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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O82312
|
PAPS2_ARATH
|
MVSTQQRTDDDSSQPVKASLKSYGITEPLSIAGPSAADVKRNLELEKFLVDEGLYESKEETMRREEVVVRIDQIVKHWVKQLTRQRGYTDQMVEDANAVIFTFGSYRLGVHGPMADIDTLCVGPSYVNREEDFFIFFRDILAEMEEVTELQPVTDAHVPVMKFKFQGISIDLLYASISLLVIPQDLDISNSSVLCDVDEQTVRSLNGCRVADQILKLVPNSEHFRTTLRCLKYWAKKRGVYSNVTGFLGGVNWALLVARLCQFYPNAIPSMLVSRFFRVYTQWRWPNPVMLCAIEEDDLSFPVWDPRKNHRDRYHLMPIITPAYPCMNSSYNVSQSTLRVMTEQFQFGNTICQEIELNKQHWSSLFQQYMFFEAYKNYLQVDVLAADAEDLLAWKGWVESRFRQLTLKIERDTNGMLMCHPQPNEYVDTSKQFRHCAFFMGLQRADGFGGQECQQFDIRGTVDEFRQEVNMYMFWRPGMDVHVSHVRRRQLPSFVFPNGYKRSRQSRHQSQQCREPGDEGVGSLSDSVERYAKRKNDDEIMNSRPEKREKRASCSLHTLDAASPDSSGITTSGTPQIGIVPGPRAECLVTGDLVCNVTSLPNVEVEAEKFISKITELRKFSQYEHTSGSEQILEVDSRALVQSYHDLAEPVAKHVRPDLSALLACEGGQNKEIGHDMGSESINDTDTQHLPRRLNVNEDVDEVEREAKLGEIAGGVLWNGHCGRNLDHEGFVTPANLDSAVENRNLHSDGLFKSGLPEELQSNSLLSGTGKLDDGARSESLQNEMMRHVFLQPIIGLCKS
|
2.7.7.19
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P25500}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P25500}; Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250|UniProtKB:P25500};
|
mRNA polyadenylation [GO:0006378]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]
|
PF04928;PF20750;PF04926;
|
1.10.1410.10;3.30.460.10;3.30.70.590;
|
Poly(A) polymerase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P25500, ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm {ECO:0000269|PubMed:19956626}.
|
CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:15297145};
| null | null | null | null |
FUNCTION: Essential protein (PubMed:19956626). Polymerase that creates the 3'-poly(A) tail of mRNA's (PubMed:15297145). Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus (By similarity). Mediates the polyadenylation of RNAs that are associated with polynucleotide phosphorylase (e.g. PNP1) (PubMed:10872823). {ECO:0000250|UniProtKB:P25500, ECO:0000269|PubMed:15297145, ECO:0000269|PubMed:19956626, ECO:0000305|PubMed:10872823}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82318
|
SKM1_ARATH
|
MSTSHHHHHPPYLITTLFFLFLNFSCLHANELELLLSFKSSIQDPLKHLSSWSYSSTNDVCLWSGVVCNNISRVVSLDLSGKNMSGQILTAATFRLPFLQTINLSNNNLSGPIPHDIFTTSSPSLRYLNLSNNNFSGSIPRGFLPNLYTLDLSNNMFTGEIYNDIGVFSNLRVLDLGGNVLTGHVPGYLGNLSRLEFLTLASNQLTGGVPVELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNLSGPIPPSLGDLKKLEYMFLYQNKLSGQIPPSIFSLQNLISLDFSDNSLSGEIPELVAQMQSLEILHLFSNNLTGKIPEGVTSLPRLKVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDSQIPPSLGMCQSLERVRLQNNGFSGKLPRGFTKLQLVNFLDLSNNNLQGNINTWDMPQLEMLDLSVNKFFGELPDFSRSKRLKKLDLSRNKISGVVPQGLMTFPEIMDLDLSENEITGVIPRELSSCKNLVNLDLSHNNFTGEIPSSFAEFQVLSDLDLSCNQLSGEIPKNLGNIESLVQVNISHNLLHGSLPFTGAFLAINATAVEGNIDLCSENSASGLRPCKVVRKRSTKSWWLIITSTFAAFLAVLVSGFFIVLVFQRTHNVLEVKKVEQEDGTKWETQFFDSKFMKSFTVNTILSSLKDQNVLVDKNGVHFVVKEVKKYDSLPEMISDMRKLSDHKNILKIVATCRSETVAYLIHEDVEGKRLSQVLSGLSWERRRKIMKGIVEALRFLHCRCSPAVVAGNLSPENIVIDVTDEPRLCLGLPGLLCMDAAYMAPETREHKEMTSKSDIYGFGILLLHLLTGKCSSSNEDIESGVNGSLVKWARYSYSNCHIDTWIDSSIDTSVHQREIVHVMNLALKCTAIDPQERPCTNNVLQALESTSSSSSSCTTYLSKILSLA
|
2.7.11.1
| null |
regulation of pollen tube growth [GO:0080092]; response to temperature stimulus [GO:0009266]
|
endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; peptide binding [GO:0042277]; peptide receptor activity [GO:0001653]; protein serine/threonine kinase activity [GO:0004674]
|
PF00560;PF13855;PF08263;PF00069;
|
3.80.10.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9SYQ8}; Single-pass type I membrane protein {ECO:0000255}.
|
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:0000305}; 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:0000305};
| null | null | null | null |
FUNCTION: Receptor with a serine/threonine-protein kinase activity (By similarity). Together with SKM2, LRR-rich receptor-like kinase (LRR-RLK) required for male fertility by the perception of CLE43 and CLE45 peptides and the transduction of their promoting action in pollen tubes, especially under relatively high temperature (at 30 degrees Celsius), thus conferring tolerance against high temperature probably through the maintenance of mitochondrial activity (PubMed:23910659). Seems to not be involved in the perception of CLE45 peptide in roots (PubMed:27354416). {ECO:0000250|UniProtKB:Q9ZWC8, ECO:0000269|PubMed:23910659, ECO:0000269|PubMed:27354416}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82330
|
SOT10_ARATH
|
MDEKDRPKNLREEEEKPSEETKILISSLPWEIDYLGNKLFNYEGYWYSEDILQSIPNIHTGFQPQETDIILASFYKSGTTWLKALTFALVQRSKHSLEDHQHPLLHHNPHEIVPNLELDLYLKSSKPDLTKFLSSSSSSPRLFSTHMSLDPLQVPLKENLCKIVYVCRNVKDVMVSVWYFRQSKKITRAEDYSLEAIFESFCNGVTLHGPFWDHALSYWRGSLEDPKHFLFMRYEDLKAEPRTQVKRLAEFLDCPFTKEEEDSGSVDKILELCSLSNLRSVEINKTRTSSRVDFKSYFRKGQVGDWKSYMTPEMVDKIDMIIEEKLKGSGLKF
|
2.8.2.-
| null |
brassinosteroid metabolic process [GO:0016131]; response to cytokinin [GO:0009735]; sulfation [GO:0051923]
|
cytoplasm [GO:0005737]
|
brassinosteroid sulfotransferase activity [GO:0080118]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for brassinolide {ECO:0000269|PubMed:17039368}; KM=14 uM for castasterone {ECO:0000269|PubMed:17039368}; KM=43 uM for 24-epibrassinolide {ECO:0000269|PubMed:17039368}; KM=19 uM for (22R, 23R)-28-homobrassinolide {ECO:0000269|PubMed:17039368}; KM=7 uM for (22R, 23R)-28-homocastasterone {ECO:0000269|PubMed:17039368}; KM=0.4 uM for 3'-phospho-5'-adenylyl sulfate {ECO:0000269|PubMed:17039368}; Vmax=5 pmol/sec/mg enzyme with brassinolide as substrate {ECO:0000269|PubMed:17039368}; Vmax=3 pmol/sec/mg enzyme with castasterone as substrate {ECO:0000269|PubMed:17039368}; Vmax=10 pmol/sec/mg enzyme with 24-epibrassinolide as substrate {ECO:0000269|PubMed:17039368}; Vmax=34 pmol/sec/mg enzyme with (22R, 23R)-28-homobrassinolide as substrate {ECO:0000269|PubMed:17039368}; Vmax=19 pmol/sec/mg enzyme with (22R, 23R)-28-homocastasterone as substrate {ECO:0000269|PubMed:17039368};
| null | null | null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to specifically catalyze the sulfate conjugation of brassinosteroids, including castasterone (CS), brassinolide (BL), related 24-epimers, and the naturally occurring (22R, 23R)-28-homobrassinosteroids. No activity on phenolic acids, desulfo-glucosinolates, flavonoids, steroids, gibberellic acids, cytokinins, phenylpropanoids, hydroxyjasmonates and coumarins. {ECO:0000269|PubMed:17039368}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82339
|
CRF5_ARATH
|
MKSRVRKSKYTVHRKITSTPFDGFPKIVKIIVTDPCATDSSSDEENDNKSVAPRVKRYVDEIRFCDEDDEPKPARKAKKKSPAAAAENGGDLVKSVVKYRGVRQRPWGKFAAEIRDPSSRTRLWLGTFATAEEAAIGYDRAAIRIKGHNAQTNFLTPPPSPTTEVLPETPVIDLETVSGCDSARESQISLCSPTSVLRFSHNDETEYRTEPTEEQNPFFLPDLFRSGDYFWDSEITPDPLFLDEFHQSLLPNINNNNTVCDKDTNLSDSFPLGVIGDFSSWDVDEFFQDHLLDK
| null | null |
cotyledon development [GO:0048825]; cytokinin-activated signaling pathway [GO:0009736]; ethylene-activated signaling pathway [GO:0009873]; leaf development [GO:0048366]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00847;
|
3.30.730.10;
|
AP2/ERF transcription factor family, ERF subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16832061}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:16832061}. Note=Relocalization from the cytoplasm into the nucleus is induced by cytokinins.
| null | null | null | null | null |
FUNCTION: Component of the cytokinin signaling pathway involved in cotyledons, leaves, and embryos development. Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). {ECO:0000250, ECO:0000269|PubMed:16832061}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82345
|
BAG6_ARATH
|
MMPVYMDPSQPCQMRPQEYYYQGFGNNSQHMAMDAPPPCHGSCVHGNFPAYWPPCYPPQVPYHQCCMNRSAFHPPHASYAPSCYVHPPFPVGYQPWFDVEKDVPGKHHCGKCSSQMCDLKKDRGVVIEEHEPEIEKGEAVLPVRSTNCPYPIIWIPHENARNQEYRSSLGLGKHNQPPAEVRAPDNMTIQKSFPESWRGCFPFDESSMKSLVQNQDSKKAQNGKTVEAPFDISKFKSLLQGQDMKEAQIQKNKEELGQLTYPTSWVPSRRKRDDVEASESSNEDRKKMQNGKTVEYPFDISMIKSLIQGQDVKEAQNQKNKEEPGQVPYPIFWIPSYGKRKDVEASESKESSNEGRNLESCPSDLHRNEGQITQAKGKEGNFECNVLSDAEEKSSVINIPVANHLQEPRNIPVKLSENHLPKPTEPTKRIAKNEPVKSTKKEQSSSSSEASKLPPVCLRVDPLPKERNGGSKSVSHPKRMEKSKETKIAAPLSSKKAESRTVPEACNVKCEDANAEMKMAEGSLNALRTEKGSVESNSNLQEESNGEIIKPCEAKENREQPAKKSFTEEEAARIIQSMYRGYDVRRWEPIKKLKEIATVREQMGDVKKRIEALEASTDQHIEEKEIVVNGELVMNLLLKLDAVEGLHPSIREFRKALATELSSIQDKLDSLKNSCASAEKEAVKEQVEIKSQPSDSPVNLEHSQLTEENKMVSDTNLEKVLRLSPEEHPMSVLNRTDEKQAESAAETEEGYGLFETLATDSKQATENAAAASSTTIPEKIGEVETVVPGNPPSADGNGMTVTNVEENKAMVVESLEEPINELPQMVEETETNSIRDPENASEVSEAETNSSENENRKGEDDIVLHSEKNVELSELPVGVIDEETQPLSQDPSSSYTREGNMTAMDPKTASQEETEVDHSPNNSKGIGQQTSEPQDEKEQSPETEVIVKEQPLETEVILNEQAPEPEITEPGISKETKKLMEENQRFKETMETLVKAGREQLEVISKLTSRVKSLEKKLSHKKKTQIRRRASKPMSVSPTDAVL
| null | null |
autophagy [GO:0006914]; defense response to fungus [GO:0050832]; induction of programmed cell death [GO:0012502]; positive regulation of autophagy [GO:0010508]; protein folding [GO:0006457]; response to heat [GO:0009408]; vegetative to reproductive phase transition of meristem [GO:0010228]
|
plasmodesma [GO:0009506]
|
calmodulin binding [GO:0005516]; protein-folding chaperone binding [GO:0051087]
|
PF02179;
|
1.20.58.120;
| null | null | null | null | null | null | null | null |
FUNCTION: Co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses (PubMed:16003391). Involved in plant basal resistance (PubMed:16636050, PubMed:26739014). Involved in basal heat response through the regulation of the heat induced small HSP (sHSP) transcriptional cascade (PubMed:26580143). {ECO:0000269|PubMed:16003391, ECO:0000269|PubMed:16636050, ECO:0000269|PubMed:26580143, ECO:0000269|PubMed:26739014}.; FUNCTION: [Cleaved BAG6]: Induces autophagy. {ECO:0000269|PubMed:26739014}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82381
|
U71C1_ARATH
|
MGKQEDAELVIIPFPFSGHILATIELAKRLISQDNPRIHTITILYWGLPFIPQADTIAFLRSLVKNEPRIRLVTLPEVQDPPPMELFVEFAESYILEYVKKMVPIIREALSTLLSSRDESGSVRVAGLVLDFFCVPMIDVGNEFNLPSYIFLTCSAGFLGMMKYLPERHREIKSEFNRSFNEELNLIPGYVNSVPTKVLPSGLFMKETYEPWVELAERFPEAKGILVNSYTALEPNGFKYFDRCPDNYPTIYPIGPILCSNDRPNLDSSERDRIITWLDDQPESSVVFLCFGSLKNLSATQINEIAQALEIVDCKFIWSFRTNPKEYASPYEALPHGFMDRVMDQGIVCGWAPQVEILAHKAVGGFVSHCGWNSILESLGFGVPIATWPMYAEQQLNAFTMVKELGLALEMRLDYVSEDGDIVKADEIAGTVRSLMDGVDVPKSKVKEIAEAGKEAVDGGSSFLAVKRFIGDLIDGVSISK
|
2.4.1.237; 2.4.1.91
| null | null | null |
daphnetin 3-O-glucosyltransferase activity [GO:0102360]; flavonol 3-O-glucosyltransferase activity [GO:0047893]; flavonol 7-O-beta-glucosyltransferase activity [GO:0033836]; myricetin 3-O-glucosyltransferase activity [GO:0102425]; quercetin 3'-O-glucosyltransferase activity [GO:0080045]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; UDP-glucosyltransferase activity [GO:0035251]
|
PF00201;
|
3.40.50.2000;
|
UDP-glycosyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:22300, ChEBI:CHEBI:15378, ChEBI:CHEBI:16816, ChEBI:CHEBI:28802, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.91; Evidence={ECO:0000269|PubMed:15352060}; CATALYTIC ACTIVITY: Reaction=a 7-O-hydroxy-flavonol + UDP-alpha-D-glucose = a flavonol 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:23164, ChEBI:CHEBI:15378, ChEBI:CHEBI:52144, ChEBI:CHEBI:52267, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.237; Evidence={ECO:0000269|PubMed:15352060};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for curcumin {ECO:0000269|PubMed:19261311}; KM=0.5 mM for trans-resveratrol {ECO:0000269|PubMed:19261311}; KM=1.12 mM for vanillin {ECO:0000269|PubMed:19261311}; KM=2.7 mM for etoposide {ECO:0000269|PubMed:19261311}; Vmax=1.2 umol/min/mg enzyme towards vanillin {ECO:0000269|PubMed:19261311}; Vmax=0.063 umol/min/mg enzyme towards trans-resveratrol {ECO:0000269|PubMed:19261311}; Vmax=0.022 umol/min/mg enzyme towards curcumin {ECO:0000269|PubMed:19261311}; Vmax=0.013 umol/min/mg enzyme towards etoposide {ECO:0000269|PubMed:19261311};
| null | null | null |
FUNCTION: Possesses quercetin 7-O-glucosyltransferase and 3'-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives. Glucosylates other secondary metabolites in vitro like trans-resveratrol, curcumin, vanillin and etoposide. {ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:19261311}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82390
|
ANTR1_ARATH
|
MNARALLCSSNIHSLYTSNRPPEKTSSSRSLRNLKPSPKSLRVWIYPRNRSSVFRVLVRSSDKSESSNSYYVEGDKVSGNNDVVSDSPSSIVLPWWEEFPKRWVIVLLCFSAFLLCNMDRVNMSIAILPMSAEYGWNPATVGLIQSSFFWGYLLTQIAGGIWADTVGGKRVLGFGVIWWSIATILTPVAAKLGLPYLLVVRAFMGVGEGVAMPAMNNILSKWVPVQERSRSLALVYSGMYLGSVTGLAFSPFLIHQFGWPSVFYSFGSLGTVWLTLWLTKAESSPLEDPTLLPEERKLIADNCASKEPVKSIPWRLILSKPPVWALISCHFCHNWGTFILLTWMPTYYHQVLKFNLMESGLLSVFPWMTMAISANAGGWIADTLVSRGFSVTNVRKIMQTIGFLGPAFFLTQLKHIDSPTMAVLCMACSQGTDAFSQSGLYSNHQDIAPRYSGVLLGLSNTAGVLAGVLGTAATGHILQHGSWDDVFTISVGLYLVGTVIWNLFSTGEKIID
| null | null |
monoatomic anion transport [GO:0006820]; response to light stimulus [GO:0009416]; response to nematode [GO:0009624]; sodium ion transport [GO:0006814]
|
chloroplast thylakoid membrane [GO:0009535]; thylakoid [GO:0009579]
|
inorganic phosphate transmembrane transporter activity [GO:0005315]; symporter activity [GO:0015293]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Sodium/anion cotransporter (TC 2.A.1.14) family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:14564522, ECO:0000269|PubMed:18353780}; Multi-pass membrane protein {ECO:0000269|PubMed:14564522, ECO:0000269|PubMed:18353780}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.17 mM for sodium {ECO:0000269|PubMed:18353780}; KM=78.7 uM for inorganic phosphate {ECO:0000269|PubMed:18353780}; Vmax=99.15 nmol/h/mg enzyme toward sodium {ECO:0000269|PubMed:18353780}; Vmax=161 nmol/h/mg enzyme toward inorganic phosphate {ECO:0000269|PubMed:18353780};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:18353780};
| null |
FUNCTION: Specific for inorganic phosphate transport across the thylakoid membrane in a sodium dependent manner. Binds glutamate but cannot transport it. May act as an ascorbate transporter at the thylakoid membrane (Probable). {ECO:0000269|PubMed:18086223, ECO:0000269|PubMed:18353780, ECO:0000305|PubMed:25557369}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82392
|
THIC_ARATH
|
MAASVHCTLMSVVCNNKNHSARPKLPNSSLLPGFDVVVQAAATRFKKETTTTRATLTFDPPTTNSERAKQRKHTIDPSSPDFQPIPSFEECFPKSTKEHKEVVHEESGHVLKVPFRRVHLSGGEPAFDNYDTSGPQNVNAHIGLAKLRKEWIDRREKLGTPRYTQMYYAKQGIITEEMLYCATREKLDPEFVRSEVARGRAIIPSNKKHLELEPMIVGRKFLVKVNANIGNSAVASSIEEEVYKVQWATMWGADTIMDLSTGRHIHETREWILRNSAVPVGTVPIYQALEKVDGIAENLNWEVFRETLIEQAEQGVDYFTIHAGVLLRYIPLTAKRLTGIVSRGGSIHAKWCLAYHKENFAYEHWDDILDICNQYDVALSIGDGLRPGSIYDANDTAQFAELLTQGELTRRAWEKDVQVMNEGPGHVPMHKIPENMQKQLEWCNEAPFYTLGPLTTDIAPGYDHITSAIGAANIGALGTALLCYVTPKEHLGLPNRDDVKAGVIAYKIAAHAADLAKQHPHAQAWDDALSKARFEFRWMDQFALSLDPMTAMSFHDETLPADGAKVAHFCSMCGPKFCSMKITEDIRKYAEENGYGSAEEAIRQGMDAMSEEFNIAKKTISGEQHGEVGGEIYLPESYVKAAQK
|
4.1.99.17
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:18048325, ECO:0000305|PubMed:24161603}; Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000269|PubMed:18048325};
|
response to vitamin B1 [GO:0010266]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; plastid [GO:0009536]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; carbon-carbon lyase activity [GO:0016830]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]
|
PF01964;
|
6.10.250.620;3.20.20.540;
|
ThiC family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:18048325, ECO:0000269|PubMed:18332905, ECO:0000269|PubMed:18431481}.
|
CATALYTIC ACTIVITY: Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine; Xref=Rhea:RHEA:24840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, ChEBI:CHEBI:58354, ChEBI:CHEBI:59789, ChEBI:CHEBI:137981; EC=4.1.99.17;
| null |
PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
| null | null |
FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. {ECO:0000269|PubMed:18048325, ECO:0000269|PubMed:18332905}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82399
|
MDHX1_ARATH
|
MDPNQRIARISAHLNPPNLHNQIADGSGLNRVACRAKGGSPGFKVAILGAAGGIGQPLAMLMKMNPLVSVLHLYDVANAPGVTADISHMDTSAVVRGFLGQPQLEEALTGMDLVIIPAGVPRKPGMTRDDLFNINAGIVRTLSEAIAKCCPKAIVNIISNPVNSTVPIAAEVFKKAGTFDPKKLMGVTMLDVVRANTFVAEVMSLDPREVEVPVVGGHAGVTILPLLSQVKPPCSFTQKEIEYLTDRIQNGGTEVVEAKAGAGSATLSMAYAAVEFADACLRGLRGDANIVECAYVASHVTELPFFASKVRLGRCGIDEVYGLGPLNEYERMGLEKAKKELSVSIHKGVTFAKK
|
1.1.1.37
| null |
glyoxylate cycle [GO:0006097]; malate metabolic process [GO:0006108]; regulation of fatty acid beta-oxidation [GO:0031998]; regulation of photorespiration [GO:0080093]; tricarboxylic acid cycle [GO:0006099]
|
chloroplast [GO:0009507]; peroxisome [GO:0005777]
|
L-malate dehydrogenase activity [GO:0030060]
|
PF02866;PF00056;
|
3.90.110.10;3.40.50.720;
|
LDH/MDH superfamily, MDH type 1 family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17376163}.
|
CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
| null | null | null | null |
FUNCTION: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Peroxisomal NAD-dependent malate dehydrogenase involved in fatty acid beta-oxidation. Reoxidizes NADH from the beta-oxidation and provides NAD for the conversion of fatty acyl-CoA to acetyl-CoA. Does not participate directly in the glyoxylate cycle (PubMed:17376163, PubMed:19812894). Required for maintenance of photosynthetic rates under photorespiratory conditions, and carbon flow during photorespiration. Supplies NADH reductant to the peroxisomal hydroxypyruvate reductase (HPR), which reduces hydroxypyruvate into glycerate in the photorespiratory cycle (PubMed:18685043). {ECO:0000269|PubMed:17376163, ECO:0000269|PubMed:18685043, ECO:0000269|PubMed:19812894, ECO:0000305|PubMed:20876337}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82415
|
TYDC_PAPSO
|
MGSLPTNNLESISLCSQNPLDPDEFRRQGHMIIDFLADYYKNVEKYPVRSQVEPGYLKKRLPESAPYNPESIETILEDVTNDIIPGLTHWQSPNYFAYFPSSGSIAGFLGEMLSTGFNVVGFNWMSSPAATELESIVMNWLGQMLTLPKSFLFSSDGSSGGGGVLQGTTCEAILCTLTAARDKMLNKIGRENINKLVVYASDQTHCALQKAAQIAGINPKNVRAIKTSKATNFGLSPNSLQSAILADIESGLVPLFLCATVGTTSSTAVDPIGPLCAVAKLYGIWVHIDAAYAGSACICPEFRHFIDGVEDADSFSLNAHKWFFTTLDCCCLWVKDSDSLVKALSTSPEYLKNKATESKQVIDYKDWQIALSRRFRSMKLWLVLRSYGVANLRTFLRSHVKMAKHFQGLIGMDNRFEIVVPRTFAMVCFRLKPTAIFKQKIVDNDYIEDQTNEVNVKLLESVNASGKIYMTHAVVGGVYMIRFAVGATLTEERHVTGAWKVVQEHTDAILGA
|
4.1.1.25
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:23204519};
|
amino acid metabolic process [GO:0006520]; carboxylic acid metabolic process [GO:0019752]
|
cytoplasm [GO:0005737]
|
pyridoxal phosphate binding [GO:0030170]; tyrosine decarboxylase activity [GO:0004837]
|
PF00282;
|
3.90.1150.10;1.20.1340.10;3.40.640.10;
|
Group II decarboxylase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315, ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000269|PubMed:23204519}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346; Evidence={ECO:0000269|PubMed:23204519};
| null | null | null | null |
FUNCTION: Tyrosine decarboxylase that converts tyrosine into tyramine, a precursor of isoquinoline alkaloids and various amides. {ECO:0000269|PubMed:23204519, ECO:0000269|PubMed:25107664}.
|
Papaver somniferum (Opium poppy)
|
O82480
|
RAC7_ARATH
|
MSASKFIKCVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSANVAVDGQIVNLGLWDTAGQEDYSRLRPLSYRGADIFVLAFSLISKASYENVLKKWMPELRRFAPNVPIVLVGTKLDLRDDKGYLADHTNVITSTQGEELRKQIGAAAYIECSSKTQQNVKAVFDTAIKVVLQPPRRKEVPRRRKNHRRSGCSIASIVCGGCTAA
| null | null |
abscisic acid-activated signaling pathway [GO:0009738]; cortical cytoskeleton organization [GO:0030865]; establishment or maintenance of cell polarity [GO:0007163]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; small GTPase-mediated signal transduction [GO:0007264]
|
cell projection [GO:0042995]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rho family
|
PTM: Although this sequence has a C-terminal -CXXX, it is palmitoylated at Cys-206, rather than prenylated. {ECO:0000269|PubMed:12368496}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12368496}; Lipid-anchor {ECO:0000269|PubMed:12368496}.
| null | null | null | null | null |
FUNCTION: Acts as a negative regulator of abscisic acid (ABA) responses. {ECO:0000269|PubMed:12417701}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82481
|
RAC10_ARATH
|
MASSASKFIKCVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSANVVVEGTTVNLGLWDTAGQEDYNRLRPLSYRGADVFVLSFSLVSRASYENVFKKWIPELQHFAPGVPLVLVGTKLDLREDKHYLADHPGLSPVTTAQGEELRKLIGATYYIECSSKTQQNVKAVFDSAIKEVIKPLVKQKEKTKKKKKQKSNHGCLSNVLCGRIVTRH
| null | null |
cortical cytoskeleton organization [GO:0030865]; establishment or maintenance of cell polarity [GO:0007163]; negative regulation of abscisic acid-activated signaling pathway [GO:0009788]; plant-type cell wall organization [GO:0009664]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of plant-type cell wall cellulose biosynthetic process [GO:2001009]; small GTPase-mediated signal transduction [GO:0007264]
|
cell projection [GO:0042995]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; secondary cell wall [GO:0009531]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rho family
| null |
SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cytoplasm. Cytoplasm, cytoskeleton. Note=Recruited along cortical microtubules upon interaction with ICR5. {ECO:0000269|PubMed:22984069}.
| null | null | null | null | null |
FUNCTION: Involved in local disassembly of cortical microtubules when associated with ICR5 and KIN13A. {ECO:0000269|PubMed:22984069, ECO:0000269|PubMed:24280391}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82486
|
MTA70_ARATH
|
METESDDATITVVKDMRVRLENRIRTQHDAHLDLLSSLQSIVPDIVPSLDLSLKLISSFTNRPFVATPPLPEPKVEKKHHPIVKLGTQLQQLHGHDSKSMLVDSNQRDAEADGSSGSPMALVRAMVAECLLQRVPFSPTDSSTVLRKLENDQNARPAEKAALRDLGGECGPILAVETALKSMAEENGSVELEEFEVSGKPRIMVLAIDRTRLLKELPESFQGNNESNRVVETPNSIENATVSGGGFGVSGSGNFPRPEMWGGDPNMGFRPMMNAPRGMQMMGMHHPMGIMGRPPPFPLPLPLPVPSNQKLRSEEEDLKDVEALLSKKSFKEKQQSRTGEELLDLIHRPTAKEAATAAKFKSKGGSQVKYYCRYLTKEDCRLQSGSHIACNKRHFRRLIASHTDVSLGDCSFLDTCRHMKTCKYVHYELDMADAMMAGPDKALKPLRADYCSEAELGEAQWINCDIRSFRMDILGTFGVVMADPPWDIHMELPYGTMADDEMRTLNVPSLQTDGLIFLWVTGRAMELGRECLELWGYKRVEEIIWVKTNQLQRIIRTGRTGHWLNHSKEHCLVGIKGNPEVNRNIDTDVIVAEVRETSRKPDEMYAMLERIMPRARKLELFARMHNAHAGWLSLGNQLNGVRLINEGLRARFKASYPEIDVQPPSPPRASAMETDNEPMAIDSITA
|
2.1.1.348
| null |
embryo development ending in seed dormancy [GO:0009793]; mRNA methylation [GO:0080009]; RNA methylation [GO:0001510]
|
chloroplast [GO:0009507]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; RNA N6-methyladenosine methyltransferase complex [GO:0036396]
|
mRNA (N6-adenosine)-methyltransferase activity [GO:0001734]; RNA binding [GO:0003723]
|
PF05063;
| null |
MT-A70-like family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19245862}.
|
CATALYTIC ACTIVITY: Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348; Evidence={ECO:0000305|PubMed:18505803};
| null | null | null | null |
FUNCTION: Catalytic subunit of the N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs (PubMed:18505803, PubMed:28503769). Associates with MTB, FIP37, VIR and HAKAI to form the m6A writer complex which is essential for adenosine methylation at specific mRNA sequences (PubMed:28503769). N6-methyladenosine (m6A) plays a role in mRNA stability, processing, translation efficiency and editing (PubMed:18505803, PubMed:28503769). {ECO:0000269|PubMed:18505803, ECO:0000269|PubMed:28503769}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82503
|
CRF1_ARATH
|
METEKKVSLPRILRISVTDPYATDSSSDEEEEVDFDALSTKRRRVKKYVKEVVLDSVVSDKEKPMKKKRKKRVVTVPVVVTTATRKFRGVRQRPWGKWAAEIRDPSRRVRVWLGTFDTAEEAAIVYDNAAIQLRGPNAELNFPPPPVTENVEEASTEVKGVSDFIIGGGECLRSPVSVLESPFSGESTAVKEEFVGVSTAEIVVKKEPSFNGSDFSAPLFSDDDVFGFSTSMSESFGGDLFGDNLFADMSFGSGFGFGSGSGFSSWHVEDHFQDIGDLFGSDPVLTV
| null | null |
cotyledon development [GO:0048825]; cytokinin-activated signaling pathway [GO:0009736]; ethylene-activated signaling pathway [GO:0009873]; leaf development [GO:0048366]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00847;
|
3.30.730.10;
|
AP2/ERF transcription factor family, ERF subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16832061}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:16832061}. Note=Relocalization from the cytoplasm into the nucleus is induced by cytokinins.
| null | null | null | null | null |
FUNCTION: Component of the cytokinin signaling pathway involved in cotyledons, leaves, and embryos development. Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). {ECO:0000250, ECO:0000269|PubMed:16832061}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82504
|
RDR2_ARATH
|
MVSETTTNRSTVKISNVPQTIVADELLRFLELHLGEDTVFALEIPTTRDNWKPRDFARVQFTTLEVKSRAQLLSSQSKLLFKTHNLRLSEAYDDIIPRPVDPRKRLDDIVLTVGFPESDEKRFCALEKWDGVRCWILTEKRRVEFWVWESGDCYKIEVRFEDIIETLSCCVNGDASEIDAFLLKLKYGPKVFKRVTVHIATKFKSDRYRFCKEDFDFMWIRTTDFSGSKSIGTSTCFCLEVHNGSTMLDIFSGLPYYREDTLSLTYVDGKTFASAAQIVPLLNAAILGLEFPYEILFQLNALVHAQKISLFAASDMELIKILRGMSLETALVILKKLHQQSSICYDPVFFVKTQMQSVVKKMKHSPASAYKRLTEQNIMSCQRAYVTPSKIYLLGPELETANYVVKNFAEHVSDFMRVTFVEEDWSKLPANALSVNSKEGYFVKPSRTNIYNRVLSILGEGITVGPKRFEFLAFSASQLRGNSVWMFASNEKVKAEDIREWMGCFRKIRSISKCAARMGQLFSASRQTLIVRAQDVEQIPDIEVTTDGADYCFSDGIGKISLAFAKQVAQKCGLSHVPSAFQIRYGGYKGVIAVDRSSFRKLSLRDSMLKFDSNNRMLNVTRWTESMPCFLNREIICLLSTLGIEDAMFEAMQAVHLSMLGNMLEDRDAALNVLQKLSGENSKNLLVKMLLQGYAPSSEPYLSMMLRVHHESQLSELKSRCRILVPKGRILIGCMDEMGILEYGQVYVRVTLTKAELKSRDQSYFRKIDEETSVVIGKVVVTKNPCLHPGDIRVLDAIYEVHFEEKGYLDCIIFPQKGERPHPNECSGGDLDGDQFFVSWDEKIIPSEMDPPMDYAGSRPRLMDHDVTLEEIHKFFVDYMISDTLGVISTAHLVHADRDPEKARSQKCLELANLHSRAVDFAKTGAPAEMPYALKPREFPDFLERFEKPTYISESVFGKLYRAVKSSLAQRKPEAESEDTVAYDVTLEEAGFESFIETAKAHRDMYGEKLTSLMIYYGAANEEEILTGILKTKEMYLARDNRRYGDMKDRITLSVKDLHKEAMGWFEKSCEDEQQKKKLASAWYYVTYNPNHRDEKLTFLSFPWIVGDVLLDIKAENAQRQSVEEKTSGLVSI
|
2.7.7.48
| null |
defense response to fungus [GO:0050832]; siRNA processing [GO:0030422]; siRNA transcription [GO:0140745]; siRNA-mediated long-distance post-transcriptional gene silencing [GO:0010495]
|
nuclear RNA-directed RNA polymerase complex [GO:0031380]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA/RNA hybrid binding [GO:0071667]; metal ion binding [GO:0046872]; RNA-dependent RNA polymerase activity [GO:0003968]; single-stranded RNA binding [GO:0003727]
|
PF05183;
| null |
RdRP family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:17526749}. Nucleus, nucleolus {ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:17526749}. Nucleus {ECO:0000269|PubMed:26119694}. Note=In the nucleolus, localized in a ring or crescent around the inner periphery and to a distinctive nucleolar dot. {ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:17526749}.
