenance via telomerase [GO:0032211]; neurotrophin TRK receptor signaling pathway [GO:0048011]; odontogenesis [GO:0042476]; oogenesis [GO:0048477]; osteoclast development [GO:0036035]; phosphorylation [GO:0016310]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic process [GO:0043065]; positive regulation of bone resorption [GO:0045780]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytokine production [GO:0001819]; positive regulation of dephosphorylation [GO:0035306]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of lamellipodium morphogenesis [GO:2000394]; positive regulation of male germ cell proliferation [GO:2000256]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of ovarian follicle development [GO:2000386]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of platelet-derived growth factor receptor-beta signaling pathway [GO:2000588]; positive regulation of podosome assembly [GO:0071803]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein processing [GO:0010954]; positive regulation of protein transport [GO:0051222]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; primary ovarian follicle growth [GO:0001545]; progesterone receptor signaling pathway [GO:0050847]; protein destabilization [GO:0031648]; regulation of caveolin-mediated endocytosis [GO:2001286]; regulation of cell projection assembly [GO:0060491]; regulation of cell-cell adhesion [GO:0022407]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of toll-like receptor 3 signaling pathway [GO:0034139]; response to acidic pH [GO:0010447]; response to electrical stimulus [GO:0051602]; response to interleukin-1 [GO:0070555]; response to mechanical stimulus [GO:0009612]; response to mineralocorticoid [GO:0051385]; response to nutrient levels [GO:0031667]; response to xenobiotic stimulus [GO:0009410]; skeletal muscle cell proliferation [GO:0014856]; spermatogenesis [GO:0007283]; stress fiber assembly [GO:0043149]; substrate adhesion-dependent cell spreading [GO:0034446]; transcytosis [GO:0045056]; transforming growth factor beta receptor signaling pathway [GO:0007179]; uterus development [GO:0060065]
|
actin filament [GO:0005884]; caveola [GO:0005901]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendritic filopodium [GO:1902737]; dendritic growth cone [GO:0044294]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; podosome [GO:0002102]; postsynaptic specialization, intracellular component [GO:0099091]; ruffle membrane [GO:0032587]; synaptic membrane [GO:0097060]
|
ATP binding [GO:0005524]; BMP receptor binding [GO:0070700]; cell adhesion molecule binding [GO:0050839]; connexin binding [GO:0071253]; enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; heme binding [GO:0020037]; insulin receptor binding [GO:0005158]; integrin binding [GO:0005178]; kinase activity [GO:0016301]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; nuclear estrogen receptor binding [GO:0030331]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; phosphoprotein binding [GO:0051219]; protein domain specific binding [GO:0019904]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; SH2 domain binding [GO:0042169]; signaling receptor binding [GO:0005102]; transmembrane transporter binding [GO:0044325]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: Myristoylated at Gly-2, and this is essential for targeting to membranes. {ECO:0000250}.; PTM: Dephosphorylated at Tyr-529 by PTPRJ (By similarity). Phosphorylated on Tyr-529 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-418. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-529, the SH3 domain engaged with the SH2-kinase linker, and Tyr-418 dephosphorylated. Dephosphorylation of Tyr-529 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-529, Tyr-418 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-529 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-74 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity (By similarity). Upon activation of IL6ST by IL6, Tyr-418 is phosphorylated and Tyr-529 dephosphorylated (PubMed:25731159). {ECO:0000250, ECO:0000269|PubMed:25731159}.; PTM: [Isoform 1]: Displays reduced levels of autophosphorylation at Tyr-418 compared to isoform 2. {ECO:0000250|UniProtKB:Q9WUD9}.; PTM: [Isoform 2]: Displays enhanced levels of autophosphorylation at Tyr-418 compared to isoform 1. {ECO:0000250|UniProtKB:Q9WUD9}.; PTM: S-nitrosylation is important for activation of its kinase activity. {ECO:0000250}.; PTM: Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-418 and may lead to lysosomal degradation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:21525037}; Lipid-anchor {ECO:0000269|PubMed:22801373}. Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}. Nucleus {ECO:0000269|PubMed:12615910}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12615910}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Cell junction, focal adhesion {ECO:0000269|PubMed:22801373}. Note=Localizes to focal adhesion sites following integrin engagement (PubMed:22801373). Localization to focal adhesion sites requires myristoylation and the SH3 domain. Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions. {ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:22801373}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:8910389}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000250|UniProtKB:Q9WUD9}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000250|UniProtKB:Q9WUD9};
| null | null | null | null |
FUNCTION: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (PubMed:9344858). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation (By similarity). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (By similarity). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'. Enhances RIGI-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (By similarity). Required for podosome formation (PubMed:21525037). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). Phosphorylates OTUB1, promoting deubiquitination of RPTOR (By similarity). {ECO:0000250|UniProtKB:P12931, ECO:0000250|UniProtKB:Q9WUD9, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:21525037, ECO:0000269|PubMed:25731159, ECO:0000269|PubMed:8641341, ECO:0000269|PubMed:9344858, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.; FUNCTION: [Isoform 1]: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. {ECO:0000250|UniProtKB:Q9WUD9}.; FUNCTION: [Isoform 2]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-418 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (By similarity). {ECO:0000250|UniProtKB:Q9WUD9}.
|
Mus musculus (Mouse)
|
P05484
|
O17A_CONMA
|
MKLTCVVIVAVLLLTACQLITADDSRGTQKHRALRSTTKLSTSTRCKGKGAKCSRLMYDCCTGSCRSGKCG
| null | null | null |
extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231]
|
calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729]
|
PF02950;
| null |
Conotoxin O1 superfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2441741, ECO:0000269|PubMed:4071055}.
| null | null | null | null | null |
FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks Cav2.2/CACNA1B calcium channels (IC(50)=0.67-208 nM) (PubMed:26344359, PubMed:34589389, PubMed:7826361). It acts by neutralizing the outer electronegativity and sterically hindering the ion access path to the entrance of the channel selectivity filter (PubMed:34234349). It also shows antiproliferative effects on different glioma cell lines (M059J, U-138MG and U-251MG) (PubMed:28202361). In vivo, is lethal to fish (PubMed:26344359, PubMed:34589389). In vivo, injection into mammals induces adverse effects, such as tremor, diminution of spontaneous locomotor activity and bad coordinated locomotion (PubMed:26344359). In addition, it causes reduction of tumor area in the mouse glioma model, that is induced by the orthotopic injection of GL261 cells into the brain (PubMed:28202361). {ECO:0000269|PubMed:26344359, ECO:0000269|PubMed:34234349, ECO:0000269|PubMed:7826361}.
|
Conus magus (Magical cone)
|
P05496
|
AT5G1_HUMAN
|
MQTAGALFISPALIRCCTRGLIRPVSASFLNSPVNSSKQPSYSNFPLQVARREFQTSVVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
| null | null |
proton motive force-driven ATP synthesis [GO:0015986]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrion [GO:0005739]
|
lipid binding [GO:0008289]; proton transmembrane transporter activity [GO:0015078]
|
PF00137;
|
1.20.20.10;
|
ATPase C chain family
|
PTM: Trimethylated by ATPSCKMT at Lys-104. Methylation is required for proper incorporation of the C subunit into the ATP synthase complex and mitochondrial respiration. {ECO:0000269|PubMed:30530489}.
|
SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
|
Homo sapiens (Human)
|
P05503
|
COX1_RAT
|
MLVNRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFSGYTLNDTWAKAHFAIMFVGVNMTFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVLVMIFMIWEAFASKREVLSISYSSTNLEWLHGCPPPYHTFEEPSYVKVK
|
7.1.1.9
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P00396}; Note=Binds 2 heme A groups non-covalently per subunit. {ECO:0000250|UniProtKB:P00396}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00396}; Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00396};
|
cerebellum development [GO:0021549]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; response to copper ion [GO:0046688]; response to electrical stimulus [GO:0051602]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277]
|
cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00115;
|
1.20.210.10;
|
Heme-copper respiratory oxidase family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00396}.
|
CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniProtKB:P00401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; Evidence={ECO:0000250|UniProtKB:P00401};
| null |
PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P00401}.
| null | null |
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}.
|
Rattus norvegicus (Rat)
|
P05523
|
FPG_ECOLI
|
MPELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK
|
3.2.2.23; 4.2.99.18
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1689309}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1689309};
|
base-excision repair [GO:0006284]; DNA damage response [GO:0006974]
|
cytoplasm [GO:0005737]
|
8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; oxidized purine nucleobase lesion DNA N-glycosylase activity [GO:0008534]; oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity [GO:0000703]; zinc ion binding [GO:0008270]
|
PF01149;PF06831;PF06827;
|
1.10.8.50;3.20.190.10;
|
FPG family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.; EC=3.2.2.23; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18;
| null | null | null | null |
FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:C, however it also acts on thymine glycol:G, 5,6-dihydrouracil:G and 5-hydroxyuracil:G. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Cleaves ssDNA containing an AP site. {ECO:0000269|PubMed:1689309, ECO:0000269|PubMed:20031487}.
|
Escherichia coli (strain K12)
|
P05524
|
FGF3_MOUSE
|
MGLIWLLLLSLLEPSWPTTGPGTRLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELGYNTYASRLYRTGSSGPGAQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLGHKDHEMVRLLQSSQPRAPGEGSQPRQRRQKKQSPGDHGKMETLSTRATPSTQLHTGGLAVA
| null | null |
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; organ induction [GO:0001759]; otic vesicle formation [GO:0030916]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; post-anal tail morphogenesis [GO:0036342]; regulation of cell migration [GO:0030334]; semicircular canal morphogenesis [GO:0048752]; thymus development [GO:0048538]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]
|
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
|
PTM: Glycosylated.
|
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum. Golgi apparatus.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal ear development (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
P05532
|
KIT_MOUSE
|
MRGARGAWDLLCVLLVLLRGQTATSQPSASPGEPSPPSIHPAQSELIVEAGDTLSLTCIDPDFVRWTFKTYFNEMVENKKNEWIQEKAEATRTGTYTCSNSNGLTSSIYVFVRDPAKLFLVGLPLFGKEDSDALVRCPLTDPQVSNYSLIECDGKSLPTDLTFVPNPKAGITIKNVKRAYHRLCVRCAAQRDGTWLHSDKFTLKVRAAIKAIPVVSVPETSHLLKKGDTFTVVCTIKDVSTSVNSMWLKMNPQPQHIAQVKHNSWHRGDFNYERQETLTISSARVDDSGVFMCYANNTFGSANVTTTLKVVEKGFINISPVKNTTVFVTDGENVDLVVEYEAYPKPEHQQWIYMNRTSANKGKDYVKSDNKSNIRYVNQLRLTRLKGTEGGTYTFLVSNSDASASVTFNVYVNTKPEILTYDRLINGMLQCVAEGFPEPTIDWYFCTGAEQRCTTPVSPVDVQVQNVSVSPFGKLVVQSSIDSSVFRHNGTVECKASNDVGKSSAFFNFAFKGNNKEQIQAHTLFTPLLIGFVVAAGAMGIIVMVLTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFIFSKQEEQAEAALYKNLLHSTEPSCDSSNEYMDMKPGVSYVVPTKTDKRRSARIDSYIERDVTPAIMEDDELALDLDDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFSCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMVSPEHAPAEMYDVMKTCWDADPLKRPTFKQVVQLIEKQISDSTKHIYSNLANCNPNPENPVVVDHSVRVNSVGSSASSTQPLLVHEDA
|
2.7.10.1
| null |
actin cytoskeleton organization [GO:0030036]; B cell differentiation [GO:0030183]; cell chemotaxis [GO:0060326]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; chemotaxis [GO:0006935]; cytokine-mediated signaling pathway [GO:0019221]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; developmental pigmentation [GO:0048066]; digestive tract development [GO:0048565]; ectopic germ cell programmed cell death [GO:0035234]; embryonic hemopoiesis [GO:0035162]; epithelial cell proliferation [GO:0050673]; erythrocyte differentiation [GO:0030218]; erythropoietin-mediated signaling pathway [GO:0038162]; Fc receptor signaling pathway [GO:0038093]; germ cell development [GO:0007281]; germ cell migration [GO:0008354]; glycosphingolipid metabolic process [GO:0006687]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell migration [GO:0035701]; hemopoiesis [GO:0030097]; immature B cell differentiation [GO:0002327]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; Kit signaling pathway [GO:0038109]; lamellipodium assembly [GO:0030032]; lymphoid progenitor cell differentiation [GO:0002320]; male gonad development [GO:0008584]; mast cell chemotaxis [GO:0002551]; mast cell degranulation [GO:0043303]; mast cell differentiation [GO:0060374]; mast cell proliferation [GO:0070662]; megakaryocyte development [GO:0035855]; melanocyte adhesion [GO:0097326]; melanocyte differentiation [GO:0030318]; melanocyte migration [GO:0097324]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of developmental process [GO:0051093]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reproductive process [GO:2000242]; ovarian follicle development [GO:0001541]; phosphorylation [GO:0016310]; pigmentation [GO:0043473]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of colon smooth muscle contraction [GO:1904343]; positive regulation of dendritic cell cytokine production [GO:0002732]; positive regulation of gene expression [GO:0010628]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mast cell cytokine production [GO:0032765]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of pseudopodium assembly [GO:0031274]; positive regulation of pyloric antrum smooth muscle contraction [GO:0120072]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of small intestine smooth muscle contraction [GO:1904349]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell differentiation [GO:1905065]; programmed cell death [GO:0012501]; regulation of bile acid metabolic process [GO:1904251]; regulation of cell shape [GO:0008360]; response to cadmium ion [GO:0046686]; response to radiation [GO:0009314]; somatic stem cell population maintenance [GO:0035019]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283]; stem cell differentiation [GO:0048863]; T cell differentiation [GO:0030217]; tongue development [GO:0043586]; visual learning [GO:0008542]
|
acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrillar center [GO:0001650]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713]; SH2 domain binding [GO:0042169]; stem cell factor receptor activity [GO:0005020]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
|
PF00047;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
|
PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation (By similarity). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding promotes autophosphorylation of isoform 1 and isoform 2. Isoform 1 shows low levels of tyrosine phosphorylation in the absence of added KITLG/SCF, while isoform 2 requires stimulation by KITLG/SCF for phosphorylation (in vitro). Phosphorylation of Tyr-573 is required for interaction with PTPN6/SHP-1. Phosphorylation of Tyr-571 is required for interaction with PTPN11/SHP-2. Phosphorylated tyrosine residues are important for interaction with specific binding partners. {ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:7527401}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Note=Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:7527401};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. {ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:18725415, ECO:0000269|PubMed:21037083, ECO:0000269|PubMed:7509796, ECO:0000269|PubMed:9528781, ECO:0000269|PubMed:9722617}.
|
Mus musculus (Mouse)
|
P05533
|
LY6A_MOUSE
|
MDTSHTTKSCLLILLVALLCAERAQGLECYQCYGVPFETSCPSITCPYPDGVCVTQEAAVIVDSQTRKVKNNLCLPICPPNIESMEILGTKVNVKTSCCQEDLCNVAVPNGGSTWTMAGVLLFSLSSVLLQTLL
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; response to bacterium [GO:0009617]
|
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
acetylcholine receptor binding [GO:0033130]; acetylcholine receptor inhibitor activity [GO:0030550]
|
PF00021;
|
2.10.60.10;
| null |
PTM: O-glycosylated. Not N-glycosylated. {ECO:0000269|PubMed:3033645}.; PTM: Not phosphorylated.
|
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: T-cell activation.
|
Mus musculus (Mouse)
|
P05538
|
DQB2_HUMAN
|
MSWKMALQIPGGFWAAAVTVMLVMLSTPVAEARDFPKDFLVQFKGMCYFTNGTERVRGVARYIYNREEYGRFDSDVGEFQAVTELGRSIEDWNNYKDFLEQERAAVDKVCRHNYEAELRTTLQRQVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTSLIRNGDWTFQILVMLEITPQRGDIYTCQVEHPSLQSPITVEWRAQSESAQSKMLSGIGGFVLGLIFLGLGLIIRHRGQKGPRGPPPAGLLH
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]; transport vesicle membrane [GO:0030658]
|
MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]
|
PF07654;PF00969;
|
2.60.40.10;
|
MHC class II family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Endosome membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Lysosome membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation.
| null | null | null | null | null |
FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. {ECO:0000269|PubMed:22407913}.