|
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;
| null | null | null | null |
FUNCTION: RNA-dependent direct polymerase involved in the production of small interfering RNAs (siRNAs). Binds to single-stranded RNA (ssRNA); engages ssRNAs longer than 7 nucleotides and initiates internal to their 3' ends (PubMed:34903670). Able to transcribe the RNA of an RNA/DNA hybrid, the transcript produced by Pol IV, if its 3' end is accessible, to generate double-stranded small interfering RNAs (dsRNAs) precursor essential for establishing and maintaining DNA methylation (PubMed:34903670, PubMed:34941388). Required for the biogenesis of endogenous siRNAs of 24 nucleotide which derive from heterochromatin and DNA repeats such as transposons or endogenous gene tandem repeats, such as repeats present in FWA gene. Involved in transcriptional gene silencing (TGS). Component of the RNA-directed DNA methylation (RdDM) silencing pathway that utilizes siRNAs to guide DNA methyltransferases to asymmetric cytosines. Involved in control of flowering time through RdDM of FWA locus. Required for reception of long-distance mRNA silencing in the shoot. Required for the formation of telomeric siRNAs and the RNA-dependent DNA methylation of asymmetric cytosines in telomeric (5'-CCCTAAA-3') repeats. {ECO:0000269|PubMed:15024409, ECO:0000269|PubMed:15692015, ECO:0000269|PubMed:16798886, ECO:0000269|PubMed:17105345, ECO:0000269|PubMed:17526749, ECO:0000269|PubMed:17785412, ECO:0000269|PubMed:20548962, ECO:0000269|PubMed:21150311, ECO:0000269|PubMed:23142082, ECO:0000269|PubMed:34903670, ECO:0000269|PubMed:34941388}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82533
|
FTZ21_ARATH
|
MATYVSPCFTPSDSRLLTVLRKNVLPENHLGRLNSIRTIDSKKNRVVVAAQKSESSPIRNSPRHYQSQAQDPFLNLHPEISMLRGEGTSTIVNPRKETSSGPVVEDFEEPSAPSNYNEARIKVIGVGGGGSNAVNRMIESEMSGVEFWIVNTDIQAMRMSPVLPDNRLQIGKELTRGLGAGGNPEIGMNAARESKEVIEEALYGSDMVFVTAGMGGGTGTGAAPVIAGIAKAMGILTVGIATTPFSFEGRRRTVQAQEGLASLRDNVDTLIVIPNDKLLTAVSQSTPVTEAFNLADDILRQGVRGISDIITIPGLVNVDFADVRAIMANAGSSLMGIGTATGKSRARDAALNAIQSPLLDIGIERATGIVWNITGGSDLTLFEVNAAAEVIYDLVDPTANLIFGAVVDPALSGQVSITLIATGFKRQEEGEGRTVQMVQADAASVGATRRPSSSFRESGSVEIPEFLKKKGSSRYPRV
| null | null |
chloroplast fission [GO:0010020]; response to gibberellin [GO:0009739]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; contractile ring [GO:0070938]; endoplasmic reticulum [GO:0005783]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein self-association [GO:0043621]
|
PF12327;PF00091;
|
3.30.1330.20;3.40.50.1440;
|
FtsZ family
|
PTM: Filaments containing FTSZ2-1 are stabilized when in complex with GTP but destabilized after conversion of GTP into GDP; ARC6 conteracts this destabilisation by preventing the dissociation of GDP-bound FTSZ2 molecules thus inhibiting filament disassembly whereas ARC3 promotes GTPase activity thus accelerating the conversion of GTP into GDP and triggering FtsZ2 filaments disassembly. {ECO:0000269|PubMed:29138260, ECO:0000269|PubMed:29769312}.; PTM: Phosphorylation at Ser-143 is necessary for interactions with ARC3, ARC6, FTSZ1 and FTSZ2-2. Phosphorylations at Ser-143 and Thr-286 are required for the formation of contractile ring at the chloroplast midpoint. {ECO:0000269|PubMed:22823492}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22823492, ECO:0000269|PubMed:29769312}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18431481}; Peripheral membrane protein. Note=Forms a contractile ring at the chloroplast midpoint that coaligns with FTSZ1 rings (PubMed:18431481, PubMed:22823492, PubMed:25731613, PubMed:29769312). Exhibits a dynamic trunover in FtsZ ring facilitated by ARC3-mediated destabilization (PubMed:25731613). {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22823492, ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29769312}.
| null | null | null | null | null |
FUNCTION: Exhibits GTPase activity which converts GTP ligands to GDP (PubMed:29769312). Component of the plastid division machinery consisting in a binary fission accomplished by the simultaneous constriction of the FtsZ ring on the stromal side of the inner envelope membrane, and the ARC5 ring on the cytosolic side of the outer envelope membrane (PubMed:25731613). Required for plastid division in a dose-dependent manner. In the vegetative shoot apex, at the shoot apical meristem (SAM), where the proplastid-to-chloroplast transition takes place, major contributor of plastid division in the L1 and L3 layers and contributes equally with FTSZ1 in the L2 layer (PubMed:29920253). {ECO:0000269|PubMed:11115884, ECO:0000269|PubMed:11743110, ECO:0000269|PubMed:18284374, ECO:0000269|PubMed:19925792, ECO:0000269|PubMed:19995726, ECO:0000269|PubMed:20421292, ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29769312, ECO:0000269|PubMed:29920253, ECO:0000269|PubMed:9836740}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82587
|
SWT12_ARATH
|
MALFDTHNTWAFVFGLLGNLISFAVFLSPVPTFYRICKKKTTEGFQSIPYVVALFSAMLWLYYATQKKDVFLLVTINSFGCFIETIYISIFVAFASKKARMLTVKLLLLMNFGGFCLILLLCQFLAKGTTRAKIIGGICVGFSVCVFAAPLSIIRTVIKTKSVEYMPFSLSLTLTISAVIWLLYGLALKDIYVAFPNVIGFVLGALQMILYVVYKYCKTPSDLVEKELEAAKLPEVSIDMVKLGTLTSPEPVAITVVRSVNTCNCNDRNAEIENGQGVRNSAATT
| null | null |
embryo development ending in seed dormancy [GO:0009793]; protein homooligomerization [GO:0051260]; seed maturation [GO:0010431]; sucrose transport [GO:0015770]
|
plasma membrane [GO:0005886]
|
sucrose transmembrane transporter activity [GO:0008515]; sugar transmembrane transporter activity [GO:0051119]
|
PF03083;
|
1.20.1280.290;
|
SWEET sugar transporter family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22157085}; Multi-pass membrane protein {ECO:0000250}. Note=Present in the plasma membrane of the phloem. {ECO:0000269|PubMed:22157085}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 mM for sucrose uptake {ECO:0000269|PubMed:22157085}; KM=10 mM for sucrose efflux {ECO:0000269|PubMed:22157085};
| null | null | null |
FUNCTION: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. Involved in phloem loading by mediating export from parenchyma cells feeding H(+)-coupled import into the sieve element/companion cell complex, thus contributing to the sucrose migration from sites of synthesis in the mesophyll to the phloem (PubMed:22157085, PubMed:25988582). Contributes to seed filling by triggering sucrose efflux involved in the transfer of sugars from seed coat to embryos (PubMed:25988582). {ECO:0000269|PubMed:22157085, ECO:0000269|PubMed:25794936, ECO:0000303|PubMed:25988582}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82645
|
IQM1_ARATH
|
MGLEVGSLCFKLKDGGLTSRTNSFKRDDTNRHQNSPKSTMERSLSFNSWEVPKETKTDSDFEVLETKKSTPNTLNGRNCERIQIKKPTVTPPEPFVFFSPRPVTELDAAATTLQKVYKSYRTRRNLADCAVVVEELWWRTLEGAALDLSSVSFFGEEKHETAVSKWARARKRAAKVGKGLSKDEKAQKLALQHWLEAIDPRHRYGHNLHFYYDVWSASKSTQPFFYWLDIGDGKDVNLEKHPRSVLQKQCIRYLGPMEREAYEVIVEDGRLMYKQGMTLINSTEEAKSIFVLSTTRNLYVGIKKKGLFQHSSFLSGGATTAAGRLVARDGILEAIWPYSGHYLPTEDNFKEFISFLEEHNVDLTNVKRCSVNEEYSSFKSTADEEEERKEVSEEVEIPSEKEERARPVFDPVKRLSCKWTSGYGPRIGCVRDYPMELQAQALEQVSLSPRVSPANSYGPIPSPRPSPKVRVSPRLAYMGIPSPRAVKC
| null | null |
regulation of stomatal movement [GO:0010119]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
calmodulin binding [GO:0005516]
| null | null | null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22572939}. Nucleus {ECO:0000269|PubMed:22572939}.
| null | null | null | null | null |
FUNCTION: Involved in the modulation of stomatal movement. Promotes stomatal opening. May play a role in the regulation of chitin signaling. May be involved in biotic and abiotic stress responses. {ECO:0000269|PubMed:22572939}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82656
|
PTP1_ARATH
|
MATGKTSSAANLFTGSTRFDLSSADSPPSKLSLSSDQLNHCHQALGVFRGKIQNPDSIAHEFTGLQANRMWPSELLLNSTVAMNSVNVEKNRYSDVVPFDKNRIVLNPCKDSSAKGYVNASLIKTSESESISQFIATQGPLPHTMEDFWEMVIQQHCPIIVMLTRLVDNNRTVKCGDYFQDEDGPREFGNISLTTKWIKTTDTSLMLRNLEVNYKETEDQPMSVLHIQYPEWPDHGVPKDTVAVREILKRLYQVPPSLGPIIVHCSAGIGRTGTYCAIHNTIQRILAGDMSALDLAKTVALFRKQRIGMVQTMDQYFFCYNAIVDELEDLTAGTNAGTSS
|
3.1.3.48
| null |
defense response [GO:0006952]; dephosphorylation [GO:0016311]; intracellular signal transduction [GO:0035556]; negative regulation of defense response [GO:0031348]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
kinase binding [GO:0019900]; MAP kinase tyrosine phosphatase activity [GO:0033550]; protein tyrosine phosphatase activity [GO:0004725]
|
PF00102;
|
3.90.190.10;
| null |
PTM: Phosphorylated by KIN10. {ECO:0000269|PubMed:27029354}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19789277}. Nucleus {ECO:0000269|PubMed:19789277}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044};
| null | null | null | null |
FUNCTION: Protein-tyrosine-phosphatase that dephosphorylates and probably inhibits MPK6 in non-oxidative stress conditions. In association with MKP1, represses salicylic acid (SA) and camalexin biosynthesis, thus modulating defense response. May also repress MPK3. Dephosphorylates and inactivates MPK4 in vitro. {ECO:0000269|PubMed:10759527, ECO:0000269|PubMed:12857797, ECO:0000269|PubMed:19789277, ECO:0000269|PubMed:9596642}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82660
|
P2SAF_ARATH
|
MASLQLCDGYLLFKPSVSPRFLSQRISHRLIPKASSSPPPSPSPSSSSSSLSFSRRELLYQSAAVSLSLSSIVGPARADEQLSEWERVFLPIDPGVVLLDIAFVPDEPSRGFLLGTRQTLLETKDGGSTWNPRSIPSAEEEDFNYRFNSISFKGKEGWIIGKPAILLYTADAGENWDRIPLSSQLPGDMVFIKATEDKSAEMVTDEGAIYVTSNRGYNWKAAIQETVSATLNRTVSSGISGASYYTGTFSAVNRSPDGRYVAVSSRGNFFLTWEPGQPYWQPHNRAVARRIQNMGWRADGGLWLLVRGGGLYLSKGTGITEEFEEVPVQSRGFGILDVGYRSEEEAWAAGGSGILLRTRNGGKSWNRDKAADNIAANLYAVKFVDDKKGFVLGNDGVLLRYVG
| null | null |
photosynthesis [GO:0015979]; plastid organization [GO:0009657]; protein-containing complex assembly [GO:0065003]
|
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast stromal thylakoid [GO:0009533]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid lumen [GO:0009543]; chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523]; plastid [GO:0009536]; thylakoid [GO:0009579]; thylakoid lumen [GO:0031977]
| null |
PF14870;
|
2.130.10.10;
|
Ycf48 family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:9736608}. Note=Restricted to the stromal lamellae (PubMed:9736608). Translocation into the thylakoid lumen occurs via the Tat pathway (Probable) (PubMed:10664464). {ECO:0000269|PubMed:10664464, ECO:0000269|PubMed:9736608, ECO:0000305|PubMed:11719511, ECO:0000305|PubMed:11826309}.
| null | null | null | null | null |
FUNCTION: Essential for photosystem II (PSII) biogenesis; required for assembly of an early intermediate in PSII assembly that includes D2 (psbD) and cytochrome b559. Has been suggested (PubMed:11826309) to be required for chlorophyll a binding. {ECO:0000269|PubMed:11826309, ECO:0000269|PubMed:12459468, ECO:0000269|PubMed:9736608}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82663
|
SDHA1_ARATH
|
MWRCVSRGFRAPASKTSSLFDGVSGSRFSRFFSTGSTDTRSSYTIVDHTYDAVVVGAGGAGLRAAIGLSEHGFNTACITKLFPTRSHTVAAQGGINAALGNMSEDDWRWHMYDTVKGSDWLGDQDAIQYMCREAPKAVIELENYGLPFSRTEEGKIYQRAFGGQSLDFGKGGQAYRCACAADRTGHALLHTLYGQAMKHNTQFFVEYFALDLLMASDGSCQGVIALNMEDGTLHRFRSSQTILATGGYGRAYFSATSAHTCTGDGNAMVARAGLPLQDLEFVQFHPTGIYGAGCLITEGSRGEGGILRNSEGERFMERYAPTAKDLASRDVVSRSMTMEIREGRGVGPHKDHIYLHLNHLPPEVLKERLPGISETAAIFAGVDVTKEPIPVLPTVHYNMGGIPTNYHGEVVTIKGDDPDAVIPGLMAAGEAACASVHGANRLGANSLLDIVVFGRACANRVAEISKPGEKQKPLEKDAGEKTIAWLDRLRNSNGSLPTSTIRLNMQRIMQNNAAVFRTQETLEEGCQLIDKAWESFGDVQVKDRSMIWNSDLIETLELENLLINASITMHSAEARKESRGAHAREDFTKREDGEWMKHTLGYWEDEKVRLDYRPVHMDTLDDEIDTFPPKARVY
|
1.3.5.1
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q0QF01};
|
anaerobic respiration [GO:0009061]; mitochondrial electron transport, succinate to ubiquinone [GO:0006121]; tricarboxylic acid cycle [GO:0006099]
|
mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; mitochondrion [GO:0005739]; plant-type cell wall [GO:0009505]; plastid [GO:0009536]; respiratory chain complex II [GO:0045273]
|
ATP binding [GO:0005524]; cobalt ion binding [GO:0050897]; electron transfer activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; succinate dehydrogenase (quinone) activity [GO:0008177]; succinate dehydrogenase activity [GO:0000104]
|
PF00890;PF02910;
|
3.50.50.60;1.20.58.100;4.10.80.40;3.90.700.10;
|
FAD-dependent oxidoreductase 2 family, FRD/SDH subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}; Peripheral membrane protein {ECO:0000269|PubMed:14671022}; Matrix side {ECO:0000269|PubMed:14671022}.
|
CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; Evidence={ECO:0000250|UniProtKB:P31040};
| null |
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1. {ECO:0000250|UniProtKB:P31040}.
| null | null |
FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250|UniProtKB:P31040}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82730
|
MGDG2_ARATH
|
MATTVMALAEKVLERVYGTSKSAVSVTSGDGEKTHRHTHHHIHRIKSYDDIDEDESSLELIQIGAERTKNVLILMSDTGGGHRASAEAIRDAFKIEFGDKYRVIVKDVWKEYTGWPLNDMERSYKFMVKHVQLWKVAFHSTSPKWIHSCYLAAIAAYYAKEVEAGLMEYKPEIIISVHPLMQHIPLWVLKWQELQKRVLFVTVITDLNTCHPTWFHPGVNRCYCPSQEVAKRALFDGLDESQVRVFGLPVRPSFARAVLVKDDLRKELEMDQDLRAVLLMGGGEGMGPVKETAKALEEFLYDKENRKPIGQMVVICGRNKKLASALEAIDWKIPVKVRGFETQMEKWMGACDCIITKAGPGTIAESLIRSLPIILNDYIPGQEKGNVPYVVENGAGVFTRSPKETARIVGEWFSTKTDELEQTSDNARKLAQPEAVFDIVKDIDELSEQRGPLASVSYNLTSSFASLV
|
2.4.1.46
| null |
cellular response to phosphate starvation [GO:0016036]; fatty acid metabolic process [GO:0006631]; galactolipid metabolic process [GO:0019374]; glycolipid biosynthetic process [GO:0009247]
|
chloroplast outer membrane [GO:0009707]
|
1,2-diacylglycerol 3-beta-galactosyltransferase activity [GO:0046509]; UDP-galactosyltransferase activity [GO:0035250]
|
PF04101;PF06925;
|
3.40.50.2000;
|
Glycosyltransferase 28 family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane {ECO:0000305|PubMed:11553816}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-galactose = a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:14945, ChEBI:CHEBI:15378, ChEBI:CHEBI:17615, ChEBI:CHEBI:17815, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.46; Evidence={ECO:0000269|PubMed:11553816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14946; Evidence={ECO:0000269|PubMed:11553816}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycerol + UDP-alpha-D-galactose = 1,2-di-(9Z,12Z-octadecadienoyl)-3-beta-D-galactosyl-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:48492, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:77127, ChEBI:CHEBI:90506; Evidence={ECO:0000269|PubMed:11553816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48493; Evidence={ECO:0000269|PubMed:11553816}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycerol + UDP-alpha-D-galactose = 1-(9Z-octadecenoyl)-2-hexadecanoyl-3-beta-D-galactosyl-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:48496, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:75447, ChEBI:CHEBI:90507; Evidence={ECO:0000269|PubMed:11553816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48497; Evidence={ECO:0000269|PubMed:11553816}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + UDP-alpha-D-galactose = 1,2-di-(9Z-octadecenoyl)-3-beta-D-galactosyl-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:48480, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333, ChEBI:CHEBI:58223, ChEBI:CHEBI:63775, ChEBI:CHEBI:66914; Evidence={ECO:0000269|PubMed:11553816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48481; Evidence={ECO:0000269|PubMed:11553816};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5.;
| null |
FUNCTION: Involved in the synthesis of monogalactosyldiacylglycerol, the major structural component of photosynthetic membranes and in the chloroplast envelope biogenesis. Can use both prokaryotic (18:1/16:0) or eukaryotic (18:2/18:2) 1,2-diacylglycerol species, but operates with some preference for the eukaryotic one. Plays a minor role in galactolipid synthesis in chloroplasts (PubMed:11553816). Is required for membrane lipid remodeling in phosphate-starved roots (PubMed:18808455, PubMed:31201686). Acts as the minor factor involved in digalactosyldiacylglycerol (DGDG) biosynthesis in phosphate-starved roots (PubMed:18808455). Does not seem to be required for plant growth under nutrient-sufficient conditions (PubMed:18808455). Required for membrane lipid remodeling in plants grown in acidic conditions (PubMed:31201686). {ECO:0000269|PubMed:11553816, ECO:0000269|PubMed:18808455, ECO:0000269|PubMed:31201686}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82733
|
PP17_ARATH
|
MDPGTLNSVINRLLEAREKPGKIVQLSETEIKQLCFVSRDIFLRQPNLLELEAPVKICGDIHGQYPDLLRLFEHGGYPPNSNYLFLGDYVDRGKQSLETICLLLAYKIKFPENFFLLRGNHESASINRIYGFYDECKRRFSVKIWRIFTDCFNCLPVAALIDERIFCMHGGLSPELLSLRQIRDIRRPTDIPDRGLLCDLLWSDPDKDVRGWGPNDRGVSYTFGSDIVSGFLKRLDLDLICRAHQVVEDGFEFFANKQLVTIFSAPNYCGEFDNAGAMMSVSEDLTCSFQILKSNDKKSKFSFGSRGGAKTSFPYPKVKSILSSQNSKEYN
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
| null |
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]
|
PF00149;PF16891;
|
3.60.21.10;
|
PPP phosphatase family, PP-1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm {ECO:0000269|PubMed:19329567}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:21222654}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:21222654};
| null | null | null | null |
FUNCTION: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro. {ECO:0000269|PubMed:21222654}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82734
|
PP18_ARATH
|
MMTSMEGMVEKGVLDDIIRRLLEGKGGKQVQLSESEIRQLCFNARQIFLSQPNLLDLHAPIRICGDIHGQYQDLLRLFEYGGYPPSANYLFLGDYVDRGKQSLETICLLLAYKIRYPSKIYLLRGNHEDAKINRIYGFYDECKRRFNVRLWKVFTDCFNCLPVAALIDEKILCMHGGLSPDLDNLNQIREIQRPIEIPDSGLLCDLLWSDPDQKIEGWADSDRGISCTFGADKVAEFLDKNDLDLICRGHQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEIMKPAPASSSHPLKKDFHNRTLGYNLSA
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
|
pollen tube growth [GO:0009860]; root hair cell tip growth [GO:0048768]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00149;PF16891;
|
3.60.21.10;
|
PPP phosphatase family, PP-1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm {ECO:0000269|PubMed:19329567}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:21222654}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:21222654};
| null | null | null | null |
FUNCTION: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro. {ECO:0000269|PubMed:21222654}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82741
|
SGR1_ARATH
|
MCSLSAIMLLPTKLKPAYSDKRSNSSSSSSLFFNNRRSKKKNQSIVPVARLFGPAIFESSKLKVLFLGVDEKKHPSTLPRTYTLTHSDITAKLTLAISQSINNSQLQGWANRLYRDEVVAEWKKVKGKMSLHVHCHISGGHFLLDLFAKFRYFIFCKELPVVLKAFVHGDGNLLNNYPELQEALVWVYFHSNVNEFNKVECWGPLWEAVSPDGHKTETLPEARCADECSCCFPTVSSIPWSHSLSNEGVNGYSGTQTEGIATPNPEKL
|
4.99.1.10
| null |
chlorophyll catabolic process [GO:0015996]
|
chloroplast thylakoid membrane [GO:0009535]
|
lyase activity [GO:0016829]
|
PF12638;
| null |
Staygreen family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:17468209, ECO:0000269|PubMed:22366162}.
|
CATALYTIC ACTIVITY: Reaction=chlorophyll a + 2 H(+) = Mg(2+) + pheophytin a; Xref=Rhea:RHEA:52788, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:58416, ChEBI:CHEBI:136840; EC=4.99.1.10; Evidence={ECO:0000269|PubMed:27604697};
| null | null | null | null |
FUNCTION: Magnesium chelatase involved in chlorophyll a degradation in the chlorophyll-protein complexes of photosystem I (PSI) and photosystem II (PSII) (PubMed:27604697). Contributes to the degradation of PSI and PSII in the thylakoid membranes (PubMed:27604697). Required to trigger chlorophyll degradation during natural and dark-induced leaf senescence (Probable) (PubMed:17468209). Mediates chlorophyll degradation during embryo degreening (PubMed:24043799, PubMed:28873256). Recombinant SGR1 possesses high dechelating activity against chlorophyll a, very low activity against chlorophyllide a, and no activity against chlorophyll b (PubMed:27604697). Magnesium dechelation of chlorophyll a by SGR1 activates chlorophyll b degradation by inducing the expression of NYC1, an enzyme involved in chlorophyll b degradation (PubMed:29425814). {ECO:0000269|PubMed:17468209, ECO:0000269|PubMed:24043799, ECO:0000269|PubMed:27604697, ECO:0000269|PubMed:28873256, ECO:0000269|PubMed:29425814, ECO:0000305|PubMed:17513504}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82777
|
SBT3_SOLLC
|
MELLHLLLFSWALSAHLFLALAQRSTYIVHLDKSLMPNVFTDHHHWHSSTIDSIKASVPSSVDRFHSAPKLVYSYDNVLHGFSAVLSKDELAALKKLPGFISAYKDRTVEPHTTHTSDFLKLNPSSGLWPASGLGQDVIVAVLDSGIWPESASFQDDGMPEIPKRWKGICKPGTQFNASMCNRKLIGANYFNKGILANDPTVNITMNSARDTDGHGTHCASITAGNFAKGVSHFGYAPGTARGVAPRARLAVYKFSFNEGTFTSDLIAAMDQAVADGVDMISISYGYRFIPLYEDAISIASFGAMMKGVLVSASAGNRGPGIGSLNNGSPWILCVASGHTDRTFAGTLTLGNGLKIRGWSLFPARAFVRDSPVIYNKTLSDCSSEELLSQVENPENTIVICDDNGDFSDQMRIITRARLKAAIFISEDPGVFRSATFPNPGVVVNKKEGKQVINYVKNSVTPTATITFQETYLDTKPAPVVAASSARGPSRSYLGISKPDILAPGVLILAAYPPNVFATSIGTNILLSTDYILESGTSMAAPHAAGIAAMLKAAHPEWSPSAIRSAMMTTADPLDNTRKPIKDSDNNKAATPLDMGAGHVDPNRALDPGLVYDATPQDYVNLLCSLNFTEEQFKTIARSSASHNCSNPSADLNYPSFIALYSIEGNFTLLEQKFKRTVTNVGKGAATYKAKLKAPKNSTISVSPQILVFKNKNEKQSYTLTIRYIGDEGQSRNVGSITWVEQNGNHSVRSPIVTSPIIEVW
|
3.4.21.-
| null |
defense response [GO:0006952]; peptide catabolic process [GO:0043171]; plant-type cell wall modification [GO:0009827]; positive regulation of defense response to insect [GO:1900367]; positive regulation of gene expression [GO:0010628]; proteolysis [GO:0006508]; regulation of cell wall pectin metabolic process [GO:1902066]; response to wounding [GO:0009611]; self proteolysis [GO:0097264]
|
extracellular space [GO:0005615]
|
identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF17766;PF05922;PF00082;
|
2.60.40.2310;3.50.30.30;3.30.70.80;3.40.50.200;
|
Peptidase S8 family
|
PTM: Propeptide is internally cleaved at Asn-38 and Asp-52 in a pH-dependent manner leading to the dissociation of the propeptide from the catalytic domain and resulting in the release of the active subtilase. Cleavage occurs at pH 5.7 and to a stronger extent at pH 5.2. {ECO:0000269|PubMed:27451395}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19407393, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395}. Note=Autocatalytic cleavage is required for the secretion of the mature protein. {ECO:0000269|PubMed:19332543}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32.8 uM for aminobenzoyl-SKRDPPKMQTDLY(NO2) derived from the plant peptide hormone systemin (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:19332543}; Vmax=0.151 nmol/min/mg enzyme with aminobenzoyl-SKRDPPKMQTDLY(NO2) derived from the plant peptide hormone systemin as substrate (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:19332543};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. 60% of the activity is retained at pH 11.0 (PubMed:19332543). No autolysis at pH 4.0-9.0 in the presence of 5 mM EDTA or 5 mM CaCl(2) (PubMed:19805099). {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable (PubMed:19332543, PubMed:19805099, PubMed:27451395). Activity is unaffected by heating to 60 degrees Celsius and only partially reduced after incubation at 70 degrees Celsius (PubMed:19332543). {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395};
|
FUNCTION: Serine protease (PubMed:19332543, PubMed:19407393, PubMed:19805099, PubMed:27259555, PubMed:27451395). Has preference for Gln in the P1 position and Lys in the P2 position of oligopeptide substrates. Active also with His in the P1 position (PubMed:19332543). Involved in resistance against insects partly by regulating expression of systemic wound response genes and possibly by its post-ingestive activity in the insect gut. Apart from the role in defense, may be involved in regulation of pectin methylesterases (PMEs) activity and pectin methylesterification of the cell wall (PubMed:27259555). {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19407393, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27259555, ECO:0000269|PubMed:27451395}.
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
|
O82794
|
AGL24_ARATH
|
MAREKIRIKKIDNITARQVTFSKRRRGIFKKADELSVLCDADVALIIFSATGKLFEFSSSRMRDILGRYSLHASNINKLMDPPSTHLRLENCNLSRLSKEVEDKTKQLRKLRGEDLDGLNLEELQRLEKLLESGLSRVSEKKGECVMSQIFSLEKRGSELVDENKRLRDKLETLERAKLTTLKEALETESVTTNVSSYDSGTPLEDDSDTSLKLGLPSWE
| null | null |
cell differentiation [GO:0030154]; floral whorl development [GO:0048438]; maintenance of inflorescence meristem identity [GO:0010077]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vernalization response [GO:0010220]; regulation of timing of transition from vegetative to reproductive phase [GO:0048510]; response to gibberellin [GO:0009739]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF01486;PF00319;
|
3.40.1810.10;
| null |
PTM: Phosphorylated by IMK3. Induced by vernalization. {ECO:0000269|PubMed:12881501}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Translocation from the cytoplasm to the nucleus in the presence of IMK3.
| null | null | null | null | null |
FUNCTION: Transcription activator that mediates floral transition in response to vernalization. Promotes inflorescence fate in apical meristems. Acts in a dosage-dependent manner. Probably involved in the transduction of RLK-mediated signaling (e.g. IMK3 pathway). Together with AP1 and SVP, controls the identity of the floral meristem and regulates expression of class B, C and E genes. When associated with SOC1, mediates effect of gibberellins on flowering under short-day conditions, and regulates the expression of LEAFY (LFY), which links floral induction and floral development. Confers inflorescence characteristics to floral primordia and early flowering. {ECO:0000269|PubMed:12451184, ECO:0000269|PubMed:12609028, ECO:0000269|PubMed:12881501, ECO:0000269|PubMed:14716314, ECO:0000269|PubMed:16679456, ECO:0000269|PubMed:18339670, ECO:0000269|PubMed:18466303, ECO:0000269|PubMed:18694458, ECO:0000269|PubMed:19656343}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82796
|
SERC_ARATH
|
MEALTTSRVVPVQVPCRKLSSLFANFSCLELRRYPCRGLVSIMNHPKLLRPVTASVQPHELSTLGHEGNIVPSKEILDLWRSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDKRPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAVQQIRKGRLYKTMAMIGDGATDLEARKPGGADLFICYAGVQLREAVAANADWLIFKFESLINSLD
|
3.1.3.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
|
dephosphorylation [GO:0016311]; embryo development ending in seed dormancy [GO:0009793]; L-serine biosynthetic process [GO:0006564]; L-serine metabolic process [GO:0006563]; pollen development [GO:0009555]; root development [GO:0048364]; sulfur amino acid metabolic process [GO:0000096]
|
chloroplast [GO:0009507]; plastid [GO:0009536]
|
L-phosphoserine phosphatase activity [GO:0036424]; magnesium ion binding [GO:0000287]
|
PF00702;
|
3.40.50.1000;
|
HAD-like hydrolase superfamily, SerB family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10196182, ECO:0000269|PubMed:23771893}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; Evidence={ECO:0000269|PubMed:10196182}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21209; Evidence={ECO:0000305|PubMed:10196182}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-D-serine = D-serine + phosphate; Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247, ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 mM for 3-phosphoserine (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:10196182};
|
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
| null | null |
FUNCTION: Catalyzes the last step in the plastidial phosphorylated pathway of serine biosynthesis (PPSB). The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Required for embryo, pollen and root development. May be required preferentially for serine biosynthesis in non-photosynthetic tissues. {ECO:0000269|PubMed:10196182, ECO:0000269|PubMed:23771893}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82798
|
ARR4_ARATH
|
MARDGGVSCLRRSEMMSVGGIGGIESAPLDLDEVHVLAVDDSLVDRIVIERLLRITSCKVTAVDSGWRALEFLGLDNEKASAEFDRLKVDLIITDYCMPGMTGYELLKKIKESSNFREVPVVIMSSENVLTRIDRCLEEGAQDFLLKPVKLADVKRLRSHLTKDVKLSNGNKRKLPEDSSSVNSSLPPPSPPLTISPESSPPLTVSTESSDSSPPLSPVEIFSTSPLSSPIDDEDDDVLTSSSEESPIRRQKMRSPGLD
| null | null |
circadian rhythm [GO:0007623]; cytokinin-activated signaling pathway [GO:0009736]; embryo development ending in seed dormancy [GO:0009793]; protein autophosphorylation [GO:0046777]; red or far-red light signaling pathway [GO:0010017]; regulation of DNA-templated transcription [GO:0006355]; response to cytokinin [GO:0009735]; response to red light [GO:0010114]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
phosphorelay response regulator activity [GO:0000156]; protein serine/threonine kinase activity [GO:0004674]
|
PF00072;
|
3.40.50.2300;
|
ARR family, Type-A subfamily
|
PTM: Two-component system major event consists of a His-to-Asp phosphorelay between a sensor histidine kinase (HK) and a response regulator (RR). In plants, the His-to-Asp phosphorelay involves an additional intermediate named Histidine-containing phosphotransfer protein (HPt). This multistep phosphorelay consists of a His-Asp-His-Asp sequential transfer of a phosphate group between first an His and an Asp of the HK protein, followed by the transfer to a conserved His of the HPt protein and finally the transfer to an Asp in the receiver domain of the RR protein.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27274065}.
| null | null | null | null | null |
FUNCTION: Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling. Modulates red light signaling through its interaction with the phytochrome B photoreceptor. {ECO:0000269|PubMed:11691995, ECO:0000269|PubMed:14973166, ECO:0000269|PubMed:9482949}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82804
|
ELF3_ARATH
|
MKRGKDEEKILEPMFPRLHVNDADKGGPRAPPRNKMALYEQLSIPSQRFGDHGTMNSRSNNTSTLVHPGPSSQPCGVERNLSVQHLDSSAANQATEKFVSQMSFMENVRSSAQHDQRKMVREEEDFAVPVYINSRRSQSHGRTKSGIEKEKHTPMVAPSSHHSIRFQEVNQTGSKQNVCLATCSKPEVRDQVKANARSGGFVISLDVSVTEEIDLEKSASSHDRVNDYNASLRQESRNRLYRDGGKTRLKDTDNGAESHLATENHSQEGHGSPEDIDNDREYSKSRACASLQQINEEASDDVSDDSMVDSISSIDVSPDDVVGILGQKRFWRARKAIANQQRVFAVQLFELHRLIKVQKLIAASPDLLLDEISFLGKVSAKSYPVKKLLPSEFLVKPPLPHVVVKQRGDSEKTDQHKMESSAENVVGRLSNQGHHQQSNYMPFANNPPASPAPNGYCFPPQPPPSGNHQQWLIPVMSPSEGLIYKPHPGMAHTGHYGGYYGHYMPTPMVMPQYHPGMGFPPPGNGYFPPYGMMPTIMNPYCSSQQQQQQQPNEQMNQFGHPGNLQNTQQQQQRSDNEPAPQQQQQPTKSYPRARKSRQGSTGSSPSGPQGISGSKSFRPFAAVDEDSNINNAPEQTMTTTTTTTRTTVTQTTRDGGGVTRVIKVVPHNAKLASENAARIFQSIQEERKRYDSSKP
| null | null |
circadian rhythm [GO:0007623]; circumnutation [GO:0010031]; entrainment of circadian clock [GO:0009649]; negative regulation of transcription by RNA polymerase II [GO:0000122]; photoperiodism, flowering [GO:0048573]; red, far-red light phototransduction [GO:0009585]; regulation of circadian rhythm [GO:0042752]; regulation of flower development [GO:0009909]; regulation of photoperiodism, flowering [GO:2000028]; regulation of stomatal movement [GO:0010119]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response to cold [GO:0009409]; unidimensional cell growth [GO:0009826]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity [GO:0003700]
| null | null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22327739}. Note=Forms nuclear bodies. {ECO:0000269|PubMed:22327739}.
| null | null | null | null | null |
FUNCTION: May be a transcription factor part of a circadian clock input pathway. Acts within a 'zeitnehmer' feedback loop and is involved in its own circadian regulation. Has no role in regulating circadian clock function in the dark. Part of a corepressor complex consisting of ELF4, ELF3, and LUX involved in the transcriptional regulation of APRR9. The activity of the protein may be decreased in long day conditions due to its interaction with phytochrome B (phyB). Can regulate the initiation of flowering independently of phyB. Also involved in responses to nematode parasitism, like the formation of the nematode feeding structure. {ECO:0000269|PubMed:11402161, ECO:0000269|PubMed:22307044, ECO:0000269|PubMed:22327739}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82811
|
NRT21_ARATH
|
MGDSTGEPGSSMHGVTGREQSFAFSVQSPIVHTDKTAKFDLPVDTEHKATVFKLFSFAKPHMRTFHLSWISFSTCFVSTFAAAPLVPIIRENLNLTKQDIGNAGVASVSGSIFSRLVMGAVCDLLGPRYGCAFLVMLSAPTVFSMSFVSDAAGFITVRFMIGFCLATFVSCQYWMSTMFNSQIIGLVNGTAAGWGNMGGGITQLLMPIVYEIIRRCGSTAFTAWRIAFFVPGWLHIIMGILVLNLGQDLPDGNRATLEKAGEVAKDKFGKILWYAVTNYRTWIFVLLYGYSMGVELSTDNVIAEYFFDRFHLKLHTAGLIAACFGMANFFARPAGGYASDFAAKYFGMRGRLWTLWIIQTAGGLFCVWLGRANTLVTAVVAMVLFSMGAQAACGATFAIVPFVSRRALGIISGLTGAGGNFGSGLTQLLFFSTSHFTTEQGLTWMGVMIVACTLPVTLVHFPQWGSMFLPPSTDPVKGTEAHYYGSEWNEQEKQKNMHQGSLRFAENAKSEGGRRVRSAATPPENTPNNV
| null | null |
cellular response to nitrate [GO:0071249]; lateral root development [GO:0048527]; nitrate assimilation [GO:0042128]; nitrate transmembrane transport [GO:0015706]; response to nitrate [GO:0010167]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
nitrate transmembrane transporter activity [GO:0015112]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Nitrate/nitrite porter (TC 2.A.1.8) family
|
PTM: Might be subject to partial proteolysis at the C-terminus.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17573350, ECO:0000269|PubMed:17583518, ECO:0000269|PubMed:19704673, ECO:0000269|PubMed:20561257}; Multi-pass membrane protein {ECO:0000269|PubMed:17573350, ECO:0000269|PubMed:17583518, ECO:0000269|PubMed:19704673, ECO:0000269|PubMed:20561257}.
| null | null | null | null | null |
FUNCTION: Involved in nitrate transport, but does not seem to be able to mediate transport by its own. Acts as a dual component transporter with NTR3.1. Acts as a repressor of lateral root initiation under high sucrose/low nitrate conditions. {ECO:0000269|PubMed:11553754, ECO:0000269|PubMed:15107992, ECO:0000269|PubMed:16157886, ECO:0000269|PubMed:16415211, ECO:0000269|PubMed:17085507, ECO:0000269|PubMed:19704673}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O82827
|
UPPS_MICLU
|
MFPIKKRKAIKNNNINAAQIPKHIAIIMDGNGRWAKQKKMPRIKGHYEGMQTVKKITRYASDLGVKYLTLYAFSTENWSRPKDEVNYLMKLPGDFLNTFLPELIEKNVKVETIGFIDDLPDHTKKAVLEAKEKTKHNTGLTLVFALNYGGRKEIISAVQLIAERYKSGEISLDEISETHFNEYLFTANMPDPELLIRTSGEERLSNFLIWQCSYSEFVFIDEFWPDFNEESLAQCISIYQNRHRRFGGL
|
2.5.1.31
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
|
polyprenol biosynthetic process [GO:0016094]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
di-trans,poly-cis-undecaprenyl-diphosphate synthase activity [GO:0008834]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; polyprenyltransferase activity [GO:0002094]; Z-farnesyl diphosphate synthase activity [GO:0033850]
|
PF01255;
|
3.40.1180.10;
|
UPP synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate; Xref=Rhea:RHEA:27551, ChEBI:CHEBI:33019, ChEBI:CHEBI:58405, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.31; Evidence={ECO:0000269|PubMed:9677368};
| null | null | null | null |
FUNCTION: Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate. UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. {ECO:0000269|PubMed:3182755, ECO:0000269|PubMed:9677368}.
|
Micrococcus luteus (Micrococcus lysodeikticus)
|
O82872
|
DTA_ARTSP
|
MSQEVIRGIALPPPAQPGDPLARVDTPSLVLDLAPFEANLRAMQAWADRHDVALRPHAKAHKCPEIALRQLALGARGICCQKVSEALPFVAAGIQDIHISNEVVGPAKLALLGQLARVAKISVCVDNAHNLSQVSQAMVQAGAQIDVLVEVDVGQGRCGVSDDALVLALAQQARDLPGVNFAGLQAYHGSVQHYRTREERAEVCRQAARIAASYAQLLRESGIACDTITGGGTGSAEFDAASGVYTELQAGSYAFMDGDYGANEWDGPLAFENSLFVLATVMSKPAPDRVILDAGLKSTTAECGPPAIFGEPGLTYTAINDEHGVVRVEPGAQAPDLGAVLRLVPSHVDPTFNLHDGLVVVRDGVVEDIWEISARGFSR
|
4.1.2.42
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Note=Binds 1 Mn(2+) ion per subunit. Can also use Co(2+), Ni(2+) and Mg(2+). {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
|
D-amino acid catabolic process [GO:0019478]; D-serine catabolic process [GO:0036088]
| null |
aldehyde-lyase activity [GO:0016832]; D-serine ammonia-lyase activity [GO:0008721]; D-threonine aldolase activity [GO:0043876]
|
PF01168;PF14031;
|
3.20.20.10;2.40.37.20;
|
DSD1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=D-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:15257, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57757; EC=4.1.2.42; Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; CATALYTIC ACTIVITY: Reaction=D-allo-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:20073, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:58645; EC=4.1.2.42; Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.81 mM for D-threonine (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=14 mM for D-allothreonine (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=1.75 mM for D-threo-beta-hydroxy-alpha-aminovaleric acid (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=46.8 mM for D-threo-beta-phenylserine (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=8.4 mM for D-threonine (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=8.8 mM for D-threonine (at pH 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=4.4 mM for D-allothreonine (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=4.3 mM for D-allothreonine (at pH 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=5.4 mM for DL-threo-phenylserine (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=5.9 mM for DL-threo-phenylserine (at pH 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=5.3 mM for DL-erythro-phenylserine (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=4.9 mM for DL-erythro-phenylserine (at pH 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=1.8 mM for DL-threo-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=1.8 mM for DL-threo-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=2.5 mM for DL-erythro-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=2 mM for DL-erythro-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=1.2 mM for DL-threo-beta-3,4-dihydroxyphenylserine (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; KM=1.4 mM for DL-threo-beta-3,4-dihydroxyphenylserine (at pH 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=38.8 umol/min/mg enzyme with D-threonine as substrate (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=102 umol/min/mg enzyme with D-allothreonine as substrate (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=9.01 umol/min/mg enzyme with D-threo-beta-hydroxy-alpha-aminovaleric acid as substrate (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=59.9 umol/min/mg enzyme with D-threo-beta-phenylserine as substrate (at pH 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=32.1 umol/min/mg enzyme with D-threonine as substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=3 umol/min/mg enzyme with D-threonine as substrate (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=34.9 umol/min/mg enzyme with D-allothreonine as substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=2.8 umol/min/mg enzyme with D-allothreonine as substrate (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=209.8 umol/min/mg enzyme with DL-threo-phenylserine as substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=4.9 umol/min/mg enzyme with DL-threo-phenylserine as substrate (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=164.4 umol/min/mg enzyme with DL-erythro-phenylserine as substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=1.9 umol/min/mg enzyme with DL-erythro-phenylserine as substrate (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=129.3 umol/min/mg enzyme with DL-threo-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=9.2 umol/min/mg enzyme with DL-threo-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=16 umol/min/mg enzyme with DL-erythro-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=1.9 umol/min/mg enzyme with DL-erythro-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=84.6 umol/min/mg enzyme with DL-threo-beta-3,4-dihydroxyphenylserine as substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}; Vmax=8.4 umol/min/mg enzyme with DL-threo-beta-3,4-dihydroxyphenylserine as substrate (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. Stable between pH 7.0 and 8.5. {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable below 55 degrees Celsius. {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
|
FUNCTION: Catalyzes the reversible cleavage of D-threonine or D-allothreonine into glycine and acetaldehyde. Can also cleave D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid, D-beta-3,4-dihydroxyphenylserine and D-beta-3,4-methylenedioxyphenylserine into glycine and the corresponding aldehyde compounds. Inactive towards D-serine, beta-hydroxyaspartate and O-phospho-DL-threonine. {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}.
|
Arthrobacter sp
|
O82882
|
STCE_ECO57
|
MNTKMNERWRTPMKLKYLSCTILAPLAIGVFSATAADNNSAIYFNTSQPINDLQGSLAAEVKFAQSQILPAHPKEGDSQPHLTSLRKSLLLVRPVKADDKTPVQVEARDDNNKILGTLTLYPPSSLPDTIYHLDGVPEGGIDFTPHNGTKKIINTVAEVNKLSDASGSSIHSHLTNNALVEIHTANGRWVRDIYLPQGPDLEGKMVRFVSSAGYSSTVFYGDRKVTLSVGNTLLFKYVNGQWFRSGELENNRITYAQHIWSAELPAHWIVPGLNLVIKQGNLSGRLNDIKIGAPGELLLHTIDIGMLTTPRDRFDFAKDKEAHREYFQTIPVSRMIVNNYAPLHLKEVMLPTGELLTDMDPGNGGWHSGTMRQRIGKELVSHGIDNANYGLNSTAGLGENSHPYVVAQLAAHNSRGNYANGIQVHGGSGGGGIVTLDSTLGNEFSHEVGHNYGLGHYVDGFKGSVHRSAENNNSTWGWDGDKKRFIPNFYPSQTNEKSCLNNQCQEPFDGHKFGFDAMAGGSPFSAANRFTMYTPNSSAIIQRFFENKAVFDSRSSTGFSKWNADTQEMEPYEHTIDRAEQITASVNELSESKMAELMAEYAVVKVHMWNGNWTRNIYIPTASADNRGSILTINHEAGYNSYLFINGDEKVVSQGYKKSFVSDGQFWKERDVVDTREARKPEQFGVPVTTLVGYYDPEGTLSSYIYPAMYGAYGFTYSDDSQNLSDNDCQLQVDTKEGQLRFRLANHRANNTVMNKFHINVPTESQPTQATLVCNNKILDTKSLTPAPEGLTYTVNGQALPAKENEGCIVSVNSGKRYCLPVGQRSGYSLPDWIVGQEVYVDSGAKAKVLLSDWDNLSYNRIGEFVGNVNPADMKKVKAWNGQYLDFSKPRSMRVVYK
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:16788173}; Note=Binds 1 zinc ion per subunit. Does not contain structural calcium, which is often associated with other metalloproteases. {ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:16788173};
|
proteolysis [GO:0006508]
|
extracellular region [GO:0005576]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF17945;PF10462;PF20944;PF12561;
|
2.60.120.1230;2.60.20.40;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12123444}. Note=Secreted via the etp type II secretion pathway.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 uM for MUC7 {ECO:0000269|PubMed:16788173}; KM=0.27 uM for SERPING1 {ECO:0000269|PubMed:16788173}; Vmax=70.2 nM/min/ug enzyme for MUC7 cleavage {ECO:0000269|PubMed:16788173}; Vmax=66.8 nM/min/ug enzyme for SERPING1 cleavage {ECO:0000269|PubMed:16788173}; Note=Proteolytic activity is 2.5-fold more efficient with the secreted mucin MUC7 than with SERPING1.;
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. Active from pH 6.1 to 9.0. {ECO:0000269|PubMed:16788173};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-42 degrees Celsius. Active from 4 to 55 degrees Celsius. Inactive above 60 degrees Celsius. {ECO:0000269|PubMed:16788173};
|
FUNCTION: Virulence factor that contributes to intimate adherence of enterohemorrhagic E.coli (EHEC) O157:H7 to host cells. Is able to cleave the secreted human mucin 7 (MUC7) and the glycoprotein 340 (DMBT1/GP340). Also cleaves human C1 inhibitor (SERPING1), a regulator of multiple inflammatory pathways, and binds and localizes it to bacterial and host cell surfaces, protecting them from complement-mediated lysis. Therefore, the current model proposes two roles for StcE during infection: it acts first as a mucinase, allowing passage of EHEC through the oral cavity by cleaving the salivary glycoproteins that are responsible for bacterial aggregation. Similarly, in the colon, StcE cleaves the glycoproteins that protect the intestinal epithelial surface, allowing EHEC to come into close contact with host cell membranes. Secondly, it acts as an anti-inflammatory agent by localizing SERPING1 to cell membranes. {ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536, ECO:0000269|PubMed:15731026, ECO:0000269|PubMed:16788173}.
|
Escherichia coli O157:H7
|
O83553
|
PFP_TREPA
|
MSISLLQQERHRYLPKVPDLLRGDFRRVCARRGLSTTAVADYDALRSLFARTYGQPLVNFVNASEKNEDSPMETAPEPRGLRVAIVLSGGQAPGGHNVIAGLFDGLKRWHADSVLIGFLGGPAGVLSGDHIEICADRVDAYRNTGGFDLIGSGRTKIESESQFAAAAQTVTRMALDALVVVGGDDSNTNAALLAEHFVNSGISTKVIGVPKTIDGDLKNEAIETSFGFDTATKTYSELIGNIARDACSARKYWHFIKLMGRSASHIALECALKTQPNVCLISEEVAAQSLTLAQIVQSLCDTIATRAQHGEHFGIVLVPEGLIEFIPEMKALITELNEVMARRAQEFEALDTPDAQRVWIEQALSASARAVFNALPAEISTQLLADRDPHGNVQVSRIDTERLLILQVTERLAQMKQEGTYTGVFSSIAHFFGYEGRCAFPSNFDADYCYTLGLTACLLAVHRFTGYVASVRNLTSSVAEWAVGGVPLTMLMNMERRHGSQKPVIKKALVDLEGMPFRVFSRRRASWALKTSYVYPGAVQYYGPPAVCDEPSVTIRLERPAPAANSSFGHRSS
|
2.7.1.90
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01980};
|
fructose 6-phosphate metabolic process [GO:0006002]; photosynthesis [GO:0015979]; response to glucose [GO:0009749]
|
cytosol [GO:0005829]
|
6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872]
|
PF00365;
|
3.40.50.450;3.40.50.460;
|
Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'Long' sub-subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01980}.
|
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|PubMed:11164318};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.39 mM for phosphate {ECO:0000269|PubMed:11164318}; KM=0.042 mM for diphosphate {ECO:0000269|PubMed:11164318}; KM=0.529 mM for fructose 6-phosphate {ECO:0000269|PubMed:11164318}; KM=0.267 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:11164318}; Vmax=141 umol/min/mg enzyme for the forward reaction {ECO:0000269|PubMed:11164318}; Vmax=42.4 umol/min/mg enzyme for the reverse reaction {ECO:0000269|PubMed:11164318};
|
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01980}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for both the forward and reverse reactions. {ECO:0000269|PubMed:11164318};
| null |
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|PubMed:11164318}.
|
Treponema pallidum (strain Nichols)
|
O84395
|
DAPAT_CHLTR
|
MKRNPHFVSLTKNYLFADLQKRVAQFRLENPQHTVINLSIGDTTQPLNASVAEAFASSIARLSSPTTCRGYGPDFGLPALRQKLSEDFYRGFVDAKEIFISDGAKVDLFRLLSFFGPNQTVAIQDPSYPAYLDIARLTGAKEIIALPCLQENAFFPEFPEDTHIDILCLCSPNNPTGTVLNKDQLRAIVHYAIEHEILILFDAAYSTFISDPSLPKSIFEIPDARFCAIEINSFSKPLGFAGIRLGWTVIPQELTYADGHFVIQDWERFLSTTFNGASIPAQEAGVAGLSILPQLEAIHYYRENSDLLRKALLATGFEVFGGEHAPYLWVKPTQANISDRDLFDFFLREYHIAITPGIGFGRSGSGFVRFSSLGKREDILAACERLQMAPALQS
|
2.6.1.83
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000269|PubMed:17093042, ECO:0000269|PubMed:21722650};
|
lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway [GO:0033362]
| null |
L,L-diaminopimelate aminotransferase activity [GO:0010285]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family, LL-diaminopimelate aminotransferase subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate; Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985, ChEBI:CHEBI:57609; EC=2.6.1.83; Evidence={ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000269|PubMed:17093042};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=116 uM for LL-2,6-diaminopimelate (at 30 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:17093042}; KM=2.1 mM for 2-oxoglutarate (at 30 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:17093042}; KM=19 uM for L-2,3,4,5-tetrahydrodipicolinate (at 30 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:17093042}; KM=4 mM for glutamic acid (at 30 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:17093042}; Vmax=0.58 umol/min/mg enzyme for the forward reaction (at 30 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:17093042}; Vmax=0.01 umol/min/mg enzyme for the reverse reaction (at 30 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:17093042};
|
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01642}.
| null | null |
FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate (PubMed:17093042, PubMed:21722650). Is also able to use meso-diaminopimelate, cystathionine, lysine or ornithine as substrates (PubMed:17093042). {ECO:0000269|PubMed:17093042, ECO:0000269|PubMed:21722650}.
|
Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
|
O84616
|
CADD_CHLTR
|
MMEVFMNFLDQLDLIIQNKHMLEHTFYVKWSKGELTKEQLQAYAKDYYLHIKAFPKYLSAIHSRCDDLEARKLLLDNLMDEENGYPNHIDLWKQFVFALGVTPEELEAHEPSEAAKAKVATFMRWCTGDSLAAGVAALYSYESQIPRIAREKIRGLTEYFGFSNPEDYAYFTEHEEADVRHAREEKALIEMLLKDDADKVLEASQEVTQSLYGFLDSFLDPGTCCSCHQSY
|
1.3.3.-
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:32967910, ECO:0000269|PubMed:36122239, ECO:0000305|PubMed:15087448}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:36122239}; Note=Binds 2 divalent metal cations per subunit (PubMed:15087448). Can use a diiron cofactor for catalysis (PubMed:32967910). However, activity is much higher in vitro in the presence of both iron and manganese, which implicates a heterodinuclear iron/manganese cofactor (PubMed:36122239). {ECO:0000269|PubMed:15087448, ECO:0000269|PubMed:32967910, ECO:0000269|PubMed:36122239};
|
cellular aromatic compound metabolic process [GO:0006725]; heterocycle metabolic process [GO:0046483]; organic cyclic compound metabolic process [GO:1901360]; small molecule metabolic process [GO:0044281]; sulfur compound metabolic process [GO:0006790]
|
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]
|
metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; toxin activity [GO:0090729]
|
PF03070;
|
1.20.910.10;
|
CADD family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11805081}. Host cytoplasm {ECO:0000269|PubMed:11805081}. Note=Secreted into the host cytoplasm, where it co-localizes with Fas in the proximity of the inclusion body. {ECO:0000269|PubMed:11805081}.
| null | null | null | null | null |
FUNCTION: Involved in de novo para-aminobenzoate (PABA) biosynthesis (PubMed:23972426, PubMed:32967910, PubMed:36122239). Acts as a self-sacrificing or 'suicide' enzyme that utilizes its own active site tyrosine residue(s) as the substrate for PABA synthesis (PubMed:32967910, PubMed:36122239). The side chain of the tyrosine residue is released from the protein backbone via cleavage of the C(alpha)-C(beta) bond, leaving a glycine in place of the original tyrosine residue (PubMed:32967910, PubMed:36122239). Reaction requires O(2) and a reduced dimetal cofactor (PubMed:32967910, PubMed:36122239). {ECO:0000269|PubMed:23972426, ECO:0000269|PubMed:32967910, ECO:0000269|PubMed:36122239}.; FUNCTION: Was also identified as a specific toxin that associates with death domains of tumor necrosis factor family (TNF) receptors and induces apoptosis in mammalian cell lines through a Caspase-dependent mechanism. {ECO:0000269|PubMed:11805081, ECO:0000269|PubMed:15087448}.
|
Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
|
O84947
|
SCTE2_SALTY
|
MNRIHSNSDSAAGVTALTHHHLSNVSCVSSGSLGKRQHRVNSTFGDGNAACLLSGKISLQEASNALKQLLDAVPGNHKRPSLPDFLQTNPAVLSMMMTSLILNVFGNNAQSLCQQLERATEVQNALRNKQVKEYQEQIQKAIEQEDKARKAGIFGAIFDWITGIFETVIGALKVVEGFLSGNPAEMASGVAYMAAGCAGMVKAGAETAMMCGADHDTCQAIIDVTSKIQFGCEAVALALDVFQIGRAFMATRGLSGAAAKVLDSGFGEEVVERMVGAGEAEIEELAEKFGEEVSESFSKQFEPLEREMAMANEMAEEAAEFSRNVENNMTRSAGKSFTKEGVKAMAKEAAKEALEKCVQEGGKFLLKKFRNKVLFNMFKKILYALLRDCSFKGLQAIRCATEGASQMNTGMVNTEKAKIEKKIEQLITQQRFLDFIMQQTENQKKIEQKRLEELYKGSGAALRDVLDTIDHYSSVQARIAGYRA
| null | null |
protein secretion by the type III secretion system [GO:0030254]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell membrane [GO:0033644]; membrane [GO:0016020]
|
protein-folding chaperone binding [GO:0051087]
|
PF04888;
| null |
SctE/SipB/YopB family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11159962, ECO:0000269|PubMed:11567004}. Cell surface {ECO:0000269|PubMed:11159962, ECO:0000269|PubMed:11567004}. Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=Secreted via the type III secretion system 2 (SPI-2 T3SS) (PubMed:11159962, PubMed:11567004). After secretion, localizes mainly on the surface of the bacterial cell (PubMed:11159962, PubMed:11567004). {ECO:0000269|PubMed:11159962, ECO:0000269|PubMed:11567004}.
| null | null | null | null | null |
FUNCTION: Component of the type III secretion system 2 (SPI-2 T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (Probable). SseC/SctE2 and SseD/SctB2 are inserted into the host membrane where they form a pore and allow the translocation of effector proteins into the cytosol of target cells (Probable). {ECO:0000305|PubMed:11567004}.; FUNCTION: Required for the translocation of SPI-2 effector proteins (PubMed:11567004). Required for systemic Salmonella infection of the mouse (PubMed:11159962). Essential for SpvB-induced actin depolymerization in the host cell cytoplasm (PubMed:18248436). {ECO:0000269|PubMed:11159962, ECO:0000269|PubMed:11567004, ECO:0000269|PubMed:18248436}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
O85040
|
RBL1_HALNC
|
MAVKKYSAGVKEYRQTYWMPEYTPLDSDILACFKITPQPGVDREEAAAAVAAESSTGTWTTVWTDLLTDMDYYKGRAYRIEDVPGDDAAFYAFIAYPIDLFEEGSVVNVFTSLVGNVFGFKAVRGLRLEDVRFPLAYVKTCGGPPHGIQVERDKMNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVQDATETAEAQTGERKGHYLNVTAPTPEEMYKRAEFAKEIGAPIIMHDYITGGFTANTGLAKWCQDNGVLLHIHRAMHAVIDRNPNHGIHFRVLTKILRLSGGDHLHTGTVVGKLEGDRASTLGWIDLLRESFIPEDRSRGIFFDQDWGSMPGVFAVASGGIHVWHMPALVNIFGDDSVLQFGGGTLGHPWGNAAGAAANRVALEACVEARNQGRDIEKEGKEILTAAAQHSPELKIAMETWKEIKFEFDTVDKLDTQNR
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01338}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
|
reductive pentose-phosphate cycle [GO:0019253]
|
carboxysome [GO:0031470]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
| null |
SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3, ECO:0000305|PubMed:16535117}. Note=When the major carboxysomal shell protein CsoS1A is disrupted most RuBisCO is found in the soluble (cytoplasmic) fraction (PubMed:16535117). Most protein is found in the carboxysome interior and not associated with the shell (PubMed:14729686). This bacterium makes alpha-type carboxysomes (PubMed:18258595, Ref.6). {ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:16535117, ECO:0000269|PubMed:18258595, ECO:0000269|Ref.6}.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3}; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|Ref.3};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=163.7 uM for CO(2); Vmax=2.9 umol/min/mg enzyme {ECO:0000269|PubMed:18258595}; Note=For enzyme freed from the carboxysome. {ECO:0000269|PubMed:18258595};
| null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (By similarity) (PubMed:18258595, PubMed:18974784, Ref.3). There are estimated to be 270 RuBisCO heterohexadecamers per carboxysome (Ref.6). {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3, ECO:0000269|Ref.6}.; FUNCTION: Alpha-carboxysomes are able to assemble in the absence of RuBisCO, unlike beta-carboxysomes. The RuBisCO large subunit is required for enzyme integration into carboxysomes; replacing it with the carboxysomally targeted gene (Tcr_0838, AC Q31HD9) of H.crungenus places RuBisCO in the carboxysome, while the non-carboxysomal large subunit of H.crungenus (Tcr_0427, AC Q31IK0) is not incorporated in the carboxysome. {ECO:0000269|PubMed:18974784}.
|
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
|
O85041
|
CSOS2_HALNC
|
MPSQSGMNPADLSGLSGKELARARRAALSKQGKAAVSNKTASVNRSTKQAASSINTNQVRSSVNEVPTDYQMADQLCSTIDHADFGTESNRVRDLCRQRREALSTIGKKAAKTTGKPSGRVRPQQSVVHNDAMIENAGDTNQSSSTSLNNELSEICSIADDMPERFGSQAKTVRDICRARRQALSERGTRAVPPKPQSQGGPGRNGYQIDGYLDTALHGRDAAKRHREMLCQYGRGTAPSCKPTGRVKNSVQSGNAAPKKVETGHTLSGGSVTGTQVDRKSHVTGNEPGTCRAVTGTEYVGTEQFTSFCNTSPKPNATKVNVTTTARGRPVSGTEVSRTEKVTGNESGVCRNVTGTEYMSNEAHFSLCGTAAKPSQADKVMFGATARTHQVVSGSDEFRPSSVTGNESGAKRTITGSQYADEGLARLTINGAPAKVARTHTFAGSDVTGTEIGRSTRVTGDESGSCRSISGTEYLSNEQFQSFCDTKPQRSPFKVGQDRTNKGQSVTGNLVDRSELVTGNEPGSCSRVTGSQYGQSKICGGGVGKVRSMRTLRGTSVSGQQLDHAPKMSGDERGGCMPVTGNEYYGREHFEPFCTSTPEPEAQSTEQSLTCEGQIISGTSVDASDLVTGNEIGEQQLISGDAYVGAQQTGCLPTSPRFNQTGNVQSMGFKNTNQPEQNFAPGEVMPTDFSIQTPARSAQNRITGNDIAPSGRITGPGMLATGLITGTPEFRHAARELVGSPQPMAMAMANRNKAAQAPVVQPEVVATQEKPELVCAPRSDQMDRVSGEGKERCHITGDDWSVNKHITGTAGQWASGRNPSMRGNARVVETSAFANRNVPKPEKPGSKITGSSGNDTQGSLITYSGGARG
| null | null |
carbon fixation [GO:0015977]
|
carboxysome [GO:0031470]
|
structural constituent of carboxysome shell [GO:0043886]
|
PF12288;
| null |
CsoS2 family
|
PTM: Seen in gels as 2 forms (of 85 and 130 kDa, equal amounts of each) which have the same N-terminus, called respectively CsoS2A and CsoS2B (PubMed:10525740). Partial tryptic digestion and mass spectrometric analysis, as well as the presence of the shorter form even when a C-terminally tagged version is engineered, suggests CsoS2A is shorter at the C-terminus, but its sequence is not known (Probable). It has been shown these 2 forms are produced by ribosomal frameshifting (PubMed:26608811). {ECO:0000269|PubMed:10525740, ECO:0000269|PubMed:26608811, ECO:0000305|PubMed:25826651}.
|
SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:10525740, ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:25826651, ECO:0000269|PubMed:26608811}. Note=Immunogold staining shows this is a shell protein (PubMed:10525740). C-terminally tagged protein immunoprecipitates whole carboxysomes, showing the C-terminus is on the exterior (PubMed:25826651). This bacterium makes alpha-type carboxysomes (PubMed:18258595, Ref.4). {ECO:0000269|PubMed:10525740, ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:25826651, ECO:0000269|Ref.4}.
| null | null | null | null | null |
FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates interaction between RuBisCO and the Cb shell (Probable) (PubMed:25826651, PubMed:32123388). The 3 C-terminal repeats act as the encapsulation signal to target proteins to the Cb; they are necessary and sufficient to target both CsoS2 and foreign proteins to the Cb (PubMed:33116131). The N-terminal repeats of this (probably) intrinsically disordered protein bind simultaneously to both subunits of RuBisCO; minimally 2 N-repeats are necessary for RuBisCO assembly into the Cb in vivo. Probably also interacts with the major shell proteins (CsoS1); that interaction would increase the local concentration of CsoS2 so that it can condense RuBisCO and full carboxysomes can be formed (PubMed:32123388). The long form is essential for Cb formation while the short form is not (PubMed:26608811). There are estimated to be 143 CsoS2A and 186 CsoS2B proteins per Cb (Ref.4). {ECO:0000269|PubMed:25826651, ECO:0000269|PubMed:26608811, ECO:0000269|PubMed:32123388, ECO:0000269|PubMed:33116131, ECO:0000269|Ref.4, ECO:0000305|PubMed:33116131}.; FUNCTION: Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell. {ECO:0000269|PubMed:25826651, ECO:0000269|PubMed:26608811, ECO:0000269|PubMed:32123388, ECO:0000269|PubMed:33116131}.
|
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
|
O85042
|
CSOCA_HALNC
|
MNTRNTRSKQRAPFGVSSSVKPRLDLIEQAPNPAYDRHPACITLPERTCRHPLTDLEANEQLGRCEDSVKNRFDRVIPFLQVVAGIPLGLDYVTRVQELAQSSLGHTLPEELLKDNWISGHNLKGIFGYATAKALTAATEQFSRKIMSEKDDSASAIGFFLDCGFHAVDISPCADGRLKGLLPYILRLPLTAFTYRKAYAGSMFDIEDDLAQWEKNELRRYREGVPNTADQPTRYLKIAVYHFSTSDPTHSGCAAHGSNDRAALEAALTQLMKFREAVENAHCCGASIDILLIGVDTDTDAIRVHIPDSKGFLNPYRYVDNTVTYAQTLHLAPDEARVIIHEAILNANRSDGWAKGNGVASEGMRRFIGQLLINNLSQIDYVVNRHGGRYPPNDIGHAERYISVGDGFDEVQIRNLAYYAHLDTVEENAIDVDVGIKIFTKLNLSRGLPIPIAIHYRYDPNVPGSRERTVVKARRIYNAIKERFSSLDEQNLLQFRLSVQAQDIGSPIEEVASA
|
4.2.1.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16407248, ECO:0000269|PubMed:17012396, ECO:0007744|PDB:2FGY}; Note=The fourth ligand is a water molecule. Binds 1 Zn(2+) per monomer, in PDB:2FGY a second Zn(2+) is seen, but one of its ligands is an accidentally introduced mutation. {ECO:0000269|PubMed:16407248, ECO:0007744|PDB:2FGY};
|
carbon fixation [GO:0015977]
|
carboxysome [GO:0031470]
|
carbonate dehydratase activity [GO:0004089]; metal ion binding [GO:0046872]
|
PF08936;PF20686;PF20687;
|
3.30.1330.140;1.20.120.1310;
|
Beta-class carbonic anhydrase family, CsoSCA subfamily
| null |
SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:10816046, ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:17012396, ECO:0000269|PubMed:18258595}. Note=Coomassie staining of gels and immunogold staining shows this is a minor shell protein (PubMed:10816046, PubMed:14729686). The protein is probably found inside the carboxysome, as its addition to mutant organelles does not complement the deletion (PubMed:18258595). This cyanobacterium makes alpha-type carboxysomes (PubMed:18258595, Ref.5). {ECO:0000269|PubMed:10816046, ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:18258595, ECO:0000269|Ref.5}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:17012396};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.2 mM for CO(2) {ECO:0000269|PubMed:17012396}; KM=9.3 mM for hydrogencarbonate {ECO:0000269|PubMed:17012396}; Note=kcat is 8.9 x 10(4) sec(-1) for CO(2) hydration at pH 8.0, and 4.6 x 10(4) sec(-1) for hydrogencarbonate dehydration at pH 7.0. {ECO:0000269|PubMed:17012396};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5 for CO(2) hydration, and pH 6.0 for hydrogencarbonate dehydration. {ECO:0000269|PubMed:17012396};
| null |
FUNCTION: Reversible hydration of carbon dioxide (PubMed:14729686, PubMed:17012396, PubMed:18258595). Essential for chemolithotrophic carbon dioxide fixation, supplies CO(2) to RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) in the carboxysome (Probable) (PubMed:18258595). There are estimated to be 40 CsoSCA dimers per carboxysome (Ref.5). {ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:17012396, ECO:0000269|PubMed:18258595, ECO:0000269|Ref.5, ECO:0000305|PubMed:14729686}.; FUNCTION: Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell. {ECO:0000269|PubMed:33116131}.
|
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
|
O85673
|
ANTDA_ACIAD
|
MTARNLAEWQNFVQGCIDFRPNDGVYRIARDMFTEPELFELEMELIFEKVWIYACHESEIPNNNDFVTVQIGRQPMIVSRDGKGELHAMVNACEHRGATLTRVAKGNQSVFTCPFHAWCYKSDGRLVKVKAPGEYCEDFDKSSRGLKQGRIASYRGFVFVSLDTQATDSLEDFLGDAKVFLDLMVDQSPTGELEVLQGKSAYTFAGNWKLQNENGLDGYHVSTVHYNYVSTVQHRQQVNAAKGDELDTLDYSKLGAGDSETDDGWFSFKNGHSVLFSDMPNPTVRPGYNTVMPYLVEKFGEKRAEWAMHRLRNLNLYPSLFFMDQISSQLRIIRPVAWNKTEVISQCIGVKGESSEARRNRIRQFEDFFNVSGLGTPDDLVEFREQQKGFQGRIERWSDISRGYHQWTYGPTQNSQDLGIEPVITGREFTHEGLYVNQHGQWQRLILDGLNKKALKMHDVTFDNQSVMDEV
|
1.14.12.1
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:11114907}; Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:11114907}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:11114907}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:11114907};
|
aromatic compound catabolic process [GO:0019439]
| null |
2 iron, 2 sulfur cluster binding [GO:0051537]; anthranilate 1,2-dioxygenase (deaminating, decarboxylating) activity [GO:0018618]; iron ion binding [GO:0005506]
|
PF00355;PF00848;
|
2.102.10.10;
|
Bacterial ring-hydroxylating dioxygenase alpha subunit family
| null | null |
CATALYTIC ACTIVITY: Reaction=anthranilate + 3 H(+) + NADH + O2 = catechol + CO2 + NAD(+) + NH4(+); Xref=Rhea:RHEA:11076, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16567, ChEBI:CHEBI:18135, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.1; Evidence={ECO:0000269|PubMed:11114907}; CATALYTIC ACTIVITY: Reaction=anthranilate + 3 H(+) + NADPH + O2 = catechol + CO2 + NADP(+) + NH4(+); Xref=Rhea:RHEA:11072, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16567, ChEBI:CHEBI:18135, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.12.1; Evidence={ECO:0000269|PubMed:11114907};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for anthranilate {ECO:0000269|PubMed:11114907, ECO:0000269|PubMed:14622009}; KM=12 uM for benzoate {ECO:0000269|PubMed:11114907, ECO:0000269|PubMed:14622009}; Note=KM values measured using the AntAB complex.;
|
PATHWAY: Aromatic compound metabolism; anthranilate degradation via hydroxylation; catechol from anthranilate: step 1/1. {ECO:0000269|PubMed:11114907}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.3 for the reverse reaction. {ECO:0000269|PubMed:11114907, ECO:0000269|PubMed:14622009};
| null |
FUNCTION: Component of anthranilate dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into anthranilate to form catechol. {ECO:0000269|PubMed:11114907}.