|
Homo sapiens (Human)
|
P05539
|
CO2A1_RAT
|
MIRLGAPQSLVLLTLLIATVLQCQGQDARKLGPKGQKGEPGDIKDIIGPKGPPGPQGPAGEQGPRGDRGDKGERGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGGNFAAQMAGGFDEKAGGAQMGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPIGPRGPPGPAGKPGDDGEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFLGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRGLPGKDGETGAAGPPGPSGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKQGDQGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDTGAPGRAGDPGLQGPAGAPGEKGEPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIAGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGTSGPAGPSGPRGPPGPVGPSGKDGSNGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGQREKGPDPLQYMRADEADSTLRQHDVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGESCVYPNPATVPRKNWWSSKSKEKKHIWFGETMNGGFHFSYGDGNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTIIEYRSQKTSRLPIVDIAPMDIGGPDQEFGVDIGPVCFL
| null | null |
anterior head development [GO:0097065]; bone development [GO:0060348]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to BMP stimulus [GO:0071773]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to mechanical stimulus [GO:0071260]; cellular response to nicotine [GO:0071316]; cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to retinoic acid [GO:0071300]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vitamin E [GO:0071306]; central nervous system development [GO:0007417]; chondrocyte differentiation [GO:0002062]; collagen fibril organization [GO:0030199]; embryonic skeletal joint morphogenesis [GO:0060272]; endochondral ossification [GO:0001958]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; growth plate cartilage development [GO:0003417]; heart morphogenesis [GO:0003007]; inner ear development [GO:0048839]; inner ear morphogenesis [GO:0042472]; limb bud formation [GO:0060174]; limb morphogenesis [GO:0035108]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; notochord development [GO:0030903]; ossification [GO:0001503]; otic vesicle development [GO:0071599]; proteoglycan metabolic process [GO:0006029]; regulation of gene expression [GO:0010468]; response to fibroblast growth factor [GO:0071774]; response to mechanical stimulus [GO:0009612]; response to X-ray [GO:0010165]; roof of mouth development [GO:0060021]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; skeletal system morphogenesis [GO:0048705]; tissue homeostasis [GO:0001894]; visual perception [GO:0007601]
|
basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen type II trimer [GO:0005585]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; MHC class II protein binding [GO:0042289]; platelet-derived growth factor binding [GO:0048407]; protein homodimerization activity [GO:0042803]; proteoglycan binding [GO:0043394]
|
PF01410;PF01391;
|
2.60.120.1000;
|
Fibrillar collagen family
|
PTM: Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains. {ECO:0000269|PubMed:21757687}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:21757687}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000305}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000305}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
|
Rattus norvegicus (Rat)
|
P05540
|
CD4_RAT
|
MCRGFSFRHLLPLLLLQLSKLLVVTQGKTVVLGKEGGSAELPCESTSRRSASFAWKSSDQKTILGYKNKLLIKGSLELYSRFDSRKNAWERGSFPLIINKLRMEDSQTYVCELENKKEEVELWVFRVTFNPGTRLLQGQSLTLILDSNPKVSDPPIECKHKSSNIVKDSKAFSTHSLRIQDSGIWNCTVTLNQKKHSFDMKLSVLGFASTSITAYKSEGESAEFSFPLNLGEESLQGELRWKAEKAPSSQSWITFSLKNQKVSVQKSTSNPKFQLSETLPLTLQIPQVSLQFAGSGNLTLTLDRGILYQEVNLVVMKVTQPDSNTLTCEVMGPTSPKMRLILKQENQEARVSRQEKVIQVQAPEAGVWQCLLSEGEEVKMDSKIQVLSKGLNQTMFLAVVLGSAFSFLVFTGLCILFCVRCRHQQRQAARMSQIKRLLSEKKTCQCSHRMQKSHNLI
| null | null |
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; defense response to Gram-negative bacterium [GO:0050829]; helper T cell enhancement of adaptive immune response [GO:0035397]; interleukin-15-mediated signaling pathway [GO:0035723]; macrophage differentiation [GO:0030225]; maintenance of protein location in cell [GO:0032507]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of viral entry into host cell [GO:0046598]; regulation of calcium ion transport [GO:0051924]; regulation of T cell activation [GO:0050863]; response to estradiol [GO:0032355]; response to vitamin D [GO:0033280]; T cell activation [GO:0042110]; T cell differentiation [GO:0030217]; T cell selection [GO:0045058]
|
cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
coreceptor activity [GO:0015026]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; immunoglobulin binding [GO:0019865]; interleukin-16 binding [GO:0042011]; interleukin-16 receptor activity [GO:0042012]; lipid binding [GO:0008289]; MHC class II protein binding [GO:0042289]; MHC class II protein complex binding [GO:0023026]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; signaling receptor binding [GO:0005102]; zinc ion binding [GO:0008270]
|
PF05790;PF09191;PF00047;PF12104;
|
2.60.40.10;1.20.5.900;
| null |
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}.; PTM: Phosphorylated by PKC; phosphorylation plays an important role for CD4 internalization. {ECO:0000250|UniProtKB:P01730}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01730}. Note=Localizes to lipid rafts. {ECO:0000250|UniProtKB:P01730}.
| null | null | null | null | null |
FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. {ECO:0000250|UniProtKB:P01730}.
|
Rattus norvegicus (Rat)
|
P05543
|
THBG_HUMAN
|
MSPFLYLVLLVLGLHATIHCASPEGKVTACHSSQPNATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA
| null | null |
thyroid hormone transport [GO:0070327]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00079;
|
2.30.39.10;3.30.497.10;2.10.310.10;
|
Serpin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Major thyroid hormone transport protein in serum.
|
Homo sapiens (Human)
|
P05545
|
SPA3K_RAT
|
MAFIAALGLLMAGICPAVLCDGILGRDTLPHEDQGKGRQLHSLTLASINTDFTLSLYKKLALRNPDKNVVFSPLSISAALAILSLGAKDSTMEEILEVLKFNLTEITEEEIHQGFGHLLQRLSQPEDQAEINTGSALFIDKEQPILSEFQEKTRALYQAEAFVADFKQCNEAKKFINDYVSNQTQGKIAELFSELDERTSMVLVNYLLFKGKWKVPFNPNDTFESEFYLDEKRSVKVPMMKIKDLTTPYIRDEELSCSVLELKYTGNASALFILPDQGKMQQVESSLQPETLKKWKDSLRPRIISELRMPKFSISTDYNLEEVLPELGIRKIFSQQADLSRITGTKNLHVSQVVHKAVLDVDETGTEGAAATAVTAALKSLPQTIPLLNFNRPFMLVITDNNGQSVFFMGKVTNPM
| null | null | null |
extracellular space [GO:0005615]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:1694763, ECO:0000269|PubMed:2440672}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Binds to and inhibits kallikreins. Inhibits trypsin but not chymotrypsin or elastase. {ECO:0000269|PubMed:1864837, ECO:0000269|PubMed:2440672}.
|
Rattus norvegicus (Rat)
|
P05546
|
HEP2_HUMAN
|
MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS
| null | null |
blood coagulation [GO:0007596]; chemotaxis [GO:0006935]
|
endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
endopeptidase inhibitor activity [GO:0004866]; heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family
|
PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.
| null | null | null | null | null | null |
FUNCTION: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner. {ECO:0000269|PubMed:1939083}.; FUNCTION: Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils. {ECO:0000269|PubMed:1939083}.
|
Homo sapiens (Human)
|
P05549
|
AP2A_HUMAN
|
MLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALSSGLGDLSIHSLPHAIEEVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK
| null | null |
bone morphogenesis [GO:0060349]; cellular response to iron ion [GO:0071281]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic forelimb morphogenesis [GO:0035115]; eyelid development in camera-type eye [GO:0061029]; inner ear morphogenesis [GO:0042472]; kidney development [GO:0001822]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of transcription by competitive promoter binding [GO:0010944]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oculomotor nerve formation [GO:0021623]; optic cup structural organization [GO:0003409]; optic vesicle morphogenesis [GO:0003404]; positive regulation of bone mineralization [GO:0030501]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of tooth mineralization [GO:0070172]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell differentiation [GO:0045595]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; retina layer formation [GO:0010842]; roof of mouth development [GO:0060021]; sensory perception of sound [GO:0007605]; trigeminal nerve development [GO:0021559]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
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 repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; nuclear receptor corepressor activity [GO:0140536]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]
|
PF03299;
| null |
AP-2 family
|
PTM: Sumoylated on Lys-10; which inhibits transcriptional activity. {ECO:0000305|PubMed:12072434}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12586840}.
| null | null | null | null | null |
FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region. {ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:12586840}.
|
Homo sapiens (Human)
|
P05554
|
CEBPA_RAT
|
MESADFYEAEPRPPMSSHLQSPPHAPSNAAFGFPRGAGPAPPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAAGPAGGGGDFDYPGAPAGPGGAVMSAGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPPHPHASPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPAMGAAGLPGPGGSLKGLAGPHPDLRTGGGGGGGAGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA
| null | null |
acute-phase response [GO:0006953]; animal organ regeneration [GO:0031100]; brown fat cell differentiation [GO:0050873]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; cellular response to lithium ion [GO:0071285]; cellular response to organic cyclic compound [GO:0071407]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to xenobiotic stimulus [GO:0071466]; cholesterol metabolic process [GO:0008203]; DNA-templated transcription [GO:0006351]; embryonic placenta development [GO:0001892]; epithelial cell maturation [GO:0002070]; fat cell differentiation [GO:0045444]; glucose homeostasis [GO:0042593]; granulocyte differentiation [GO:0030851]; hematopoietic stem cell proliferation [GO:0071425]; inner ear development [GO:0048839]; interleukin-6-mediated signaling pathway [GO:0070102]; lipid homeostasis [GO:0055088]; liver development [GO:0001889]; lung development [GO:0030324]; macrophage differentiation [GO:0030225]; memory [GO:0007613]; mitochondrion organization [GO:0007005]; myeloid cell differentiation [GO:0030099]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of hematopoietic stem cell proliferation [GO:1902034]; negative regulation of transcription by RNA polymerase II [GO:0000122]; Notch signaling pathway [GO:0007219]; osteoblast development [GO:0002076]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of gene expression [GO:0010628]; positive regulation of inflammatory response [GO:0050729]; positive regulation of macrophage activation [GO:0043032]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to dexamethasone [GO:0071548]; response to nutrient [GO:0007584]; response to phenylpropanoid [GO:0080184]; response to vitamin B2 [GO:0033274]; transcription by RNA polymerase I [GO:0006360]; urea cycle [GO:0000050]; white fat cell differentiation [GO:0050872]
|
C/EBP complex [GO:1990647]; CHOP-C/EBP complex [GO:0036488]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; Rb-E2F complex [GO:0035189]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; 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]; histone deacetylase binding [GO:0042826]; HMG box domain binding [GO:0071837]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; RNA polymerase I transcription regulatory region sequence-specific DNA binding [GO:0001163]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; STAT family protein binding [GO:0097677]; transcription cis-regulatory region binding [GO:0000976]
|
PF07716;
|
1.20.5.170;
|
BZIP family, C/EBP subfamily
|
PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2. {ECO:0000269|PubMed:16735515}.; PTM: Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation. Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-222 and Thr-226 are phosphorylated only during feeding but not during fasting. Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters. {ECO:0000250|UniProtKB:P53566}.; PTM: Ubiquitinated by COP1 upon interaction with TRIB1. {ECO:0000250|UniProtKB:P49715}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8367486}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleolus {ECO:0000269|PubMed:20075868}.
| null | null | null | null | null |
FUNCTION: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta (PubMed:11672531, PubMed:16735515, PubMed:20176812, PubMed:8367486). Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (By similarity). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:11672531). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (PubMed:11672531). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Down-regulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters (PubMed:11672531). Proliferation arrest also depends on a functional binding to SWI/SNF complex (By similarity). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC1. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity). {ECO:0000250|UniProtKB:P49715, ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:16735515, ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:8367486}.; FUNCTION: [Isoform 3]: Can act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation. {ECO:0000250|UniProtKB:P49715, ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:8367486}.; FUNCTION: [Isoform 4]: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation. {ECO:0000250|UniProtKB:P49715}.
|
Rattus norvegicus (Rat)
|
P05555
|
ITAM_MOUSE
|
MTLKALLVTALALCHGFNLDTEHPMTFQENAKGFGQNVVQLGGTSVVVAAPQEAKAVNQTGALYQCDYSTSRCHPIPLQVPPEAVNMSLGLSLAVSTVPQQLLACGPTVHQNCKENTYVNGLCYLFGSNLLRPPQQFPEALRECPQQESDIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKSKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTKTASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDYKDVIPEADRAGVIRYVIGVGNAFNKPQSRRELDTIASKPAGEHVFQVDNFEALNTIQNQLQEKIFAIEGTQTGSTSSFEHEMSQEGFSASITSNGPLLGSVGSFDWAGGAFLYTSKDKVTFINTTRVDSDMNDAYLGYASAVILRNRVQSLVLGAPRYQHIGLVVMFRENFGTWEPHTSIKGSQIGSYFGASLCSVDMDADGNTNLILIGAPHYYEKTRGGQVSVCPLPRGRARWQCEALLHGDQGHPWGRFGAALTVLGDVNGDKLTDVAIGAPGEQENQGAVYIFYGASIASLSASHSHRIIGAHFSPGLQYFGQSLSGGKDLTMDGLMDLAVGAQGHLLLLRAQPVLRLEATMEFSPKKVARSVFACQEQVLKNKDAGEVRVCLRVRKNTKDRLREGDIQSTVTYDLALDPVRSRIRAFFDETKNNTRRRTQVFGLMQKCETLKLILPDCVDDSVSPIILRLNYTLVGEPLRSFGNLRPVLAMDAQRFFTAMFPFEKNCGNDSICQDDLSITMSAMGLDTLVVGGPQDFNMSVTLRNDGEDSYGTQVTVYYPSGLSYRKDSASQNPLTKKPWFVKPAESSSSSEGHGALKSTTWNINHPIFPANSEVTFNVTFDVDSHASFGNKLLLKAIVASENNMSRTHKTKFQLELPVKYAIYMIVTSDESSIRYLNFTASEMTSKVIQHQYQFNNLGQRSLPVSVVFWIPVQINNVTVWDHPQVIFSQNLSSACHTEQKSPPHSNFRDQLERTPVLNCSVAVCKRIQCDLPSFNTQEIFNVTLKGNLSFDWYIKTSHGHLLLVSSTEILFNDSAFALLPGQESYVRSKTETKVEPYEVHNPVPLIVGSSIGGLVLLALITAGLYKLGFFKRQYKDMMNEAAPQDAPPQ
| null | null |
activated T cell proliferation [GO:0050798]; amyloid-beta clearance [GO:0097242]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; cellular extravasation [GO:0045123]; complement receptor mediated signaling pathway [GO:0002430]; complement-mediated synapse pruning [GO:0150062]; forebrain development [GO:0030900]; integrin-mediated signaling pathway [GO:0007229]; leukocyte adhesion to vascular endothelial cell [GO:0061756]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration involved in inflammatory response [GO:0002523]; microglia development [GO:0014005]; microglial cell activation [GO:0001774]; negative regulation of dopamine metabolic process [GO:0045963]; neutrophil apoptotic process [GO:0001781]; neutrophil chemotaxis [GO:0030593]; phagocytosis [GO:0006909]; phagocytosis, engulfment [GO:0006911]; positive regulation of mast cell differentiation [GO:0060376]; positive regulation of microglial cell mediated cytotoxicity [GO:1904151]; positive regulation of prostaglandin-E synthase activity [GO:2000363]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of superoxide anion generation [GO:0032930]; receptor-mediated endocytosis [GO:0006898]; vertebrate eye-specific patterning [GO:0150064]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; integrin alphaM-beta2 complex [GO:0034688]; integrin complex [GO:0008305]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
cargo receptor activity [GO:0038024]; complement component C3b binding [GO:0001851]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; opsonin binding [GO:0001846]
|
PF01839;PF08441;PF20805;PF00357;PF21520;PF00092;
|
1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530;3.40.50.410;
|
Integrin alpha chain family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9862668}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11215}. Membrane raft {ECO:0000250|UniProtKB:P11215}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11215}.
| null | null | null | null | null |
FUNCTION: Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (By similarity). It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration. In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (By similarity). May regulate phagocytosis-induced apoptosis in extravasated neutrophils (By similarity). May play a role in mast cell development (By similarity). Required with TYROBP/DAP12 in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (PubMed:18685038). {ECO:0000250|UniProtKB:P11215, ECO:0000269|PubMed:18685038, ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9382884, ECO:0000269|PubMed:9862668}.
|
Mus musculus (Mouse)
|
P05556
|
ITB1_HUMAN
|
MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK
| null | null |
axon extension [GO:0048675]; B cell differentiation [GO:0030183]; basement membrane organization [GO:0071711]; calcium-independent cell-matrix adhesion [GO:0007161]; cardiac cell fate specification [GO:0060912]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379]; CD40 signaling pathway [GO:0023035]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell projection organization [GO:0030030]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by integrin [GO:0033631]; cell-matrix adhesion [GO:0007160]; cell-substrate adhesion [GO:0031589]; cellular defense response [GO:0006968]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; formation of radial glial scaffolds [GO:0021943]; G1/S transition of mitotic cell cycle [GO:0000082]; germ cell migration [GO:0008354]; heterotypic cell-cell adhesion [GO:0034113]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; in utero embryonic development [GO:0001701]; integrin-mediated signaling pathway [GO:0007229]; lamellipodium assembly [GO:0030032]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte tethering or rolling [GO:0050901]; maintenance of blood-brain barrier [GO:0035633]; mesodermal cell differentiation [GO:0048333]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fate specification [GO:0048626]; myoblast fusion [GO:0007520]; negative regulation of anoikis [GO:2000811]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of vasoconstriction [GO:0045906]; neuroblast proliferation [GO:0007405]; phagocytosis [GO:0006909]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell migration [GO:0030335]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of glutamate uptake involved in transmission of nerve impulse [GO:0051951]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of vascular endothelial growth factor signaling pathway [GO:1900748]; positive regulation of wound healing [GO:0090303]; reactive gliosis [GO:0150103]; receptor internalization [GO:0031623]; regulation of cell cycle [GO:0051726]; regulation of collagen catabolic process [GO:0010710]; regulation of inward rectifier potassium channel activity [GO:1901979]; regulation of spontaneous synaptic transmission [GO:0150003]; regulation of synapse pruning [GO:1905806]; sarcomere organization [GO:0045214]; visual learning [GO:0008542]; wound healing, spreading of epidermal cells [GO:0035313]
|
cell surface [GO:0009986]; cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; glial cell projection [GO:0097386]; integrin alpha1-beta1 complex [GO:0034665]; integrin alpha10-beta1 complex [GO:0034680]; integrin alpha11-beta1 complex [GO:0034681]; integrin alpha2-beta1 complex [GO:0034666]; integrin alpha3-beta1 complex [GO:0034667]; integrin alpha4-beta1 complex [GO:0034668]; integrin alpha5-beta1 complex [GO:0034674]; integrin alpha7-beta1 complex [GO:0034677]; integrin alpha8-beta1 complex [GO:0034678]; integrin alpha9-beta1 complex [GO:0034679]; integrin alphav-beta1 complex [GO:0034682]; integrin complex [GO:0008305]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; myelin sheath abaxonal region [GO:0035748]; neuromuscular junction [GO:0031594]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; recycling endosome [GO:0055037]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic membrane [GO:0097060]
|
actin binding [GO:0003779]; C-X3-C chemokine binding [GO:0019960]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]; collagen binding involved in cell-matrix adhesion [GO:0098639]; coreceptor activity [GO:0015026]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; integrin binding involved in cell-matrix adhesion [GO:0098640]; laminin binding [GO:0043236]; magnesium ion binding [GO:0000287]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; protein-containing complex binding [GO:0044877]; virus receptor activity [GO:0001618]
|
PF07974;PF18372;PF08725;PF07965;PF00362;PF17205;
|
4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410;
|
Integrin beta chain family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:32487760, ECO:0000269|PubMed:35687021, ECO:0000303|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:11919189}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:16256741}. Melanosome {ECO:0000269|PubMed:17081065}. Cleavage furrow {ECO:0000269|PubMed:17956333}. Cell projection, lamellipodium {ECO:0000269|PubMed:11919189}. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:35687021}. Note=Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in a few intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent manner. Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. {ECO:0000269|PubMed:10455171}.; SUBCELLULAR LOCATION: [Isoform 2]: Note=Does not localize to focal adhesions. {ECO:0000269|PubMed:10455171}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P09055}. Cell junction {ECO:0000250|UniProtKB:P09055}. Note=In cardiac muscle, found in costameres and intercalated disks. {ECO:0000250|UniProtKB:P09055}.
| null | null | null | null | null |
FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity). Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415, PubMed:24789099). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (PubMed:31331973). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (PubMed:35802072). {ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055, ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:33962943, ECO:0000269|PubMed:35802072, ECO:0000269|PubMed:7523423}.; FUNCTION: [Isoform 2]: Interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). {ECO:0000305|PubMed:2249781}.; FUNCTION: [Isoform 5]: Isoform 5 displaces isoform 1 in striated muscles. {ECO:0000250|UniProtKB:P09055}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8. {ECO:0000269|PubMed:8411387}.; FUNCTION: (Microbial infection) Acts as a receptor for Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:20660204}.; FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr virus/HHV-4. {ECO:0000269|PubMed:17945327}.; FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for Human parvovirus B19. {ECO:0000269|PubMed:12907437}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus. {ECO:0000269|PubMed:12941907}.; FUNCTION: (Microbial infection) Acts as a receptor for Mammalian reovirus. {ECO:0000269|PubMed:16501085}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, integrin ITGA5:ITGB1 binding to extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. {ECO:0000269|PubMed:10397733}.; FUNCTION: (Microbial infection) Interacts with CotH proteins expressed by fungi of the order mucorales, the causative agent of mucormycosis, which plays an important role in epithelial cell invasion by the fungi (PubMed:32487760). Integrin ITGA3:ITGB1 may act as a receptor for R.delemar CotH7 in alveolar epithelial cells, which may be an early step in pulmonary mucormycosis disease progression (PubMed:32487760). {ECO:0000269|PubMed:32487760}.; FUNCTION: (Microbial infection) May serve as a receptor for adhesin A (nadA) of N.meningitidis. {ECO:0000305|PubMed:21471204}.
|
Homo sapiens (Human)
|
P05618
|
CDGT_BACS0
|
MKRFMKLTAVWTLWLSLTLGLLSPVHAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGSCTNLRLYCGGDWQGIINKINDGYLTGMGITAIWISQPVENIYSVINYSGVNNTAYHGYWARDFKKTNPAYGTMQDFKNLIDTAHAHNIKVIIDFAPNHTSPASSDDPSFAENGRLYDNGNLLGGYTNDTQNLFHHYGGTDFSTIENGIYKNLYDLADLNHNNSSVDVYLKDAIKMWLDLGVDGIRVDAVKHMPFGWQKSFMATINNYKPVFTFGEWFLGVNEISPEYHQFANESGMSLLDFRFAQKARQVFRDNTDNMYGLKAMLEGSEVDYAQVNDQVTFIDNHDMERFHTSNGDRRKLEQALAFTLTSRGVPAIYYGSEQYMSGGNDPDNRARLPSFSTTTTAYQVIQKLAPLRKSNPAIAYGSTHERWINNDVIIYERKFGNNVAVVAINRNMNTPASITGLVTSLRRASYNDVLGGILNGNTLTVGAGGAASNFTLAPGGTAVWQYTTDATTPIIGNVGPMMAKPGVTITIDGRGFGSGKGTVYFGTTAVTGADIVAWEDTQIQVKIPAVPGGIYDIRVANAAGAASNIYDNFEVLTGDQVTVRFVINNATTALGQNVFLTGNVSELGNWDPNNAIGPMYNQVVYQYPTWYYDVSVPAGQTIEFKFLKKQGSTVTWEGGANRTFTTPTSGTATVNVNWQP
|
2.4.1.19
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.;
|
carbohydrate metabolic process [GO:0005975]
|
extracellular region [GO:0005576]
|
alpha-amylase activity [GO:0004556]; cyclomaltodextrin glucanotransferase activity [GO:0043895]; metal ion binding [GO:0046872]; starch binding [GO:2001070]
|
PF00128;PF02806;PF00686;PF01833;
|
3.20.20.80;2.60.40.1180;2.60.40.10;
|
Glycosyl hydrolase 13 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.; EC=2.4.1.19;
| null | null | null | null | null |
Bacillus sp. (strain 1011)
|
P05620
|
VSP1_PROFL
|
MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHPFLVALYDAWSGRFLCGGTLINPEWVLTAAHCDSKNFKMKLGAHSKKVLNEDEQIRNPKEKFICPNKKNDEVLDKDIMLIKLDSPVSYSEHIAPLSLPSSPPSVGSVCRIMGWGSITPVEETFPDVPHCANINLLDDVECKPGYPELLPEYRTLCAGVLQGGIDTCGFDSGTPLICNGQFQGIVSYGGHPCGQSRKPGIYTKVFDYNAWIQSIIAGNTAATCLP
|
3.4.21.74
| null |
proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Snake venom subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74;
| null | null | null | null |
FUNCTION: Thrombin-like snake venom serine protease that clots fibrinogen (FGA) by releasing fibrinopeptide A. According to PubMed:8585090, only cleaves rabbit fibrinogen, whereas no specificity is described in PubMed:3910643 (tests done on bovine fibrinogen). Also acts as a C3 convertase that independently cleaves human C3 and kick-starts the complement cascade. Also increases urokinase-type plasminogen activator (PLAU) and plasminogen activator inhibitor (SERPINE1) in cultured bovine pulmonary artery endothelial cells. Dose-dependently inhibits collagen-induced platelet aggregation. {ECO:0000269|PubMed:10708795, ECO:0000269|PubMed:12225369, ECO:0000269|PubMed:3910643, ECO:0000269|PubMed:8585090, ECO:0000269|PubMed:8817813, ECO:0000269|PubMed:9241744}.
|
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
|
P05622
|
PGFRB_MOUSE
|
MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLETLGDVEIAELHRSRTLRVVFEAYPMPSVLWLKDNRTLGDSGAGELVLSTRNMSETRYVSELILVRVKVSEAGYYTMRAFHEDDEVQLSFKLQVNVPVRVLELSESHPANGEQTIRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGGDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSAELYSNALPVGFSLPSHLNLTGESDGGYMDMSKDESIDYVPMLDMKGDIKYADIESPSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMDFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARFPGIHSLRSPLDTSSVLYTAVQPNESDNDYIIPLPDPKPDVADEGLPEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQQAEPEAQLEQPQDSGCPGPLAEAEDSFL
|
2.7.10.1
| null |
adrenal gland development [GO:0030325]; aorta morphogenesis [GO:0035909]; blood vessel development [GO:0001568]; cardiac myofibril assembly [GO:0055003]; cardiac vascular smooth muscle cell differentiation [GO:0060947]; cell chemotaxis [GO:0060326]; cell migration involved in coronary angiogenesis [GO:0060981]; cell migration involved in vasculogenesis [GO:0035441]; cellular response to hydrogen peroxide [GO:0070301]; embryonic organ development [GO:0048568]; glycosaminoglycan biosynthetic process [GO:0006024]; in utero embryonic development [GO:0001701]; intracellular signal transduction [GO:0035556]; kidney development [GO:0001822]; lung growth [GO:0060437]; metanephric glomerular capillary formation [GO:0072277]; metanephric glomerular mesangial cell proliferation involved in metanephros development [GO:0072262]; metanephric glomerular mesangium development [GO:0072223]; metanephric mesenchymal cell migration [GO:0035789]; negative regulation of apoptotic process [GO:0043066]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic process [GO:0043065]; positive regulation of calcium ion import [GO:0090280]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway [GO:0038091]; positive regulation of chemotaxis [GO:0050921]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of hepatic stellate cell activation [GO:2000491]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway [GO:0035793]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; protein autophosphorylation [GO:0046777]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; response to ceramide [GO:0106096]; retina vasculature development in camera-type eye [GO:0061298]; ruffle assembly [GO:0097178]; signal transduction [GO:0007165]; skeletal system morphogenesis [GO:0048705]; smooth muscle cell chemotaxis [GO:0071670]; smooth muscle tissue development [GO:0048745]; tissue homeostasis [GO:0001894]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; ruffle [GO:0001726]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; phosphatidylinositol 3-kinase binding [GO:0043548]; platelet-derived growth factor beta-receptor activity [GO:0005019]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor activity [GO:0005017]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]
|
PF00047;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
|
PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-578, and to a lesser degree, Tyr-580 is important for interaction with SRC. Phosphorylation at Tyr-715 is important for interaction with GRB2. Phosphorylation at Tyr-739 and Tyr-750 is important for interaction with PIK3R1. Phosphorylation at Tyr-750 is important for interaction with NCK1. Phosphorylation at Tyr-770 and Tyr-856 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-856 is important for efficient phosphorylation of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased cell proliferation. Phosphorylation at Tyr-1008 is important for interaction with PTPN11. Phosphorylation at Tyr-1008 and Tyr-1020 is important for interaction with PLCG1. Dephosphorylated by PTPRJ at Tyr-750, Tyr-856, Tyr-1008 and Tyr-1020 (By similarity). Dephosphorylated by PTPN2 at Tyr-578 and Tyr-1020. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation. {ECO:0000269|PubMed:15753096}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle {ECO:0000250}. Lysosome lumen {ECO:0000250}. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:15284236};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM (By similarity). Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000250, ECO:0000269|PubMed:14624252, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:15284236, ECO:0000269|PubMed:17620338, ECO:0000269|PubMed:18948621, ECO:0000269|PubMed:19030102, ECO:0000269|PubMed:19742316, ECO:0000269|PubMed:21664579, ECO:0000269|PubMed:8440729}.
|
Mus musculus (Mouse)
|
P05623
|
A70A_DROME
|
MKTLALFLVLVCVLGLVQSWEWPWNRKPTKFPIPSPNPRDKWCRLNLGPAWGGRC
| null | null |
adult feeding behavior [GO:0008343]; G protein-coupled receptor signaling pathway [GO:0007186]; multi-organism reproductive process [GO:0044703]; negative regulation of female receptivity [GO:0007621]; negative regulation of female receptivity, post-mating [GO:0045434]; regulation of egg-laying behavior [GO:0046662]; regulation of female receptivity, post-mating [GO:0046008]; regulation of juvenile hormone biosynthetic process [GO:0007557]; sexual reproduction [GO:0019953]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]
|
PF08138;
| null |
Drosophila sex peptide family
|
PTM: Sperm-bound protein is cleaved to release an active C-terminal peptide. Gradual release from stored sperm may function to prolong PMR and enhance male reproductive success. {ECO:0000269|PubMed:15694303}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3135120}.
| null | null | null | null | null |
FUNCTION: Male seminal protein which triggers short- and long-term post-mating behavioral responses (PMR) in female Drosophila (PubMed:15694303, PubMed:19249273, PubMed:19793753, PubMed:20308537, PubMed:24089336, PubMed:3135120). Binds initially to sperm where it is later cleaved to release an active peptide within the female reproductive tract. Signals via the sex peptide receptor (SPR) in female flies; may also act via other receptors (PubMed:20308537, PubMed:20458515, PubMed:24089336). Moderates the activity of distinct neuronal circuitries in the female genital tract to promote specific PMRs including: enhanced ovulation, increased egg laying rate, increased feeding/foraging rate, induced antimicrobial peptide synthesis, reduced mating receptivity, reduced day-time sleep and reduced lifespan in multiple mated females (PubMed:15694303, PubMed:19249273, PubMed:19793753, PubMed:24089336, PubMed:3135120). {ECO:0000269|PubMed:15694303, ECO:0000269|PubMed:19249273, ECO:0000269|PubMed:19793753, ECO:0000269|PubMed:20308537, ECO:0000269|PubMed:24089336, ECO:0000269|PubMed:3135120}.
|
Drosophila melanogaster (Fruit fly)
|
P05625
|
RAF1_CHICK
|
MEHIQGAWKTISNGFGLKDSVFDGPNCISPTIVQQFGYQRRASDDGKISDTSKTSNTIRVFLPNKQRTVVNVRNGMTLHDCLMKALKVRGLQPECCAVFRLVTEPKGKKVRLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSNISDSGVPALPPLTMRRMRESVSRIPVSSQHRYSTPHVFTFNTSNPSSEGTLSQRQRSTSTPNVHMVSTTMPVDSRIIEDAIRNHSESASPSALSGSPNNMSPTGWSQPKTPVPAQRERAPGTNTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIRMQDSNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCLKKVREERPLFPQILSSIELLQHSLPKINRSASEPSLHRASHTEDINSCTLTSTRLPVF
|
2.7.11.1
| null |
MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; Ras protein signal transduction [GO:0007265]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]
|
PF00130;PF00069;PF02196;
|
3.30.60.20;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily
|
PTM: Phosphorylation at Ser-259 inactivates kinase activity. Dephosphorylation of Ser-259 by a complex containing protein phosphatase 1 relieves inactivation, leading to stimulate RAF1 activity (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}.
|
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:0000250|UniProtKB:P04049}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:P04049}; 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:0000250|UniProtKB:P04049}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:P04049};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2) (By similarity). {ECO:0000250|UniProtKB:P04049}.