|
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
|
O85746
|
TYRB_KLEPN
|
MFQKVDAYAGDPILSLMERFKEDPRSDKVNLSIGLYYNDDGIIPQLQAVAEAEARLNAEPHGASLYLPMEGFSGYRQAIAPLLFGAEHTALKQNRIASIQTVGGSGALKVGADFLKRYFPESHVWVSDPTWENHIAIFEGAGFEVSTYPWFDKATNGVRFENLLAMLQTLPARDIVLLHPCCHNPTGADLTPAQWDRVVEVLKARQLIPFLDIAYQGFGGGLEEDAYAIRAIASAGMPMLVSNSFSKIFSLYGERVGGLSVVCEDSETAGRVLGQLKATVRRNYSSPPSFGAQVVATVLNDAALKATWQAEVDAMRAHILTMRQALVDALQQVAPGSKVDYLLKQRGMFSYTGFSAAQVDRLRDEFGVYLIASGRMRVAGLNSRNVQQVAKAFVAVM
|
2.6.1.1; 2.6.1.5; 2.6.1.57
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305};
|
L-methionine salvage from methylthioadenosine [GO:0019509]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]
|
cytosol [GO:0005829]
|
identical protein binding [GO:0042802]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-phenylalanine:2-oxoglutarate aminotransferase activity [GO:0080130]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.57; CATALYTIC ACTIVITY: Reaction=4-methylsulfanyl-2-oxobutanoate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-methionine; Xref=Rhea:RHEA:47084, ChEBI:CHEBI:16723, ChEBI:CHEBI:36242, ChEBI:CHEBI:57844, ChEBI:CHEBI:58315; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.42 mM for tryptophan (at pH 7.4 and 10 mM KMTB) {ECO:0000269|PubMed:10074065}; KM=2.01 mM for tyrosine (at pH 7.4 and 10 mM KMTB) {ECO:0000269|PubMed:10074065}; KM=2.01 mM for phenylalanine (at pH 7.4 and 10 mM KMTB) {ECO:0000269|PubMed:10074065}; KM=2.46 mM for KMTB (at pH 7.4 and 5 mM tyrosine) {ECO:0000269|PubMed:10074065}; KM=3 mM for alpha-ketoglutarate (at pH 7.4 and 5 mM tyrosine) {ECO:0000269|PubMed:10074065}; KM=6 mM for oxaloacetate (at pH 7.4 and 5 mM tyrosine) {ECO:0000269|PubMed:10074065}; KM=11.93 mM for glutamate (at pH 7.4 and 10 mM KMTB) {ECO:0000269|PubMed:10074065}; KM=20.13 mM for pyruvate (at pH 7.4 and 5 mM tyrosine) {ECO:0000269|PubMed:10074065}; Vmax=0.09 umol/min/mg enzyme with pyruvate and tyrosine as substrates(at pH 7.4) {ECO:0000269|PubMed:10074065}; Vmax=1.8 umol/min/mg enzyme with phenylalanine and KMTB as substrates (at pH 7.4) {ECO:0000269|PubMed:10074065}; Vmax=2.63 umol/min/mg enzyme with tryptophan and KMTB as substrates(at pH 7.4) {ECO:0000269|PubMed:10074065}; Vmax=3.25 umol/min/mg enzyme with tyrosine and KMTB as substrates(at pH 7.4) {ECO:0000269|PubMed:10074065}; Vmax=3.29 umol/min/mg enzyme with phenylalanine and tyrosine as substrates(at pH 7.4) {ECO:0000269|PubMed:10074065}; Vmax=5.21 umol/min/mg enzyme with alpha-ketoglutarate and tyrosine as substrates(at pH 7.4) {ECO:0000269|PubMed:10074065}; Vmax=7.39 umol/min/mg enzyme with oxaloacetate and tyrosine as substrates(at pH 7.4) {ECO:0000269|PubMed:10074065}; Vmax=7.65 umol/min/mg enzyme with glutamate and KMTB as substrates (at pH 7.4) {ECO:0000269|PubMed:10074065};
|
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 6/6.
| null | null |
FUNCTION: catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) or glutamate as the amino donors. Histidine, leucine, asparagine, or arginine are also functional amino donors but to a lesser extent. Can also use alpha-ketoglutarate, oxaloacetate and pyruvate as the amino acceptors.
|
Klebsiella pneumoniae
|
O86028
|
MCM_RHIME
|
MTEKTIKDWEALAEKELRVSPEGLVWHTPEGIDVKPLYTSDDMSGIGHLNSLPGFEPFVRGPRATMYAGRPWTVRQYAGFSTAEASNAFYRRNLAAGQQGVSVAFDLATHRGYDSDHPRVQGDVGKAGVAIDSVEDMKILFDGIPLDRISVSMTMNGAVIPILASFIVAGEEQGVSRDKLSGTIQNDILKEFMVRNTYIYPPEPSMRIVADIIEYTAKEMPKFNSISISGYHMQEAGATLVQELAFTLADGREYVRAALAKGLNVDDFAGRLSFFFAIGMNFFMEAAKLRAARLLWTRIMQEFKPEKASSLMLRTHCQTSGVSLQEQDPYNNIVRTAFEAMSAVLGGTQSLHTNSFDEAMALPTDFSARIARNTQLILQHETGVTKVVDPLAGSYYVESLTNELAEKAWGLIEEVEALGGMTKAVNAGLPKRLIEEAATRRQAAVDRAEEVIVGVNKYRLENEQPIDILQIDNAAVRTAQVKRIEETRRRRDSQKMKQALDALADVARSGKGNLLAAAVEAARARATVGEITDAMREAFGDYTAIPEVVTDIYGKAYEGDPELGVLAGRLGEATKRLGHKPKIMVAKLGQDGHDRGAKVIASAFGDIGFDVVAGPLFQTPEEAADLALAEEVTVIGVSSLAAGHRTLMPQLAEALKKRGGEDIIVVCGGVIPRQDYDYLMENGVAAVFGPGTQVLDAARAVLDLIEGKRRNV
|
5.4.99.2
|
COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:12844209}; COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000269|PubMed:12844209}; Note=Monovalent cations such as NH4(+), Rb(+), Cs(+), K(+), Li(+) or Na(+) are required for enzyme activity. {ECO:0000269|PubMed:12844209};
|
propionate metabolic process, methylmalonyl pathway [GO:0019678]
| null |
cobalamin binding [GO:0031419]; metal ion binding [GO:0046872]; methylmalonyl-CoA mutase activity [GO:0004494]
|
PF02310;PF01642;
|
3.40.50.280;3.20.20.240;
|
Methylmalonyl-CoA mutase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888, ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2; Evidence={ECO:0000269|PubMed:12844209, ECO:0000305|PubMed:9889346};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.11 mM for (R,S)-methylmalonyl-CoA (in the presence of 3 mM NH4(+)) {ECO:0000269|PubMed:12844209}; KM=0.13 mM for (R,S)-methylmalonyl-CoA (in the absence of 3 mM NH4(+)) {ECO:0000269|PubMed:12844209};
|
PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 3/3. {ECO:0000305}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:12844209};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:12844209};
|
FUNCTION: Radical enzyme that catalyzes the transformation of methylmalonyl-CoA to succinyl-CoA. Is required for growth on the polyhydroxyalkanoate degradation pathway intermediates 3-hydroxybutyrate and acetoacetate as sole carbon source. {ECO:0000269|PubMed:12844209, ECO:0000269|PubMed:9889346}.
|
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
|
O86308
|
RPF_MICLU
|
MDTMTLFTTSATRSRRATASIVAGMTLAGAAAVGFSAPAQAATVDTWDRLAECESNGTWDINTGNGFYGGVQFTLSSWQAVGGEGYPHQASKAEQIKRAEILQDLQGWGAWPLCSQKLGLTQADADAGDVDATEAAPVAVERTATVQRQSAADEAAAEQAAAAEQAVVAEAETIVVKSGDSLWTLANEYEVEGGWTALYEANKGAVSDAAVIYVGQELVLPQA
|
3.-.-.-
| null | null |
cell surface [GO:0009986]; extracellular region [GO:0005576]
|
hydrolase activity [GO:0016787]
|
PF01476;PF06737;
|
1.10.530.10;3.10.350.10;
|
Transglycosylase family, Rpf subfamily
|
PTM: May be subject to further C-terminal cleavage as the protein identified in gels is smaller than is expected.
|
SUBCELLULAR LOCATION: Secreted. Cell surface. Note=Found in culture supernatant, also accumulates on the cell surface.
| null | null | null | null | null |
FUNCTION: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity. In pM quantities promotes the resuscitation and growth of dormant, nongrowing cells from M.luteus in addition to Mycobacterium tuberculosis, M.avium, M.bovis, M.kansaii and M.smegmatis. Hydrolyzes endogeneous cell walls, peptidoglycan preparations from Mycobacterium tuberculosis and M.smegmatis as well as an artificial lysozyme substrate 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (MUF tri-NAG). Overexpression in E.coli (when the enzyme is targeted to the periplasm) causes cell lysis. {ECO:0000269|PubMed:16359320, ECO:0000269|PubMed:20016836, ECO:0000269|PubMed:22864992, ECO:0000269|PubMed:9671779}.
|
Micrococcus luteus (Micrococcus lysodeikticus)
|
O87008
|
TFTC_BURCE
|
MHAGEAVQQLKKAFETVASFDFRDALSKASTPVTVVATNGPFGLAGLTCSAVCSVCDRPPTVLLCINRKSYAAGIIKSNGVLSVNWLAAGQAVISQTFAGVGSVPMEERFADKGWQTIATGAPYRMDAAVSFDCTIANIVDVGSHSVIFAEVVARNHAEECTPLIYHRRQYATTRSLAE
|
1.5.1.37
| null |
aromatic compound catabolic process [GO:0019439]; pyrimidine nucleobase catabolic process [GO:0006208]
| null |
FMN binding [GO:0010181]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor [GO:0016646]; protein homodimerization activity [GO:0042803]; riboflavin reductase (NADPH) activity [GO:0042602]
|
PF01613;
| null |
Non-flavoprotein flavin reductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=FADH2 + NAD(+) = FAD + 2 H(+) + NADH; Xref=Rhea:RHEA:30147, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692, ChEBI:CHEBI:57945, ChEBI:CHEBI:58307; EC=1.5.1.37; Evidence={ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.3 uM for FMN (with fixed NADH concentration at 300 uM) {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}; KM=2 uM for FAD {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}; KM=4.8 uM for FAD (with fixed NADH concentration at 300 uM) {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}; KM=45.3 uM for NADH {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}; KM=40.1 uM for NADH (with fixed FAD concentration at 18 uM) {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}; KM=164 uM for NADH (with fixed FMN concentration at 20 uM) {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}; Vmax=120 umol/min/mg enzyme {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
|
PATHWAY: Xenobiotic degradation.
| null | null |
FUNCTION: Reductase component of a two-component system that degrades 2,4,5-trichlorophenol. TftC provides the FADH(2) required by TftD. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone. {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}.
|
Burkholderia cepacia (Pseudomonas cepacia)
|
O87170
|
LIGI_SPHSK
|
MTNDERILSWNETPSKPRYTPPPGAIDAHCHVFGPMAQFPFSPKAKYLPRDAGPDMLFALRDHLGFARNVIVQASCHGTDNAATLDAIARAQGKARGIAVVDPAIDEAELAALHEGGMRGIRFNFLKRLVDDAPKDKFLEVAGRLPAGWHVVIYFEADILEELRPFMDAIPVPIVIDHMGRPDVRQGPDGADMKAFRRLLDSREDIWFKATCPDRLDPAGPPWDDFARSVAPLVADYADRVIWGTDWPHPNMQDAIPDDGLVVDMIPRIAPTPELQHKMLVTNPMRLYWSEEM
|
3.1.1.57
| null |
3,4-dihydroxybenzoate catabolic process [GO:0019619]; lignin catabolic process [GO:0046274]
| null |
2-pyrone-4,6-dicarboxylate lactonase activity [GO:0047554]
|
PF04909;
|
3.20.20.140;
|
Metallo-dependent hydrolases superfamily, PDC hydrolase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+); Xref=Rhea:RHEA:10644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57471, ChEBI:CHEBI:58304; EC=3.1.1.57; Evidence={ECO:0000269|PubMed:22475079, ECO:0000269|PubMed:29658701};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for a mixture of (4E)-oxalomesaconate/4-carboxy-2-hydroxymuconate (at pH 8.25) {ECO:0000269|PubMed:22475079}; KM=48 uM for 2-pyrone-4,6-dicarboxylate (at pH 8.25) {ECO:0000269|PubMed:22475079}; KM=49 uM for 4-carboxy-2-hydroxymuconate (at pH 7 and at 30 degrees Celsius) {ECO:0000269|PubMed:9864312}; KM=74 uM for 2-pyrone-4,6-dicarboxylate (at pH 8.5 and at 30 degrees Celsius) {ECO:0000269|PubMed:9864312}; Note=kcat is 342 sec(-1) for the hydrolysis of 2-pyrone-4,6-dicarboxylate (at pH 8.25). kcat is 116 sec(-1) for the synthesis of 2-pyrone-4,6-dicarboxylat from OMA/CHM (at pH 8.25). {ECO:0000269|PubMed:22475079};
|
PATHWAY: Secondary metabolite metabolism; lignin degradation. {ECO:0000269|PubMed:9864312}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for hydrolysis of PDC is 8.5 and optimum pH for synthesis of PDC is between 6.0 to 7.5. {ECO:0000269|PubMed:9864312};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:9864312};
|
FUNCTION: Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway (PubMed:9864312). Catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to (4E)-oxalomesaconate (OMA) (PubMed:22475079, PubMed:29658701). The keto form of OMA can tautomerize into the enol form, 4-carboxy-2-hydroxymuconate (CHM), under certain pH conditions (PubMed:22475079). Also catalyzes the reverse reaction (PubMed:22475079, PubMed:9864312). Is essential for the growth of Sphingobium sp. SYK-6 on vanillate but is not responsible for the growth of this strain on syringate (PubMed:9864312). {ECO:0000269|PubMed:22475079, ECO:0000269|PubMed:29658701, ECO:0000269|PubMed:9864312}.
|
Sphingobium sp. (strain NBRC 103272 / SYK-6)
|
O87198
|
HOSA_THET2
|
MREWKIIDSTLREGEQFEKANFSTQDKVEIAKALDEFGIEYIEVTTPVASPQSRKDAEVLASLGLKAKVVTHIQCRLDAAKVAVETGVQGIDLLFGTSKYLRAAHGRDIPRIIEEAKEVIAYIREAAPHVEVRFSAEDTFRSEEQDLLAVYEAVAPYVDRVGLADTVGVATPRQVYALVREVRRVVGPRVDIEFHGHNDTGCAIANAYEAIEAGATHVDTTILGIGERNGITPLGGFLARMYTLQPEYVRRKYKLEMLPELDRMVARMVGVEIPFNNYITGETAFSHKAGMHLKAIYINPEAYEPYPPEVFGVKRKLIIASRLTGRHAIKARAEELGLHYGEEELHRVTQHIKALADRGQLTLEELDRILREWITA
|
2.3.3.14
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19996101}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19996101};
|
lysine biosynthetic process via aminoadipic acid [GO:0019878]
|
cytoplasm [GO:0005737]
|
citrate synthase activity [GO:0036440]; homocitrate synthase activity [GO:0004410]; metal ion binding [GO:0046872]
|
PF00682;
|
1.10.238.260;3.20.20.70;
|
Alpha-IPM synthase/homocitrate synthase family, Homocitrate synthase LYS20/LYS21 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58884; EC=2.3.3.14; Evidence={ECO:0000269|PubMed:19996101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930; Evidence={ECO:0000305|PubMed:19996101}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; Evidence={ECO:0000269|PubMed:12095615};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44 uM for 2-oxoglutarate {ECO:0000269|PubMed:12095615}; KM=32 uM for acetyl-CoA (in the presence of 2-oxoglutarate) {ECO:0000269|PubMed:12095615}; KM=255 uM for oxaloacetate (in the presence of KCl, necessary for activity) {ECO:0000269|PubMed:12095615}; KM=28 uM for acetyl-CoA (in the presence of oxaloacetate and KCl) {ECO:0000269|PubMed:12095615}; KM=5.4 uM for 2-oxoglutarate {ECO:0000269|PubMed:19996101}; KM=33 uM for acetyl-CoA {ECO:0000269|PubMed:19996101}; Note=kcat is 92 min(-1) using 2-oxoglutarate as substrate (PubMed:12095615). kcat is 58 min(-1) using oxaloacetate as substrate (in the presence of KCl, necessary for activity) (PubMed:12095615). kcat is 41 min(-1) using 2-oxoglutarate as substrate (PubMed:19996101). {ECO:0000269|PubMed:12095615, ECO:0000269|PubMed:19996101};
|
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5. {ECO:0000269|PubMed:9868782, ECO:0000305|PubMed:19996101}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. Activity is rapidly lost above 70 degrees Celsius. {ECO:0000269|PubMed:12095615};
|
FUNCTION: Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate (PubMed:12095615, PubMed:19996101). Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway (PubMed:9868782). To a lesser extent, can also use oxaloacetate in place of 2-oxoglutarate, leading to citrate. Does not display 2-isopropylmalate synthase activity since it cannot use 2-oxoisovalerate (PubMed:12095615). {ECO:0000269|PubMed:12095615, ECO:0000269|PubMed:19996101, ECO:0000269|PubMed:9868782}.
|
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
|
O87236
|
LANA1_LACLL
|
MNKNEIETQPVTWLEEVSDQNFDEDVFGACSTNTFSLSDYWGNNGAWCTLTHECMAWCK
| null | null |
defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]
|
extracellular region [GO:0005576]
|
signaling receptor binding [GO:0005102]
|
PF14867;
| null | null |
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor. {ECO:0000269|PubMed:15023056}.; PTM: It is not established whether the 2,3-didehydrobutyrines are the E- or Z-isomers (PubMed:10608807, PubMed:15023056). In the NMR model they were assumed to be the Z-isomer.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10608807, ECO:0000269|PubMed:10971756}.
| null | null | null | null | null |
FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A1 exhibits strong activity towards L.lactis strain AM2, weak activity towards L.lactis strain HP and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A2 it displays strong activity towards all three strains. {ECO:0000269|PubMed:10608807, ECO:0000269|PubMed:10971756}.
|
Lactococcus lactis subsp. lactis (Streptococcus lactis)
|
O87237
|
LANA2_LACLL
|
MKEKNMKKNDTIELQLGKYLEDDMIELAEGDESHGGTTPATPAISILSAYISTNTCPTTKCTRAC
| null | null |
defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]
|
extracellular region [GO:0005576]
|
signaling receptor binding [GO:0005102]
| null | null | null |
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor. {ECO:0000269|PubMed:15023056}.; PTM: It is not established whether the 2,3-didehydrobutyrines are the E- or Z-isomers (PubMed:10608807, PubMed:15023056). In the NMR model they were assumed to be the Z-isomer.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10608807, ECO:0000269|PubMed:10971756}.
| null | null | null | null | null |
FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A2 exhibits weak activity towards L.lactis strain AM2 and L.lactis strain HP, and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A1 it displays strong activity towards all three strains. {ECO:0000269|PubMed:10608807, ECO:0000269|PubMed:10971756}.
|
Lactococcus lactis subsp. lactis (Streptococcus lactis)
|
O87393
|
GLNA3_RHIME
|
MTLDLSTFAREKGVKYFMISYTDLFGGQRAKLVPAEAIADMQKGGAGFAGFATWFDLTPAHPDLFALPDASAVIQLPWKKDVAWVAADCIMDDAPVEQAPRVVLKKLVAEAAQEGLRVKTGVEPEFFLISPDGSKISDTFDTAEKPCYDQQAIMRRYDVIAEICDYMLELGWKPYQNDHEDANGQFEMNWEYDDALRTADKHSFFKFMVKSIAEKHGLRATFMPKPFKGLTGNGCHCHISVWDLAGEVNAFADNKAEFGLSAEGRHFLGGIMKHASALAAVTNPTVNSYKRINAPRTISGATWAPNSVTWTGNNRTHMVRVPGPGRFELRLPDGAVNPYLLQAIIIAAGLSGVRSKADPGRHYDIDMYKDGHKVTDAPKLPLNLLDALREYNRDEELQEALGREFSAAYLKLKQGEWNTYCSQFTEWEHQTTLDV
|
6.3.1.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8093245}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
|
glutamine biosynthetic process [GO:0006542]; nitrogen fixation [GO:0009399]; polyamine catabolic process [GO:0006598]
| null |
ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; metal ion binding [GO:0046872]
|
PF00120;
|
3.10.20.70;3.30.590.10;
|
Glutamine synthetase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:8093245};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.3 mM for glutamate {ECO:0000269|PubMed:8093245}; KM=33 mM for ammonium {ECO:0000269|PubMed:8093245};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:8093245};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:8093245};
|
FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. {ECO:0000269|PubMed:8093245}.
|
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
|
O87605
|
PIKC_STRVZ
|
MRRTQQGTTASPPVLDLGALGQDFAADPYPTYARLRAEGPAHRVRTPEGDEVWLVVGYDRARAVLADPRFSKDWRNSTTPLTEAEAALNHNMLESDPPRHTRLRKLVAREFTMRRVELLRPRVQEIVDGLVDAMLAAPDGRADLMESLAWPLPITVISELLGVPEPDRAAFRVWTDAFVFPDDPAQAQTAMAEMSGYLSRLIDSKRGQDGEDLLSALVRTSDEDGSRLTSEELLGMAHILLVAGHETTVNLIANGMYALLSHPDQLAALRADMTLLDGAVEEMLRYEGPVESATYRFPVEPVDLDGTVIPAGDTVLVVLADAHRTPERFPDPHRFDIRRDTAGHLAFGHGIHFCIGAPLARLEARIAVRALLERCPDLALDVSPGELVWYPNPMIRGLKALPIRWRRGREAGRRTG
|
1.14.15.33
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
|
cholesterol catabolic process [GO:0006707]; macrolide biosynthetic process [GO:0033068]
| null |
cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; steroid hydroxylase activity [GO:0008395]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 H(+) + narbomycin + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + 2 oxidized [2Fe-2S]-[ferredoxin] + pikromycin; Xref=Rhea:RHEA:39887, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:76800, ChEBI:CHEBI:76801; EC=1.14.15.33; Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}; CATALYTIC ACTIVITY: Reaction=2 H(+) + narbomycin + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + neopikromycin + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:40531, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:76801, ChEBI:CHEBI:77350; EC=1.14.15.33; Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}; CATALYTIC ACTIVITY: Reaction=4 H(+) + narbomycin + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + novapikromycin + 4 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:40535, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:76801, ChEBI:CHEBI:77351; EC=1.14.15.33; Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}; CATALYTIC ACTIVITY: Reaction=10-deoxymethymycin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + methymycin + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:40539, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:63307, ChEBI:CHEBI:77352; EC=1.14.15.33; Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}; CATALYTIC ACTIVITY: Reaction=10-deoxymethymycin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + neomethymycin + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:40543, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:63307, ChEBI:CHEBI:77353; EC=1.14.15.33; Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}; CATALYTIC ACTIVITY: Reaction=10-deoxymethymycin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + novamethymycin + 4 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:40547, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:63307, ChEBI:CHEBI:77354; EC=1.14.15.33; Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for narbomycin {ECO:0000269|PubMed:9778370}; KM=20.4 uM for 10-deoxymethymycin {ECO:0000269|PubMed:9831532}; KM=44 uM for narbomycin {ECO:0000269|PubMed:9831532};
|
PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9770448, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}.
| null | null |
FUNCTION: Catalyzes the hydroxylation of narbomycin to give rise to pikromycin, and of 10-deoxymethymycin (YC-17) to give rise to methymycin and neomethymycin during macrolide antibiotic biosynthesis. In addition, produces low amounts of neopicromycin, novapikromycin and novamethymycin. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase. {ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}.
|
Streptomyces venezuelae
|
O87761
|
PYRG_LACLM
|
MSTKYIFVTGGGTSSMGKGIVAASLGRLLKNRGLKVTVQKFDPYLNIDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKYSNVTSGKVYSEILRKERKGEYLGATVQMVPHVTNMLKEKIKRAATTTDADIIITEVGGTVGDMESLPFIEALRQMKAEVGADNVMYIHTVPILHLRAAGELKTKIAQNATKTLREYGIQANMLVLRSEVPITTEMRDKIAMFCDVAPEAVIQSLDVEHLYQIPLNLQAQNMDQIVCDHLKLDAPKADMAEWSAMVDHVMNLKKKVKIALVGKYVELPDAYISVTEALKHAGYASDAEVDINWVNANDVTDENVAELVGDAAGIIVPGGFGQRGTEGKIAAIKYARENDVPMLGICLGMQLTAVEFARNVLGLEGAHSFELDPETKYPVIDIMRDQVDVEDMGGTLRLGLYPAKLKNGSRAKAAYNDAEVVQRRHRHRYEFNNKYREDFEKAGFVFSGVSPDNRLVEIVELSGKKFFVACQYHPELQSRPNRPEELYTEFIRVAVENSK
|
6.3.4.2
| null |
'de novo' CTP biosynthetic process [GO:0044210]; glutamine metabolic process [GO:0006541]; pyrimidine nucleobase biosynthetic process [GO:0019856]
|
cytoophidium [GO:0097268]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
|
PF06418;PF00117;
|
3.40.50.880;3.40.50.300;
|
CTP synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000269|PubMed:11500486}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000255|HAMAP-Rule:MF_01227}; CATALYTIC ACTIVITY: Reaction=ATP + NH4(+) + UTP = ADP + CTP + 2 H(+) + phosphate; Xref=Rhea:RHEA:16597, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000269|PubMed:11500486};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.52 mM for L-glutamine {ECO:0000269|PubMed:11500486}; KM=42.9 mM for ammonia {ECO:0000269|PubMed:11500486};
|
PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000269|PubMed:11500486}.
| null | null |
FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Is essential for the synthesis of CTP de novo. Contrary to other bacterial CTP synthases, the lactococcal enzyme is also able to convert dUTP to dCTP, but this reaction may not play a significant physiological role (PubMed:11500486). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity). {ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000269|PubMed:11500486}.
|
Lactococcus lactis subsp. cremoris (strain MG1363)
|
O87953
|
KTRB_VIBAL
|
MTQFHQRGVFYVPDGKRDKAKGGEPRIILLSFLGVLLPSAVLLTLPVFSVSGLSITDALFTATSAISVTGLGVVDTGQHFTLAGKILLMCLMQIGGLGQMTLSAVLLYMFGVRLSLRQQALAKEALGQERQVNLRRLVKKIVTFALVAEAIGFVFLSYRWVPEMGWQTGMFYALFHSISAFNNAGFALFSDSMMSFVNDPLVSFTLAGLFIFGGLGFTVIGDVWRHWRKGFHFLHIHTKIMLIATPLLLLVGTVLFWLLERHNPNTMGSLTTGGQWLAAFFQSASARTAGFNSVDLTQFTQPALLIMIVLMLIGAGSTSTGGGIKVSTFAVAFMATWTFLRQKKHVVMFKRTVNWPTVTKSLAIIVVSGAILTTAMFLLMLTEKASFDKVMFETISAFATVGLTAGLTAELSEPGKYIMIVVMIIGRIGPLTLAYMLARPEPTLIKYPEDTVLTG
| null | null | null |
plasma membrane [GO:0005886]
|
potassium:chloride symporter activity [GO:0015379]
|
PF02386;
| null |
TrkH potassium transport family, Ktr (TC 2.A.38.4) subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10359077, ECO:0000269|PubMed:16210320, ECO:0000269|PubMed:20097755}; Multi-pass membrane protein {ECO:0000269|PubMed:10359077, ECO:0000269|PubMed:16210320, ECO:0000269|PubMed:20097755}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.025 mM for K(+) {ECO:0000269|PubMed:16210320}; KM=6 mM for Na(+) {ECO:0000269|PubMed:16210320}; Vmax=200 nmol/min/mg enzyme with K(+) as substrate {ECO:0000269|PubMed:16210320}; Vmax=110 nmol/min/mg enzyme with Na(+) as substrate {ECO:0000269|PubMed:16210320};
| null | null | null |
FUNCTION: Part of the Na(+)-dependent high affinity K(+) uptake system KtrAB. KtrB is the K(+)-translocating subunit. {ECO:0000269|PubMed:10359077, ECO:0000269|PubMed:16210320, ECO:0000269|PubMed:9642210}.
|
Vibrio alginolyticus
|
O88037
|
RAMC_STRCO
|
MTAATVRGGTPRDSVVSVSNRWEGAGVNKGYAVYCDADPYFYDAPHRTADRTGAARSRYAAASSPVPEGWQRHESGDWLALRPADADLPAQGWKIHVSACLDNAESVLDRVWRHCVDGGTAFKFVPSRYLLHQRNAKYADRAGSGKFVTVYPADEAEFERLVGELSELLAGEPGPHILSDLRIGDGPVHVRYGGFTRRDCYDADGELRPAVSGPDGVLVPDLRGPVFRIPEWVDPPAFLRPHLDARSAVTVTGMPYTVESALHFSNGGGVYLARDTRTGARVVLKEARPHAGLAADGADAVTRLHRERRALERLSGLACTPEVLDHRTVGEHHFLVLEHIDGKPLNTFFARRHPLIEADPGERRLAEYTDWALDVHARVERAVAEVHARGVVFNDLHLFNIMVRDDDSVALLDFEAAHHVDEAGRQIVANPGFVAPPDRRGVAVDRYALACLRIVLFLPLTSLLAVDRHKAAHLAEVVAEQFPVDRAFLDAAVEEITRVDGSTRVDGSTRADETTRADETTRLDVTTRVHGAPDAARRPAGPVAPVRPDDWPRSRDSMAAAIRASATPSRTDRLFPGDIAQFATAGGGLAFAHGAAGVLYALAESGAGRDEDGEQWLLERTKRPPSGMPLGFHDGLAGLAWTLERLGHRDRALDLAELLLDQPLDHLGPDLHGGTAGLGLALESLAATTGQAALHSAALHCAELAADGLPGGSVPADRVSRGRARAGLLYGGAGRALLFLRLFERTRDSALLDLARDALRQDLARCVRGAGGALQVDEGWRTMPYLGAGSVGIGMVLDDYLAHRADEEFARAANEIVAAAQAMFYAQPGLYRGVAGMVLHLGRTTATAPGTGPRAVRRQLDALSWHAMSYRDRLAFPGEQMMRLSMDLSTGTAGCLLAVASVLGDAPAGLPFLPPPRRSGGPLTRPHQEP
|
2.7.-.-
| null |
peptide modification [GO:0031179]; phosphorylation [GO:0016310]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.50.10.20;1.10.510.10;
|
Protein kinase superfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12169618}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Required for aerial hyphae formation (PubMed:12100547, PubMed:12169618, PubMed:12453210). Probably involved in processing the precursor of SapB to its mature form (Probable). {ECO:0000269|PubMed:12100547, ECO:0000269|PubMed:12169618, ECO:0000269|PubMed:12453210, ECO:0000305|PubMed:15277670}.
|
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
|
O88038
|
LANSB_STRCO
|
MNLFDLQSMETPKEEAMGDVETGSRASLLLCGDSSLSITTCN
| null | null | null |
extracellular region [GO:0005576]; plasma membrane [GO:0005886]; spore wall [GO:0031160]
| null |
PF19402;
| null |
Lanthionine-containing morphogen family
|
PTM: Maturation involves the enzymatic conversion of Ser into dehydrated AA and the formation of thioether bonds with cysteine, probably by RamC (PubMed:15277670). This is followed by membrane translocation and cleavage of the modified precursor (Probable). The RamS precursor protein (detected by an anti-propeptide antibody and by a C-terminal His-tag) is detected from at least 16 hours post-germination; its apparent molecular weight decreases starting from about 34 hours, when its probable modifying enzyme ramC is transcribed. Surfactin, a B.subtilis cyclic lipopeptide antibiotic which prevents aerial hyphae formation in S.coelicolor, decreases localization of RamS precursor protein to the cell membrane, suggesting that processing only occurs at the cell membrane (PubMed:22486809). {ECO:0000269|PubMed:15277670, ECO:0000269|PubMed:22486809, ECO:0000305|PubMed:15277670}.
|
SUBCELLULAR LOCATION: [Lanthionine-containing peptide SapB precursor RamS]: Cell membrane {ECO:0000269|PubMed:22486809}. Note=RamS precursor protein (detected by an anti-propeptide antibody and by a C-terminal His-tag) is associated with the cell membrane in a non ramR-dependent fashion (PubMed:22486809). {ECO:0000269|PubMed:22486809}.; SUBCELLULAR LOCATION: [Lanthionine-containing peptide SapB]: Secreted {ECO:0000269|PubMed:2032288, ECO:0000269|PubMed:22309453}. Spore wall {ECO:0000269|PubMed:22309453, ECO:0000269|PubMed:2450872, ECO:0000269|PubMed:9822824, ECO:0000305|PubMed:17462011}. Note=Present in a zone around colonies undergoing aerial hyphae formation and around spores (PubMed:2032288). Expression levels are media-dependent; well expressed in spores grown on rich R5, about 4-fold less on rich MS and less again on minimal mannitol media. Secreted in rich R5 but not in minimal mannitol media (PubMed:22309453). {ECO:0000269|PubMed:2032288, ECO:0000269|PubMed:22309453}.
| null | null | null | null | null |
FUNCTION: [Lanthionine-containing peptide SapB precursor RamS]: Stably accumulated precursor of SapB (PubMed:22486809). {ECO:0000269|PubMed:22486809}.; FUNCTION: [Lanthionine-containing peptide SapB]: Lanthionine-containing peptide devoid of antibiotic properties (PubMed:15277670). A surface active peptide involved in the efficient formation of aerial mycelium when cells are grown in rich media. Has an overlapping function with the surface-active chaplin proteins; chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation (PubMed:17462011). Required under conditions of high osmolarity where it may change the physical properties of the chaplin layer to allow hyphae to grow into air (Probable). Suggested to self-assemble at air-water interfaces, thus providing a film of surfactant through which nascent aerial hyphae can emerge; the aerial hyphae differentiate further into spores (PubMed:2032288). Application to bald mutants (bld, unable to make aerial hyphae) restores hyphae growth (PubMed:2032288, PubMed:9822824). Application to chaplin negative mutants as well as ramC-ramS-ramA-ramB and ramR deletions also restores aerial hyphae growth and sporulation (PubMed:17462011). Reduces surface tension of water from 72 to 30 mJ/m(2) (PubMed:9822824). {ECO:0000269|PubMed:15277670, ECO:0000269|PubMed:17462011, ECO:0000269|PubMed:2032288, ECO:0000269|PubMed:9822824, ECO:0000305|PubMed:22309453}.
|
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
|
O88070
|
GLNA4_STRCO
|
MSPGQKEALPVADRTPPLGVEELHALVAAGDIDTVVLAFPDMQGRLQGKRFAARFFLDEVLEHGTEGCNYLLAVDADMNTVDGYAMSSWDRGYGDFAMRADPATLRRLPWNEGTAMAVADLAWEDGSPVLAAPRQILRRQLERLAGHGYTAQVGTELEFIVFRDTYEHAWDANYRGLTPANQYNVDYSVLGTGRVEPLLRRIRNEMAGAGLTVESAKGECNPGQHEIAFRYDEALVTCDQHAVYKTGAKEIAAQEGMSLTFMAKYNELEGNSCHIHLSLADADGRNAMAEGGGMSDVMRHFLAGQLVALREFSLLYAPHINSYKRFQPGSFAPTAVAWGHDNRTCALRVVGHGRSLRFENRLPGGDVNPYLAVAGLVAAGLHGIEQRLELPEPCPGNAYTADFAHVPTTLREAAELWENSTLAKAAFGDEVVAHYRNMARVELDAFDAAVTDWELRRSFERM
|
6.3.1.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P12425}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
|
ethanolamine catabolic process [GO:0046336]; glutamate metabolic process [GO:0006536]; glutamine biosynthetic process [GO:0006542]; response to carbon starvation [GO:0090549]; response to nitrate starvation [GO:0090548]; response to nitrogen compound [GO:1901698]
| null |
acid-ammonia (or amide) ligase activity [GO:0016880]; ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; ligase activity [GO:0016874]; magnesium ion binding [GO:0000287]
|
PF00120;
|
3.10.20.70;3.30.590.10;
|
Glutamine synthetase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + ethanolamine + L-glutamate = ADP + gamma-L-glutamylethanolamide + H(+) + phosphate; Xref=Rhea:RHEA:73903, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57603, ChEBI:CHEBI:193054, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31113893}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73904; Evidence={ECO:0000269|PubMed:31113893};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.47 mM for ethanolamine {ECO:0000269|PubMed:31113893}; KM=85.41 mM for glutamate {ECO:0000269|PubMed:31113893}; KM=2.5 mM for ATP {ECO:0000269|PubMed:31113893};
|
PATHWAY: Amine and polyamine degradation; ethanolamine degradation. {ECO:0000269|PubMed:31113893}.
| null | null |
FUNCTION: Involved in the catabolism of monoamine ethanolamine. Catalyzes the ATP-dependent gamma-glutamylation of ethanolamine. No activity with polyamines (PubMed:31113893). No complementation of the L-glutamine auxotrophy of an E.coli glnA mutant (PubMed:16932908). Enables survival of S.coelicolor under high local environmental ethanolamine conditions. May play a role during starvation conditions to limit intracellular ethanolamine concentration, which in excess is toxic to the cells (PubMed:31113893). {ECO:0000269|PubMed:16932908, ECO:0000269|PubMed:31113893}.
|
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
|
O88093
|
HBP_ECOLX
|
MNRIYSLRYSAVARGFIAVSEFARKCVHKSVRRLCFPVLLLIPVLFSAGSLAGTVNNELGYQLFRDFAENKGMFRPGATNIAIYNKQGEFVGTLDKAAMPDFSAVDSEIGVATLINPQYIASVKHNGGYTNVSFGDGENRYNIVDRNNAPSLDFHAPRLDKLVTEVAPTAVTAQGAVAGAYLDKERYPVFYRLGSGTQYIKDSNGQLTKMGGAYSWLTGGTVGSLSSYQNGEMISTSSGLVFDYKLNGAMPIYGEAGDSGSPLFAFDTVQNKWVLVGVLTAGNGAGGRGNNWAVIPLDFIGQKFNEDNDAPVTFRTSEGGALEWSFNSSTGAGALTQGTTTYAMHGQQGNDLNAGKNLIFQGQNGQINLKDSVSQGAGSLTFRDNYTVTTSNGSTWTGAGIVVDNGVSVNWQVNGVKGDNLHKIGEGTLTVQGTGINEGGLKVGDGKVVLNQQADNKGQVQAFSSVNIASGRPTVVLTDERQVNPDTVSWGYRGGTLDVNGNSLTFHQLKAADYGAVLANNVDKRATITLDYALRADKVALNGWSESGKGTAGNLYKYNNPYTNTTDYFILKQSTYGYFPTDQSSNATWEFVGHSQGDAQKLVADRFNTAGYLFHGQLKGNLNVDNRLPEGVTGALVMDGAADISGTFTQENGRLTLQGHPVIHAYNTQSVADKLAASGDHSVLTQPTSFSQEDWENRSFTFDRLSLKNTDFGLGRNATLNTTIQADNSSVTLGDSRVFIDKNDGQGTAFTLEEGTSVATKDADKSVFNGTVNLDNQSVLNINDIFNGGIQANNSTVNISSDSAVLGNSTLTSTALNLNKGANALASQSFVSDGPVNISDATLSLNSRPDEVSHTLLPVYDYAGSWNLKGDDARLNVGPYSMLSGNINVQDKGTVTLGGEGELSPDLTLQNQMLYSLFNGYRNIWSGSLNAPDATVSMTDTQWSMNGNSTAGNMKLNRTIVGFNGGTSPFTTLTTDNLDAVQSAFVMRTDLNKADKLVINKSATGHDNSIWVNFLKKPSNKDTLDIPLVSAPEATADNLFRASTRVVGFSDVTPILSVRKEDGKKEWVLDGYQVARNDGQGKAAATFMHISYNNFITEVNNLNKRMGDLRDINGEAGTWVRLLNGSGSADGGFTDHYTLLQMGADRKHELGSMDLFTGVMATYTDTDASADLYSGKTKSWGGGFYASGLFRSGAYFDVIAKYIHNENKYDLNFAGAGKQNFRSHSLYAGAEVGYRYHLTDTTFVEPQAELVWGRLQGQTFNWNDSGMDVSMRRNSVNPLVGRTGVVSGKTFSGKDWSLTARAGLHYEFDLTDSADVHLKDAAGEHQINGRKDSRMLYGVGLNARFGDNTRLGLEVERSAFGKYNTDDAINANIRYSF
|
3.4.21.-
| null |
proteolysis [GO:0006508]
|
cell outer membrane [GO:0009279]; cell surface [GO:0009986]; extracellular region [GO:0005576]; periplasmic space [GO:0042597]
|
serine-type endopeptidase activity [GO:0004252]
|
PF03797;PF02395;
|
2.160.20.20;2.40.10.120;3.30.160.280;2.40.128.130;
| null |
PTM: Cleaved to release the mature protein from the outer membrane.
|
SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp autotransporter]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. {ECO:0000250}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:9743528};
| null |
FUNCTION: Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation. {ECO:0000269|PubMed:11748157, ECO:0000269|PubMed:9743528}.
|
Escherichia coli
|
O88174
|
MCP_MOUSE
|
MTAAPLMPDSTHPCRRRKSYTFFWCSLGVYAEALLFLLSHLSDACELPRPFEAMELKGTPKLFYAVGEKIEYKCKKGYLYLSPYLMIATCEPNHTWVPISDAGCIKVQCTMLQDPSFGKVYYIDGSFSWGARAKFTCMEGYYVVGMSVLHCVLKGDDEAYWNGYPPHCEKIYCLPPPKIKNGTHTLTDINVFKYHEAVSYSCDPTPGPDKFSLVGTSMIFCAGHNTWSNSPPECKVVKCPNPVLQNGRLISGAGEIFSYQSTVMFECLQGFYMEGSSMVICSANNSWEPSIPKCLKGPRPTHPTKPPVYNYTGYPSPREGIFSQELDAWIIALIVITSIVGVFILCLIVLRCFEHRKKTNVSAAR
| null | null |
negative regulation of complement activation, classical pathway [GO:0045959]; positive regulation of proteolysis [GO:0045862]; single fertilization [GO:0007338]; T cell mediated immunity [GO:0002456]
|
acrosomal vesicle [GO:0001669]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular space [GO:0005615]; inner acrosomal membrane [GO:0002079]; plasma membrane [GO:0005886]
| null |
PF00084;
|
2.10.70.10;
| null |
PTM: May be O-glycosylated. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12640142}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein. Note=Inner acrosomal membrane of spermatozoa.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in the fusion of the spermatozoa with the oocyte during fertilization. {ECO:0000269|PubMed:12640142}.
|
Mus musculus (Mouse)
|
O88181
|
BARH2_RAT
|
MTAMEGASGSSFGIDTILSGAGSGSPGMMNGDFRSLGEARTTDFRSQATPSPCSEIDTVGTAPSSPISVTLEPPEPHLVTDGPQHHHHLHHGQQPPPPSAPPAQSLQPSPQQQPPPQPQSAAQQLGSAAAAPRTSTSSFLIKDILGDSKPLAACAPYSTSVSSPHHTPKQECNAAHESFRPKLEQEDSKTKLDKREDSQSDIKCHGTKEEGDREITSSRESPPVRAKKPRKARTAFSDHQLNQLERSFERQKYLSVQDRMDLAAALNLTDTQVKTWYQNRRTKWKRQTAVGLELLAEAGNYSALQRMFPSPYFYHPSLLGSMDSTTAAAAAAAMYSSMYRTPPAPHPQLQRPLVPRVLIHGLGPGGQPALNPLSNPIPGTPHPR
| null | null |
amacrine cell differentiation [GO:0035881]; cell fate commitment [GO:0045165]; cell fate determination [GO:0001709]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; neuron migration [GO:0001764]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translation [GO:0045727]; regulation of axon extension [GO:0030516]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
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]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
|
BAR homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Potential regulator of neural basic helix-loop-helix genes. It may down-regulate expression of ASCL1 and, within the thalamus, up-regulate NGN2, thereby regulating distinct patterns of neuronal differentiation. {ECO:0000269|PubMed:9698441}.
|
Rattus norvegicus (Rat)
|
O88182
|
FGF18_RAT
|
MYSAPSACTCLCLHFLLLCFQVQVLAAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQTELQKPFKYTTVTKRSRRIRPTHPG
| null | null |
angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; chondrocyte development [GO:0002063]; chondrocyte differentiation [GO:0002062]; endochondral ossification [GO:0001958]; ERK1 and ERK2 cascade [GO:0070371]; fibroblast growth factor receptor signaling pathway [GO:0008543]; intramembranous ossification [GO:0001957]; lung development [GO:0030324]; nervous system development [GO:0007399]; ossification [GO:0001503]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of endothelial cell chemotaxis to fibroblast growth factor [GO:2000546]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of hepatocyte proliferation [GO:2000347]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; regulation of cell migration [GO:0030334]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; type 1 fibroblast growth factor receptor binding [GO:0005105]; type 2 fibroblast growth factor receptor binding [GO:0005111]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88188
|
LY86_MOUSE
|
MNGVAAALLVWILTSPSSSDHGSENGWPKHTACNSGGLEVVYQSCDPLQDFGLSIDQCSKQIQSNLNIRFGIILRQDIRKLFLDITLMAKGSSILNYSYPLCEEDQPKFSFCGRRKGEQIYYAGPVNNPGLDVPQGEYQLLLELYNENRATVACANATVTSS
| null | null |
inflammatory response [GO:0006954]; innate immune response [GO:0045087]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]
|
extracellular region [GO:0005576]
| null |
PF02221;
|
2.60.40.770;
| null | null |
SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Associated with CD180 at the cell surface.
| null | null | null | null | null |
FUNCTION: May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression. {ECO:0000269|PubMed:10925274}.
|
Mus musculus (Mouse)
|
O88196
|
TTC3_MOUSE
|
MDDFAEGGLSLADDILLEDYPYEDDCICTPDFTTDDYVRVTQLYYEGVGMQYKDYAQSEKNLEYDICNIWCSKPLSILQDYCDAIKLYIFWPLLFQHQHSSIISRLHPCVEAIRSRAAEISLKKLQHLELMEDIVDLAKKVANDSFLIEGLLKIGYKIENKILAMEDALNWIKYTGDVTILPKLGSVDNCWPMLSIFFTEYKYHITRVVTENCNLLEEFRRHSCMQCVKQGELMKMRGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQGRTSNKNPIKAFYESRAYIPRNSSAPAFRTSLNFVETERGFRKTKYKMANGGDQNQKVADEALKGDDCDCHPEFLPPPSQPPRHKGKQKSRNNESEKPSFNSEVSLQVDLKSILEKQFSKSSRAAHQDFANIMKMLRSLIQDGYTALLEQRCRSAAQAFTELLNGLDPQKIKQLNLAMINYVLVVYGLAVSLLGIGRPEELSEAENQFKRIIEHYPNEGLDCLAYCGIGKVYLKKNRFLEALNHFEKAKTLISRLPGILTWPTSNVIIEESKPEKVKVMLEKFVEECKFPPVPDAVCCYQKCRGYSKIQIYLTDPDFKGFIRISCCQYCKVEFHMNCWKKLKTTTFNDKIDKDFLQGICLTPDCEGIISKIIIYSSGGQVKCEFEHKVIKEKVPSRPVLKQKCSSLEKLRLKEDKKLKRKIQKQEAKKLAQERMEEDLRESNPPKNEEPEETSDSAQRCQFLDDRILQCIKQNADKIKSVVLNTSTLLKELLSWKVLSTEDYTTCFSSKNFVHEAVDYVIGHLIQEKNRVKTRIFLHVLSELKELDPKLAPWIQRLNSFGLDAIGPFFTRYGASLKELDFHVVTVLWDEKYGHKLGSIEGKQLDYFFEPASAMEARCLIWLLEEHRDKFPALHSALDEFFDIMDSRCTVLRKQDSDEMPFGCIKVKNKGKKKKPKDSKPMLVGSGAASVAPSSEAVTPEDHSRRNSDSAGPFAVPDHLRQDVEEFEALYDQHSSEYVVRNKKLWDINPKQKCSTLYDYFSQLLEEHGPLDMSDRMFSEEYEFFPEETRQILEKAGGLKSFLLGCPRFVVIDNCIALKKVASRLKKKRKKKNMKAKVEDISKTGEYLRVKLPLNPTAREFQPDVKSEALSEDVKSIPGPADSSTLAAEDLKAQLDSDSSSGSASEDSRLEVASPDSPTPLCEDASPSPTPAPEEAKPTYWAQSHLVTGFCTYLPFQGFGITQRPAYINMVPSLSQFTSIYTPLANISSEYPMQRSMPVVPSFVASNRADENAAAYFESPNLNTEHDSGDHMASETQILEDTLGVCVRSQGSAADADPALSEPEGNSEHSGSSDSLWEASLENVSGTTDAPAAPSVAIQVSRSMVHQEVNTEPYEPFETQQGDLSQKEKECHLLREQLKVACENCEQIELRSSQEIKDLEEKLQRHTEENKISKTELDWFLQDLDREIKKWQQEKKEIQERLKALKKKIKKVINTSEMSAQKNDGFDKECEPHPDQSLGFSSALTDEKTKAEESVRKGKELYEESHQRAVAAEVSVLENWKEREVCKLQGVASQSEAYLKSLKLMSSDSATYPDVEYDILSWESFLSTVREEIESKKSQFEEHIKAIKNGSRLSDLSSVQLSEVSFPGCSTIHPQFLSESSGHEDPGLVACVDSMTGAVLNDPYMDSASGCPEEVPELSLGSPTHQPEVTQQLELKGASQVSPSEQSPEADEKLSGQATRSSQSPKKPSNSIIEHLSVIFPCYTSTELAGFIKKVRNKTKNSFSGLTIEEIVEKVTEHIVDEQKKKKPNPGKDKKTSEAHSAASVAKSSQSPPLAAAGPSARTKGQKKDDVPAPDGNSCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTCGSSDLLSEE
|
2.3.2.27
| null |
negative regulation of axon extension [GO:0030517]; negative regulation of neuron differentiation [GO:0045665]; protein K48-linked ubiquitination [GO:0070936]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; vacuole [GO:0005773]
|
metal ion binding [GO:0046872]; ubiquitin-protein transferase activity [GO:0004842]
|
PF19179;PF13639;
|
1.10.533.10;1.25.40.10;3.30.40.10;
| null |
PTM: Phosphorylation on Ser-378 by Akt is required for ubiquitin ligase activity. {ECO:0000250|UniProtKB:P53804}.; PTM: Proteolytically cleaved into differently sized N- and C-terminal fragments. {ECO:0000250|UniProtKB:P53804}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53804}. Cytoplasm {ECO:0000250|UniProtKB:P53804}. Golgi apparatus {ECO:0000250|UniProtKB:D3ZSP7}. Note=Nuclear localization may be dependent on the proteolytic cleavage of full length protein in the cytoplasm (By similarity). This cleavage may reveal an N-terminal nuclear localization signal, allowing N-terminal fragments to enter the nucleus (By similarity). {ECO:0000250|UniProtKB:P53804}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P53804};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:P53804}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which catalyzes the formation of 'Lys-48'-polyubiquitin chains (By similarity). Mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus (By similarity). Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation (By similarity). Positively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation by mediating the ubiquitination and subsequent degradation of SMURF2 (By similarity). Regulates neuronal differentiation by regulating actin remodeling and Golgi organization via a signaling cascade involving RHOA, CIT and ROCK (By similarity). Inhibits cell proliferation (By similarity). {ECO:0000250|UniProtKB:P53804}.
|
Mus musculus (Mouse)
|
O88199
|
CHST3_MOUSE
|
MEKGLALPQDFRDLVHSLKIRGRYVLFLAFVVIVFIFIEKENKIISRVSDKLKQIPHFVADANSTDPALLLSENASLLSLSELDSTFSHLRSRLHNLSLQLGVEPAMESQEAGAEKPSQQAGAGTRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVFFQQRGASAAGSALVYRDVLKQLLLCDLYVLEPFISPPPEDHLTQFLFRRGSSRSLCEDPVCTPFVKKVFEKYHCRNRRCGPLNVTLAGEACRRKDHVALKAVRIRQLEFLQPLVEDPRLDLRVIQLVRDPRAVLASRIVAFAGKYENWKKWLSEGQDQLSEDEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARRPLQKAREMYSFAGIPLTPQVEDWIQKNTQATRDSSDVYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPTMHLFGYKLARDAASLTNRSISLLEERGTFWVT
|
2.8.2.17; 2.8.2.21
| null |
carbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; N-acetylglucosamine metabolic process [GO:0006044]; T cell homeostasis [GO:0043029]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; trans-Golgi network [GO:0005802]
|
chondroitin 6-sulfotransferase activity [GO:0008459]; N-acetylglucosamine 6-O-sulfotransferase activity [GO:0001517]; proteoglycan sulfotransferase activity [GO:0050698]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family, Gal/GlcNAc/GalNAc subfamily
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92179}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+); Xref=Rhea:RHEA:11108, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9828, ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:62065; EC=2.8.2.17; Evidence={ECO:0000269|PubMed:11696535, ECO:0000269|PubMed:9597547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11109; Evidence={ECO:0000269|PubMed:11696535}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21; Evidence={ECO:0000269|PubMed:11696535};
| null | null | null | null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin (PubMed:11696535, PubMed:9597547). Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices (PubMed:9597547). Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan (PubMed:11696535). Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May play a role in the maintenance of naive T-lymphocytes in the spleen (PubMed:11696535). {ECO:0000250|UniProtKB:Q92179, ECO:0000269|PubMed:11696535, ECO:0000269|PubMed:9597547, ECO:0000303|PubMed:9597547}.
|
Mus musculus (Mouse)
|
O88202
|
LPP60_RAT
|
MARATGPEQRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLRTLHMLHDEEYARAHSLPEDTLVLPPASSDQRIIYKVLECQPLFDSSDMTITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASWKSHLVVHSNMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYAPGMAMAGAGIISGFDMTSEAALAKLSYVLGQPGLSLSDRKKLLAKDLRGEMTLPTTDDLLGDDMLGCRATWLLSMNGSQDADAMKDVLLPGLALAAAHAGDLDTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELEDVGTELCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSLEDRVSAQPQPH
|
3.1.1.47; 3.1.1.5; 3.5.1.1
| null |
asparagine metabolic process [GO:0006528]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
cytosol [GO:0005829]
|
1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; asparaginase activity [GO:0004067]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]
|
PF12796;PF00710;PF17763;
|
3.40.50.40;1.25.40.20;3.40.50.1170;
|
Asparaginase 1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000305|PubMed:10320809, ECO:0000305|PubMed:8119970, ECO:0000305|PubMed:9575212}; CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000269|PubMed:9575212}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21017; Evidence={ECO:0000305|PubMed:9575212}; CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000269|PubMed:9575212}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000305|PubMed:9575212}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000305|PubMed:8119970, ECO:0000305|PubMed:9575212}; CATALYTIC ACTIVITY: Reaction=2 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40879, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880; Evidence={ECO:0000305|PubMed:10320809, ECO:0000305|PubMed:8119970}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + octadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40887, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:25629, ChEBI:CHEBI:73858; Evidence={ECO:0000269|PubMed:8119970}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40888; Evidence={ECO:0000305|PubMed:8119970}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823; Evidence={ECO:0000269|PubMed:8119970}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808; Evidence={ECO:0000305|PubMed:8119970}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = H(+) + hexadecanoate + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73004, ChEBI:CHEBI:143890; Evidence={ECO:0000269|PubMed:8119970}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40892; Evidence={ECO:0000305|PubMed:8119970}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890; Evidence={ECO:0000269|PubMed:8119970}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896; Evidence={ECO:0000305|PubMed:8119970}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40899, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998, ChEBI:CHEBI:73004, ChEBI:CHEBI:73005; Evidence={ECO:0000269|PubMed:10320809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40900; Evidence={ECO:0000305|PubMed:10320809}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40827, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395, ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:10320809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828; Evidence={ECO:0000305|PubMed:10320809}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40903, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:10320809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40904; Evidence={ECO:0000305|PubMed:10320809}; CATALYTIC ACTIVITY: Reaction=2 2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40907, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:10320809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40908; Evidence={ECO:0000305|PubMed:10320809}; CATALYTIC ACTIVITY: Reaction=1-O-(9Z)-octadecenoyl-2-O-acetyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-acetyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78044, ChEBI:CHEBI:78045; Evidence={ECO:0000269|PubMed:8119970}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41321; Evidence={ECO:0000305|PubMed:8119970}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) = a 1-acyl-2-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:41352, ChEBI:CHEBI:16870, ChEBI:CHEBI:64771, ChEBI:CHEBI:64874, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:10320809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41353; Evidence={ECO:0000305|PubMed:10320809}; CATALYTIC ACTIVITY: Reaction=2 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40959, ChEBI:CHEBI:16870, ChEBI:CHEBI:60657, ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:10320809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40960; Evidence={ECO:0000305|PubMed:10320809};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=91 uM for 1-palmitoyl-glycerophosphocholine {ECO:0000269|PubMed:8119970}; Vmax=12.9 nmol/min/mg enzyme for 1-palmitoyl-glycerophosphocholine {ECO:0000269|PubMed:8119970};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:8119970};
| null |
FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities (PubMed:10320809, PubMed:8119970, PubMed:9575212). Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer) (PubMed:10320809). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid (PubMed:10320809). {ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212}.
|
Rattus norvegicus (Rat)
|
O88207
|
CO5A1_MOUSE
|
MDVHTRWKAARPGALLLSSPLLLFLLLLWAPPSSRAAQPADLLEMLDFHNLPSGVTKTTGFCATRRSSSEPDVAYRVSKDAQLSMPTKQLYPESGFPEDFSILTTVKAKKGSQAFLVSIYNEQGIQQLGLELGRSPVFLYEDHTGKPGPEEYPLFPGINLSDGKWHRIALSVYKKNVTLILDCKKKITKFLSRSDHPIIDTNGIVMFGSRILDDEIFEGDIQQLLFVSDNRAAYDYCEHYSPDCDTAVPDTPQSQDPNPDEYYPEGEGETYYYEYPYYEDPEDPGKEPAPTQKPVEAARETTEVPEEQTQPLPEAPTVPETSDTADKEDSLGIGDYDYVPPDDYYTPPPYEDFGYGEGVENPDQPTNPDSGAEVPTSTTVTSNTSNPAPGEGKDDLGGEFTEETIKNLEENYYDPYFDPDSDSSVSPSEIGPGMPANQDTIFEGIGGPRGEKGQKGEPAIIEPGMLIEGPPGPEGPAGLPGPPGTTGPTGQMGDPGERGPPGRPGLPGADGLPGPPGTMLMLPFRFGGGGDAGSKGPMVSAQESQAQAILQQARLALRGPAGPMGLTGRPGPMGPPGSGGLKGEPGDMGPQGPRGVQGPPGPTGKPGRRGRAGSDGARGMPGQTGPKGDRGFDGLAGLPGEKGHRGDPGPSGPPGIPGDDGERGDDGEVGPRGLPGEPGPRGLLGPKGPPGPPGPPGVTGMDGQPGPKGNVGPQGEPGPPGQQGNPGAQGLPGPQGAIGPPGEKGPLGKPGLPGMPGADGPPGHPGKEGPPGEKGGQGPPGPQGPIGYPGPRGVKGADGIRGLKGTKGEKGEDGFPGFKGDMGIKGDRGEIGPPGPRGEDGPEGPKGRGGPNGDPGPLGPTGEKGKLGVPGLPGYPGRQGPKGSIGFPGFPGANGEKGGRGTPGKPGPRGQRGPTGPRGERGPRGITGKPGPKGNSGGDGPAGPPGERGPNGPQGPTGFPGPKGPPGPPGKDGLPGHPGQRGETGFQGKTGPPGPPGVVGPQGPTGETGPMGERGHPGPPGPPGEQGLPGAAGKEGTKGDPGPAGLPGKDGPPGLRGFPGDRGLPGPVGALGLKGSEGPPGPPGPAGSPGERGPAGAAGPIGIPGRPGPQGPPGPAGEKGLPGEKGPQGPAGRDGLQGPVGLPGPAGPVGPPGEDGDKGEIGEPGQKGSKGDKGEQGPPGPTGPQGPIGQPGPSGADGEPGPRGQQGLFGQKGDEGSRGFPGPPGPVGLQGLPGPPGEKGETGDVGQMGPPGPPGPRGPSGAPGADGPQGPPGGIGNPGAVGEKGEPGEAGDPGLPGEGGPLGPKGERGEKGEAGPSGAAGPPGPKGPPGDDGPKGSPGPVGFPGDPGPPGEPGPAGQDGPPGDKGDDGEPGQTGSPGPTGEPGPSGPPGKRGPPGPAGPEGRQGEKGAKGEAGLEGPPGKTGPIGPQGAPGKPGPDGLRGIPGPVGEQGLPGSPGPDGPPGPMGPPGLPGLKGDSGPKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSSGPKGDQGITGPSGPLGPPGPPGLPGPPGPKGAKGSSGPTGPKGEAGHPGLPGPPGPPGEVIQPLPIQASRTRRNIDASQLLDDGAGESYVDYADGMEEIFGSLNSLKLEIEQMKRPLGTQQNPARTCKDLQLCHPDFPDGEYWVDPNQGCSRDSFKVYCNFTAGGSTCVFPDKKSEGARITSWPKENPGSWFSEFKRGKLLSYVDAEGNPVGVVQMTFLRLLSASAHQNVTYNCYQSVAWQDAATGSYDKAIRFLGSNDEEMSYDNNPYIRALVDGCATKKGYQKTVLEIDTPKVEQVPIVDIMFNDFGEASQKFGFEVGPACFLG
| null | null |
blood vessel development [GO:0001568]; cell adhesion [GO:0007155]; collagen biosynthetic process [GO:0032964]; collagen fibril organization [GO:0030199]; eye morphogenesis [GO:0048592]; heart morphogenesis [GO:0003007]; integrin biosynthetic process [GO:0045112]; negative regulation of endodermal cell differentiation [GO:1903225]; regulation of cellular component organization [GO:0051128]; skin development [GO:0043588]; tendon development [GO:0035989]; wound healing, spreading of epidermal cells [GO:0035313]
|
basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen type V trimer [GO:0005588]; collagen type XI trimer [GO:0005592]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; heparin binding [GO:0008201]; platelet-derived growth factor binding [GO:0048407]; proteoglycan binding [GO:0043394]
|
PF01410;PF01391;PF02210;
|
2.60.120.1000;2.60.120.200;
|
Fibrillar collagen family
|
PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}.; PTM: Sulfated on 40% of tyrosines. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin (By similarity). Transcriptionally activated by CEBPZ, which recognizes a CCAAT-like motif, CAAAT in the COL5A1 promoter. {ECO:0000250, ECO:0000269|PubMed:15246108}.
|
Mus musculus (Mouse)
|
O88267
|
ACOT1_RAT
|
MEATLSLEPAGRSCWDEPLSITVRGLVPEQPVTLRAALRDEKGALFRARALYRADAHGELDLARAPALGGSFTGLEPMGLIWAMEPERPFWRLVKRDVQTPFVVELEVLDGHEPDGGRLLARAVHERHFMAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTICYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVEQKSFIPVERSDTTFLFLVGQDDHNWKSEFYANEISKRLQAHGKEKPQIICYPEAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLGGKSHGVSPKI
|
3.1.2.-; 3.1.2.2
| null |
acyl-CoA metabolic process [GO:0006637]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid metabolic process [GO:0001676]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; very long-chain fatty acid metabolic process [GO:0000038]
|
cytosol [GO:0005829]
|
carboxylic ester hydrolase activity [GO:0052689]; fatty acyl-CoA hydrolase activity [GO:0047617]
|
PF08840;PF04775;
|
2.60.40.2240;3.40.50.1820;
|
C/M/P thioester hydrolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9490035}.
|
CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:7906114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:7906114}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:7906114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:7906114}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:7906114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:7906114}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000250|UniProtKB:Q86TX2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000250|UniProtKB:Q86TX2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence={ECO:0000250|UniProtKB:Q86TX2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:Q86TX2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000250|UniProtKB:Q86TX2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537; Evidence={ECO:0000250|UniProtKB:Q86TX2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence={ECO:0000250|UniProtKB:Q86TX2};
| null |
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:7906114}.
| null | null |
FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20). {ECO:0000269|PubMed:7906114}.
|
Rattus norvegicus (Rat)
|
O88269
|
MRP6_RAT
|
MNGEHSMATPGESCAGLRVWNQTEQEPVAYHLLNLCFLRAAGSWVPPMYLWVLGPIYLLYIHRHGCCYLRMSRLFKIKMVLGFALILLYTFNAAVPLWRIHRGMPQAPELLIHPTVWLTTMSFATFLIHMERKKGVRASGLLFGYWLLCCLVPAIDTVQQASAGSFRQEPLHHLATYLCLSLVVAELVLSCLVDQPPFFSEDSKPLNPCPEAEASFPSKAMFWWASGLLWKGYRKLLGPKDLWSLERENSSEELVSQLEREWRRNFSELPGHKGHSGMGTPETEAFLQPERSQRGPLLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVFAVHTLVAEDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRLAAFLCLEEVDPNGMVLSPSRCSSKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGPSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLLDGARQPAGEGEGEAHAAATSDDLGGFSGGGTPTRRPERPRPSDAAPVKGSTSEAQMEPSLDDVEVTGLTAGEDSVQYGRVKSATYLSYLRAVGTPLCTYTLFLFLCQQVASFCQGYWLSLWADDPVVDGKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTPKEAPWRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQESGLA
|
7.6.2.-; 7.6.2.3
| null |
ATP metabolic process [GO:0046034]; ATP transport [GO:0015867]; calcium ion homeostasis [GO:0055074]; gene expression [GO:0010467]; inhibition of non-skeletal tissue mineralization [GO:0140928]; inorganic diphosphate transport [GO:0030505]; intracellular phosphate ion homeostasis [GO:0030643]; leukotriene transport [GO:0071716]; phosphate ion homeostasis [GO:0055062]; response to magnesium ion [GO:0032026]; response to sodium phosphate [GO:1904383]; transmembrane transport [GO:0055085]; xenobiotic transmembrane transport [GO:0006855]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; extracellular region [GO:0005576]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; inorganic diphosphate transmembrane transporter activity [GO:0030504]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
|
PTM: Glycosylated. {ECO:0000250|UniProtKB:O95255}.
|
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:10692506, ECO:0000269|PubMed:28111129}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:33058196}; Multi-pass membrane protein {ECO:0000255}. Lateral cell membrane {ECO:0000269|PubMed:10692506}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:O95255}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence={ECO:0000250|UniProtKB:O95255}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence={ECO:0000250|UniProtKB:O95255}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95255}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000250|UniProtKB:O95255};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for BQ-123 {ECO:0000269|PubMed:10692506};
| null | null | null |
FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of glutathione conjugates such as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS) (in vitro) (By similarity). Transports also an anionic cyclopentapeptide endothelin antagonist, BQ-123 (PubMed:10692506). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:O95255, ECO:0000269|PubMed:10692506}.; FUNCTION: Mediates the release of nucleoside triphosphates, predominantly ATP, into the circulation, where it is rapidly converted into AMP and the mineralization inhibitor inorganic pyrophosphate (PPi) by the ecto-enzyme ectonucleotide pyrophosphatase phosphodiesterase 1 (ENPP1), therefore playing a role in PPi homeostasis. {ECO:0000269|PubMed:28111129, ECO:0000269|PubMed:33058196}.
|
Rattus norvegicus (Rat)
|
O88271
|
CFDP1_MOUSE
|
MEEFDSEDFSTSDEDEDYLPSGGEYSEDDVNELVKEDEVDGEEQAEKTKGKRRKAQGIPARKRKQSGLLLEEEEDGKEDSGGSSSEEDEEEQEGGLGSENARKKKEDELWASFLNDVGPKSKAAPGSQTKVAEETEEISSNKPLVKADELDKPRESEKVKITKVFDFAGEEVRVTKEVDAASKEAKSFLKQTEREKPQALVTSPATPLPAGSGIKRASGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP
| null | null |
cell adhesion [GO:0007155]; chromatin remodeling [GO:0006338]; fibroblast apoptotic process [GO:0044346]; negative regulation of fibroblast apoptotic process [GO:2000270]; regulation of cell population proliferation [GO:0042127]; regulation of cell shape [GO:0008360]
|
basement membrane [GO:0005604]; kinetochore [GO:0000776]; nucleus [GO:0005634]; Swr1 complex [GO:0000812]
| null |
PF07572;
| null | null | null |
SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9UEE9}.
| null | null | null | null | null |
FUNCTION: May play a role during embryogenesis. May modulate tooth organogenesis since alterations of this protein function affect tooth organs size as well as individual cell fate and survival. In embryonic cells, blockage of the function results in increased number of apoptotic cells, reduced proliferation, alterations in cell shape and fibronection matrix synthesis. {ECO:0000269|PubMed:10415329, ECO:0000269|PubMed:11992732, ECO:0000269|PubMed:12153613}.