|
Gallus gallus (Chicken)
|
P05626
|
ATPF_YEAST
|
MSMSMGVRGLALRSVSKTLFSQGVRCPSMVIGARYMSSTPEKQTDPKAKANSIINAIPGNNILTKTGVLGTSAAAVIYAISNELYVINDESILLLTFLGFTGLVAKYLAPAYKDFADARMKKVSDVLNASRNKHVEAVKDRIDSVSQLQNVAETTKVLFDVSKETVELESEAFELKQKVELAHEAKAVLDSWVRYEASLRQLEQRQLAKSVISRVQSELGNPKFQEKVLQQSISEIEQLLSKLK
| null | null |
protein-containing complex assembly [GO:0065003]; proton motive force-driven ATP synthesis [GO:0015986]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrial proton-transporting ATP synthase, stator stalk [GO:0000274]; mitochondrion [GO:0005739]
|
proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]
|
PF05405;
|
1.20.5.2210;
|
Eukaryotic ATPase B chain family
| null |
SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
| null | null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05627
|
JUN_MOUSE
|
MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGMVAPAVASVAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
| null | null |
angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; axon regeneration [GO:0031103]; cell population proliferation [GO:0008283]; cellular response to anisomycin [GO:0072740]; cellular response to calcium ion [GO:0071277]; cellular response to potassium ion starvation [GO:0051365]; DNA-templated transcription [GO:0006351]; eyelid development in camera-type eye [GO:0061029]; leading edge cell differentiation [GO:0035026]; learning [GO:0007612]; liver development [GO:0001889]; membrane depolarization [GO:0051899]; microglial cell activation [GO:0001774]; monocyte differentiation [GO:0030224]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein autophosphorylation [GO:0031953]; outflow tract morphogenesis [GO:0003151]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA replication [GO:0045740]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; release of cytochrome c from mitochondria [GO:0001836]; response to muscle stretch [GO:0035994]; response to oxygen-containing compound [GO:1901700]; response to xenobiotic stimulus [GO:0009410]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053]
|
chromatin binding [GO:0003682]; 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]; HMG box domain binding [GO:0071837]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF00170;PF03957;
|
1.20.5.170;
|
BZIP family, Jun subfamily
|
PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-246; this primes the protein for subsequent phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246 and Ser-252 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-289 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity (By similarity). Phosphorylated by VRK1 (By similarity). {ECO:0000250|UniProtKB:P05412}.; PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation. Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7. {ECO:0000250|UniProtKB:P05412}.; PTM: Acetylated at Lys-271 by EP300. {ECO:0000250|UniProtKB:P05412}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}.
| null | null | null | null | null |
FUNCTION: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:14707112). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (PubMed:2498083). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). Involved in activated KRAS-mediated transcriptional activation of USP28 (By similarity). Binds to the USP28 promoter (By similarity). {ECO:0000250|UniProtKB:P05412, ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:2498083}.
|
Mus musculus (Mouse)
|
P05630
|
ATPD_BOVIN
|
MLPSALLRRPGLGRLVRQVRLYAEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIRIEANEALVKALE
| null | null |
aerobic respiration [GO:0009060]; mitochondrial proton-transporting ATP synthase complex assembly [GO:0033615]; proton motive force-driven ATP synthesis [GO:0015986]; proton transmembrane transport [GO:1902600]
|
mitochondrial envelope [GO:0005740]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) [GO:0000275]; proton-transporting ATP synthase complex [GO:0045259]
|
proton transmembrane transporter activity [GO:0015078]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]
|
PF02823;PF21335;
|
1.20.5.440;2.60.15.10;
|
ATPase epsilon chain family
| null |
SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
| null | null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. {ECO:0000250|UniProtKB:P30049}.
|
Bos taurus (Bovine)
|
P05637
|
APAH_ECOLI
|
MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYALDTGCCWGGTLTCLRWEDKQYFVQPSNRHKDLGEAAAS
|
3.6.1.41
| null |
nucleobase-containing small molecule interconversion [GO:0015949]; response to X-ray [GO:0010165]; RNA decapping [GO:0110154]
|
cytoplasm [GO:0005737]
|
bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity [GO:0008803]; bis(5'-nucleosyl)-tetraphosphatase activity [GO:0008796]; phosphatase activity [GO:0016791]
|
PF00149;
|
3.60.21.10;
|
Ap4A hydrolase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=3.6.1.41; Evidence={ECO:0000269|PubMed:6317672};
| null | null | null | null |
FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. {ECO:0000269|PubMed:6317672}.
|
Escherichia coli (strain K12)
|
P05655
|
LSC_BACSU
|
MNIKKFAKQATVLTFTTALLAGGATQAFAKETNQKPYKETYGISHITRHDMLQIPEQQKNEKYQVPEFDSSTIKNISSAKGLDVWDSWPLQNADGTVANYHGYHIVFALAGDPKNADDTSIYMFYQKVGETSIDSWKNAGRVFKDSDKFDANDSILKDQTQEWSGSATFTSDGKIRLFYTDFSGKHYGKQTLTTAQVNVSASDSSLNINGVEDYKSIFDGDGKTYQNVQQFIDEGNYSSGDNHTLRDPHYVEDKGHKYLVFEANTGTEDGYQGEESLFNKAYYGKSTSFFRQESQKLLQSDKKRTAELANGALGMIELNDDYTLKKVMKPLIASNTVTDEIERANVFKMNGKWYLFTDSRGSKMTIDGITSNDIYMLGYVSNSLTGPYKPLNKTGLVLKMDLDPNDVTFTYSHFAVPQAKGNNVVITSYMTNRGFYADKQSTFAPSFLLNIKGKKTSVVKDSILEQGQLTVNK
|
2.4.1.10
| null |
carbohydrate utilization [GO:0009758]
|
extracellular region [GO:0005576]
|
levansucrase activity [GO:0050053]; metal ion binding [GO:0046872]
|
PF02435;
| null |
Glycosyl hydrolase 68 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167, ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10; Evidence={ECO:0000269|PubMed:14517548, ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, ECO:0000269|PubMed:33303628, ECO:0000269|PubMed:4206083};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for sucrose {ECO:0000269|PubMed:18596022}; KM=9 mM for sucrose {ECO:0000269|PubMed:33303628}; KM=8.3 mM for sucrose (for hydrolysis, in the absence of levan F4) {ECO:0000269|PubMed:32553967}; KM=6.9 mM for sucrose (for hydrolysis, in the presence of 5 g/L levan F4) {ECO:0000269|PubMed:32553967}; KM=6.8 mM for sucrose (for hydrolysis, in the presence of 55 g/L levan F4) {ECO:0000269|PubMed:32553967}; KM=57.6 mM for sucrose (for transfructosylation, in the absence of levan F4) {ECO:0000269|PubMed:32553967}; KM=20.9 mM for sucrose (for transfructosylation, in the presence of 5 g/L levan F4) {ECO:0000269|PubMed:32553967}; KM=10.9 mM for sucrose (for transfructosylation, in the presence of 55 g/L levan F4) {ECO:0000269|PubMed:32553967}; Note=kcat is 164.6 sec(-1) with sucrose as substrate (PubMed:18596022). kcat is 236.7 sec(-1) with sucrose as substrate (PubMed:33303628). kcat is 71.2 sec(-1) with sucrose as substrate (for hydrolysis, in the absence of levan F4). kcat is 69.8 sec(-1) with sucrose as substrate (for hydrolysis, in the presence of 5 g/L levan F4). kcat is 65.9 sec(-1) with sucrose as substrate (for hydrolysis, in the presence of 55 g/L levan F4). kcat is 26.6 sec(-1) with sucrose as substrate (for transfructosylation, in the absence of levan F4). kcat is 33.0 sec(-1) with sucrose as substrate (for transfructosylation, in the presence of 5 g/L levan F4). kcat is 33.7 sec(-1) with sucrose as substrate (for transfructosylation, in the presence of 55 g/L levan F4) (PubMed:32553967). {ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, ECO:0000269|PubMed:33303628};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:18596022};
| null |
FUNCTION: Catalyzes the synthesis of levan, a fructose polymer, by transferring the fructosyl moiety from sucrose to a growing acceptor molecule (PubMed:14517548, PubMed:18596022, PubMed:32553967, PubMed:33303628, PubMed:4206083). Also displays sucrose hydrolase activity (PubMed:18596022, PubMed:32553967, PubMed:33303628, PubMed:4206083). At low sucrose concentrations, functions as an hydrolase with water as acceptor, whereas at higher substrate concentrations it adds fructosyl units to a growing levan chain (PubMed:4206083). {ECO:0000269|PubMed:14517548, ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, ECO:0000269|PubMed:33303628, ECO:0000269|PubMed:4206083}.
|
Bacillus subtilis (strain 168)
|
P05656
|
SACC_BACSU
|
MKKRLIQVMIMFTLLLTMAFSADAADSSYYDEDYRPQYHFTPEANWMNDPNGMVYYAGEYHLFYQYHPYGLQWGPMHWGHAVSKDLVTWEHLPVALYPDEKGTIFSGSAVVDKNNTSGFQTGKEKPLVAIYTQDREGHQVQSIAYSNDKGRTWTKYAGNPVIPNPGKKDFRDPKVFWYEKEKKWVMVLAAGDRILIYTSKNLKQWTYASEFGQDQGSHGGVWECPDLFELPVDGNPNQKKWVMQVSVGNGAVSGGSGMQYFVGDFDGTHFKNENPPNKVLWTDYGRDFYAAVSWSDIPSTDSRRLWLGWMSNWQYANDVPTSPWRSATSIPRELKLKAFTEGVRVVQTPVKELETIRGTSKKWKNLTISPASHNVLAGQSGDAYEINAEFKVSPGSAAEFGFKVRTGENQFTKVGYDRRNAKLFVDRSESGNDTFNPAFNTGKETAPLKPVNGKVKLRIFVDRSSVEVFGNDGKQVITDIILPDRSSKGLELYAANGGVKVKSLTIHPLKKVWGTTPFMSNMTGWTTVNGTWADTIEGKQGRSDGDSFILSSASGSDFTYESDITIKDGNGRGAGALMFRSDKDAKNGYLANVDAKHDLVKFFKFENGAASVIAEYKTPIDVNKKYHLKTEAEGDRFKIYLDDRLVIDAHDSVFSEGQFGLNVWDATAVFQNVTKES
|
3.2.1.80
| null |
sucrose catabolic process [GO:0005987]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
fructan beta-fructosidase activity [GO:0051669]; sucrose alpha-glucosidase activity [GO:0004575]
|
PF06439;PF08244;PF00251;
| null |
Glycosyl hydrolase 32 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10217495}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.; EC=3.2.1.80;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for levan (at pH 5.5 and 55 degrees Celsius) {ECO:0000269|PubMed:7646030}; KM=6.7 mM for inulin (at pH 5.5 and 55 degrees Celsius) {ECO:0000269|PubMed:7646030}; KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius) {ECO:0000269|PubMed:7646030};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 for inulin hydrolysis. {ECO:0000269|PubMed:7646030};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius for inulin hydrolysis. Is rapidly inactivated at 60 degrees Celsius. High stable at 50 and 55 degrees Celsius. {ECO:0000269|PubMed:7646030};
|
FUNCTION: Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose. Is also able to hydrolyze sucrose and to a small extent raffinose, but not melezitose, stachylose, cellobiose, maltose, and lactose. {ECO:0000269|PubMed:7646030}.
|
Bacillus subtilis (strain 168)
|
P05661
|
MYSA_DROME
|
MPKPVANQEDEDPTPYLFVSLEQRRIDQSKPYDSKKSCWIPDEKEGYLLGEIKATKGDIVSVGLQGGEVRDIKSEKVEKVNPPKFEKIEDMADMTVLNTPCVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHIMFVMEQEEYKKEGINWDFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTKVFFRAGVLGQMEEFRDERLGKIMSWMQAWARGYLSRKGFKKLQEQRVALKVVQRNLRKYLQLRTWPWYKLWQKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEHDRQTCHNELNQTRTACDQLGRDKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPRATSVRPQFDGLAFPPRFDLAPENEF
| null | null |
adult somatic muscle development [GO:0007527]; border follicle cell migration [GO:0007298]; epithelial cell migration, open tracheal system [GO:0007427]; flight [GO:0060361]; locomotion [GO:0040011]; mitotic actomyosin contractile ring contraction [GO:1902404]; muscle cell differentiation [GO:0042692]; muscle contraction [GO:0006936]; muscle organ development [GO:0007517]; muscle thin filament assembly [GO:0071689]; myofibril assembly [GO:0030239]; myosin filament organization [GO:0031033]; protein stabilization [GO:0050821]; regulation of myosin II filament assembly [GO:0043520]; sarcomere organization [GO:0045214]; skeletal muscle myosin thick filament assembly [GO:0030241]
|
A band [GO:0031672]; cytoplasm [GO:0005737]; mitotic actomyosin contractile ring [GO:0110085]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; polytene chromosome puff [GO:0005703]; sarcomere [GO:0030017]; striated muscle myosin thick filament [GO:0005863]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; protein homodimerization activity [GO:0042803]; structural constituent of muscle [GO:0008307]
|
PF00063;PF02736;PF01576;
|
1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
| null | null | null | null | null |
FUNCTION: Muscle contraction.
|
Drosophila melanogaster (Fruit fly)
|
P05674
|
POLS_EEVV8
|
MFPFQPMYPMQPMPYRNPFAAPRRPWFPRTDPFLAMQVQELTRSMANLTFKQRRDAPPEGPSAKKPKKEASQKQKGGGQGKKKKNQGKKKAKTGPPNPKAQNGNKKKTNKKPGKRQRMVMKLESDKTFPIMLEGKINGYACVVGGKLFRPMHVEGKIDNDVLAALKTKKASKYDLEYADVPQNMRADTFKYTHEKPQGYYSWHHGAVQYENGRFTVPKGVGAKGDSGRPILDNQGRVVAIVLGGVNEGSRTALSVVMWNEKGVTVKYTPENCEQWSLVTTMCLLANVTFPCAQPPICYDRKPAETLAMLSVNVDNPGYDELLEAAVKCPGRKRRSTEELFNEYKLTRPYMARCIRCAVGSCHSPIAIEAVKSDGHDGYVRLQTSSQYGLDSSGNLKGRTMRYDMHGTIKEIPLHQVSLYTSRPCHIVDGHGYFLLARCPAGDSITMEFKKDSVRHSCSVPYEVKFNPVGRELYTHPPEHGVEQACQVYAHDAQNRGAYVEMHLPGSEVDSSLVSLSGSSVTVTPPDGTSALVECECGGTKISETINKTKQFSQCTKKEQCRAYRLQNDKWVYNSDKLPKAAGATLKGKLHVPFLLADGKCTVPLAPEPMITFGFRSVSLKLHPKNPTYLITRQLADEPHYTHELISEPAVRNFTVTEKGWEFVWGNHPPKRFWAQETAPGNPHGLPHEVITHYYHRYPMSTILGLSICAAIATVSVAASTWLFCRSRVACLTPYRLTPNARIPFCLAVLCCARTARAETTWESLDHLWNNNQQMFWIQLLIPLAALIVVTRLLRCVCCVVPFLVMAGAAAPAYEHATTMPSQAGISYNTIVNRAGYAPLPISITPTKIKLIPTVNLEYVTCHYKTGMDSPAIKCCGSQECTPTYRPDEQCKVFTGVYPFMWGGAYCFCDTENTQVSKAYVMKSDDCLADHAEAYKAHTASVQAFLNITVGEHSIVTTVYVNGETPVNFNGVKITAGPLSTAWTPFDRKIVQYAGEIYNYDFPEYGAGQPGAFGDIQSRTVSSSDLYANTNLVLQRPKAGAIHVPYTQAPSGFEQWKKDKAPSLKFTAPFGCEIYTNPIRAENCAVGSIPLAFDIPDALFTRVSETPTLSAAECTLNECVYSSDFGGIATVKYSASKSGKCAVHVPSGTATLKEAAVELTEQGSATIHFSTANIHPEFRLQICTSYVTCKGDCHPPKDHIVTHPQYHAQTFTAAVSKTAWTWLTSLLGGSAVIIIIGLVLATIVAMYVLTNQKHN
|
3.4.21.90
| null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]
|
PF01589;PF00943;PF01563;PF00944;
|
1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10;
| null |
PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2. The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle. {ECO:0000250|UniProtKB:P03315}.; PTM: [Capsid protein]: Phosphorylated on serine and threonine residues. {ECO:0000250|UniProtKB:P09592}.; PTM: [Spike glycoprotein E2]: Palmitoylated via thioester bonds. These palmitoylations may induce disruption of the C-terminus transmembrane. This would result in the reorientation of E2 C-terminus from lumenal to cytoplasmic side. {ECO:0000250|UniProtKB:P03315}.; PTM: [Spike glycoprotein E1]: N-glycosylated. {ECO:0000250|UniProtKB:P03315}.; PTM: [Spike glycoprotein E2]: N-glycosylated. {ECO:0000250|UniProtKB:P03315}.; PTM: [Assembly protein E3]: N-glycosylated. {ECO:0000250|UniProtKB:P03315}.; PTM: [6K protein]: Palmitoylated via thioester bonds. {ECO:0000250|UniProtKB:P03315}.