|
Mus musculus (Mouse)
|
O88272
|
MMP23_RAT
|
MGWRACLRPEASGAVQGRWLGAVLSGLCLLSALAFLEWLGSPTETAWNAAQGNVDAPDVGGSTPQVPSLLSMLVTRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQQDQALMHLNATLRGWKALSQDELWGLHRLYGCLDRIFVCTSWARKGFCDVRQRLMKRLCPRSCDFCYEFPFPTVATTTSPTRTKTRFVREGRNMTFHCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEARLSIIANAVNEGTYTCVVRHRQRVLTTYSWRVRVRS
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; reproduction [GO:0000003]
|
endoplasmic reticulum membrane [GO:0005789]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00413;PF01549;
|
1.10.10.1940;3.40.390.10;2.60.40.10;
|
Peptidase M10A family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:11328856}.; PTM: Proteolytic cleavage might yield an active form. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Single-pass type II membrane protein. Note=A secreted form produced by proteolytic cleavage may also exist. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum. {ECO:0000269|PubMed:19965868}.
|
Rattus norvegicus (Rat)
|
O88273
|
GREM2_MOUSE
|
MFWKLSLTLLLVAVLVKVAETRKNRPAGAIPSPYKDGSSNNSERWHHQIKEVLASSQEALVVTERKYLKSDWCKTQPLRQTVSEEGCRSRTILNRFCYGQCNSFYIPRHVKKEEDSFQSCAFCKPQRVTSVIVELECPGLDPPFRIKKIQKVKHCRCMSVNLSDSDKQ
| null | null |
animal organ morphogenesis [GO:0009887]; cytokine-mediated signaling pathway [GO:0019221]; determination of dorsal identity [GO:0048263]; embryonic body morphogenesis [GO:0010172]; negative regulation of BMP signaling pathway [GO:0030514]; regulation of cytokine activity [GO:0060300]; sequestering of BMP from receptor via BMP binding [GO:0038098]
|
extracellular space [GO:0005615]
|
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; receptor ligand activity [GO:0048018]
|
PF03045;
|
2.10.90.10;
|
DAN family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:23063586}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells. {ECO:0000269|PubMed:15039429, ECO:0000269|PubMed:23063586, ECO:0000269|PubMed:23850456}.
|
Mus musculus (Mouse)
|
O88275
|
PPARG_RAT
|
MGETLGDPPVDPEHGAFADALPMSTSQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNRPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFINLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKVLQKMTDLRQIVTEHVQLLHVIKKTETDMSLHPLLQEIYKDLY
| null | null |
animal organ regeneration [GO:0031100]; BMP signaling pathway [GO:0030509]; brown fat cell differentiation [GO:0050873]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cell maturation [GO:0048469]; cell population proliferation [GO:0008283]; cellular response to hyperoxia [GO:0071455]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to lithium ion [GO:0071285]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to organic cyclic compound [GO:0071407]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to prostaglandin E stimulus [GO:0071380]; cellular response to prostaglandin stimulus [GO:0071379]; cellular response to retinoic acid [GO:0071300]; cellular response to vitamin E [GO:0071306]; cold-induced thermogenesis [GO:0106106]; diet induced thermogenesis [GO:0002024]; epithelial cell differentiation [GO:0030855]; epithelial cell proliferation [GO:0050673]; fat cell differentiation [GO:0045444]; fatty acid metabolic process [GO:0006631]; fatty acid oxidation [GO:0019395]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; hormone-mediated signaling pathway [GO:0009755]; lipoprotein transport [GO:0042953]; long-chain fatty acid transport [GO:0015909]; macrophage derived foam cell differentiation [GO:0010742]; monocyte differentiation [GO:0030224]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cellular response to insulin stimulus [GO:1900077]; negative regulation of cellular response to transforming growth factor beta stimulus [GO:1903845]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of collagen biosynthetic process [GO:0032966]; negative regulation of connective tissue replacement involved in inflammatory response wound healing [GO:1904597]; negative regulation of cytokine production [GO:0001818]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of extracellular matrix assembly [GO:1901202]; negative regulation of gene expression [GO:0010629]; negative regulation of inflammatory response [GO:0050728]; negative regulation of lipid storage [GO:0010888]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of mitochondrial fission [GO:0090258]; negative regulation of neuroinflammatory response [GO:0150079]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of pancreatic stellate cell proliferation [GO:2000230]; negative regulation of peptide hormone secretion [GO:0090278]; negative regulation of receptor signaling pathway via STAT [GO:1904893]; negative regulation of sequestering of triglyceride [GO:0010891]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of type II interferon-mediated signaling pathway [GO:0060336]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; negative regulation of vascular endothelial cell proliferation [GO:1905563]; peroxisome proliferator activated receptor signaling pathway [GO:0035357]; placenta development [GO:0001890]; positive regulation of adiponectin secretion [GO:0070165]; positive regulation of adipose tissue development [GO:1904179]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of fatty acid metabolic process [GO:0045923]; positive regulation of fatty acid oxidation [GO:0046321]; positive regulation of gene expression [GO:0010628]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of phagocytosis, engulfment [GO:0060100]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular associated smooth muscle cell apoptotic process [GO:1905461]; regulation of blood pressure [GO:0008217]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; regulation of fat cell differentiation [GO:0045598]; regulation of gene expression [GO:0010468]; regulation of lipid metabolic process [GO:0019216]; regulation of transcription by RNA polymerase II [GO:0006357]; response to caffeine [GO:0031000]; response to dietary excess [GO:0002021]; response to estrogen [GO:0043627]; response to food [GO:0032094]; response to immobilization stress [GO:0035902]; response to light stimulus [GO:0009416]; response to lipid [GO:0033993]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to starvation [GO:0042594]; response to vitamin A [GO:0033189]; response to xenobiotic stimulus [GO:0009410]; retinoic acid receptor signaling pathway [GO:0048384]; rhythmic process [GO:0048511]; signal transduction [GO:0007165]; white fat cell differentiation [GO:0050872]; wound healing involved in inflammatory response [GO:0002246]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; receptor complex [GO:0043235]; RNA polymerase II transcription regulator complex [GO:0090575]; SUMO ligase complex [GO:0106068]
|
alpha-actinin binding [GO:0051393]; arachidonic acid binding [GO:0050544]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA binding domain binding [GO:0050692]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; double-stranded DNA binding [GO:0003690]; E-box binding [GO:0070888]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; LBD domain binding [GO:0050693]; nuclear estrogen receptor binding [GO:0030331]; nuclear receptor activity [GO:0004879]; nuclear receptor coactivator activity [GO:0030374]; nuclear retinoid X receptor binding [GO:0046965]; nucleic acid binding [GO:0003676]; peptide binding [GO:0042277]; promoter-specific chromatin binding [GO:1990841]; protein phosphatase binding [GO:0019903]; protein self-association [GO:0043621]; R-SMAD binding [GO:0070412]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; STAT family protein binding [GO:0097677]; transcription cis-regulatory region binding [GO:0000976]; transcription coactivator binding [GO:0001223]; transcription coregulator binding [GO:0001221]; zinc ion binding [GO:0008270]
|
PF00104;PF12577;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
|
PTM: Phosphorylated by MAPK. The phosphorylation inhibits PPAR gamma activity. {ECO:0000269|PubMed:8943212, ECO:0000269|PubMed:8953045, ECO:0000269|PubMed:9030579}.; PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. {ECO:0000250|UniProtKB:P37238}.; PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation at induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9; leading to proteasomal degradation (By similarity). Ubiquitinated at Lys-252 by TRIM55 leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
Rattus norvegicus (Rat)
|
O88277
|
FAT2_RAT
|
MTLVLLGLAILLLHRAACEKSLEETIPPLSWRFTHSLYNATIYENSAPKTYVESPVKMGMYLAEPHWVVKYRIISGDAAGVFKTEEHVVGNFCFLRIRTKSSNTALLNREVRDSYTLIVQASDKSLEFEALTQVVVHILDQNDLKPLFSPPSYRVTISEDRPLKSPICKVTATDADLGQNAEFYYAFNARSEVFAIHPTSGVVTVAGKLNVTRRGKYELQVLAVDRMRKISEGNGFGNLASLVIRVEPVHRKPPAINLVVLNPPEGDEGDIYAIVTVDTNGSGAEVDSLEVVGGDPGKYFKVLRSYAQGNEFNLVAVRDINWAEHPHGFNISLQTHSWSRFPPHSIIRAFHLPSWKLANLRFEKAVYRVKLSEFSPPGSRVALVKVTTALPNLRYSLKPSSRNTAFKLNARTGLITTTKLVDFHEQNQYQLHVKTSLGQATTTVIIDIVDCNNHAPVFNRSSYEGTLDENIPPGTSVLTVTATDQDHGDNGHITYSIAGPKAVPFSIDPLLGVISTTKPMDYELMKRIYTFRVRASDWGSPFRQEKEVSVSLRLKNLNDNQPMFEEVNCTVSLRQDVPVGKSIMAVSAIDMDELQNLKYEIVSGNEQDYFHLNHFSGVISLKRSFMNLTAVRPTIYSLKITASDGKNYASPTTLKVTVVKDPHSEVPVQCDKTGVLTHITKTILQSAGLQSQELGEEEFTSLSNYQINHHSPQFEDHFPQSIDILEQVPINTPLARLAATDPDTGFHGKLVYVISDGNEEGCFDIELETGLLMVAAALDYETTSFYVLNVTVYDLGTPPKSSWKLLTVTVKDWNDNPPRFPPGGYQLTISEDTEVGTTIAELKTEDADSEDNRRVRYTLLTPTEKFSLHPFTGELVVTGHLDRESESQYILKAEARDQPTKGHQLFSVTDLIVTLEDINDNPPQCITEHRRLKVPEDMPLGTVLTFLDASDPDLGPAGEVKYILVEDAHGTFQVHPMTGALSLEKELDFERRAGYNLSFWASDSGKPLSRRTLCHVEVLVMDVNENLHSPHFSSFVYQGQVQENSPAGTPVMVVTAQDDDSGLDGELQYFLRAGTGLETFSINQDTGMLETLAPLDREFTPYYWLTVLAVDRGSVPLSAVTEVYIEVTDINDNIPSMSRPVFYPSVLEDAPLGTSVLQLEAWDPDSSSQGKLTFNLTSGNHLGHFIVHPFTGLLTTAKQLDRENKDEYVLEVTVQDNGDPSLRSTSRVVVCILDVNDNPPMFSHKLFNVRLSERLSPLSPEPVYRLVASDPDEGLNGSVTYSIEESDEESFRIDPVTGVVSSSSTFAAGEYNILTIKATDSGQPALSTSVRLHIEWIPQPRPSSIPLSFDESYYSFTVMETDPVNHMVGVISVEGRPGLFWFHISDGDKDMDFDIEKTTGSIVIARPLDTRRKSSYNLTVEVTDGFHTIATQVHIFMIANINHHRPQFLQDHYEIRVPQDTLPGVELLRVQATDQDHGKGLIYTILSSQDPGSANLFQLDPSSGVLVTVGTLELHSGPSQHILTVMVRDQEMPIKRNFVWVTIHVEDGNLHSPHFTQLRYEANVPDTTAPGTELLQVRAVDADRGANAEIHYSFLKGNSDGFFNIDSLLGIITVAQRLYHVHLTRHALTVKAEDQGSPRRHDLALVVIHVHPSDSSAPVFSKDEYFIEIPESVPIGSPILLLSAGSSSEVTYELREGNKDSVFSMNSYSGLISTQKRLDHEKVPSYRLRIRGSNMAGVFTEVVALVYIIDENDNPPAFGKPTFLGHISEAAPLHSLILGEDNSPLVVRASDSDREANSLLVYKILEPEALKFFKIDPSMGTLTTTSELDFEDTPLFQFNIYVHDQGTPILFAPRSAKVIIHVRDVNDSPPRFSEQIYEVAVVEPIHPGMGLLTVQAEDNDSRVTYSIKTSNADEAVTIHPTTGQISVVNPATLRLFQKFSIRASDGLYHDTAVVKISLTQVLDKSLQFDQDVYRARVTENTPHRKALVILGVHGNHLNDTLSYFLLNGTDLFHMIESAGVLQTRGGTFDREQQDTHEVAVEVRDNRVPQRVAQALVRVSVEDVNDNIPEFQHLPYYTVIQDGTEPGDVLFQVSATDKDLGANGSVTYGFAEDYAYFRIDPYVGDISLKKPFDYQALNKYHLRVIARDSGIPPLQTEVEVHVTVRNKSNPLFQSPYYKVKVPENITLYTPILHTQARSPEGLRLIYNIVEEEPLMLFTTDFKTGVLTVTGPLDYESKNKHVFTVRATDTALGSFSEATVEVLVEDINDNPPTFSQLVYTTSVSEGSPAQTPVIQLLASDQDSGQNQDVSYQIVEDGSDVSKFFRINGSTGEIFTIQELDYETHQHFRVKVRAMDKGDPPLTGETLVVVNVSDINDNPPKFREPQYEANVSELATCGHLVLKVQALDPDIGDTSRLEYLILSGNQDRHFSINSTSGIISMFNLCKKQLDSSYNLRVGASDGVFRATVPVYINTTNANKYSPEFQQNVYEAELAENAKVGTKVIELLAIDKDSGPYGTVDYTIINKLAGERFFINPRGQITTLQKLDRENSTERVIAIKVMARDGGGKVAFCTVKIILTDENDNAPQFKASGYTVSIPSNVSRDSPIIQVLAYDADEGRNADVTYSVDSTEDLAEEIIEVNPTTGVVKVKESLVGLENRAVDFNIKAQDGGPPHWDSLVPVRLQVVPNEIPLPKFSEPLYTFSAPEDLPEGSEIGSVKAVAAQDPIIYSLVQGTTPESNSDDVFSLDQDTGVLKVRKAMDHESTKWYQIDLMAHCPHEDTDLVSLVSVSIQVEDVNDNRPVFEADPYKAFLTENMPGGTTVIQVTANDQDTGSDGQVSYRLSVEPGSNIHELFAVDSESGWITTLQELDCETQQTYRFYVVAFDHGQTIQLSSQALVEVSITDENDNPPRFASEDYRGSVVENNEPGELVATLKTLDADVSDQNRQVTCYITEGDPLGQFSISQVGDEWRISSRKTLDREHIAKYLLRVTASDGKFQASVPVEVFVVDINDNSPQCSQLLYTGKVREDVTPGHFILKVSAIDVDMDTNAQITYSLHGPGAQEFKLDPHTGELTTLTVLDRERKDVYNLVAKATDGGGQSCQAEVTLHIEDVNDNAPRFFPSHCDVAVFDNTTVKTPVAVVFARDPDQGANAQVVYSLTDSADGQFSIDATSGVIRLEKPLQVRASSAVELTVRASDLGTPIPLSTLGTVTVSVVGLEDYLPIFLNAEHSTQVPEDAPIDMEVLHLATLTRPGSEKTGYHITGGNEQGKFRLDAHTGILYVNGSLDFETNPKYFLSIECSRKSSSSLSDVTTIVINVTDVNEHHPRFTHDLYTVRVLENAVVGDVILTVSASDDDGPVNSAITYSLVGGNQLGHFTINPKKGKLQVAKALDWEQTPSYSLRLRATDSGQPPLHEDTEVAVEVVDVNDNPPRFFQLNYSTSVQENSPIGIKVLQLILDDPDSPQNGPPYFFRITEGNTGSVFRVTPDGWLVTAASLSKKAREWYQLHIEVSDSGLPPLSSSTLVRVQVTEQSRYPPSTLPLEISITKGEEEFQGGMIGKIHATDRDPQDTLTYSLEQEGGLDRYFTVGASDGKIIASQGLPHGRYSFNVTVSDGTFTTTTGVHVHVWHMEPEVPQQAVWLGFHQLTPEELVSDHWRNLQRFLSNLLDVKRANIHLASLQPAEVTAGVDVLLVFERHSGTSYDLQELASAIAHSVREIEHSVGIRMRSALPVVPCQGQSCQDQTCQETVSLEPRVGPSYSTARLSILTPRHHLGRNCSCNGTTLRFSGQSYVQYRPLEAQNWQIHFYLKTLQPWALLMFTNETASISLKLANGFSHLEYHCPGGFYGNLSSRYPVNDGQWHSMLLEERDTSVHLLVDITDNASLVIPEECQGLRTERQLLLGGLVPSNPSSNVSLGFEGCLDAVVVNGERLELLGREKKMEGRLETWALSQCCWPGTACSQSPCLNGGSCSPALGSGYLCRCPPPFSGRNCELGRENCTSAPCQEGGTCVSSPEGTSCNCPHPYTGDRCEMEARGCSGGHCLITPEIKRGDWGQQEFLVITVALPLVIIATVGLLLYCRRRKSHKPVTMEDPDLLARSIGVDTQASPAIELDPLNTSSCNNLNQPEPSKTSVPNELVTFGPSSKQRPMVCSVPPRLPPAAVSSHPGHEPIIKRTWSGEELVYPSGAAVWPPTYSRKKHWEYPHPETMQGTLPPSPRRHVGPAVMPDPTGLYGGFPFPLELENKRAPLPPRYSNQNLEDLMPPRPPSPREHLLAPCLNEYTAISYYHSQFRQGGGGPCLAEGGYKGVSMRLSRAGPSYADCEVNGGPATGRSQPRAPPNYEGSDMVESDYGSCEEVMF
| null | null |
cell-cell adhesion [GO:0098609]; cell-substrate adhesion [GO:0031589]; epithelial cell migration [GO:0010631]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]
|
adherens junction [GO:0005912]; catenin complex [GO:0016342]; Golgi apparatus [GO:0005794]
|
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]
|
PF00028;PF00008;PF02210;
|
2.60.120.200;2.60.40.60;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cell junction {ECO:0000250|UniProtKB:Q9NYQ8}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12213440, ECO:0000269|PubMed:29053796}. Note=Localized at adhesion zippers (early state of adherens junctions) of keratinocytes. {ECO:0000250|UniProtKB:Q9NYQ8}.
| null | null | null | null | null |
FUNCTION: Involved in the regulation of cell migration (PubMed:29053796). May be involved in mediating the organization of the parallel fibers of granule cells during cerebellar development (PubMed:12213440). {ECO:0000269|PubMed:29053796, ECO:0000303|PubMed:12213440}.
|
Rattus norvegicus (Rat)
|
O88278
|
CELR3_RAT
|
MARRPLWWGLPGPSTPLLLLLLFSLFPSSREEMGGGGDQGWDPGVATATGPRAQIGSGAVALCPESPGVWEDGDPGLGVREPVFMKLRVGRQNARNGRGAPEQPNREPVVQALGSREQEAGQGSGYLLCWHPEISSCGRTGHLRRGSLPLDALSPGDSDLRNSSPHPSELLAQPDSPRPVAFQRNGRRSIRKRVETFRCCGKLWEPGHKGQGERSATSTVDRGPLRRDCLPGSLGSGLGEDSAPRAVRTAPAPGSAPHESRTAPERMRSRGLFRRGFLFERPGPRPPGFPTGAEAKRILSTNQARSRRAANRHPQFPQYNYQTLVPENEAAGTAVLRVVAQDPDPGEAGRLVYSLAALMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHGSPRLSATTMVAVTVADRNDHAPVFEQAQYRETLRENVEEGYPILQLRATDGDAPPNANLRYRFVGSPAARTAAAAAFEIDPRSGLISTSGRVDREHMESYELVVEASDQGQEPGPRSATVRVHITVLDENDNAPQFSEKRYVAQVREDVRPHTVVLRVTATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPPLSNNTGLASIQVVDINDHSPIFVSTPFQVSVLENAPLGHSVIHIQAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSPPLSASASVTVTVLDVNDNRPEFTMKEYHLRLNEDAAVGTSVVSVTAVDRDANSAISYQITGGNTRNRFAISTQGGMGLVTLALPLDYKQERYFKLVLTASDRALHDHCYVHINITDANTHRPVFQSAHYSVSMNEDRPVGSTVVVISASDDDVGENARITYLLEDNLPQFRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIPQKADTTYVEVMVNDVNDNAPQFVASHYTGLVSEDAPPFTSVLQISATDRDAHANGRVQYTFQNGEDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGVPPLRTPVSIQVTVQDVNDNAPVFPAEEFEVRVKENSIVGSVVAQITAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQATSAPLVSRATVHVRLVDQNDNSPVLNNFQILFNNYVSNRSDTFPSGIIGRIPAYDPDVSDHLFYSFERGNELQLLVVNQTSGELRLSRKLDNNRPLVASMLVTVTDGLHSVTAQCVLRVVIITEELLANSLTVRLENMWQERFLSPLLGHFLEGVAAVLATPTEDVFIFNIQNDTDVGGTVLNVSFSALAPRGAGAGAAGPWFSSEELQEQLYVRRAALAARSLLDVLPFDDNVCLREPCENYMKCVSVLRFDSSAPFLASASTLFRPIQPIAGLRCRCPPGFTGDFCETELDLCYSNPCRNGGACARREGGYTCVCRPRFTGEDCELDTEAGRCVPGVCRNGGTCTNAPNGGFRCQCPAGGAFEGPRCEVAARSFPPSSFVMFRGLRQRFHLTLSLSFATVQPSGLLFYNGRLNEKHDFLALELVAGQVRLTYSTGESSTVVSPTVPGGLSDGQWHTVHLRYYNKPRTDALGGAQGPSKDKVAVLSVDDCNVAVALRFGAEIGNYSCAAAGVQTSSKKSLDLTGPLLLGGVPNLPENFPVSRKDFIGCMRDLHIDGRRVDMAAFVANNGTTAGCQAKSHFCASGPCKNGGLCSERWGGFSCDCPVGFGGKDCRLTMAHPYHFQGNGTLSWDFGNDMPVSVPWYLGLSFRTRATKGVLMQVQLGPHSVLLCKLDQGLLSVTLSRASGHAVHLLLDQMTVSDGRWHDLRLELQEEPGGRRGHHIFMVSLDFTLFQDTMAMGSELEGLKVKHLHVGGPPPSSKEEGPQGLVGCIQGVWTGFTPFGSSALPPPSHRINVEPGCTVTNPCASGPCPPHANCKDLWQTFSCTCWPGYYGPGCVDACLLNPCQNQGSCRHLQGGPHGYTCDCASGYFGQHCEHRMDQQCPRGWWGSPTCGPCNCDVHKGFDPNCNKTSGQCHCKEFHYRPRGSDSCLPCDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSCDSPFAEVTASGCRVLYDACPKSLRSGVWWPQTKFGVLATVPCPRGALGLRGTGAAVRLCDEDHGWLEPDFFNCTSPAFRELSLLLDGLELNKTALDTVEAKKLAQRLREVTGQTDHYFSQDVRVTARLLAYLLAFESHQQGFGLTATQDAHFNENLLWAGSALLAPETGDLWAALGQRAPGGSPGSAGLVRHLEEYAATLARNMDLTYLNPVGLVTPNIMLSIDRMEQPSSSQGAHRYPRYHSNLFRGQDAWDPHTHVLLPSQSPQPSPSEVLPTSSNAENATASGVVSPPAPLEPESEPGISIVILLVYRALGGLLPAQFQAERRGARLPQNPVMNSPVVSVAVFRGRNFLRGALVSPINLEFRLLQTANRSKAICVQWDPPGPADQHGMWTARDCELVHRNGSHARCRCSRTGTFGVLMDASPRERLEGDLELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMNGIMFLLAARTSCSTGQREAKKTSVLRTLRSSFLLLLLVSASWLFGLLAVNHSVLAFHYLHAGLCGLQGLAVLLLFCVLNADARAAWTPACLGKKAAPEETRPAPGPGSGAYNNTALFEESGLIRITLGASTVSSVSSARSGRAQDQDSQRGRSYLRDNVLVRHGSTAEHAEHSLQAHAGPTDLDVAMFHRDAGADSDSDSDLSLEEERSLSIPSSESEDNGRTRGRFQRPLRRAAQSERLLAHPKDVDGNDLLSYWPALGECEAAPCALQAWGSERRLGLDSNKDAANNNQPELALTSGDETSLGRAQRQRKGILKNRLQYPLVPQTRGTPELSWCRAATLGHRAVPAASYGRIYAGGGTGSLSQPASRYSSREQLDLLLRRQLSRERLEEVPVPAPVLHPLSRPGSQERLDTAPARLEPRDRGSTLPRRQPPRDYPGTMAGRFGSRDALDLGAPREWLSTLPPPRRNRDLDPQHPPLPLSPQRPLSRDPLLPSRPLDSLSRISNSRERLDQVPSRHPSREALGPAPQLLRAREDPASGPSHGPSTEQLDILSSILASFNSSALSSVQSSSTPSGPHTTATPSATASALGPSTPRSATSHSISELSPDSEVPRSEGHS
| null | null |
axonal fasciculation [GO:0007413]; cell-cell adhesion [GO:0098609]; cilium assembly [GO:0060271]; dopaminergic neuron axon guidance [GO:0036514]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; motor neuron migration [GO:0097475]; regulation of protein localization [GO:0032880]; regulation of protein phosphorylation [GO:0001932]; serotonergic neuron axon guidance [GO:0036515]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]
|
plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; G protein-coupled receptor activity [GO:0004930]
|
PF00002;PF00028;PF00008;PF16489;PF01825;PF02793;PF00053;PF02210;
|
2.60.120.200;2.60.220.50;2.60.40.60;4.10.1240.10;2.10.25.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, LN-TM7 subfamily
|
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation.
|
Rattus norvegicus (Rat)
|
O88279
|
SLIT1_RAT
|
MALTPQRGSSSGLSRPELWLLLWAAAWRLGATACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLQVLPELLFQNNQALSRLDLSENSLQAVPRKAFRGATDLKNLQLDKNQISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKSEFSCSGQGEAAQVPACTLSSGSCPAMCSCSNGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETTGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYHLNSECTSDVACPHKCRCEASVVECSGLKLSKIPERIPQSTTELRLNNNEISILEATGLFKKLSHLKKINLSNNKVSEIEDGTFEGATSVSELHLTANQLESVRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNHITTISPGAFDTLQALSTLNLLANPFNCNCQLAWLGDWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEVGCLPRPQCPQECACLDTVVRCSNKHLQALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDVSTLQEGIFADVTSLSHLAIGANPLYCDCHLRWLSSWVKTGYKEPGIARCAGPPEMEGKLLLTTPAKKFECQGPPSLAVQAKCDPCLSSPCQNQGTCHNDPLEVYRCTCPSGYKGRNCEVSLDSCSSNPCGNGGTCHAQEGEDAGFTCSCPSGFEGLTCGMNTDDCVKHDCVNGGVCVDGIGNYTCQCPLQYTGRACEQLVDFCSPDLNPCQHEAQCVGTPEGPRCECVPGYTGDNCSKNQDDCKDHQCQNGAQCVDEINSYACLCAEGYSGQLCEIPPAPRNSCEGTECQNGANCVDQGSRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVTFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTSFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPVCHCEAGWGGLHCDQPVDGPCHGHKCVHGKCVPLDALAYSCQCQDGYSGALCNQVGAVAEPCGGLQCLHGHCQASATRGAHCVCSPGFSGELCEQESECRGDPVRDFHRVQRGYAICQTTRPLSWVECRGACPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKCGCAPCA
| null | null |
axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; dorsal/ventral axon guidance [GO:0033563]; motor neuron axon guidance [GO:0008045]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of synapse assembly [GO:0051964]; neuron projection morphogenesis [GO:0048812]; nuclear migration [GO:0007097]; olfactory bulb development [GO:0021772]; retinal ganglion cell axon guidance [GO:0031290]; spinal cord development [GO:0021510]; tangential migration from the subventricular zone to the olfactory bulb [GO:0022028]; telencephalon cell migration [GO:0022029]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495]
|
PF00008;PF12661;PF02210;PF13855;PF01463;PF01462;
|
2.60.120.200;2.10.25.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb (By similarity). {ECO:0000250, ECO:0000269|PubMed:10864956}.
|
Rattus norvegicus (Rat)
|
O88280
|
SLIT3_RAT
|
MAPGRTGAGAAVRARLALALALASILSGPPAAACPTKCTCSAASVDCHGLGLRAVPRGIPRNAERLDLDRNNITRITKMDFTGLKNLRVLHLEDNQVSVIERGAFQDLKQLERLRLNKNKLQVLPELLFQSTPKLTRLDLSENQIQGIPRKAFRGVTGVKNLQLDNNHISCIEDGAFRALRDLEILTLNNNNISRILVTSFNHMPKIRTLRLHSNHLYCDCHLAWLSDWLRQRRTIGQFTLCMAPVHLRGFSVADVQKKEYVCPGPHSEAPACNANSLSCPSACSCSNNIVDCRGKGLTEIPANLPEGIVEIRLEQNSIKSIPAGAFIQYKKLKRIDISKNQISDIAPDAFQGLKSLTSLVLYGNKITEIPKGLFDGLVSLQLLLLNANKINCLRVNTFQDLQNLNLLSLYDNKLQTISKGLFAPLQSIQTLHLAQNPFVCDCHLKWLADYLQDNPIETSGARCSSPRRLANKRISQIKSKKFRCSGSEDYRNRFSSECFMDLVCPEKCRCEGTIVDCSNQKLSRIPSHLPEYTTDLRLNDNDIAVLEATGIFKKLPNLRKINLSNNRIKEVREGAFDGAAGVQELMLTGNQLETMHGRMFRGLSGLKTLMLRSNLISCVNNDTFAGLSSVRLLSLYDNRITTISPGAFTTLVSLSTINLLSNPFNCNCHMAWLGRWLRKRRIVSGNPRCQKPFFLKEIPIQDVAIQDFTCEGNEENSCQLSPRCPEQCTCVETVVRCSNRGLHTLPKGMPKDVTELYLEGNHLTAVPKELSTFRQLTLIDLSNNSISMLTNHTFSNMSHLSTLILSYNRLRCIPVHAFNGLRSLRVLTLHGNDISSVPEGSFNDLTSLSHLALGINPLHCDCSLRWLSEWIKAGYKEPGIARCSSPESMADRLLLTTPTHRFQCKGPVDINIVAKCNACLSSPCKNNGTCSQDPVEQYRCTCPYSYKGKDCTVPINTCVQNPCQHGGTCHLSESHRDGFSCSCPLGFEGQRCEINPDDCEDNDCENSATCVDGINNYACVCPPNYTGELCDEVIDYCVPEMNLCQHEAKCISLDKGFRCECVPGYSGKLCETDNDDCVAHKCRHGAQCVDAVNGYTCICPQGFSGLFCEHPPPMVLLQTSPCDQYECQNGAQCIVVQQEPTCRCPPGFAGPRCEKLITVNFVGKDSYVELASAKVRPQANISLQVATDKDNGILLYKGDNDPLALELYQGHVRLVYDSLSSPPTTVYSVETVNDGQFHSVELVMLNQTLNLVVDKGAPKSLGKLQKQPAVGINSPLYLGGIPTSTGLSALRQGADRPLGGFHGCIHEVRINNELQDFKALPPQSLGVSPGCKSCTVCRHGLCRSVEKDSVVCECHPGWTGPLCDQEAQDPCLGHSCSHGTCVATGNSYVCKCAEGYEGPLCDQKNDSANACSAFKCHHGQCHISDRGEPYCLCQPGFSGNHCEQENPCLGEIVREAIRRQKDYASCATASKVPIMVCRGGCGSQCCQPIRSKRRKYVFQCTDGSSFVEEVERHLECGCRECS
| null | null |
animal organ morphogenesis [GO:0009887]; aortic valve morphogenesis [GO:0003180]; apoptotic process involved in luteolysis [GO:0061364]; atrioventricular valve morphogenesis [GO:0003181]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cellular response to hormone stimulus [GO:0032870]; negative chemotaxis [GO:0050919]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; negative regulation of gene expression [GO:0010629]; response to cortisol [GO:0051414]; Roundabout signaling pathway [GO:0035385]; spinal cord development [GO:0021510]; ventricular septum morphogenesis [GO:0060412]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495]
|
PF00008;PF02210;PF13855;PF01463;PF01462;
|
2.60.120.200;2.10.25.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May act as molecular guidance cue in cellular migration, and function may be mediated by interaction with roundabout homolog receptors.
|
Rattus norvegicus (Rat)
|
O88282
|
BCL6B_MOUSE
|
MGSTAAPEGALGYVREFTRHSSDVLSNLNELRLRGILTDVTLLVGGQPLRAHKAVLIACSGFFYSIFRGRAGLGVDVLSLPGGPEARGFAPLLDFMYTSRLRLSPATAPAVLAAATYLQMEHVVQACHRFIQASYEPLGISLRPVEVEPPRPPTVAPPGSPRRSEGHPDPPTESRSCSQGSPSPASPDPKACNWKKYKFIVLNSQTSQAGSLVGESSGQPCPQARLPSGDEACSSSSSSEEGTTPGLQSRLSLATTTARFKCGALANNSYLFTPRAQETSLPASKQANPPPGSEFFSCQNCEAVAGCSSGLELLAPGDEDKPYKCQLCRSAFRYKGNLASHRTVHTGEKPYRCSICGARFNRPANLKTHSRIHSGEKPYKCETCGSRFVQVAHLRAHVLIHTGEKPYPCPTCGTRFRHLQTLKSHVRIHTGEKPYHCDPCGLHFRHKSQLRLHLRQKHGAATNTKVRYHILGGP
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of cytokine production [GO:0001817]; regulation of immune system process [GO:0002682]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00651;PF00096;
|
3.30.160.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Acts as a sequence-specific transcriptional repressor in association with BCL6. Necessary for activation of naive T-cells to antigenic stimulation. May attenuate the regulatory effect of BCL6 on antigenic activation of naive CD4 T-cells by forming a heterodimer with BCL6. {ECO:0000269|PubMed:15314041, ECO:0000269|PubMed:9632807}.
|
Mus musculus (Mouse)
|
O88286
|
WIZ_MOUSE
|
MEGLLAGGLAAPDHPRGPAPREDIESGAEAAEGEGDIFPSSHYLPITKEGPRDILDGRSGISDGQPHPGLSEALPRATSATHRISSCYWDGDSLDFQPGSPPPHLLGPFPASLDVQGSWEHPMVQEAREGTPSEQRFKDSVIVRTMKPYAKLKGSRKFLHHQGEVKFLEKYSPSHHKFDWLQDTDEQGPLKDTGLHLDLPAQPPTVTSFRRVIVPVDNTPKTLDMEVMGTREDLEDFGQVAQPSEWGLHTSASEVATQTWTVNSEASVERLQPLLSPVQTGPYLCELLQEVAGGVDSNEEEEEEPAVFPCIECSIYFKHKEHLLEHMSQHRRAPGQEPPADLAPLACSECGWAFTEPTALEQHWQLHQASREKIIEEIQKLKQFPGDEGREARLQCSKCVFGTNSSRAFMQHAKLHVRGSLPSRQATEPFRGGSPVLDVSTLVYPSYGDSSGLNTCVHCGFTAPSKSLLREHTRLVHAHHAHWEEVGEAFEDLTSQPCTSQDAYTHSPDTATVDYFSKSEPLLASVWQENPSGYDPDLAFGPDYQQPGMRNFPLLNSGQQSLGKLAFPSPMASASYSIQRNRNKSTVHLQRMEDKSHLWSEEEEEEDEDVVLTSERDFTPENGAFPPLAIPSLIPQPALELKQTFQDALQAVDASETQQQQLQGMVPIVLMAKLRPQVIAATTRASPQLPPEEPELRSTHPLDFLLLDAPLGGSLGLNTLLEGDPAMALKHEERKCPYCPDRFHYGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTISPINILQELLATSAAELPPSPLGREPGGPPRSFLTSRRPRLPLTMPFPPTWAEDPGPIYGDAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAPLGLTPSLTKKSNSPKEFLAGAARPGLLTLAKPMDAPAVNKAIKSPPGFSAKGLTHPSSSPLLKKAPLTLAGSPTPKNPEDKSPQLSLSPRPTSPKAQWPQSEDEGPLNLTSGPEPTRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGHLHPPGPSPKALAKVLSTGGPGSSLEARSPSDLHISPLTKKLPPPPGSPLGHSPTASPPPTARKMFSGLATPSLPKKLKPEHMRVEIKREMLPGTLHGEPHPSEGPWGTPREDMAPLNLSARAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKLCLIKKEPPAGDLAPALTEDGSPTAAPGALHSPLPLSPLASRPGKPGAGPTQVPRELSLSPITGSKPSAASYLGPVATKRPLQEDRFLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPPLGLAPGGLSLVGRSAGGEPGLEAGRAADSGERPLATSPPGTVKSEEHQRQNINKFERRQARPSDASAARGGEEVNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEEPQAPQAQTAAVEAP
| null | null |
protein stabilization [GO:0050821]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; SET domain binding [GO:0070984]
| null |
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16702210}.