|
SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:P09592}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:P09592}.; SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR LOCATION: [6K protein]: Host cell membrane {ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein {ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03316};
| null | null | null | null |
FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity). Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (By similarity). Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles (By similarity). The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (By similarity). In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (By similarity). This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (By similarity). The uncoating might be triggered by the interaction of capsid proteins with ribosomes (By similarity). Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (By similarity). Inhibits host transcription (By similarity). Forms a tetrameric complex with XPO1/CRM1 and the nuclear import receptor importin (By similarity). This complex blocks the central channel of host nuclear pores thereby inhibiting the receptor-mediated nuclear transport and thus the host mRNA and rRNA transcription (By similarity). The inhibition of transcription is linked to a cytopathic effect on the host cell (By similarity). {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P09592, ECO:0000250|UniProtKB:P27284, ECO:0000250|UniProtKB:P36329}.; FUNCTION: [Assembly protein E3]: Provides the signal sequence for the translocation of the precursor of protein E3/E2 to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with spike glycoprotein E1 and mediates pH protection of the latter during the transport via the secretory pathway. After virion release from the host cell, the assembly protein E3 is gradually released in the extracellular space. {ECO:0000250|UniProtKB:P03315}.; FUNCTION: [Spike glycoprotein E2]: Plays a role in viral attachment to target host cell, by binding to the cell receptor LDLRAD3. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:P03315}.; FUNCTION: [6K protein]: Constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins. {ECO:0000250|UniProtKB:P03315}.; FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to cell receptor LDLRAD3 and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group. {ECO:0000250|UniProtKB:P03315}.
|
Venezuelan equine encephalitis virus (strain TC-83) (VEEV)
|
P05690
|
VIT2_CAEEL
|
MRSIIIASLVALALASSPAFERTFEPKTDYHYKFDGLVLSGLPSASSELSQSRISARARIQAVDDRYIHLQLVNIRMAASHLPESEQMPSLNSMEQRELSEEYKQMLELPLRAQLRNGLISELQFDKEDAEWSKNMKRAVVNMISFNPIAPRNEIEKIESSYDKEEQSEENTSFFTNEKTLEGDCQVAYTVIREQKKTIITKSINFDKCTERSEIAYGLRYSSECPECEKDTELIRPQTVYTYVLENEELKESEVRSLYTVNVNGQEVMKTETRSKLVLEENHSIKSHIKKVNGEKESIIYSSRWEQLVEDFFKNGDKAEFAPFEKFPLDKKMHLIKTITEQIQEVENNMPETSHFLARLVRIFRTTSTSQLKEIHETLYVKADKKIQSLMEHALAIAGTKNTIQHILVHMENEDILPLGQILKTIQETPFPSQSIAEALIKFAESRVAKNNLVVRQAAWLAAGSVVRGIVDYKNIRPLVREDKRELKEKFLRVFMQQYKDAETTYEKILALKTIGNAGLDISVNQLNEIIVDKRQPLPVRKEAIDALRLLKDTMPRKIQKVLLPIYKNRQYEPEIRMLALWRMMHTRPEESLLVQVVSQMEKETNQQVAALTHQMIRHFAMSTNPCYQRVAIVCSKVLSFTRYQPQEQMIASSYAQLPLFLQNSFSGAQFDFAAIFEKNSFLPKDLHASLDAVFGGNWNKYFAQIGFSQQHMDKYVQMALEKLESLEKESTTVVRGRRIQTGIKLLKELAQKMNIRARPATYTEKDAFAMVYLRYKDMDYAFLPIDRQLVENLIEKFTSNGKVQFSEIRRLLNQELEFETHHAAYFYEAIRKFPTTLGLPLTISGKIPTVISAEGQFSLELEGTELRLTVEARPSVAATHVYEMRMFTPLFEQGVKSVQSVRAYTPIKIQAVAGMKRNFEIVYKVVVPENQKSIVSLTTRPVVFLRFPGFSKFEYIEAEERTVVVPQWQQKTQEIEKVFNFLGLEVSTRGNILNQHTLENWLLAEQDFEVSVENKNRPAEFTARLTVGQLEKTELSQIKYNKIFEKEFELEQENTESRREYFNKMVKNIQKEQGYKSVISLKLEAPRDYTMNTELTTVCDKQVRMCQWEVEIRRSPILEETKEWTLRSQLLVVRPEMPSSLRQLRDQPHREVQLSLTSTWGSQKKSEVTVNAQLQQSKEQKKYERNMDRQFNGMPEYELLIKAARLNQINAVAEYKLTRETEQVLARYFDLVKTYNYWTVSSRPENNENDRVVVQLTVEPMSRQYVNITMQSPMERIELKNVQVPRVYLPSIAQRSVKHQLTEASGSVCKVQKNQIRTFDDVLYNTPLTTCYSLIAKDCSEEPTFAVLSKKTEKNSEEMIIKVIRGEQEIVAQLQNEEIRVKVDGKKIQSEDYSAYQIERLGESAIVIELPEGEVRFDGYTIKTQLPSYSRKNQLCGLCGNNDDESTNEFYTSDNTETEDIEEFHRSYLLKNEECEAEEERLSEKKNYRKYERDEEQSDEYSSEETYDYEQENTKKSQKNQRSQKKSDLVEKTQIKEFSHRICFSVEPVAECRRGYEVEQQQQRKIRFTCLQRHNRDASRLLKESRQQPLQLDDYPVSFVESVKVPTACVAY
| null | null | null |
cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; vesicle lumen [GO:0031983]; yolk granule [GO:0042718]
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lipid transporter activity [GO:0005319]; nutrient reservoir activity [GO:0045735]
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PF09172;PF01347;PF00094;
|
2.20.80.10;1.25.10.20;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26671266}.
| null | null | null | null | null |
FUNCTION: Precursor of the egg-yolk proteins that are sources of nutrients during embryonic development (Probable). Together with other vitellogenins, may play a role in modulating life-span, acting via induction of autophagy and lysosomal lipolysis (PubMed:26671266). {ECO:0000269|PubMed:26671266, ECO:0000305}.
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Caenorhabditis elegans
|
P05694
|
METE_YEAST
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MVQSAVLGFPRIGPNRELKKATEGYWNGKITVDELFKVGKDLRTQNWKLQKEAGVDIIPSNDFSFYDQVLDLSLLFNVIPDRYTKYDLSPIDTLFAMGRGLQRKATETEKAVDVTALEMVKWFDSNYHYVRPTFSKTTQFKLNGQKPVDEFLEAKELGIHTRPVLLGPVSYLFLGKADKDSLDLEPLSLLEQLLPLYTEILSKLASAGATEVQIDEPVLVLDLPANAQAAIKKAYTYFGEQSNLPKITLATYFGTVVPNLDAIKGLPVAALHVDFVRAPEQFDEVVAAIGNKQTLSVGIVDGRNIWKNDFKKSSAIVNKAIEKLGADRVVVATSSSLLHTPVDLNNETKLDAEIKGFFSFATQKLDEVVVITKNVSGQDVAAALEANAKSVESRGKSKFIHDAAVKARVASIDEKMSTRAAPFEQRLPEQQKVFNLPLFPTTTIGSFPQTKDIRINRNKFNKGTISAEEYEKFINSEIEKVIRFQEEIGLDVLVHGEPERNDMVQYFGEQINGYAFTVNGWVQSYGSRYVRPPIIVGDLSRPKAMSVKESVYAQSITSKPVKGMLTGPITCLRWSFPRDDVDQKTQAMQLALALRDEVNDLEAAGIKVIQVDEPALREGLPLREGTERSAYYTWAAEAFRVATSGVANKTQIHSHFCYSDLDPNHIKALDADVVSIEFSKKDDANYIAEFKNYPNHIGLGLFDIHSPRIPSKDEFIAKISTILKSYPAEKFWVNPDCGLKTRGWEETRLSLTHMVEAAKYFREQYKN
|
2.1.1.14
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
|
methionine biosynthetic process [GO:0009086]; methylation [GO:0032259]
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cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
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5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity [GO:0003871]; methionine synthase activity [GO:0008705]; zinc ion binding [GO:0008270]
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PF08267;PF01717;
|
3.20.20.210;
|
Vitamin-B12 independent methionine synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14;
| null |
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
| null | null |
FUNCTION: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
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Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05696
|
KPCA_RAT
|
MADVYPANDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVTDEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNVELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV
|
2.7.11.13
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:10562545, ECO:0000269|PubMed:19346474}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000269|PubMed:10562545, ECO:0000269|PubMed:19346474};
|
angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; cell population proliferation [GO:0008283]; cellular response to carbohydrate stimulus [GO:0071322]; central nervous system neuron axonogenesis [GO:0021955]; chondrocyte differentiation [GO:0002062]; desmosome assembly [GO:0002159]; establishment of protein localization [GO:0045184]; induction of positive chemotaxis [GO:0050930]; intracellular calcium ion homeostasis [GO:0006874]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway [GO:0097193]; learning or memory [GO:0007611]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of glucose import [GO:0046325]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of translation [GO:0017148]; neutrophil chemotaxis [GO:0030593]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of angiogenesis [GO:0045766]; positive regulation of angiotensin-activated signaling pathway [GO:0110063]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of bone resorption [GO:0045780]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of dense core granule biogenesis [GO:2000707]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exocytosis [GO:0045921]; positive regulation of inflammatory response [GO:0050729]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of synapse assembly [GO:0051965]; post-translational protein modification [GO:0043687]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of muscle contraction [GO:0006937]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of platelet aggregation [GO:0090330]; regulation of receptor-mediated endocytosis [GO:0048259]; regulation of response to osmotic stress [GO:0047484]; regulation of synaptic vesicle exocytosis [GO:2000300]; regulation of the force of heart contraction [GO:0002026]; response to corticosterone [GO:0051412]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to interleukin-1 [GO:0070555]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to reactive oxygen species [GO:0000302]; response to toxic substance [GO:0009636]; stem cell differentiation [GO:0048863]
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alphav-beta3 integrin-PKCalpha complex [GO:0035866]; apical part of cell [GO:0045177]; axon [GO:0030424]; calyx of Held [GO:0044305]; ciliary basal body [GO:0036064]; cone photoreceptor outer segment [GO:0120199]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; intercalated disc [GO:0014704]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; ooplasm [GO:1990917]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; presynaptic cytosol [GO:0099523]; protein-containing complex [GO:0032991]
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ATP binding [GO:0005524]; calcium,diacylglycerol-dependent serine/threonine kinase activity [GO:0004698]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; enzyme binding [GO:0019899]; histone H3T6 kinase activity [GO:0035403]; integrin binding [GO:0005178]; lipid binding [GO:0008289]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270]
|
PF00130;PF00168;PF00069;PF00433;
|
3.30.60.20;2.60.40.150;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15271671}. Cell membrane {ECO:0000269|PubMed:15271671, ECO:0000269|PubMed:19346474}; Peripheral membrane protein {ECO:0000305|PubMed:15271671}. Mitochondrion membrane {ECO:0000250|UniProtKB:P17252}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17252}. Nucleus {ECO:0000269|PubMed:15271671}. Note=Translocated to the nucleus upon treatment with PMA or IGF1. {ECO:0000269|PubMed:15271671}.
|
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=2.7.11.13; 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=2.7.11.13;
| null | null | null | null |
FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascades involving MAPK1/3 (ERK1/2) and RAP1GAP. Depending on the cell type, is involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation. In cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Depending on the cell type, exhibits anti-apoptotic function and protects cells from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, or mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (By similarity). Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (By similarity). Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteasomal degradation (By similarity). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (By similarity). {ECO:0000250|UniProtKB:P17252, ECO:0000250|UniProtKB:P20444, ECO:0000269|PubMed:11076962, ECO:0000269|PubMed:11864993, ECO:0000269|PubMed:15271671, ECO:0000269|PubMed:19176525}.
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Rattus norvegicus (Rat)
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P05704
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MCP3_ECOLI
|
MNTTPSQRLGFLHHIRLVPLFACILGGILVLFALSSALAGYFLWQADRDQRDVTAEIEIRTGLANSSDFLRSARINMIQAGAASRIAEMEAMKRNIAQAESEIKQSQQGYRAYQNRPVKTPADEALDTELNQRFQAYITGMQPMLKYAKNGMFEAIINHESEQIRPLDNAYTDILNKAVKIRSTRANQLAELAHQRTRLGGMFMIGAFVLALVMTLITFMVLRRIVIRPLQHAAQRIEKIASGDLTMNDEPAGRNEIGRLSRHLQQMQHSLGMTVGTVRQGAEEIYRGTSEISAGNADLSSRTEEQAAAIEQTAASMEQLTATVKQNADNAHHASKLAQEASIKASDGGQTVSGVVKTMGAISTSSKKISEITAVINSIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTLASRSAQAAKEIEGLISESVRLIDLGSDEVATAGKTMSTIVDAVASVTHIMQEIAAASDEQSRGITQVSQAISEMDKVTQQNASLVEEASAAAVSLEEQAARLTEAVDVFRLHKHSVSAEPRGAGEPVSFATV
| null | null |
chemotaxis [GO:0006935]; signal transduction [GO:0007165]
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methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886]
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protein homodimerization activity [GO:0042803]; transmembrane signaling receptor activity [GO:0004888]
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PF00672;PF00015;PF02203;
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1.20.120.30;1.10.287.950;
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Methyl-accepting chemotaxis (MCP) protein family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles.
| null | null | null | null | null |
FUNCTION: Mediates taxis to the sugars ribose and galactose via an interaction with the periplasmic ribose- or galactose-binding proteins.; FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
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Escherichia coli (strain K12)
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P05708
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HXK1_RAT
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MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGIQNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPDSDVRFLLSESGTGKGAAMVTAVAYRLAEQHRQIEETLAHFRLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCTVSFLLSEDGSGKGAALITAVGVRLRGDPSIA
|
2.7.1.1
| null |
canonical glycolysis [GO:0061621]; carbohydrate phosphorylation [GO:0046835]; establishment of protein localization to mitochondrion [GO:0072655]; fructose 6-phosphate metabolic process [GO:0006002]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intracellular glucose homeostasis [GO:0001678]; maintenance of protein location in mitochondrion [GO:0072656]; mannose metabolic process [GO:0006013]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cytokine production involved in immune response [GO:0002720]; positive regulation of interleukin-1 beta production [GO:0032731]; response to brassinosteroid [GO:0009741]; response to hypoxia [GO:0001666]; response to ischemia [GO:0002931]; response to ketamine [GO:1901986]
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caveola [GO:0005901]; cytosol [GO:0005829]; membrane raft [GO:0045121]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]
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ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucosamine kinase activity [GO:0047931]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; identical protein binding [GO:0042802]; mannokinase activity [GO:0019158]; peptidoglycan binding [GO:0042834]; protein kinase activity [GO:0004672]; protein-containing complex binding [GO:0044877]
|
PF00349;PF03727;
|
3.30.420.40;3.40.367.20;
|
Hexokinase family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P19367}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19367}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P19367}. Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane. Dissociates from the mitochondrial outer membrane following inhibition by N-acetyl-D-glucosamine, leading to relocation to the cytosol. {ECO:0000250|UniProtKB:P19367}.
|
CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:3579310, ECO:0000269|PubMed:5871820}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:3579310, ECO:0000269|PubMed:5871820}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:5871820}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:5871820}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:5871820}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000269|PubMed:5871820}; CATALYTIC ACTIVITY: Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+); Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:13211595}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; Evidence={ECO:0000269|PubMed:13211595}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+); Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000250|UniProtKB:P19367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10949; Evidence={ECO:0000250|UniProtKB:P19367};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44 uM for D-glucose {ECO:0000269|PubMed:5871820}; KM=3.1 mM for D-fructose {ECO:0000269|PubMed:5871820}; KM=0.42 mM for ATP {ECO:0000269|PubMed:5871820};
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PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:5871820}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:5871820}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively) (PubMed:13211595, PubMed:3579310, PubMed:5871820). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:13211595, PubMed:5871820). Involved in innate immunity and inflammation by acting as a pattern recognition receptor for bacterial peptidoglycan (By similarity). When released in the cytosol, N-acetyl-D-glucosamine component of bacterial peptidoglycan inhibits the hexokinase activity of HK1 and causes its dissociation from mitochondrial outer membrane, thereby activating the NLRP3 inflammasome (By similarity). {ECO:0000250|UniProtKB:P19367, ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:3579310, ECO:0000269|PubMed:5871820}.