| null | null | null | null | null |
FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization. {ECO:0000269|PubMed:16702210}.
|
Mus musculus (Mouse)
|
O88291
|
ZN326_MOUSE
|
MDFEDDYVHSTCRGAYQDFNGMDRDYGPGSYGGLDRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGGGSRFGPYESYDSRSSLGGRDLYRSGYGFNEPEQTRFGGSYGGRFESSYRNSLDSFGGRNQGGSSWEAPYSRSKLRPGFMEDRGRENYSSYSSFSSPHMKPAPVGSRGRGTPAYPESTFGSRSYDAFGGPSTGRGRGRGHMGDFGSFHRPGIIVDYQNKPANVTIATARGIKRKMMQIFIKPGGAFIKKPKLAKPMDKMNLSKSPTKTDPKNEEEEKRRIEARREKQRRRREKNSEKYGDGYRMAFTCSFCKFRTFEEKDIELHLESSSHQETLDHIQKQTKFDKVVMEFLHECMVNKFKKASIRKQQTLNHPEAYKIIEKDIMEGVTADDHMMKVETVHCSACSVYIPALHSSVQLHLKSPDHSKGKQAYKEQIKRESVLTATSILNNPIVKARYERFVKGENPFEIQDHPQDQQIEGDEEDEEKIDEPIEEEEEEEEEEEEEGEEAGSVEEEGDVEGEEGTAEAAAAGEADAVGEAEGAGEAEEAEEEEEEEGTQEFAAQACATEQCEHRQM
| null | null |
mRNA processing [GO:0006397]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription elongation [GO:0032784]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]
|
DBIRD complex [GO:0044609]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; RNA polymerase II complex binding [GO:0000993]; zinc ion binding [GO:0008270]
|
PF04988;
| null |
AKAP95 family
| null |
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10798446, ECO:0000269|PubMed:9809746}.
| null | null | null | null | null |
FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (By similarity). May also play a role in neuronal differentiation. Able to bind DNA and activate expression in vitro. {ECO:0000250, ECO:0000269|PubMed:10798446}.
|
Mus musculus (Mouse)
|
O88307
|
SORL_MOUSE
|
MATRSSRRESRLPFLFALVALLPRGALGGGWTQRLHGGPAPLPQDRGFFVVQGDPRDLRLGTHGDAPGASPAARKPLRTRRSAALQPQPIQVYGQVSLNDSHNQMVVHWAGEKSNVIVALARDSLALARPKSSDVYVSYDYGKSFSKISEKLNFGVGNNSEAVISQFYHSPADNKRYIFVDAYAQYLWITFDFCSTIHGFSIPFRAADLLLHSKASNLLLGFDRSHPNKQLWKSDDFGQTWIMIQEHVKSFSWGIDPYDQPNAIYIERHEPFGFSTVLRSTDFFQSRENQEVILEEVRDFQLRDKYMFATKVVHLPGSQQQSSVQLWVSFGRKPMRAAQFVTKHPINEYYIADAAEDQVFVCVSHSNNSTNLYISEAEGLKFSLSLENVLYYSPGGAGSDTLVRYFANEPFADFHRVEGLQGVYIATLINGSMNEENMRSVITFDKGGTWEFLQAPAFTGYGEKINCELSQGCSLHLAQRLSQLLNLQLRRMPILSKESAPGLIIATGSVGKNLASKTNVYISSSAGARWREALPGPHYYTWGDHGGIIMAIAQGMETNELKYSTNEGETWKTFVFSEKPVFVYGLLTEPGEKSTVFTIFGSNKESVHSWLILQVNATDALGVPCTENDYKLWSPSDERGNECLLGHKTVFKRRTPHATCFNGEDFDRPVVVSNCSCTREDYECDFGFKMSEDLSLEVCVPDPEFSGKPYSPPVPCPVGSSYRRTRGYRKISGDTCSGGDVEARLEGELVPCPLAEENEFILYAMRKSIYRYDLASGATEQLPLSGLRAAVALDFDYERNCLYWSDLALDTIQRLCLNGSTGQEVIINSGLETVEALAFEPLSQLLYWVDAGFKKIEVANPDGDFRLTIVNSSVLDRPRALVLVPQEGVMFWTDWGDLKPGIYRSYMDGSAAYRLVSEDVKWPNGISVDSQWIYWTDAYLDCIERITFSGQQRSVILDSLPHPYAIAVFKNEIYWDDWSQLSIFRASKHSRSQVEILASQLTGLMDMKVFYKGKNAGSNACVPQPCSLLCLPKANNSKSCRCPEGVASSVLPSGDLMCDCPQGYQRKNNTCVKEENTCLRNQYRCSNGNCINSIWWCDFDNDCGDMSDERNCPTTVCDADTQFRCQESGTCIPLSYKCDLEDDCGDNSDESHCEMHQCRSDEFNCSSGMCIRSSWVCDGDNDCRDWSDEANCTAIYHTCEASNFQCHNGHCIPQRWACDGDADCQDGSDEDPVSCEKKCNGFHCPNGTCIPSSKHCDGLRDCPDGSDEQHCEPFCTRFMDFVCKNRQQCLFHSMVCDGIVQCRDGSDEDAAFAGCSQDPEFHKECDEFGFQCQNGVCISLIWKCDGMDDCGDYSDEANCENPTEAPNCSRYFQFHCENGHCIPNRWKCDRENDCGDWSDEKDCGDSHVLPSPTPGPSTCLPNYFHCSSGACVMGTWVCDGYRDCADGSDEEACPSLANSTAASTPTQFGQCDRFEFECHQPKKCIPNWKRCDGHQDCQDGQDEANCPTHSTLTCTSREFKCEDGEACIVLSERCDGFLDCSDESDEKACSDELTVYKVQNLQWTADFSGDVTLTWMRPKKMPSASCVYNVYYRVVGESIWKTLETHSNKTSTVLKVLKPDTTYQVKVQVHCLNKVHNTNDFVTLRTPEGLPDAPRNLQLSLNSEEEGVILGHWAPPVHTHGLIREYIVEYSRSGSKMWASQRAASNSTEIKNLLLNALYTVRVAAVTSRGIGNWSDSKSITTIKGKVIQAPNIHIDSYDENSLSFTLTMDGDIKVNGYVVNLFWSFDAHKQEKKTLSFRGGSALSHRVSNLTAHTSYEISAWAKTDLGDSPLAFEHILTRGSSPPAPSLKAKAINQTAVECIWTGPKNVVYGIFYATSFLDLYRNPKSVTTSLHNKTVIVSKDEQYLFLVRVLIPYQGPSSDYVVVKMIPDSRLPPRHLHAVHIGKTSALIKWESPYDSPDQDLFYAIAVKDLIRKTDRSYKVRSRNSTVEYSLSKLEPGGKYHIIVQLGNMSKDSSIKITTVSLSAPDALKIITENDHVLLFWKSLALKEKQFNETRGYEIHMSDSAVNLTAYLGNTTDNFFKVSNLKMGHNYTFTVQARCLFGSQICGEPAVLLYDELSSGADAAVIQAARSTDVAAVVVPILFLILLSLGVGFAILYTKHRRLQSSFSAFANSHYSSRLGSAIFSSGDDLGEDDEDAPMITGFSDDVPMVIA
| null | null |
adaptive thermogenesis [GO:1990845]; cell migration [GO:0016477]; diet induced thermogenesis [GO:0002024]; endosome to plasma membrane protein transport [GO:0099638]; insulin receptor recycling [GO:0038020]; negative regulation of amyloid precursor protein catabolic process [GO:1902992]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of neurofibrillary tangle assembly [GO:1902997]; negative regulation of neurogenesis [GO:0050768]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of triglyceride catabolic process [GO:0010897]; neuropeptide signaling pathway [GO:0007218]; positive regulation of adipose tissue development [GO:1904179]; positive regulation of early endosome to recycling endosome transport [GO:1902955]; positive regulation of endocytic recycling [GO:2001137]; positive regulation of ER to Golgi vesicle-mediated transport [GO:1902953]; positive regulation of glial cell-derived neurotrophic factor production [GO:1900168]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein exit from endoplasmic reticulum [GO:0070863]; positive regulation of protein localization to early endosome [GO:1902966]; post-Golgi vesicle-mediated transport [GO:0006892]; protein localization to Golgi apparatus [GO:0034067]; protein maturation [GO:0051604]; protein retention in Golgi apparatus [GO:0045053]; protein targeting [GO:0006605]; protein targeting to lysosome [GO:0006622]; receptor-mediated endocytosis [GO:0006898]; regulation of smooth muscle cell migration [GO:0014910]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; multivesicular body [GO:0005771]; multivesicular body membrane [GO:0032585]; neuronal cell body [GO:0043025]; nuclear envelope lumen [GO:0005641]; perinuclear region of cytoplasm [GO:0048471]; perinucleolar compartment [GO:0097356]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; transport vesicle membrane [GO:0030658]
|
amyloid-beta binding [GO:0001540]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; low-density lipoprotein particle binding [GO:0030169]; neuropeptide binding [GO:0042923]; small GTPase binding [GO:0031267]; transmembrane signaling receptor activity [GO:0004888]
|
PF00041;PF00057;PF00058;PF15902;PF15901;
|
2.10.70.80;3.30.60.270;2.60.40.10;4.10.400.10;2.120.10.30;2.130.10.10;
|
VPS10-related sortilin family, SORL1 subfamily
|
PTM: Within the Golgi apparatus, the propeptide may be cleaved off by FURIN or a furin-like protease. After cleavage, the propeptide interacts with the mature protein N-terminus, preventing the association with other ligands. At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain in the extracellular milieu. The shedding may be catalyzed by ADAM17/TACE. Following shedding, PSEN1/presenilin-1 cleaves the remaining transmembrane fragment and catalyzes the release of a C-terminal fragment in the cytosol and of a soluble N-terminal beta fragment in the extracellular milieu. The C-terminal cytosolic fragment localizes to the nucleus. {ECO:0000250|UniProtKB:Q92673}.; PTM: Phosphorylation at Ser-2207 facilitates the interaction with GGA1. {ECO:0000250|UniProtKB:Q92673}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Endosome membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Early endosome membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Cell membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Secreted {ECO:0000269|PubMed:11082041, ECO:0000269|PubMed:26584636}. Note=Mostly intracellular, predominantly in the trans-Golgi network (TGN) and in endosome, as well as in endosome-to-TGN recycling compartments; found at low levels on the plasma membrane (By similarity). At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain (also called soluble SORLA, solLR11 or sLR11) in the extracellular milieu (PubMed:11082041). The shedding may be catalyzed by ADAM17/TACE. Following shedding, PSEN1/presenilin-1 cleaves the remaining transmembrane fragment and catalyzes the release of a C-terminal fragment in the cytosol and of a soluble N-terminal beta fragment in the extracellular milieu. The C-terminal cytosolic fragment localizes to the nucleus. At the cell surface, the full-length protein undergoes partial clathrin-dependent endocytosis guided by clathrin adapter protein 2 (AP-2) (By similarity). {ECO:0000250|UniProtKB:Q92673, ECO:0000269|PubMed:11082041}.
| null | null | null | null | null |
FUNCTION: Sorting receptor that directs several proteins to their correct location within the cell. Along with AP-1 complex, involved Golgi apparatus - endosome sorting. Sorting receptor for APP, regulating its intracellular trafficking and processing into amyloidogenic-beta peptides. Retains APP in the trans-Golgi network, hence preventing its transit through late endosomes where amyloid beta peptides Abeta40 and Abeta42 are generated. May also sort newly produced amyloid-beta peptides to lysosomes for catabolism. Does not affect APP trafficking from the endoplasmic reticulum to Golgi compartments (By similarity). Sorting receptor for the BDNF receptor NTRK2/TRKB that facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling by controlling the intracellular location of its receptor (PubMed:23977241). Sorting receptor for GDNF that promotes GDNF regulated, but not constitutive secretion (PubMed:21994944). Sorting receptor for the GDNF-GFRA1 complex, directing it from the cell surface to endosomes. GDNF is then targeted to lysosomes and degraded, while its receptor GFRA1 recycles back to the cell membrane, resulting in a GDNF clearance pathway. The SORL1-GFRA1 complex further targets RET for endocytosis, but not for degradation, affecting GDNF-induced neurotrophic activities (PubMed:23333276). Sorting receptor for ERBB2/HER2. Regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulating phosphoinositide 3-kinase (PI3K)-dependent ERBB2 signaling (By similarity). Sorting receptor for lipoprotein lipase LPL. Promotes LPL localization to endosomes and later to the lysosomes, leading to degradation of newly synthesized LPL (By similarity). Potential sorting receptor for APOA5, inducing APOA5 internalization to early endosomes, then to late endosomes, wherefrom a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network (By similarity). Sorting receptor for the insulin receptor INSR. Promotes recycling of internalized INSR via the Golgi apparatus back to the cell surface, thereby preventing lysosomal INSR catabolism, increasing INSR cell surface expression and strengthening insulin signal reception in adipose tissue. Does not affect INSR internalization (PubMed:27322061). Plays a role in renal ion homeostasis, controlling the phospho-regulation of SLC12A1/NKCC2 by STK39/SPAK kinase and PPP3CB/calcineurin A beta phosphatase, possibly through intracellular sorting of STK39 and PPP3CB (PubMed:20385770, PubMed:25967121). Stimulates, via the N-terminal ectodomain, the proliferation and migration of smooth muscle cells, possibly by increasing cell surface expression of the urokinase receptor uPAR/PLAUR. This may promote extracellular matrix proteolysis and hence facilitate cell migration (By similarity). By acting on the migration of intimal smooth muscle cells, may accelerate intimal thickening following vascular injury (PubMed:14764453). Promotes adhesion of monocytes (By similarity). Stimulates proliferation and migration of monocytes/macrophages. Through its action on intimal smooth muscle cells and macrophages, may accelerate intimal thickening and macrophage foam cell formation in the process of atherosclerosis (PubMed:17332490). Regulates hypoxia-enhanced adhesion of hematopoietic stem and progenitor cells to the bone marrow stromal cells via a PLAUR-mediated pathway. This function is mediated by the N-terminal ectodomain (PubMed:23486467). Metabolic regulator, which functions to maintain the adequate balance between lipid storage and oxidation in response to changing environmental conditions, such as temperature and diet. The N-terminal ectodomain negatively regulates adipose tissue energy expenditure, acting through the inhibition the BMP/Smad pathway (PubMed:26584636). May regulate signaling by the heterodimeric neurotrophic cytokine CLCF1-CRLF1 bound to the CNTFR receptor by promoting the endocytosis of the tripartite complex CLCF1-CRLF1-CNTFR and lysosomal degradation (PubMed:26858303). May regulate IL6 signaling, decreasing cis signaling, possibly by interfering with IL6-binding to membrane-bound IL6R, while up-regulating trans signaling via soluble IL6R (PubMed:28265003). {ECO:0000250|UniProtKB:Q92673, ECO:0000269|PubMed:14764453, ECO:0000269|PubMed:17332490, ECO:0000269|PubMed:20385770, ECO:0000269|PubMed:21994944, ECO:0000269|PubMed:23333276, ECO:0000269|PubMed:23486467, ECO:0000269|PubMed:23977241, ECO:0000269|PubMed:25967121, ECO:0000269|PubMed:26584636, ECO:0000269|PubMed:26858303, ECO:0000269|PubMed:27322061, ECO:0000269|PubMed:28265003}.
|
Mus musculus (Mouse)
|
O88310
|
ITL1A_MOUSE
|
MTQLGFLLFIMVATRGCSAAEENLDTNRWGNSFFSSLPRSCKEIKQEHTKAQDGLYFLRTKNGVIYQTFCDMTTAGGGWTLVASVHENNMRGKCTVGDRWSSQQGNRADYPEGDGNWANYNTFGSAEAATSDDYKNPGYFDIQAENLGIWHVPNKSPLHNWRKSSLLRYRTFTGFLQHLGHNLFGLYKKYPVKYGEGKCWTDNGPALPVVYDFGDARKTASYYSPSGQREFTAGYVQFRVFNNERAASALCAGVRVTGCNTEHHCIGGGGFFPEGNPVQCGDFASFDWDGYGTHNGYSSSRKITEAAVLLFYR
| null | null |
positive regulation of glucose import [GO:0046326]; positive regulation of protein phosphorylation [GO:0001934]; response to nematode [GO:0009624]
|
brush border membrane [GO:0031526]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; receptor complex [GO:0043235]; side of membrane [GO:0098552]
|
calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; oligosaccharide binding [GO:0070492]
|
PF00147;
|
3.90.215.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WWA0}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8WWA0}. Secreted {ECO:0000250|UniProtKB:Q8WWA0}. Note=Enriched in lipid rafts. {ECO:0000269|PubMed:16866365}.
| null | null | null | null | null |
FUNCTION: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner (PubMed:26148048). Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris. Does not bind mammalian glycans. Probably plays a role in the defense system against microorganisms. May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption (By similarity). {ECO:0000250|UniProtKB:Q8WWA0, ECO:0000269|PubMed:26148048}.
|
Mus musculus (Mouse)
|
O88312
|
AGR2_MOUSE
|
MEKFSVSAILLLVAISGTLAKDTTVKSGAKKDPKDSRPKLPQTLSRGWGDQLIWTQTYEEALYRSKTSNRPLMVIHHLDECPHSQALKKVFAEHKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIVFVDPSLTVRADITGRYSNRLYAYEPSDTALLYDNMKKALKLLKTEL
| null | null |
cell chemotaxis [GO:0060326]; digestive tract morphogenesis [GO:0048546]; endoplasmic reticulum unfolded protein response [GO:0030968]; inflammatory response [GO:0006954]; lung goblet cell differentiation [GO:0060480]; mucus secretion [GO:0070254]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of developmental growth [GO:0048639]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of gene expression [GO:0010628]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896]; positive regulation of PERK-mediated unfolded protein response [GO:1903899]; positive regulation of protein localization to plasma membrane [GO:1903078]; protein folding in endoplasmic reticulum [GO:0034975]
|
endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]
|
dystroglycan binding [GO:0002162]; epidermal growth factor receptor binding [GO:0005154]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF13899;
|
3.40.30.10;
|
AGR family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O95994}. Endoplasmic reticulum {ECO:0000269|PubMed:19359471}.
| null | null | null | null | null |
FUNCTION: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth (By similarity). Promotes cell adhesion (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O95994, ECO:0000269|PubMed:19359471}.
|
Mus musculus (Mouse)
|
O88319
|
NTR1_MOUSE
|
MHLNSSVQQGAPSEPGAQPFPHPQFGLETMLLALSLSNGSGNSSESILEPNSNLDVNTDIYSKVLVTAVYLALFVVGTVGNSVTAFTLARKKSLQSLQSTVHYHLGSLALSDLLILLLAMPVELYNFIWVHHPWAFGDAGCRGYYFLRDACTYATALNVASLSVERYLAICHPFKAKTLMSRSRTKKFISAIWLASALLAVPMLFTMGLQNRSADGQHPGGLVCTPTVDTATVKVVIQVNTFMSFLFPMLIISILNTVIANKLTVMVHQAAEQGRGVCTVGTHNSLEHSTFNMSIEPGRVQALRHGVLVLRAVVIAFVVCWLPYHVRRLMFCYISDEQWTTFLFDFYHYFYMLTNALFYVSSAINPILYNLVSANFRQVFLSTLACLCPGWRRRRKKRPTFSRKPNSMSSNHAFSTSATRETLY
| null | null |
adult locomotory behavior [GO:0008344]; D-aspartate import across plasma membrane [GO:0070779]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; inositol phosphate catabolic process [GO:0071545]; L-glutamate import across plasma membrane [GO:0098712]; learning [GO:0007612]; negative regulation of apoptotic process [GO:0043066]; negative regulation of release of sequestered calcium ion into cytosol [GO:0051280]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; positive regulation of apoptotic process [GO:0043065]; positive regulation of arachidonic acid secretion [GO:0090238]; positive regulation of gamma-aminobutyric acid secretion [GO:0014054]; positive regulation of gene expression [GO:0010628]; positive regulation of glutamate secretion [GO:0014049]; positive regulation of inhibitory postsynaptic potential [GO:0097151]; positive regulation of inositol phosphate biosynthetic process [GO:0060732]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; regulation of membrane depolarization [GO:0003254]; regulation of respiratory gaseous exchange [GO:0043576]; response to lipid [GO:0033993]; temperature homeostasis [GO:0001659]
|
axon [GO:0030424]; axon terminus [GO:0043679]; cell surface [GO:0009986]; cytoplasmic side of plasma membrane [GO:0009898]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; membrane raft [GO:0045121]; neuron spine [GO:0044309]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; symmetric synapse [GO:0032280]; terminal bouton [GO:0043195]
|
G protein-coupled neurotensin receptor activity [GO:0016492]; identical protein binding [GO:0042802]; neuropeptide receptor activity [GO:0008188]; protein-containing complex binding [GO:0044877]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Neurotensin receptor subfamily, NTSR1 sub-subfamily
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P30989}.; PTM: Palmitoylated; this is required for normal localization at membrane rafts and normal GNA11-mediated activation of down-stream signaling cascades. The palmitoylation level increases in response to neurotensin treatment. {ECO:0000250|UniProtKB:P30989}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30989}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30989}. Membrane raft {ECO:0000250|UniProtKB:P30989}. Note=Palmitoylation is required for localization at CAV1-enriched membrane rafts. {ECO:0000250|UniProtKB:P30989}.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for the tridecapeptide neurotensin (NTS). Signaling is effected via G proteins that activate a phosphatidylinositol-calcium second messenger system. Signaling leads to the activation of downstream MAP kinases and protects cells against apoptosis. {ECO:0000250|UniProtKB:P30989}.
|
Mus musculus (Mouse)
|
O88322
|
NID2_MOUSE
|
MFRDPTAGWLTPPSPLSLLVMLLLLSRVGALRPDELFPYGESWGDQLLPEGDDESSAAVKLAIPLRFYDAQFSSLYVGTNGIISTQDFPRETQYVDDDFPTDFPAIAPFLADIDTSHSRGRILYREDTSGAVLSLAARYVRTGFPLSGSSFTPTHAFLATWEHVGAYEEVSRGAAPSGELNTFQAVLASDESDTYALFLYPANGLQFFGTRPKESYNVQLQLPARVGFCRGEADDLKREALYFSLTNTEQSVKNLYQLSNLGIPGVWAFHIGSRFALDNVRPATVGGDPSTARSSALEHPFSHAAALESYTEDSFHYYDENEEDVEYPPVEPGEAPEGHSRIDVSFNSKADPGLVDVGTSSPGSDRASPWPYPAPGNWPSYRETESASLDPQTKQGRPVGEGEVLDFRDPAELLDQMGTRAPAPPEADAALLTPVNEDLGGRNTQSYPEAGPVPSEPDVPVPPLEGEVLPHYPESGHVPPLRGGKYVIGLEDHVGSNDQVFTYNGANLETCEHSHGRCSQHAFCTDYTTGFCCHCQSRFYGNGKHCLPEGAPHRVNGKVSGRLRVGHIPVHFTDVDLHAYIVGNDGRAYTAISHVPQPAAQALLPVLPIGGLFGWLFALEKPGSENGFSLTGATFVHDVEVTFHPGEERVRITQTAEGLDPENYLSIKTNIEGQVPFIPANFTAHITPYKEFYHYRDSVVTSSSSRSFSLTSGSINQTWSYHIDQNITYQACRHAPRHLAIPATQQLTVDRAFALYSEDEGVLRFAVTNQIGPVEVDSAPVGVNPCYDGSHTCDTTARCHPGTGVDYTCECTPGFQGDGRSCVDVNECATGFHRCGPNSVCVNLVGSYRCECRSGYEFADDQHTCILIAPPPNPCLDGSHTCAPEGQARCIHHGGSSFSCACLPGFIGTGHQCSDVDECAENRCHEAAICYNTPGSFSCRCQPGYRGDGFHCTSDTVPEDSISGLKPCEYQQRYAQTQHAYPGSRIHIPQCDDQGNFVPLQCHGSTGFCWCVDRNGHEVPGTQTPPGSTPPHCGPPPEPTQRPRTVCERWRESLLEHYGGTPRDDQYVPQCDDLGHFIPLQCHGKSDFCWCVDKDGRELQGTRSQPGTRPACIPTVAPPVVRPTPRPDVTPPSVGTFLLYAQGQQIGHLPLNGSRLQKDAARTLLSLHGSIVVGIDYDCRERMVYWTDVAGRTISRASLEAGAEPETIITSGLISPEGLAIDHFRRTMYWTDSGLDKIERAELDGSERKVLFHTDLVNPRAITVDPIRGNLYWTDWNREAPKIETSSLDGENRRILINKDIGLPNGLTFDPFSKLLCWADAGTKKLECTLPDGTGRRVIQNHLNYPFSIVSYADHFYHTDWRRDGVISVNKDSGQFTDEFLPEQRSHLYGITAVYPYCPTGRK
| null | null |
cell-matrix adhesion [GO:0007160]
|
basement membrane [GO:0005604]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]
|
PF07645;PF07474;PF00058;PF06119;PF00086;
|
2.40.155.10;2.10.25.10;4.10.800.10;2.120.10.30;
| null |
PTM: Highly N- and O-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane.
| null | null | null | null | null |
FUNCTION: Cell adhesion glycoprotein. Might be involved in osteoblast differentiation. It probably has a role in cell-extracellular matrix interactions.
|
Mus musculus (Mouse)
|
O88329
|
MYO1A_MOUSE
|
MPLLEGPVGVEDLILLEPLDEESLIKNLQLRYENKEIYTYIGNVVISMNPYEQLPIYGPEFIAKYRDYTFYELKPHIYALANVAYQSLKDRDRDQCILITGESGAGKTEASKLVMSYVAAVCGKGEQVNSVKEQLLQSNPVLEAFGNAKTIRNNNSSRFGKYMDIEFDFKGSPLGGVITNYLLEKSRVVKQLKGERNFHIFYQLLAGADAQLLKALKLEEDTSVYGYLNGEVSKVNGMDDASNFRAVQHAMSVIGFSEEEIRQVLEVTALVLKLGNVKLTDEFQANGIPASGICDGKGIQEIGEMMGLNSTELERALCSRTMETGKEKVVTVLNVTQAQYARDALAKNIYSRLFDWIVKRINESIKVGTGEKKKVMGVLDIYGFEILEDNSFEQFVINYCNERLQQVFIELTLKEEQEEYKREGIPWTKVEYFDNGIICNLIEHSQRGILAMLDEECLRPGVVSDSTFLAKLNQLFSKHSHYESKVSQNAQRQYDRTMGLSCFRISHYAGKVTYNVTGFIDKNNDLLFRDLSQTMWKAQHPLLKSLFPEGNPKEASLKRPPTAGTQFKNSVAVLMKNLYSKNPNYIRCIKPNDQQQKGRFTSEMVMVQARYLGLLENVRVRRAGYAFRQGYKPFLERYRLLSRSTWPRWNGDDREGVEKVLGSLTLSSEELAYGKTKIFIRSPKTLFYLEEQRRLRLQQLATLIQKVYRGWRCRTHYQQMRKSQILISAWFRGNKQKKHYGKIRSSVLLIQAFVRGWRARKNYRKYFRSGAALTLANFIYQSMAQKFLLNLKKNLPSTKVLDNTWPAAPYRCFNTANQELQRLFYQWKCKKFRDQLSPKQVQTLREKLCASELFKGKKASYPQSVPIPFRGDYIGLQGNPKLQRLKGREEGPVLVADTVKKVNRGNGKTSARILLLTKGHVILTDAKKSQAQIVIGLEDVAGVSVSSLQDGLFSLHLSEMSSAVSKGDILLVSDHVVELLTKMYQAVLDATQRQLSVTVTEKFSVRFKEGSVAVKVIQGPEGGGNRKLICKKKGSNAMEVTVR
| null | null |
actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; cell projection organization [GO:0030030]; endocytosis [GO:0006897]; microvillus assembly [GO:0030033]; regulation of protein localization [GO:0032880]; sensory perception of sound [GO:0007605]; vesicle localization [GO:0051648]; vesicle transport along actin filament [GO:0030050]
|
actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; brush border [GO:0005903]; cell leading edge [GO:0031252]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; filamentous actin [GO:0031941]; growth cone [GO:0030426]; lateral plasma membrane [GO:0016328]; microvillus [GO:0005902]; myosin complex [GO:0016459]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; vesicle [GO:0031982]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]
|
PF00612;PF00063;PF06017;
|
1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
|
PTM: Phosphorylated by ALPK1. {ECO:0000250|UniProtKB:Q9UBC5}.
| null | null | null | null | null | null |
FUNCTION: Involved in directing the movement of organelles along actin filaments. {ECO:0000305}.
|
Mus musculus (Mouse)
|
O88335
|
KCNJ1_MOUSE
|
MFKHLRRWFVTHIFGRSRQRARLVSKDGRCNIEFGNVDAQSRFIFFVDIWTTVLDLKWRYKMTVFITAFLGSWFLFGLLWYVVAYVHKDLPEFYPPDNRTPCVENINGMTSAFLFSLETQVTIGYGFRFVTEQCATAIFLLIFQSILGVIINSFMCGAILAKISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTITPEGETIILDQTNINFVVDAGNENLFFISPLTIYHIIDHNSPFFHMAAETLSQQDFELVVFLDGTVESTSATCQVRTSYIPEEVLWGYRFVPIVSKTKEGKYRVDFHNFGKTVEVETPHCAMCLYNEKDARARMKRGYDNPNFVLSEVDETDDTQM
| null | null |
cellular response to magnesium ion [GO:0071286]; circulatory system development [GO:0072359]; gene expression [GO:0010467]; kidney development [GO:0001822]; negative regulation of apoptotic process [GO:0043066]; post-embryonic development [GO:0009791]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; regulation of monoatomic ion transmembrane transport [GO:0034765]; renal sodium ion absorption [GO:0070294]; tissue homeostasis [GO:0001894]
|
monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP-activated inward rectifier potassium channel activity [GO:0015272]; inward rectifier potassium channel activity [GO:0005242]; peptide binding [GO:0042277]; potassium ion binding [GO:0030955]
|
PF01007;PF17655;
|
1.10.287.70;2.60.40.1400;
|
Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ1 subfamily
|
PTM: Phosphorylation at Ser-25 by SGK1 is necessary for its expression at the cell membrane. {ECO:0000250|UniProtKB:P48048}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48048}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48048}. Note=Phosphorylation at Ser-44 by SGK1 is necessary for its expression at the cell membrane. {ECO:0000250|UniProtKB:P48048}.
| null | null | null | null | null |
FUNCTION: In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium (By similarity). {ECO:0000250|UniProtKB:P48048}.
|
Mus musculus (Mouse)
|
O88338
|
CAD16_MOUSE
|
MISARPWLLYLSVIQAFTTEAQPAESLHTEVPENYGGNFPFYILKLPLPLGRDEGHIVLSGDSNTADQNTFAVDTDSGFLVATRTLDREEKAEYQLQVTLESEDGRILWGPQLVTVHVKDENDQVPQFSQAIYRAQLSQGTRPGVPFLFLEASDGDAPGTANSDLRFHILSQSPPQPLPDMFQLDPHLGALALSPSGSTSLDHALEETYQLLVQVKDMGDQPSGHQAIATVEISIVENSWAPLEPVHLAENLKVVYPHSIAQVHWSGGDVHYQLESQPPGPFDVDTEGMLHVTMELDREAQAEYQLQVRAQNSHGEDYAEPLELQVVVMDENDNAPVCSPHDPTVNIPELSPPGTEIARLSAEDLDAPGSPNSHIVYQLLSPEPEEGAENKAFELDPTSGSVTLGTAPLHAGQSILLQVLAVDLAGSESGLSSTCEVTVMVTDVNNHAPEFINSQIGPVTLPEDVKPGALVATLMATDADLEPAFRLMDFAIEEGDPEGIFDLSWEPDSDHVQLRLRKNLSYEAAPDHKVVVVVSNIEELVGPGPGPAATATVTILVERVVAPLKLDQESYETSIPVSTPAGSLLLTIQPSDPMSRTLRFSLVNDSEGWLCIKEVSGEVHTAQSLQGAQPGDTYTVLVEAQDTDKPGLSTSATVVIHFLKASPVPALTLSAGPSRHLCTPRQDYGVVVSGVSEDPDLANRNGPYSFALGPNPTVQRDWRLQPLNDSHAYLTLALHWVEPGEYMVPVVVHHDTHMWQLQVKVIVCRCNVEGQCMRKVGRMKGMPTKLSAVGVLLGTLAAIGFILILVFTHLALARKDLDQPADSVPLKAAV
| null | null |
adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; cell morphogenesis [GO:0000902]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]
|
adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; catenin complex [GO:0016342]; plasma membrane [GO:0005886]
|
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]
|
PF00028;
|
2.60.40.60;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
|
Mus musculus (Mouse)
|
O88339
|
EPN1_RAT
|
MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
| null | null |
clathrin coat assembly [GO:0048268]; embryonic organ development [GO:0048568]; endocytosis [GO:0006897]; female pregnancy [GO:0007565]; in utero embryonic development [GO:0001701]; membrane fission [GO:0090148]; negative regulation of sprouting angiogenesis [GO:1903671]; Notch signaling pathway [GO:0007219]; positive regulation of clathrin coat assembly [GO:1905445]
|
clathrin vesicle coat [GO:0030125]; clathrin-coated pit [GO:0005905]; cytosol [GO:0005829]; endosome [GO:0005768]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic membrane [GO:0045211]; presynapse [GO:0098793]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; terminal bouton [GO:0043195]
|
clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; molecular sequestering activity [GO:0140313]; phospholipid binding [GO:0005543]; transmembrane transporter binding [GO:0044325]
|
PF01417;
|
1.25.40.90;
|
Epsin family
|
PTM: Ubiquitinated. {ECO:0000269|PubMed:11919637}.; PTM: Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. {ECO:0000269|PubMed:9920862}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145.