|
Rattus norvegicus (Rat)
|
P05709
|
SIM_DROME
|
MTNHRRVRKDCYESRLHDIAKTCAMKEKSKNAARTRREKENTEFCELAKLLPLPAAITSQLDKASVIRLTTSYLKMRQVFPDGLGEAWGSSPAMQRGATIKELGSHLLQTLDGFIFVVAPDGKIMYISETASVHLGLSQVELTGNSIFEYIHNYDQDEMNAILSLHPHINQHPLAQTHTPIGSPNGVQHPSAYDHDRGSHTIEIEKTFFLRMKCVLAKRNAGLTTSGFKVIHCSGYLKARIYPDRGDGQGSLIQNLGLVAVGHSLPSSAITEIKLHQNMFMFRAKLDMKLIFFDARVSQLTGYEPQDLIEKTLYQYIHAADIMAMRCSHQILLYKGQVTTKYYRFLTKGGGWVWVQSYATLVHNSRSSREVFIVSVNYVLSEREVKDLVLNEIQTGVVKREPISPAAQAAQAAQAAQAAQAAQAAQAAQAAQAAQAAHVAQAVQAQVVVVPQQSVVVQPQCAGATGQPVGPGTPVSLALSASPKLDPYFEPELPLQPAVTPVPPTNNSSSSSNNNNGVWHHHHVQQQQQSGSMDHDSLSYTQLYPPLNDLVVSSSSSVGGGTASSAGGGSSASASSSGVYSTEMQYPDTTTGNLYYNNNNHYYYDYDATVDVATSMIRPFSANSNSCSSSSESERQLSTGNASIVNETSPSQTTYSDLSHNFELSYFSDNSSQQHQHQQQQQHLMEQQHLQYQYATW
| null | null |
adult walking behavior [GO:0007628]; axonogenesis [GO:0007409]; brain development [GO:0007420]; determination of genital disc primordium [GO:0035225]; ectoderm development [GO:0007398]; locomotion [GO:0040011]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; ventral cord development [GO:0007419]; ventral midline development [GO:0007418]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF00010;PF00989;PF08447;
|
4.10.280.10;3.30.450.20;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:3345560}.
| null | null | null | null | null |
FUNCTION: Transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord (PubMed:12221007, PubMed:1760843, PubMed:9840810). Required to correctly specify the formation of the central brain complex, which controls walking behavior (PubMed:12221007, PubMed:1760843, PubMed:9840810). Also required for correct patterning of the embryonic genital disk and anal pad anlage (PubMed:12221007, PubMed:1760843, PubMed:9840810). Plays a role in synapse development (PubMed:23644463). {ECO:0000269|PubMed:12221007, ECO:0000269|PubMed:1760843, ECO:0000269|PubMed:23644463, ECO:0000269|PubMed:9840810}.
|
Drosophila melanogaster (Fruit fly)
|
P05710
|
PRLR_RAT
|
MPSALAFVLLVLNISLLKGQSPPGKPEIHKCRSPDKETFTCWWNPGTDGGLPTNYSLTYSKEGEKTTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNQMGSSSSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWSPPTITDVKTGWFTMEYEIRLKPEEAEEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWSQESSVEMPNDFTLKDTTVWIIVAILSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERLMPSHSKEYPGQGVKPTHLDPDSDSGHGSYDSHSLLSEKCEEPQAYPPTLHIPEITEKPENPEANIPPTVDPQSTNPNFHVDAPKSSTWPLLPGQHMPRSPYHSVADVCKLAGSPVNTLDSFLDKAEENVLKLSKALETGEEEVAEQKGAKSFPSDKQNTPWPLLQEKSPTVYVKPPDYVEIHKVNKDGVLSLFPKQRENNQTEKPGVPETSKEYAKVSGITDNNILVLVPDSRAQNTALLEESAKKAPPSFEADQSEKDLASFTATSSNRRLQLGRLDYLDPTCFMHSFH
| null | null |
cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cytokine-mediated signaling pathway [GO:0019221]; lactation [GO:0007595]; mammary gland alveolus development [GO:0060749]; mammary gland epithelial cell differentiation [GO:0060644]; mammary gland epithelium development [GO:0061180]; negative regulation of apoptotic process [GO:0043066]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of protein autophosphorylation [GO:0031954]; prostate gland growth [GO:0060736]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cell adhesion [GO:0030155]; regulation of epithelial cell differentiation [GO:0030856]; response to bacterium [GO:0009617]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
cytokine binding [GO:0019955]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; peptide hormone binding [GO:0017046]; prolactin receptor activity [GO:0004925]; protein kinase binding [GO:0019901]
|
PF09067;PF00041;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 1 subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: This is a receptor for the anterior pituitary hormone prolactin.
|
Rattus norvegicus (Rat)
|
P05712
|
RAB2A_RAT
|
MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTMGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHAATNASHGGNQGGQQAGGGCC
|
3.6.5.2
| null |
Golgi organization [GO:0007030]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; vesicle-mediated transport [GO:0016192]
|
acrosomal vesicle [GO:0001669]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; melanosome [GO:0042470]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; synaptic vesicle membrane [GO:0030672]
|
GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P61019}; Lipid-anchor {ECO:0000250|UniProtKB:P61019}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P61019}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61019}; Lipid-anchor {ECO:0000250|UniProtKB:P61019}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P61019}; Lipid-anchor {ECO:0000250|UniProtKB:P61019}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53994}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P53994}; Lipid-anchor {ECO:0000250|UniProtKB:P61019}; Cytoplasmic side {ECO:0000305}. Note=Localized in the Golgi apparatus in the round spermatids and in the acrosome in the elongating spermatid (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P53994, ECO:0000250|UniProtKB:P61019}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P53994}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P53994};
| null | null | null | null |
FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Required for protein transport from the endoplasmic reticulum to the Golgi complex. Regulates the compacted morphology of the Golgi (By similarity). Together with RAB2B redundantly required for efficient autophagic flux (By similarity). {ECO:0000250|UniProtKB:P53994, ECO:0000250|UniProtKB:P61019}.
|
Rattus norvegicus (Rat)
|
P05714
|
RAB4A_RAT
|
MAQTAMSETYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFMQCARKILNKIESGELDPERMGSGIQYGDAALRQLRSPRRTQAPSAQECGC
|
3.6.5.2
| null |
antigen processing and presentation [GO:0019882]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; regulation of endocytosis [GO:0030100]; small GTPase-mediated signal transduction [GO:0007264]; vesicle-mediated transport [GO:0016192]
|
cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; insulin-responsive compartment [GO:0032593]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic recycling endosome [GO:0098837]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; synaptic vesicle membrane [GO:0030672]; vesicle [GO:0031982]
|
ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ionotropic glutamate receptor binding [GO:0035255]; syntaxin binding [GO:0019905]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
|
PTM: Serotonylation of Gln-72 by TGM2 during activation and aggregation of platelets leads to constitutive activation of GTPase activity. {ECO:0000250|UniProtKB:P56371}.; PTM: Phosphorylated by CDK1 kinase during mitosis. {ECO:0000250|UniProtKB:P20338}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P20338}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20338}. Cytoplasm {ECO:0000250|UniProtKB:P20338}. Early endosome membrane {ECO:0000269|PubMed:20098723}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:20098723}; Peripheral membrane protein {ECO:0000305}. Note=Generally associated with membranes. Cytoplasmic when phosphorylated by CDK1. {ECO:0000250|UniProtKB:P20338}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P20338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P20338};
| null | null | null | null |
FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (By similarity). Involved in protein transport. Plays a role in vesicular traffic. Mediates VEGFR2 endosomal trafficking to enhance VEGFR2 signaling (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity). {ECO:0000250|UniProtKB:P20338, ECO:0000250|UniProtKB:P56371}.
|
Rattus norvegicus (Rat)
|
P05725
|
DNE1_CHLRE
|
MNTKYNKEFLLYLAGFVDGDGSIIAQIKPNQSYKFKHQLSLTFQVTQKTQRRWFLDKLVDEIGVGYVRDRGSVSDYILSEIKPLHNFLTQLQPFLKLKQKQANLVLKIIEQLPSAKESPDKFLEVCTWVDQIAALNDSKTRKTTSETVRAVLDSLSEKKKSSP
|
3.1.-.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550}; Note=Binds 3 Mg(2+) ions per homodimer. The enzyme can also utilize Mn(2+) or Co(2+), but has lower cleavage activity with Ni(2+) or Zn(2+). Ca(2+) Co(2+) give no enzyme activity. {ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550};
|
intron homing [GO:0006314]
|
chloroplast [GO:0009507]
|
endonuclease activity [GO:0004519]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
|
PF00961;
|
3.10.28.10;
|
LAGLIDADG endonuclease family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast.
| null | null | null | null | null |
FUNCTION: Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site.
|
Chlamydomonas reinhardtii (Chlamydomonas smithii)
|
P05737
|
RL7A_YEAST
|
MAAEKILTPESQLKKSKAQQKTAEQVAAERAARKAANKEKRAIILERNAAYQKEYETAERNIIQAKRDAKAAGSYYVEAQHKLVFVVRIKGINKIPPKPRKVLQLLRLTRINSGTFVKVTKATLELLKLIEPYVAYGYPSYSTIRQLVYKRGFGKINKQRVPLSDNAIIEANLGKYGILSIDDLIHEIITVGPHFKQANNFLWPFKLSNPSGGWGVPRKFKHFIQGGSFGNREEFINKLVKSMN
| null | null |
cytoplasmic translation [GO:0002181]; maturation of LSU-rRNA [GO:0000470]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; ribosomal large subunit biogenesis [GO:0042273]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]
|
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF00327;PF08079;
|
3.30.1390.20;
|
Universal ribosomal protein uL30 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05739
|
RL6B_YEAST
|
MTAQQAPKWYPSEDVAAPKKTRKAVRPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLVTGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQTKEIKTERVEDQKVVDKALLAEIKKTPLLKQYLSASFSLKNGDKPHLLKF
| null | null |
cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027]
|
cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]
|
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF01159;
|
2.30.30.30;
|
Eukaryotic ribosomal protein eL6 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05740
|
RL17A_YEAST
|
MARYGATSTNPAKSASARGSYLRVSFKNTRETAQAINGWELTKAQKYLEQVLDHQRAIPFRRFNSSIGRTAQGKEFGVTKARWPAKSVKFVQGLLQNAAANAEAKGLDATKLYVSHIQVNQAPKQRRRTYRAHGRINKYESSPSHIELVVTEKEEAVAKAAEKKVVRLTSRQRGRIAAQKRIAA
| null | null |
cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000448]; cytoplasmic translation [GO:0002181]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; preribosome, large subunit precursor [GO:0030687]
|
structural constituent of ribosome [GO:0003735]
|
PF00237;
|
3.90.470.10;
|
Universal ribosomal protein uL22 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05744
|
RL33A_YEAST
|
MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQDAQFYLGKRIAYVYRASKEVRGSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI
| null | null |
cytoplasmic translation [GO:0002181]; ribosomal large subunit biogenesis [GO:0042273]
|
cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]
|
structural constituent of ribosome [GO:0003735]
|
PF01247;
|
2.40.10.190;
|
Eukaryotic ribosomal protein eL33 family
|
PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05745
|
RL36A_YEAST
|
MTVKTGIAIGLNKGKKVTSMTPAPKISYKKGAASNRTKFVRSLVREIAGLSPYERRLIDLIRNSGEKRARKVAKKRLGSFTRAKAKVEEMNNIIAASRRH
| null | null |
cytoplasmic translation [GO:0002181]
|
cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]
|
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF01158;
|
1.10.10.1760;
|
Eukaryotic ribosomal protein eL36 family
|
PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05748
|
RL15A_YEAST
|
MGAYKYLEELQRKKQSDVLRFLQRVRVWEYRQKNVIHRAARPTRPDKARRLGYKAKQGFVIYRVRVRRGNRKRPVPKGATYGKPTNQGVNELKYQRSLRATAEERVGRRAANLRVLNSYWVNQDSTYKYFEVILVDPQHKAIRRDARYNWICDPVHKHREARGLTATGKKSRGINKGHKFNNTKAGRRKTWKRQNTLSLWRYRK
| null | null |
cytoplasmic translation [GO:0002181]
|
cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]
|
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF00827;
|
3.40.1120.10;
|
Eukaryotic ribosomal protein eL15 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05750
|
RS3_YEAST
|
MVALISKKRKLVADGVFYAELNEFFTRELAEEGYSGVEVRVTPTKTEVIIRATRTQDVLGENGRRINELTLLVQKRFKYAPGTIVLYAERVQDRGLSAVAQAESMKFKLLNGLAIRRAAYGVVRYVMESGAKGCEVVVSGKLRAARAKAMKFADGFLIHSGQPVNDFIDTATRHVLMRQGVLGIKVKIMRDPAKSRTGPKALPDAVTIIEPKEEEPILAPSVKDYRPAEETEAQAEPVEA
| null | null |
cytoplasmic translation [GO:0002181]; positive regulation of apoptotic signaling pathway [GO:2001235]; ribosomal small subunit export from nucleus [GO:0000056]; ribosomal subunit export from nucleus [GO:0000054]
|
90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]; preribosome, small subunit precursor [GO:0030688]
|
DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF07650;PF00189;
|
3.30.300.20;3.30.1140.32;
|
Universal ribosomal protein uS3 family
|
PTM: Ubiquitinated at Lys-212 in response to stalled ribosomes (PubMed:28757607, PubMed:28943311, PubMed:30718516, PubMed:30893611, PubMed:31819057). Ubiquitination leads to activation of the No-Go Decay (NGD) pathway and degradation of non-functional 18S rRNA: first monoubiquitinated at Lys-212 by MAG2, followed by formation of 'Lys-63'-linked polyubiquitin chains on monoubiquitin by HEL2 and RSP5 (PubMed:30893611). {ECO:0000269|PubMed:28757607, ECO:0000269|PubMed:28943311, ECO:0000269|PubMed:30718516, ECO:0000269|PubMed:30893611, ECO:0000269|PubMed:31819057}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05755
|
RS9B_YEAST
|
MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKREIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAAEEAEDEE
| null | null |
maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; positive regulation of translational fidelity [GO:0045903]; ribosomal small subunit biogenesis [GO:0042274]; translation [GO:0006412]
|
90S preribosome [GO:0030686]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; small-subunit processome [GO:0032040]
|
rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]
|
PF00163;PF01479;
|
3.10.290.10;
|
Universal ribosomal protein uS4 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835). {ECO:0000269|PubMed:15590835, ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05756
|
RS13_YEAST
|
MGRMHSAGKGISSSAIPYSRNAPAWFKLSSESVIEQIVKYARKGLTPSQIGVLLRDAHGVTQARVITGNKIMRILKSNGLAPEIPEDLYYLIKKAVSVRKHLERNRKDKDAKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVN
| null | null |
cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]
|
90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]
|
small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735]
|
PF08069;PF00312;
|
4.10.860.130;1.10.287.10;
|
Universal ribosomal protein uS15 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05759
|
RS31_YEAST
|
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKVYTTPKKIKHKHKKVKLAVLSYYKVDAEGKVTKLRRECSNPTCGAGVFLANHKDRLYCGKCHSVYKVNA
| null | null |
cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) [GO:0002109]; modification-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567]; ribosomal small subunit assembly [GO:0000028]; ribosome biogenesis [GO:0042254]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; protein tag activity [GO:0031386]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625]
|
PF01599;PF00240;
|
6.20.50.150;
|
Ubiquitin family; Eukaryotic ribosomal protein eS31 family
| null |
SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Cytoplasm {ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). {ECO:0000250}.; FUNCTION: [Small ribosomal subunit protein eS31]: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05764
|
RS21_SCHPO
|
MENEAGQLVDLYVPRKCSATNRIIQAKDHASVQINVCAVDAEGRQIPGEKTTYAISGFVRSKGESDDCINRLTTQDGLLEGVWSYQR
| null | null |
cytoplasmic translational elongation [GO:0002182]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000461]; ribosomal small subunit biogenesis [GO:0042274]
|
cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]
|
structural constituent of ribosome [GO:0003735]
|
PF01249;
|
3.30.1230.20;
|
Eukaryotic ribosomal protein eS21 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14623272, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (By similarity). eS21 is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability (PubMed:14623272). {ECO:0000250|UniProtKB:P0C0V8, ECO:0000269|PubMed:14623272}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P05769
|
POLG_MVEV5
|
MSKKPGGPGKPRVVNMLKRGIPRVFPLVGVKRVVMNLLDGRGPIRFVLALLAFFRFTALAPTKALMRRWKSVNKTTAMKHLTSFKKELGTLIDVVNKRGKKQKKRGGSETSVLMLIFMLIGFAAALKLSTFQGKIMMTVNATDIADVIAIPTPKGPNQCWIRAIDIGFMCDDTITYECPKLESGNDPEDIDCWCDKQAVYVNYGRCTRARHSKRSRRSITVQTHGESTLVNKKDAWLDSTKATRYLTKTENWIIRNPGYALVAVVLGWMLGSNTGQKVIFTVLLLLVAPAYSFNCLGMSSRDFIEGASGATWVDLVLEGDSCITIMAADKPTLDIRMMNIEATNLALVRNYCYAATVSDVSTVSNCPTTGESHNTKRADHNYLCKRGVTDRGWGNGCGLFGKGSIDTCAKFTCSNSAAGRLILPEDIKYEVGVFVHGSTDSTSHGNYSTQIGANQAVRFTISPNAPAITAKMGDYGEVTVECEPRSGLNTEAYYVMTIGTKHFLVHREWFNDLLLPWTSPASTEWRNREILVEFEEPHATKQSVVALGSQEGALHQALAGAIPVEFSSSTLKLTSGHLKCRVKMEKLKLKGTTYGMCTEKFTFSKNPADTGHGTVVLELQYTGSDGPCKIPISSVASLNDMTPVGRMVTANPYVASSTANAKVLVEIEPPFGDSYIVVGRGDKQINHHWHKEGSSIGKAFSTTLKGAQRLAALGDTAWDFGSVGGVFNSIGKAVHQVFGGAFRTLFGGMSWISPGLLGALLLWMGVNARDKSIALAFLATGGVLLFLATNVHADTGCAIDITRRELKCGSGIFIHNDVEAWIDRYKYLPETPKQLAKVVENAHKSGICGIRSVNRFEHQMWESVRDELNALLKENAIDLSVVVEKQKGMYRAAPNRLRLTVEELDIGWKAWGKSLLFAAELANSTFVVDGPETAECPNSKRAWNSFEIEDFGFGITSTRGWLKLREENTSECDSTIIGTAVKGNHAVHSDLSYWIESGLNGTWKLERAIFGEVKSCTWPETHTLWGDAVEETELIIPVTLAGPRSKHNRREGYKVQVQGPWDEEDIKLDFDYCPGTTVTVSEHCGKRGPSVRTTTDSGKLVTDWCCRSCTLPPLRFTTASGCWYGMEIRPMKHDESTLVKSRVQAFNGDMIDPFQLGLLVMFLATQEVLRKRWTARLTLPAAVGALLVLLLGGITYTDLVRYLILVGSAFAESNNGGDVIHLALIAVFKVQPAFLVASLTRSRWTNQENLVLVLGAAFFQMAASDLELTIPGLLNSAATAWMVLRAMAFPSTSAIAMPMLAMLAPGMRMLHLDTYRIVLLLIGICSLLNERRRSVEKKKGAVLIGLALTSTGYFSPTIMAAGLMICNPNKKRGWPATEVLTAVGLMFAIVGGLAELDIDSMSVPFTIAGLMLVSYVISGKATDMWLERAADVSWEAGAAITGTSERLDVQLDDDGDFHLLNDPGVPWKIWVLRMTCLSVAAITPRAILPSAFGYWLTLKYTKRGGVFWDTPSPKVYPKGDTTPGVYRIMARGILGRYQAGVGVMHEGVFHTLWHTTRGAAIMSGEGRLTPYWGNVKEDRVTYGGPWKLDQKWNGVDDVQMIVVEPGKPAINVQTKPGIFKTAHGEIGAVSLDYPIGTSGSPIVNSNGEIIGLYGNGVILGNGAYVSAIVQGERVEEPVPEAYNPEMLKKRQLTVLDLHPGAGKTRRILPQIIKDAIQKRLRTAVLAPTRVVAAEMAEALRGLPVRYLTPAVQREHSGNEIVDVMCHATLTHRLMSPLRVPNYNLFVMDEAHFTDPASIAARGYIATRVEAGEAAAIFMTATPPGTSDPFPDTNSPVHDVSSEIPDRAWSSGFEWITDYAGKTVWFVASVKMSNEIAQCLQRAGKRVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILDEGEGRVILSVPSAITSASAAQRRGRVGRNPSQIGDEYHYGGGTSEDDTMLAHWTEAKILLDNIHLPNGLVAQLYGPERDKTYTMDGEYRLRGEERKTFLELIKTADLPVWLAYKVASNGIQYNDRKWCFDGPRSNIILEDNNEVEIITRIGERKVLKPRWLDARVYSDHQSLKWFKDFAAGKRSAIGFFEVLGRMPEHFAGKTREALDTMYLVATSEKGGKAHRMALEELPDALETITLIAALGVMTAGFFLLMMQRKGIGKLGLGALVLVVATFFLWMSDVSGTKIAGVLLLALLMMVVLIPEPEKQRSQTDNQLAVFLICVLLVVGLVAANEYGMLERTKTDIRNLFGKSLIEENEVHIPPFDFFTLDLKPATAWALYGGSTVVLTPLIKHLVTSQYVTTSLASINAQAGSLFTLPKGIPFTDFDLSVALVFLGCWGQVTLTTLIMATILVTLHYGYLLPGWQAEALRAAQKRTAAGIMKNAVVDGIVATDVPELERTTPQMQKRLGQILLVLASVAAVCVNPRITTIREAGILCTAAALTLWDNNASAAWNSTTATGLCHVMRGSWIAGASIAWTLIKNAEKPAFKRGRAGGRTLGEQWKEKLNAMGKEEFFSYRKEAILEVDRTEARRARREGNKVGGHPVSRGTAKLRWLVERRFVQPIGKVVDLGCGRGGWSYYAATMKNVQEVRGYTKGGPGHEEPMLMQSYGWNIVTMKSGVDVFYKPSEISDTLLCDIGESSPSAEIEEQRTLRILEMVSDWLSRGPKEFCIKILCPYMPKVIEKLESLQRRFGGGLVRVPLSRNSNHEMYWVSGASGNIVHAVNMTSQVLIGRMDKKIWKGPKYEEDVNLGSGTRAVGKGVQHTDYKRIKSRIEKLKEEYAATWHTDDNHPYRTWTYHGSYEVKPSGSASTLVNGVVRLLSKPWDAITGVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPQGVKTVMDETTNWLWAYLARNKKARLCTREEFVKKVNSHAALGAMFEEQNQWKNAREAVEDPKFWEMVDEERECHLRGECRTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWMSRENSGGGVEGAGIQKLGYILRDVAQKPGGKIYADDTAGWDTRITQADLENEAKVLELMEGEQRTLARAIIELTYRHKVVKVMRPAAGGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEAVIGPDDIESIERKKKFAVRTWLFENAEERVQRMAVSGDDCVVKPLDDRFSTALHFLNAMSKVRKDIQEWKPSQGWYDWQQVPFCSNHFQEVIMKDGRTLVVPCRGQDELIGRARISPGSGWNVRDTACLAKAYAQMWLVLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLSVWNRVWILENEWMEDKTTVSDWTEVPYVGKREDIWCGSLIGTRTRATWAENIYAAINQVRSVIGKEKYVDYVQSLRRYEETHVSEDRVL
|
2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13
| null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]
|
PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949;
|
1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10;
|
Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family
|
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000269|PubMed:20207389, ECO:0000269|PubMed:26377679, ECO:0000269|PubMed:7494334, ECO:0000269|PubMed:8392191, ECO:0000269|PubMed:9499070}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000269|PubMed:2441520}.; PTM: [Non-structural protein 1]: N-glycosylated (PubMed:11514736). The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:11514736}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.
|
SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
|
CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; 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; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:19793813}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
| null | null | null | null |
FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:19793813}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
|
Murray valley encephalitis virus (strain MVE-1-51) (MVEV)
|
P05770
|
APOE_PAPAN
|
MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH
| null | null |
cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of neuron apoptotic process [GO:0043524]; neuron projection development [GO:0031175]; positive regulation of amyloid-beta clearance [GO:1900223]; triglyceride-rich lipoprotein particle clearance [GO:0071830]; very-low-density lipoprotein particle clearance [GO:0034447]
|
chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361]
|
amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326]
|
PF01442;
|
1.20.120.20;
|
Apolipoprotein A1/A4/E family
|
PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02649}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000250|UniProtKB:P02649}.
| null | null | null | null | null |
FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. {ECO:0000250|UniProtKB:P02649}.
|
Papio anubis (Olive baboon)
|
P05771
|
KPCB_HUMAN
|
MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV
|
2.7.11.13
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P68403};
|
adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; calcium ion transport [GO:0006816]; cellular response to carbohydrate stimulus [GO:0071322]; dibenzo-p-dioxin metabolic process [GO:0018894]; intracellular calcium ion homeostasis [GO:0006874]; intracellular signal transduction [GO:0035556]; lipoprotein transport [GO:0042953]; mitotic nuclear membrane disassembly [GO:0007077]; negative regulation of glucose transmembrane transport [GO:0010829]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway [GO:0007207]; positive regulation of angiogenesis [GO:0045766]; positive regulation of B cell receptor signaling pathway [GO:0050861]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of insulin secretion [GO:0032024]; positive regulation of odontogenesis of dentin-containing tooth [GO:0042488]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; post-translational protein modification [GO:0043687]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; protein phosphorylation [GO:0006468]; regulation of dopamine secretion [GO:0014059]; regulation of glucose transmembrane transport [GO:0010827]; regulation of growth [GO:0040008]; regulation of synaptic vesicle exocytosis [GO:2000300]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ethanol [GO:0045471]; response to glucose [GO:0009749]; response to vitamin D [GO:0033280]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]
|
brush border membrane [GO:0031526]; calyx of Held [GO:0044305]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynaptic cytosol [GO:0099523]; spectrin [GO:0008091]
|
ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein kinase C binding [GO:0005080]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270]
|
PF00130;PF00168;PF00069;PF00433;
|
3.30.60.20;2.60.40.150;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
|
PTM: Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Autophosphorylation on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20228790}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
|
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=2.7.11.13; Evidence={ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25982116}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25982116}; 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=2.7.11.13; Evidence={ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25313067}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:20228790};
| null | null | null | null |
FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity (PubMed:11598012). Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A (PubMed:20228790). In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1 (PubMed:25982116). Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (PubMed:19176525). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). {ECO:0000250|UniProtKB:P68404, ECO:0000269|PubMed:11598012, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25313067, ECO:0000269|PubMed:25982116}.
|
Homo sapiens (Human)
|
P05772
|
KPCB_RABIT
|
MADPAAGQPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDREVLIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPEGSEGNEELRQKFERAKIGQGTKTPEEKTTNTISKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKDHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV
|
2.7.11.13
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P68403};
|
adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; intracellular signal transduction [GO:0035556]; negative regulation of glucose transmembrane transport [GO:0010829]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of B cell receptor signaling pathway [GO:0050861]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; post-translational protein modification [GO:0043687]; regulation of glucose transmembrane transport [GO:0010827]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein serine kinase activity [GO:0106310]; zinc ion binding [GO:0008270]
|
PF00130;PF00168;PF00069;PF00433;
|
3.30.60.20;2.60.40.150;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
|
PTM: Phosphorylation on 'Thr-499' of isoform beta-I, within the activation loop, renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly, isoform beta-II is autophosphorylated on 'Thr-640' and 'Ser-659', subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
|
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=2.7.11.13; 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=2.7.11.13;
| null | null | null | null |
FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1. Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (By similarity). {ECO:0000250|UniProtKB:P05771, ECO:0000250|UniProtKB:P68404}.
|
Oryctolagus cuniculus (Rabbit)
|
P05777
|
M1_I33A0
|
MSLLTEVETYVLSIVPSGPLKAEIAQRLEDVFAGKNTDLEVLMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQRRRFVQNALNGNGDPNNMDKAVKLYRKLKREITFHGAKEIALSYSAGALASCMGLIYNRMGAVTTEVAFGLVCATCEQIADSQHRSHRQMVTTTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMDIASQARQMVQAMRTIGTHPSSSAGLKDDLLENLQAYQKRMGVQMQRFK
| null | null |
viral budding from plasma membrane [GO:0046761]
|
host cell nucleus [GO:0042025]; membrane [GO:0016020]; virion membrane [GO:0055036]
|
RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]
|
PF00598;PF08289;
|
1.10.10.180;1.20.91.10;
|
Influenza viruses Matrix protein M1 family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04068}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04068}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04068}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04068}.
| null | null | null | null | null |
FUNCTION: Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place. {ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:12604801}.; FUNCTION: Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms. {ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:12604801}.
|
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
|
P05779
|
M2_I30A0
|
MSLPTEVETPTRNEWGCRCNDSSDHITIAAKFIGILHLILWILDRLFFKCIYRRLKYGPKRGPSTEGVPDSMREEYRQKQQNAADVDDGHFVNIELE
| null | null |
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
|
monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
|
PF00599;
|
6.10.250.1640;
|
Influenza viruses matrix protein M2 family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
| null | null | null | null | null |
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
Influenza A virus (strain A/Swine/Iowa/15/1930 H1N1)
|
P05780
|
M2_I33A0
|
MSLLTEVETPIRNEWGCRCNDSSDPLVIAANIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRKEQQNAVDVDDGHFVNIELE
| null | null |
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
|
monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
|
PF00599;
|
6.10.250.1640;
|
Influenza viruses matrix protein M2 family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069, ECO:0000269|PubMed:1501289}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069, ECO:0000269|PubMed:1501289}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069, ECO:0000269|PubMed:1501289}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
| null | null | null | null | null |
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
|
P05783
|
K1C18_HUMAN
|
MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFNLGDALDSSNSMQTIQKTTTRRIVDGKVVSETNDTKVLRH
| null | null |
anatomical structure morphogenesis [GO:0009653]; cell cycle [GO:0007049]; extrinsic apoptotic signaling pathway [GO:0097191]; Golgi to plasma membrane protein transport [GO:0043001]; hepatocyte apoptotic process [GO:0097284]; intermediate filament cytoskeleton organization [GO:0045104]; negative regulation of apoptotic process [GO:0043066]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
adherens junction [GO:0005912]; cell periphery [GO:0071944]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; microtubule organizing center [GO:0005815]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]
|
cadherin binding involved in cell-cell adhesion [GO:0098641]; RNA binding [GO:0003723]; scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6. {ECO:0000269|PubMed:15368451, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8609167, ECO:0000269|PubMed:9524113}.; PTM: Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7. {ECO:0000269|PubMed:9298992}.; PTM: O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.
|
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
| null | null | null | null | null |
FUNCTION: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}.
|
Homo sapiens (Human)
|
P05784
|
K1C18_MOUSE
|
MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGIQTEKETMQDLNDRLASYLDKVKSLETENRRLESKIREHLEKKGPQGVRDWGHYFKIIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVKYETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSKIMADIRAQYEALAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLTELRRTLQTLEIDLDSMKNQNINLENSLGDVEARYKAQMEQLNGVLLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFSLNDALDSSNSMQTVQKTTTRKIVDGRVVSETNDTRVLRH
| null | null |
extrinsic apoptotic signaling pathway [GO:0097191]; Golgi to plasma membrane protein transport [GO:0043001]; hepatocyte apoptotic process [GO:0097284]; intermediate filament cytoskeleton organization [GO:0045104]; negative regulation of apoptotic process [GO:0043066]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
cell periphery [GO:0071944]; centriolar satellite [GO:0034451]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
|
scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: Phosphorylation increases by IL-6. {ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:20724476}.; PTM: Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-6 or caspase-7. {ECO:0000269|PubMed:9298992}.; PTM: O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
| null | null | null | null | null |
FUNCTION: When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:17213200}.
|
Mus musculus (Mouse)
|
P05786
|
K2C8_BOVIN
|
MSIRVTQKSYKVSTSAPRSFSSRSYTSGPGSRISSSAFSRVGSSSSFRGGLGTGMSMAGSYGGAPGLGGITAVTVNQSLLSPLKLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRHLEQQNKVLETKWNLLQQQKTARSNIDNMFESYINNLRRQLETLAQEKLKLEVELGNMQGLVEDFKTKYEDEIQKRTDMENEFVIIKKDVDEAYMNKVELESRLEGLTDEINFYRQLYEEEIREMQSQISDTSVVLEMDNNRNLDLDGIIAEVKAQYEEIANRSRAEAEAMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEGLKGQRASLEAAIADAEQRGEMAVKDAQAKLAELEAALRNAKQDMARQLREYQELMNVKLALDVEIATYRKLLEGEESRLESGMQNMSIHTKTTSGYAGGLTSSYGTPGFNYSLSPGSFSRTSSKPVVVKKIETRDGKLVSESSDVLSK
| null | null |
intermediate filament organization [GO:0045109]; keratinization [GO:0031424]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; keratin filament [GO:0045095]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]
|
structural constituent of skin epidermis [GO:0030280]
|
PF00038;PF16208;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation (By similarity). {ECO:0000250}.; PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix {ECO:0000250|UniProtKB:Q10758}.
| null | null | null | null | null |
FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000250}.
|
Bos taurus (Bovine)
|
P05787
|
K2C8_HUMAN
|
MSIRVTQKSYKVSTSGPRAFSSRSYTSGPGSRISSSSFSRVGSSNFRGGLGGGYGGASGMGGITAVTVNQSLLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLESGMQNMSIHTKTTSGYAGGLSSAYGGLTSPGLSYSLGSSFGSGAGSSSFSRTSSSRAVVVKKIETRDGKLVSESSDVLPK
| null | null |
cell differentiation involved in embryonic placenta development [GO:0060706]; extrinsic apoptotic signaling pathway [GO:0097191]; hepatocyte apoptotic process [GO:0097284]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; response to hydrostatic pressure [GO:0051599]; response to other organism [GO:0051707]; sarcomere organization [GO:0045214]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
apicolateral plasma membrane [GO:0016327]; cell-cell junction [GO:0005911]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; keratin filament [GO:0045095]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; sarcolemma [GO:0042383]; Z disc [GO:0030018]
|
protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; structural constituent of skin epidermis [GO:0030280]
|
PF00038;PF16208;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-74 phosphorylation plays an important role in keratin filament reorganization. {ECO:0000269|PubMed:11781324, ECO:0000269|PubMed:11788583, ECO:0000269|PubMed:1374067, ECO:0000269|PubMed:9054461}.; PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation.; PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:19188445}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix {ECO:0000250|UniProtKB:Q10758}.
| null | null | null | null | null |
FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}.
|
Homo sapiens (Human)
|
P05791
|
ILVD_ECOLI
|
MPKYRSATTTHGRNMAGARALWRATGMTDADFGKPIIAVVNSFTQFVPGHVHLRDLGKLVAEQIEAAGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDSQSDQVERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADRKQLFLNAGKRIVELTKRYYEQNDESALPRNIASKAAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMSDIDKLSRKVPQLCKVAPSTQKYHMEDVHRAGGVIGILGELDRAGLLNRDVKNVLGLTLPQTLEQYDVMLTQDDAVKNMFRAGPAGIRTTQAFSQDCRWDTLDDDRANGCIRSLEHAYSKDGGLAVLYGNFAENGCIVKTAGVDDSILKFTGPAKVYESQDDAVEAILGGKVVAGDVVVIRYEGPKGGPGMQEMLYPTSFLKSMGLGKACALITDGRFSGGTSGLSIGHVSPEAASGGSIGLIEDGDLIAIDIPNRGIQLQVSDAELAARREAQDARGDKAWTPKNRERQVSFALRAYASLATSADKGAVRDKSKLGG
|
4.2.1.9
|
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor. {ECO:0000255|HAMAP-Rule:MF_00012}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
|
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]
|
cytosol [GO:0005829]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; dihydroxy-acid dehydratase activity [GO:0004160]; hydro-lyase activity [GO:0016836]; iron-sulfur cluster binding [GO:0051536]; magnesium ion binding [GO:0000287]
|
PF00920;
|
3.50.30.80;
|
IlvD/Edd family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:49072; EC=4.2.1.9; Evidence={ECO:0000269|PubMed:13727223, ECO:0000269|PubMed:7771772, ECO:0000269|PubMed:8325851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810; Evidence={ECO:0000305|PubMed:13727223, ECO:0000305|PubMed:8325851}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-oxopentanoate + H2O; Xref=Rhea:RHEA:27694, ChEBI:CHEBI:15377, ChEBI:CHEBI:35146, ChEBI:CHEBI:49258; EC=4.2.1.9; Evidence={ECO:0000269|PubMed:13727223}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695; Evidence={ECO:0000305|PubMed:13727223};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for racemic 2,3-dihydroxy-3-methylbutanoate {ECO:0000269|PubMed:8325851}; KM=0.75 mM for (2R)-2,3-dihydroxy-3-methylbutanoate {ECO:0000269|PubMed:8325851}; Note=Since only one of the isomers present in the racemic substrate is active, the corrected Km would be 0.75 mM. {ECO:0000269|PubMed:8325851};
|
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012, ECO:0000269|PubMed:3550695}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012, ECO:0000269|PubMed:3550695}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8-7.9. {ECO:0000269|PubMed:13727223};
| null |
FUNCTION: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. {ECO:0000269|PubMed:13727223, ECO:0000269|PubMed:8325851}.
|
Escherichia coli (strain K12)
|
P05793
|
ILVC_ECOLI
|
MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGYMTDMKRIAVAG
|
1.1.1.86
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:23036858, ECO:0000269|PubMed:2653423}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858, ECO:0000269|PubMed:2653423};
|
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; pantothenate biosynthetic process [GO:0015940]; valine biosynthetic process [GO:0009099]
|
cytosol [GO:0005829]; protein-containing complex [GO:0032991]
|
2-dehydropantoate 2-reductase activity [GO:0008677]; identical protein binding [GO:0042802]; ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661]
|
PF01450;PF07991;
|
3.40.50.720;
|
Ketol-acid reductoisomerase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2653423}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:2653423, ECO:0000269|PubMed:9015391}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for NADPH {ECO:0000269|PubMed:21515217}; KM=0.042 mM for NADP {ECO:0000269|PubMed:9015391}; KM=0.073 mM for NADPH {ECO:0000269|PubMed:9015391}; KM=0.17 mM for 2-ketopantoate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; KM=0.206 mM for NADH {ECO:0000269|PubMed:9015391}; KM=0.21 mM for 3-hydroxy-2-ketobutyrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; KM=0.25 mM for 2-acetolactate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; KM=0.27 mM for 3-hydroxy-3-methyl-2-ketobutyrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; KM=0.42 mM for magnesium (with S2AL and NADPH as substrates) {ECO:0000269|PubMed:2653423}; KM=1.08 mM for NADH {ECO:0000269|PubMed:21515217}; KM=1.54 mM for pyruvate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:2653423}; KM=2.96 mM for 3-hydroxypyruvate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:2653423}; KM=3.15 mM for 2-ketovalerate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:2653423}; KM=4.56 mM for 2-ketobutyrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:2653423}; KM=6.91 mM for 2-ketoisovalerate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:2653423}; Vmax=5.421 umol/min/mg enzyme with 3-hydroxypyruvate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=3.541 umol/min/mg enzyme with 3-hydroxy-3-methyl-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=2.25 umol/min/mg enzyme with 2-acetolactate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=0.599 umol/min/mg enzyme with 3-hydroxy-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=0.196 umol/min/mg enzyme with 2-ketopantoate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=0.184 umol/min/mg enzyme with 2-ketoisovalerate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=0.168 umol/min/mg enzyme with 2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=0.05 umol/min/mg enzyme with 2-ketovalerate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Vmax=0.021 umol/min/mg enzyme with pyruvate as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; Note=kcat is 7.2 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 3.1 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 0.11 min(-1) for reductoisomerase activity with NADH as substrate (PubMed:9015391). kcat is 5.376 sec(-1) for reductoisomerase activity with 3-hydroxypyruvate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 3.6 sec(-1) for reductoisomerase activity with NADPH as substrate (PubMed:21515217). kcat is 3.511 sec(-1) for reductoisomerase activity with 3-hydroxy-3-methyl-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 2.231 sec(-1) for reductoisomerase activity with 2-acetolactate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 0.594 sec(-1) for reductoisomerase activity with 3-hydroxy-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 0.3 sec(-1) for reductoisomerase activity with NADH as substrate (PubMed:21515217). kcat is 0.194 sec(-1) for reductoisomerase activity with 2-ketopantoate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 0.182 sec(-1) for reductoisomerase activity with 2-ketoisovalerate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 0.167 sec(-1) for reductoisomerase activity with 2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 0.05 sec(-1) for reductoisomerase activity with 2-ketovalerate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). kcat is 0.021 sec(-1) for reductoisomerase activity with pyruvate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). {ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:9015391};
|
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:2653423}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:2653423}.
| null | null |
FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate, 3-hydroxypyruvate, 3-hydroxy-2-ketobutyrate and pyruvate (PubMed:15654896). {ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:2653423, ECO:0000269|PubMed:9015391}.
|
Escherichia coli (strain K12)
|
P05803
|
NRAM_I84A1
|
MNPNQKILCTSATALVIGTIAVLIGIVNLGLNIGLHLKPSCNCSRSQPEATNASQTIINNYYNETNITQISNTNIQVEERASREFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRDLISWPLSSPPTVYNSRVECIGWSSTSCHDGRARMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCQNGVCPVVFTDGSATGPAETRIYYFKEGKILKWEPLTGTAKHIEECSCYGEQAGVTCTCRDNWQGSNRPVIQIDPVAMTHTSQYICSPVLTDNPRPNDPTVGKCNDPYPGNNNNGVKGFSYLDGGNTWLGRTISIASRSGYEMLKVPNALTDDRSKPTQGQTIVLNTDWSGYSGSFMDYWAEGECYRACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWNWPDGAKIEYFL
|
3.2.1.18
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; Note=Binds 1 Ca(2+) ion per subunit.;
|
carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
|
exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872]
|
PF00064;
|
2.120.10.10;
|
Glycosyl hydrolase 34 family
|
PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7517697, ECO:0000269|PubMed:7994573}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. {ECO:0000255|HAMAP-Rule:MF_04071}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071};
| null | null | null | null |
FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. {ECO:0000255|HAMAP-Rule:MF_04071}.
|
Influenza A virus (strain A/Whale/Maine/1/1984 H13N9)
|
P05804
|
BGLR_ECOLI
|
MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQGGKQ
|
3.2.1.31
| null |
carbohydrate metabolic process [GO:0005975]; glucuronoside catabolic process [GO:0019391]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
beta-glucuronidase activity [GO:0004566]; carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102]
|
PF00703;PF02836;PF02837;
|
2.60.120.260;3.20.20.80;2.60.40.10;
|
Glycosyl hydrolase 2 family
| null | null |
CATALYTIC ACTIVITY: Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; Evidence={ECO:0000269|PubMed:21051639, ECO:0000269|PubMed:23690068, ECO:0000269|PubMed:26364932, ECO:0000269|PubMed:3105604, ECO:0000269|PubMed:33664385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17634; Evidence={ECO:0000305|PubMed:26364932}; CATALYTIC ACTIVITY: Reaction=4-methylumbelliferone beta-D-glucuronate + H2O = 4-methylumbelliferone + D-glucuronate; Xref=Rhea:RHEA:76111, ChEBI:CHEBI:15377, ChEBI:CHEBI:17224, ChEBI:CHEBI:58720, ChEBI:CHEBI:144582; Evidence={ECO:0000269|PubMed:21051639, ECO:0000269|PubMed:33664385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76112; Evidence={ECO:0000305|PubMed:21051639};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for p-nitrophenyl-beta-D-glucuronide {ECO:0000269|PubMed:26364932}; Note=kcat is 120 sec(-1) with p-nitrophenyl-beta-D-glucuronide as substrate. {ECO:0000269|PubMed:26364932};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-7.5.;
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Resistant to thermal inactivation at 50 degrees Celsius.;
|
FUNCTION: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG) and with 4-methylumbelliferyl-glucuronide (PubMed:21051639, PubMed:23690068, PubMed:26364932, PubMed:3105604, PubMed:33664385). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme is able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract (PubMed:26364932). {ECO:0000269|PubMed:21051639, ECO:0000269|PubMed:23690068, ECO:0000269|PubMed:26364932, ECO:0000269|PubMed:3105604, ECO:0000269|PubMed:33664385}.
|
Escherichia coli (strain K12)
|
P05806
|
NPRE_BACCE
|
MKKKSLALVLATGMAVTTFGGTGSAFADSKNVLSTKKYNETVQSPEFISGDLTEATGKKAESVVFDYLNAAKGDYKLGEKSAQDSFKVKQVKKDAVTDSTVVRMQQVYEGVPVWGSTQVAHVSKDGSLKVLSGTVAPDLDKKEKLKNKNKIEGAKAIEIAQQDLGVTPKYEVEPKADLYVYQNGEETTYAYVVNLNFLDPSPGNYYYFIEADSGKVLNKFNTIDHVTNDDKSPVKQEAPKQDAKAVVKPVTGTNKVGTGKGVLGDTKSLNTTLSGSSYYLQDNTRGATIFTYDAKNRSTLPGTLWADADNVFNAAYDAAAVDAHYYAGKTYDYYKATFNRNSINDAGAPLKSTVHYGSNYNNAFWNGSQMVYGDGDGVTFTSLSGGIDVIGHELTHAVTENSSNLIYQNESGALNEAISDIFGTLVEFYDNRNPDWEIGEDIYTPGKAGDALRSMSDPTKYGDPDHYSKRYTGSSDNGGVHTNSGIINKQAYLLANGGTHYGVTVTGIGKDKLGAIYYRANTQYFTQSTTFSQARAGAVQAAADLYGANSAEVAAVKQSFSAVGVN
|
3.4.24.28
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 4 Ca(2+) ions per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
proteolysis [GO:0006508]
|
extracellular region [GO:0005576]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF07504;PF03413;PF01447;PF02868;
|
3.10.170.10;3.10.450.40;3.10.450.490;1.10.390.10;
|
Peptidase M4 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Similar, but not identical, to that of thermolysin.; EC=3.4.24.28;
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermolabile.;
|
FUNCTION: Extracellular zinc metalloprotease.
|
Bacillus cereus
|
P05807
|
NTP1_VACCW
|
MSKSHAAYIDYALRRTTNMPVEMMGSDVVRLKDYQHFVARVFLGLDSMHSLLLFHETGVGKTMTTVYILKHLKDIYTNWAIILLVKKALIEDPWMNTILRYAPEITKDCIFINYDDQNFRNKFFTNIKTINSKSRICVIIDECHNFISKSLIKEDGKIRPTRSVYNFLSKTIALKNHKMICLSATPIVNSVQEFTMLVNLLRPGSLQHQSLFENKRLVDEKELVSKLGGLCSYIVNNEFSIFDDVEGSASFAKKTVLMRYVNMSKKQEEIYQKAKLAEIKTGISSFRILRRMATTFTFDSFPERQNRDPGEYAQEIATLYNDFKNSLRDREFSKSALDTFKRGELLGGDASAADISLFTELKEKSVKFIDVCLGILASHGKCLVFEPFVNQSGIEILLLYFKVFGISNIEFSSRTKDTRIKAVAEFNQESNTNGECIKTCVFSSSGGEGISFFSINDIFILDMTWNEASLRQIVGRAIRLNSHVLTPPERRYVNVHFIMARLSNGMPTVDEDLFEIIQSKSKEFVQLFRVFKHTSLEWIHANEKDFSPIDNESGWKTLVSRAIDLSSNKNITNKLIEGTNIWYSNSNRLMSINRGFKGVDGRVYDVDGNYLHDMPDNPVIKIHDGKLIYIF
|
3.6.1.15
| null |
DNA-templated transcription [GO:0006351]
|
virion component [GO:0044423]
|
ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; ribonucleoside triphosphate phosphatase activity [GO:0017111]
|
PF00271;PF08469;PF00176;
|
3.40.50.300;
|
Helicase family, NPH I subfamily
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16474121}. Note=Virion core enzyme.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000269|PubMed:22069335};
| null | null | null | null |
FUNCTION: DNA-dependent ATPase that acts as a 5' to 3' translocase on single-stranded DNA and thereby plays a role in transcription termination of viral early genes (PubMed:27189950). Uses forward translocation in concert with the viral RNA polymerase RAP94/OPG109 subunit and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex (PubMed:22069335). In addition, acts as a positive elongation factor to assist transcription through problematic sequences (PubMed:9472022). {ECO:0000269|PubMed:11279216, ECO:0000269|PubMed:22069335, ECO:0000269|PubMed:27189950}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P05811
|
CRYAB_MESAU
|
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRMEKDRFSVNLDVKHFSPEELKVKVLGDVVEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK
| null | null |
apoptotic process involved in morphogenesis [GO:0060561]; cellular response to gamma radiation [GO:0071480]; lens development in camera-type eye [GO:0002088]; muscle organ development [GO:0007517]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of intracellular transport [GO:0032387]; negative regulation of protein-containing complex assembly [GO:0031333]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; tubulin complex assembly [GO:0007021]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; Z disc [GO:0030018]
|
amyloid-beta binding [GO:0001540]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; structural constituent of eye lens [GO:0005212]; unfolded protein binding [GO:0051082]
|
PF00525;PF00011;
|
2.60.40.790;
|
Small heat shock protein (HSP20) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus {ECO:0000250|UniProtKB:P02511}. Secreted {ECO:0000250|UniProtKB:P02511}. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Localizes at the Z-bands and the intercalated disk in cardiomyocytes. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:P02511}.
| null | null | null | null | null |
FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P23927}.
|
Mesocricetus auratus (Golden hamster)
|
P05813
|
CRBA1_HUMAN
|
METQAEQQELETLPTTKMAQTNPTPGSLGPWKITIYDQENFQGKRMEFTSSCPNVSERSFDNVRSLKVESGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKMTIFEKENFIGRQWEISDDYPSLQAMGWFNNEVGSMKIQSGAWVCYQYPGYRGYQYILECDHHGGDYKHWREWGSHAQTSQIQSIRRIQQ
| null | null |
lens development in camera-type eye [GO:0002088]; negative regulation of cytokine production [GO:0001818]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of TOR signaling [GO:0032007]; phagocytosis [GO:0006909]; positive regulation of anoikis [GO:2000210]; regulation of autophagy [GO:0010506]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
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structural constituent of eye lens [GO:0005212]
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PF00030;
|
2.60.20.10;
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Beta/gamma-crystallin family
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PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility. {ECO:0000269|PubMed:15576560}.; PTM: S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental. {ECO:0000269|PubMed:15576560}.
| null | null | null | null | null | null |
FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.
|
Homo sapiens (Human)
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