| null | null | null | null | null |
FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:11161217). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (PubMed:12353027, PubMed:9723620). Regulates receptor-mediated endocytosis (By similarity). {ECO:0000250|UniProtKB:Q9Y6I3, ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:12353027, ECO:0000269|PubMed:9723620}.
|
Rattus norvegicus (Rat)
|
O88342
|
WDR1_MOUSE
|
MPYEIKKVFASLPQVERGVSKILGGDPKGDHFLYTNGKCVILRNIDNPAIADIYTEHAHQVVVAKYAPSGFYIASGDISGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDTGSSVGEITGHNKVINSVDIKQTRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIFIYDGKTGEKVCALGESKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVNVNSVVSTFPMGSNVLDQQLGCLWQKDHLLSISLSGYINYLDKNNPSKPLRVIKGHSKSIQCLTVHRNGGKSYIYSGSHDGHINYWDSETGENDSFSGKGHTNQVSRMTVNESEQLVSCSMDDTVRYTNLTLRDYSGQGVVKLDVQPKCVAVGPGGYTVVVCIGQIVLLKDQKKCFSIDNPGYEPEVVAVHPGGDTVAVGGTDGNVRVYSILASTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETKVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament depolymerization [GO:0030042]; actin filament fragmentation [GO:0030043]; apical junction assembly [GO:0043297]; cortical cytoskeleton organization [GO:0030865]; establishment of planar polarity of follicular epithelium [GO:0042247]; locomotion [GO:0040011]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; neutrophil mediated immunity [GO:0002446]; neutrophil migration [GO:1990266]; platelet formation [GO:0030220]; positive regulation of actin filament depolymerization [GO:0030836]; regulation of cell shape [GO:0008360]; regulation of oligodendrocyte differentiation [GO:0048713]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; sarcomere organization [GO:0045214]; sensory perception of sound [GO:0007605]
|
actin cytoskeleton [GO:0015629]; cell projection [GO:0042995]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; podosome [GO:0002102]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]
|
PF00400;
|
2.130.10.10;
|
WD repeat AIP1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5RKI0}. Cell projection, podosome {ECO:0000250|UniProtKB:O75083}.
| null | null | null | null | null |
FUNCTION: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins (By similarity). Enhances cofilin-mediated actin severing (PubMed:25915128). Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions (By similarity). Involved in myocardium sarcomere organization. Required for cardiomyocyte growth at the postnatal and maintenance at the adult stage (PubMed:24840128). Involved in neutrophil actin dynamics and migration. Involved in megakaryocyte maturation and platelet shedding (PubMed:17515402). Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP; the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension (PubMed:25915128). Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt (By similarity). {ECO:0000250|UniProtKB:O75083, ECO:0000250|UniProtKB:Q9W7F2, ECO:0000269|PubMed:24840128, ECO:0000269|PubMed:25915128}.
|
Mus musculus (Mouse)
|
O88343
|
S4A4_MOUSE
|
MEDEAVLDRGASFLKHVCDEEEVEGHHTIYIGVHVPKSYRRRRRHKRKAGHKEKKEKERISENYSDKSDVENADESSSSILKPLISPAAERIRFILGEEDDSPAPPQLFTELDELLAVDGQEMEWKETARWIKFEEKVEQGGERWSKPHVATLSLHSLFELRTCMEKGSIMLDREASSLPQLVEMIADHQIETGLLKPDLKDKVTYTLLRKHRHQTKKSNLRSLADIGKTVSSASRMFSNPDNGSPAMTHRNLTSSSLNDISDKPEKDQLKNKFMKKLPRDAEASNVLVGEVDFLDTPFIAFVRLQQAVMLGALTEVPVPTRFLFILLGPKGKAKSYHEIGRAIATLMSDEVFHDIAYKAKDRHDLIAGIDEFLDEVIVLPPGEWDPTIRIEPPKSLPSSDKRKNMYSGGENVQMNGDTPHDGGHGGGGHGDCEELQRTGRFCGGLIKDIKRKAPFFASDFYDALNIQALSAILFIYLATVTNAITFGGLLGDATDNMQGVLESFLGTAVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFDYLEFRLWIGLWSAFMCLVLVATDASFLVQYFTRFTEEGFSSLISFIFIYDAFKKMIKLADYYPINSDFKVGYNTHFSCACLPPDPVNLSVSNDTTLAPEDLPTISSTDMYHNVTFDWAYLSKKECVKYGGKLVGNNCDFVPDITLMSFILFLGTYTSSMAMKKFKTSRYFPTTARKLISDFAIILSILIFCVIDALVGVDTPKLIVPSEFKPTSPNRGWFVPPFGGNPWWVCLAAAIPALLVTILIFMDQQITAVIVNRKEHKLKKGAGYHLDLFWVAILMVVCSFMALPWYVAATVISIAHIDSLKMETETSAPGEQPKFLGVREQRVTGTLVFILTGLSVFMAPILKFIPMPVLYGVFLYMGVASLNGVQFMDRLKLLLMPLKHQPDFIYLRHVPLRRVHLFTFLQVLCLALLWILKSTVAAIIFPVMILALVAVRKGMDYLFSQHDLSFLDDVIPEKDKKKKEDEKKKKKKKGSLDSDNDDSDCPYSEKVPSIKIPMDIMEQQPFLSDNKPLDRERSSTFLERHTSC
| null | null |
bicarbonate transport [GO:0015701]; establishment of localization in cell [GO:0051649]; positive regulation of glycolytic process [GO:0045821]; regulation of intracellular pH [GO:0051453]; regulation of membrane potential [GO:0042391]; regulation of pH [GO:0006885]; sodium ion transport [GO:0006814]; transmembrane transport [GO:0055085]
|
basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
monoatomic anion transmembrane transporter activity [GO:0008509]; sodium:bicarbonate symporter activity [GO:0008510]; solute:inorganic anion antiporter activity [GO:0005452]
|
PF07565;PF00955;
|
1.10.287.570;
|
Anion exchanger (TC 2.A.31) family
|
PTM: Phosphorylation of Ser-1026 by PKA increases the binding of CA2 and changes the Na(+):HCO3(-) stoichiometry of the transporter from 3:1 to 2:1. Phosphorylated in presence of STK39 and dephosphorylated in presence of PP1 phosphatase; phosphorylation seems to inhibit SLC4A4 activity (PubMed:21317537). {ECO:0000250|UniProtKB:Q9Y6R1, ECO:0000269|PubMed:21317537}.; PTM: N-glycosylated. May not be necessary for the transporter basic functions. {ECO:0000269|PubMed:12604466}.
|
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:11171615}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21317537}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Na(+)(out) = 2 hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72215, ChEBI:CHEBI:17544, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:12388213, ECO:0000269|PubMed:19033647}; CATALYTIC ACTIVITY: Reaction=3 hydrogencarbonate(out) + Na(+)(out) = 3 hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72219, ChEBI:CHEBI:17544, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:12388213, ECO:0000269|PubMed:19033647}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=2 hydrogencarbonate(out) + Na(+)(out) = 2 hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72215, ChEBI:CHEBI:17544, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:11171615}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=3 hydrogencarbonate(out) + Na(+)(out) = 3 hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72219, ChEBI:CHEBI:17544, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:11171615};
| null | null | null | null |
FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH. {ECO:0000269|PubMed:11171615, ECO:0000269|PubMed:12388213, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:9651366}.
|
Mus musculus (Mouse)
|
O88351
|
IKKB_MOUSE
|
MSWSPSLPTQTCGAWEMKERLGTGGFGNVIRWHNQATGEQIAIKQCRQELSPKNRNRWCLEIQIMRRLNHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRRYLNQFENCCGLREGAVLTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEKRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGAVKFSSSLPFPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPQYGPNGCFRALDDILNLKLVHVLNMVTGTVHTYPVTEDESLQSLKTRIQENTGILETDQELLQKAGLVLLPDKPATQCISDSKTNEGLTLDMDLVFLLDNSKINYETQITPRPPPESVSCILQEPKRNLSFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMSLLRNNSCLSKMKNAMASTAQQLKAKLDFFKTSIQIDLEKYKEQTEFGITSDKLLLAWREMEQAVEQCGRENDVKHLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRKLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDERTVVRLQEKRQKELWNLLKIACSKVRGPVSGSPDSMNVSRLSHPGQLMSQPSSACDSLPESDKKSEELVAEAHALCSRLESALQDTVKEQDRSFTTLDWSWLQMEDEERCSLEQACD
|
2.7.11.1; 2.7.11.10
| null |
B cell homeostasis [GO:0001782]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to tumor necrosis factor [GO:0071356]; neuron projection development [GO:0031175]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of neuron projection development [GO:0010976]; positive regulation of sodium ion transport [GO:0010765]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to cholecystokinin [GO:0061847]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; IkappaB kinase complex [GO:0008385]; membrane raft [GO:0045121]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; IkappaB kinase activity [GO:0008384]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein phosphatase binding [GO:0019903]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]
|
PF18397;PF12179;PF00069;
|
1.20.1270.250;6.10.250.2110;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, I-kappa-B kinase subfamily
|
PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity. Phosphorylated by MAP3K7/TAK1 in response to NOD1 and NOD2 signaling, promoting activation and phosphorylation of NF-kappa-B inhibitors, leading to NF-kappa-B activation. Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response. Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription. Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B. {ECO:0000250|UniProtKB:O14920}.; PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may not serve as a monoubiquitination site. Ubiquitination on 'Ser-163' may modulate phosphorylation on C-terminal serine residues. {ECO:0000250|UniProtKB:O14920}.; PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappa-B. {ECO:0000250|UniProtKB:O14920}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14920}. Nucleus {ECO:0000250|UniProtKB:O14920}. Membrane raft {ECO:0000250|UniProtKB:O14920}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:O14920}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.10; Evidence={ECO:0000250|UniProtKB:O14920}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:25326420, ECO:0000269|PubMed:30988283}; 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:0000305};
| null | null | null | null |
FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (By similarity). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (By similarity). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (By similarity). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (By similarity). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (By similarity). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (By similarity). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (By similarity). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (By similarity). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (By similarity). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (PubMed:30988283). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326420). {ECO:0000250|UniProtKB:O14920, ECO:0000269|PubMed:25326420, ECO:0000269|PubMed:30988283}.
|
Mus musculus (Mouse)
|
O88354
|
LIPP_ICTTR
|
MLLVWSLALLLGAVAGKEVCYDRLGCFSDDSPWSGIVERPLKVLPWSPADVNTRFLLYTNENQDNYQQITADSSRIQSSNFKTNRKTRFIIHGFIDKGEESWLANMCKKMFQVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVDFLRTQLGYSPSNVHVIGHSLGSHAAGEAGRRTNGAIGRITGLDPAEPCFEGTPELVRLDPSDAQFVDAIHTDGAPIVPNLGFGMSQTVGHLDFFPNGGIEMPGCQKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPTGFAAFSCASYSVFSANKCFPCPSGGCPQMGHYADRYSGKTNGVGQKFYLNTGDKSNFSRWRYKVSVTLSGQKVTGHILVSLFGNAGNSKQYEIYKGSLHPGYTHSNEFDSDVDVGDLQRVKFIWYNNVINPSLPRVGASSISVERNDGRVFKFCSAETVREDVLLTLNAC
|
3.1.1.3
| null |
hibernation [GO:0042750]; lipid catabolic process [GO:0016042]
|
extracellular space [GO:0005615]
|
all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806]
|
PF00151;PF01477;
|
3.40.50.1820;2.60.60.20;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}.
|
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456; Evidence={ECO:0000250|UniProtKB:P16233};
| null | null | null | null |
FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones (By similarity). Plays a role in hibernation as a key enzyme that shows high activity at low temperatures. When expressed in the hibernating heart it liberates fatty acids from triglycerides at temperatures as low as 0 degrees Celsius. {ECO:0000250|UniProtKB:P16233, ECO:0000269|PubMed:9653197}.
|
Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus tridecemlineatus)
|
O88368
|
MITF_RAT
|
MQSESGIVADFEVGEEFHEEPKTYYELKSQPLKSSSSAEHSGASKPPLSSSTMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVAVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRHQVKQYLSTTLANKHAGQVLSPPCPNQPGDHAMPPVPGSSAPNSPMAMLTLNSNCEKEAFYKFEEQSRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYSNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQRAKDLENRQKKLEHANRHLLLRVQELEMQARAHGLSLIPSTGLCSPDLVNRIIKQEPVLENCSQELVQHQADLTCTTTLDLTDGTISFTNNLGTMPESSPAYSIPRKMASNLEDILMDDALSPVGVTDPLLSSVSPGASKTSSRRSSMSAEETEHAC
| null | null |
bone remodeling [GO:0046849]; camera-type eye development [GO:0043010]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cellular response to zinc ion starvation [GO:0034224]; DNA-templated transcription [GO:0006351]; melanocyte apoptotic process [GO:1902362]; melanocyte differentiation [GO:0030318]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell migration [GO:0030336]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoclast differentiation [GO:0030316]; pigmentation [GO:0043473]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of DNA-templated transcription initiation [GO:2000144]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-containing complex assembly [GO:0065003]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; regulation of osteoclast differentiation [GO:0045670]; regulation of RNA biosynthetic process [GO:2001141]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ethanol [GO:0045471]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; lysosomal membrane [GO:0005765]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
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]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF11851;PF00010;PF15951;
|
4.10.280.10;
|
MiT/TFE family
|
PTM: Phosphorylation at Ser-405 significantly enhances the ability to bind the tyrosinase promoter (By similarity). Phosphorylated at Ser-180 and Ser-516 following KIT signaling, triggering a short live activation: Phosphorylation at Ser-180 and Ser-516 by MAPK and RPS6KA1, respectively, activate the transcription factor activity but also promote ubiquitination and subsequent degradation by the proteasome (By similarity). Phosphorylated in response to blue light (415nm) (By similarity). {ECO:0000250|UniProtKB:O75030}.; PTM: Ubiquitinated following phosphorylation at Ser-180, leading to subsequent degradation by the proteasome. Deubiquitinated by USP13, preventing its degradation. {ECO:0000250|UniProtKB:O75030}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75030}. Cytoplasm {ECO:0000250|UniProtKB:O75030}. Note=Found exclusively in the nucleus upon phosphorylation. {ECO:0000250|UniProtKB:O75030}.
| null | null | null | null | null |
FUNCTION: Transcription factor that regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium. {ECO:0000250|UniProtKB:O75030}.
|
Rattus norvegicus (Rat)
|
O88370
|
PI42C_RAT
|
MASSSVPPATAPAAAGGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEGPVREEESEWDGDCNLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAEGAPEGGVFHGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFISNIFA
|
2.7.1.149
| null |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process [GO:1902635]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; positive regulation of autophagosome assembly [GO:2000786]; regulation of autophagy [GO:0010506]
|
autophagosome [GO:0005776]; endoplasmic reticulum [GO:0005783]; intracellular organelle [GO:0043229]; plasma membrane [GO:0005886]
|
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]
|
PF01504;
|
3.30.810.10;3.30.800.10;
| null |
PTM: Phosphorylated, phosphorylation is induced by EGF. {ECO:0000269|PubMed:9685379}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:9685379}. Cytoplasm {ECO:0000269|PubMed:9685379}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149; Evidence={ECO:0000269|PubMed:9685379}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281; Evidence={ECO:0000305|PubMed:9685379}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55992, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q8TBX8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55993; Evidence={ECO:0000250|UniProtKB:Q8TBX8}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + GDP + H(+); Xref=Rhea:RHEA:55964, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:Q8TBX8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55965; Evidence={ECO:0000250|UniProtKB:Q8TBX8};
| null | null | null | null |
FUNCTION: Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic activity (PubMed:9685379). May be a GTP sensor, has higher GTP-dependent kinase activity than ATP-dependent kinase activity (By similarity). PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity). {ECO:0000250|UniProtKB:Q8TBX8, ECO:0000269|PubMed:9685379}.
|
Rattus norvegicus (Rat)
|
O88377
|
PI42B_RAT
|
MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLRVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEETEVEDRAEEEECENDGVGGGLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESAPKKEVYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT
|
2.7.1.149
| null |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process [GO:1902635]; autophagosome-lysosome fusion [GO:0061909]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; positive regulation of autophagosome assembly [GO:2000786]; regulation of autophagy [GO:0010506]
|
autophagosome [GO:0005776]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; protein homodimerization activity [GO:0042803]
|
PF01504;
|
3.30.810.10;3.30.800.10;
| null |
PTM: Ubiquitinated by the SPOP/CUL3 complex. Ubiquitination is stimulated by PtdIns5P levels. {ECO:0000250|UniProtKB:P78356}.; PTM: Phosphorylated on serine residues. {ECO:0000250|UniProtKB:P78356}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Associated with the plasma membrane and the endoplasmic reticulum. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149; Evidence={ECO:0000269|PubMed:9685379}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281; Evidence={ECO:0000305|PubMed:9685379}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55992, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P78356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55993; Evidence={ECO:0000250|UniProtKB:P78356}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + GDP + H(+); Xref=Rhea:RHEA:55964, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:P78356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55965; Evidence={ECO:0000250|UniProtKB:P78356};
| null | null | null | null |
FUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate (PubMed:9685379). Preferentially utilizes GTP, rather than ATP, for PI(5)P phosphorylation and its activity reflects changes in direct proportion to the physiological GTP concentration. Its GTP-sensing activity is critical for metabolic adaptation (By similarity). PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity). {ECO:0000250|UniProtKB:P78356, ECO:0000269|PubMed:9685379}.
|
Rattus norvegicus (Rat)
|
O88379
|
BAZ1A_MOUSE
|
MPLLHRKPFVRQKPPGDLRPDEEVFYCKVTNEIFRHYDDFFERTILCNSLVWSCAVTGRPGLTYQEALESERKARQNLQSFPEPLIIPVLYLTNLTRRSRLHEICDDIFAYVKDRYFVEETVEVIRNNGTRLQCRILEVLPPLHQNGFANGHLSSADGETIVISDSDDSETQSSSFHHGKKKDAIDPLLFRYRVQPTKKEMYESAVVKATQISRRKHLFSRDKLKLFLKQHCEAQDGVIKIKASSFSAYNIAEQDFSYFFPDDPPTFIFSPANRRRGRPPKRISFGQEDSIASKQTAARYRNKAIKERDKLLKQEEMRALAFEKAKLKRERADALEARKREKEDKEKKREELKKMVEEERLKKKEEKERLKIEREKEREKLREEKRKYMEYLKQWSKPREDMECDDLKELPEPTPVKTRLPPEVFGDALMVLEFLNAFGELFDLQDEFPEGVTLAEVLEEALVGNDSEGPLCELLFFFLTAIFQAMAEEEEEVAKEQITDADTKDLTEALDEDADPTKSALSAVAALAAAWPQLHQGCSLKSLDLDSCTLSEILRLHILASGADVTSANAKYRYQKRGGFDATDDACMELRLSNPSLVKKLSSTSVYDLTPGEKMKILHALCGKLLTLVSTRDFIEDYVDVLRQAKQEFRELKAEQHRKEREATAARIRRRKEEKLKEQEQKMKEKQEKLKEDEQRNSAAVPGYGEEEREDFDTSTENKNIEQKDLDPDVVTEDEDDPGSHKRSRRGKVGQTAVKQCIKQEEMNYCIKQEPLSADAEEALRQEQQQKEKELLDKIQSAIACTNIFPLGRDRLYRRYWIFPSIPGLFIEEDYSGLTEDMLLPRPSSFHNNAQPRDPQVSIKTEESFLSESTSSLDQGPFDDSVLLPKPVHKPNRWCFYSSCAQLDQLIDALNSRGHRESALKETLLQEKSRICAQLAHFSEEKFHFSDKPQADSKPVSSRGRSSGACDISQMSAERQLELRLRDFLLDIEDRIYQGTLGAIKVTDRQVWRSALENGRYELLSEESKENGVIKTVNEDVEEMEMEQARVIVRDRLLGIKTETPSTISTSASTPQSVSNVVHYLALALFQIEQGIERRFLKAPLDGNDSGRSYKTVLDRWRESLLSSASLSQVFLHLSTLDRSVMWSKSILNARCKICRKKGDAENMVLCDGCDRGHHTYCVRPKLKAVPDGDWFCPECRPKQRSRRLSSRQRPSLESDEEMEEGMEDDDDEVDDDDEEGQSEEEEYEVEQDEEDSDDDEALSPPKRGRPQVRLPIKTKGRFGPSFPSRSQRQDPGRYPSRSQQSTPKNTAKSASKNLRKTRSAPPTETRSLRVGSRSTRHSPSALQDVFVELLSPHSKRRGRKGADHTPEHSPSFTNFRVSTSRSSRQLIPLNTAESLSLQHSESKRRGRKRQSTESSPVPLNRRSSGRQGGVHELSAFEQLVVELVRHDDSWPFLKLVSKIQVPDYYDIIKKPIALNIIREKVNKCEYKLASEFIDDIELMFSNCFEYNPRNTSEAKAGTRLQAFFHIQAQKLGLHVSPSTVDQVSTPLAAKKSRI
| null | null |
chromatin remodeling [GO:0006338]; nucleosome assembly [GO:0006334]; positive regulation of DNA replication [GO:0045740]; regulation of DNA replication [GO:0006275]; regulation of DNA-templated transcription [GO:0006355]; regulation of heterochromatin formation [GO:0031445]
|
ACF complex [GO:0016590]; CHRAC [GO:0008623]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]
|
PF00439;PF02791;PF00628;PF10537;PF15612;PF15613;
|
1.20.920.10;3.30.40.10;
|
WAL family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12434153}. Note=Localizes to pericentric heterochromatin (PubMed:12434153). May target the CHRAC complex to heterochromatin (By similarity). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9NRL2, ECO:0000269|PubMed:12434153}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the ATP-dependent ACF-1 and ACF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and slide edge- and center-positioned histone octamers away from their original location on the DNA template to facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (By similarity). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template in an ATP-dependent manner (By similarity). The ACF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the ACF-5 ISWI chromatin remodeling complex (By similarity). Has a role in sensing the length of DNA which flank nucleosomes, which modulates the nucleosome spacing activity of the ACF-5 ISWI chromatin remodeling complex (By similarity). Involved in DNA replication and together with SMARCA5/SNF2H is required for replication of pericentric heterochromatin in S-phase (By similarity). May have a role in nuclear receptor-mediated transcription repression (By similarity). {ECO:0000250|UniProtKB:Q9NRL2}.
|
Mus musculus (Mouse)
|
O88382
|
MAGI2_RAT
|
MSKSLKKKSHWTSKVHESVIGRNPEGQLGFELKGGAENGQFPYLGEVKPGKVAYESGSKLVSEELLLEVNETPVAGLTIRDVLAVIKHCKDPLRLKCVKQGGIVDKDLRHYLNLRFQKGSVDHELQQIIRDNLYLRTVPCTTRPHKEGEVPGVDYIFITVEDFMELEKSGALLESGTYEDNYYGTPKPPAEPAPLLLNVTDQILPGATPSAEGKRKRNKSVTNMEKASIEPPEEEEEERPVVNGNGVVITPESSEHEDKSAGASGETPSQPYPAPVYSQPEELKDQMDDTKSTKPEENEDSDPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRLAKKAKPAEECKENELPYGWEKIDDPIYGTYYVDHINRRTQFENPVLEAKRKLQQHNMPHTELGTKPLQAPGFREKPLFTRDASQLKGTFLSTTLKKSNMGFGFTIIGGDEPDEFLQVKSVIPDGPAAQDGKMETGDVIVYINEVCVLGHTHADVVKLFQSVPIGQSVNLVLCRGYPLPFDPEDPANSMVPPLAIMERPPPVMVNGRHNYETYLEYISRTSQSVPDITDRPPHSLHSMPADGQLDGTYPPPVHDDNVSVASSGATQAELMTLTIVKGAKGFGFTIADSPTGQRVKQILDIQGCPGLCEGDLIVEINQQNVQNLSHTEVVDILKDCPVGSETSLIIHRGGFFSPWKTPKPMVDRWENQGSPQTSLSAPAVPQSLPFPPALHRSSFPDSTEAFDPRKPDPYELYEKSRAIYESRQQVPPRTSFRMDSSGPDYKELDVHLRRMESGFGFRILGGDEPGQPILIGAVIAMGSADRDGRLHPGDELVYVDGIPVAGKTHRYVIDLMHHAARNGQVNLTVRRKVLCGGEPCPENGRSPGSVSTHHSSPRSDYATYANSNHAAPSNNASPPEGFASHSLQTSDVIIHRKENEGFGFVIISSLNRPESGATITVPHKIGRIIDGSPADRCAKLKVGDRILAVNGQSIINMPHADIVKLIKDAGLSVTLRIIPQEELNNPTSAPSSEKQSPMAQQHSPLAQQHSPLAQPSPATPNSPVAQPAPPQPLQLQGHENSYRSEVKARQDVKPDIRQPPFTDYRQPPLDYRQPPGGDYSQPSPLDYRQHSPDTRQYPLSDYRQPQDFDYFTVDMEKGAKGFGFSIRGGREYKMDLYVLRLAEDGPAIRNGRMRVGDQIIEINGESTRDMTHARAIELIKSGGRRVRLLLKRGTGQVPEYGMVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGALPLPPPQACRK
| null | null |
cellular response to nerve growth factor stimulus [GO:1990090]; clathrin-dependent endocytosis [GO:0072583]; glomerular filtration [GO:0003094]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; nerve growth factor signaling pathway [GO:0038180]; neuroligin clustering involved in postsynaptic membrane assembly [GO:0097118]; podocyte development [GO:0072015]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of receptor internalization [GO:0002092]; positive regulation of synaptic vesicle clustering [GO:2000809]; receptor clustering [GO:0043113]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of synaptic membrane adhesion [GO:0099179]; signal transduction [GO:0007165]; SMAD protein signal transduction [GO:0060395]
|
bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extrinsic component of postsynaptic membrane [GO:0098890]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; late endosome [GO:0005770]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991]; slit diaphragm [GO:0036057]; synapse [GO:0045202]
|
activin receptor binding [GO:0070697]; beta-1 adrenergic receptor binding [GO:0031697]; kinesin binding [GO:0019894]; phosphatase binding [GO:0019902]; protein-containing complex binding [GO:0044877]; signaling receptor complex adaptor activity [GO:0030159]; SMAD binding [GO:0046332]; structural constituent of postsynaptic density [GO:0098919]; structural constituent of postsynaptic specialization [GO:0098879]; type II activin receptor binding [GO:0070699]
|
PF00625;PF16663;PF00595;PF00397;
|
2.20.70.10;2.30.42.10;3.30.63.10;
|
MAGUK family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Late endosome. Synapse, synaptosome. Cell membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9WVQ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9WVQ1}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q9WVQ1}. Note=Membrane-associated in synaptosomes. Localized diffusely in the cytoplasm before nerve growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation.
| null | null | null | null | null |
FUNCTION: Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins (PubMed:9694864). Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth (PubMed:17724123). May play a role in regulating activin-mediated signaling in neuronal cells (By similarity). Enhances the ability of PTEN to suppress AKT1 activation (By similarity). Plays a role in receptor-mediated clathrin-dependent endocytosis which is required for ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q86UL8, ECO:0000250|UniProtKB:Q9WVQ1, ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:9694864}.
|
Rattus norvegicus (Rat)
|
O88384
|
VTI1B_MOUSE
|
MAASAASSEHFEKLHEIFRGLLEDLQGVPERLLGTAGTEEKKKLVRDFDENQQEANETLAEMEEELRYAPLTFRNPMMSKLRNYRKDLAKLHREVRSTPLTAAPGGRGDLKYGTYTLENEHLNRLQSQRALLLQGTESLNRATQSIERSHRIATETDQIGTEIIEELGEQRDQLERTKSRLVNTNENLSKSRKILRSMSRKVITNKLLLSVIILLELAILVGLVYYKFFRHH
| null | null |
Golgi to vacuole transport [GO:0006896]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; macroautophagy [GO:0016236]; regulation of protein localization to plasma membrane [GO:1903076]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle fusion with Golgi apparatus [GO:0048280]
|
cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome membrane [GO:0055038]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]
|
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
|
PF05008;PF12352;
|
1.20.5.110;1.20.58.400;
|
VTI1 family
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9UEU0}. Lysosome membrane {ECO:0000250|UniProtKB:Q9UEU0}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9UEU0}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. {ECO:0000305|PubMed:15363411}.
|
Mus musculus (Mouse)
|
O88387
|
FGD4_RAT
|
MEESNPAPTSCASKGKHSKVSDLISHFEGGSVLSSYTDVQKDSTMNLNIPQTPRQHGLTSTTPQKLPSHKSPQKQEKDSDQNQGQHGCLANGVAAAQSQMECETEKEAALSPETDTQTAAASPDAHVLNGVRNETTTDSASSVTNSHDENACDSSCRTQGTDLGLPSKEGEPVIEAELQERENGLSTEGLNPLDQHHEVKETNEQKLHKIATELLLTERAYVSRLNLLDQVFYCKLLEEANRGSFPAEMVNKIFSNISSINAFHSKFLLPELEKRMQEWETTPRIGDILQKLAPFLKMYGEYVKGFDNAVELVKNMTERVPQFKSVTEEIQKQKICGSLTLQHHMLEPIQRIPRYEMLLKDYLKKLSPDAPDWNDAKKSLEIISTAASHSNSAIRKMENLKKLLEIYEMLGEEEDIVNPSNELIKEGQILKLAARNTSAQERYLFLFNNMLLYCVPRFSLVGSKFTVRTRVGIDGMKIVETHNEEYPHTFQVSGKERTLELQASSEQDKEEWIKALQESIDAFHQRHETFRNAIAKENDIPLEVSTAELGKRAPRWIRDNEVTMCMKCKESFNALTRRRHHCRACGHVVCWKCSDYKAQLEYDGGRLNKVCKDCYQIMSGFAESEEKKRRGILEIESAEVSGNSEVCSFLQYMEKSKPWQKIWCVIPKQDPLVLYMYGAPQDVRAQATIPLLGYIVDDMPKSADLPHSFKLTQSKSVHSFAADSEELKQKWLKIILLAVTGETPDGPSEHLDTLDNLPGPKEKSEC
| null | null |
cytoskeleton organization [GO:0007010]; filopodium assembly [GO:0046847]; lamellipodium assembly [GO:0030032]; microspike assembly [GO:0030035]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; regulation of cell shape [GO:0008360]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; filopodium [GO:0030175]; lamellipodium [GO:0030027]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]
|
PF01363;PF00169;PF00621;
|
1.20.900.10;2.30.29.30;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10464238}. Cell projection, filopodium {ECO:0000269|PubMed:10464238}. Note=Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers.
| null | null | null | null | null |
FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8. {ECO:0000269|PubMed:10464238, ECO:0000269|PubMed:9668039}.
|
Rattus norvegicus (Rat)
|
O88393
|
TGBR3_MOUSE
|
MAVTSHHMVPVFVLMSACLATAGPEPSTRCELSPISASHPVQALMESFTVLSGCASRGTTGLPREVHILNLRSTDQGLGQPQREVTLHLNPIASVHTHHKPVVFLLNSPQPLVWHVKTERLAAGVPRLFLVSEGSVVQFSSGNFSLTAETEERSFPQENEHLLHWAQKEYGAVTSFTELKIARNIYIKVGEDQVFPPTCNIGKNFLSLNYLAEYLQPKAAEGCVLASQPHEKEVHIIELISPNSNPYSTFQVDIIIDIRPAREDPEVVKNLVLILKCKKSVNWVIKSFDVKGNLKVIAPDSIGFGKESERSMTVTKLVRNDYPSTQENLMKWALDNGYSPVTSYTIAPVANRFHLRLENNEEMRDEEVHTIPPELRILLGPDHLPALDSPPFQGEIPNGGFPFPFPDIPRRGWKEGEDRIPRPKEPIIPRVQLLPDHREPEEVQGGVNIALSVKCDNEKMVVAVDKDSFQTNGYSGMELTLLDPSCKAKMNGTHFVLESPLNGCGTRHRRSAPDGVVYYNSIVVQAPSPGDSSGWPDGYEDLESGDNGFPGDTDEGETAPLSRAGVVVFNCSLRQLRSPSGFQDQLDGNATFNMELYNTDLFLVPSPGVFSVAENEHVYVEVSVTKADQDLGFAIQTCFISPYSNPDRMSDYTIIENICPKDDSVKFYSSKRVHFPIPHAEVDKKRFSFVFKSVFNTSLLFLHCELTLCSRNKGSQKLPKCVTPDDACTSLDATMIWTMMQNKKTFTKPLAVVLQVDYKENVPNMKESSPVPPPPQIFHGLDTLTVMGIAFAAFVIGALLTGALWYIYSHTGETARRQQVPTSPPASENSSAAHSIGSTQSTPCSSSSTA
| null | null |
apoptotic process involved in morphogenesis [GO:0060561]; blastocyst development [GO:0001824]; blood vessel development [GO:0001568]; blood vessel diameter maintenance [GO:0097746]; blood vessel remodeling [GO:0001974]; BMP signaling pathway [GO:0030509]; cardiac muscle cell proliferation [GO:0060038]; cell migration [GO:0016477]; cell population proliferation [GO:0008283]; collagen metabolic process [GO:0032963]; coronary vasculature development [GO:0060976]; coronary vasculature morphogenesis [GO:0060977]; definitive erythrocyte differentiation [GO:0060318]; definitive hemopoiesis [GO:0060216]; epicardial cell to mesenchymal cell transition [GO:0003347]; epicardium-derived cardiac fibroblast cell development [GO:0060939]; epithelial to mesenchymal transition [GO:0001837]; heart trabecula formation [GO:0060347]; heart trabecula morphogenesis [GO:0061384]; in utero embryonic development [GO:0001701]; liver development [GO:0001889]; muscular septum morphogenesis [GO:0003150]; negative regulation of apoptotic process involved in morphogenesis [GO:1902338]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of gene expression [GO:0010629]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; osteoblast differentiation [GO:0001649]; outflow tract morphogenesis [GO:0003151]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; protein-containing complex assembly [GO:0065003]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; roof of mouth development [GO:0060021]; secondary palate development [GO:0062009]; transforming growth factor beta receptor complex assembly [GO:0007181]; transforming growth factor beta receptor signaling pathway [GO:0007179]; vasculogenesis [GO:0001570]; vasculogenesis involved in coronary vascular morphogenesis [GO:0060979]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; ventricular compact myocardium morphogenesis [GO:0003223]; ventricular septum morphogenesis [GO:0060412]; visceral serous pericardium development [GO:0061032]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
activin binding [GO:0048185]; fibroblast growth factor binding [GO:0017134]; glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; PDZ domain binding [GO:0030165]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity [GO:0005024]; transforming growth factor beta receptor activity, type III [GO:0070123]; transforming growth factor beta receptor binding [GO:0005160]; type II transforming growth factor beta receptor binding [GO:0005114]
|
PF00100;
|
2.60.40.4100;2.60.40.3210;
| null |
PTM: Extensively modified by glycosaminoglycan (GAG), either chondroitin sulfate or heparan sulfate depending upon the tissue of origin.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26342}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:P26342}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P26342}. Note=Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix. {ECO:0000250|UniProtKB:P26342}.
| null | null | null | null | null |
FUNCTION: Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors (By similarity). In gonadotrope cells, acts as an inhibin A coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility (PubMed:30364975, PubMed:34910520). {ECO:0000250|UniProtKB:P26342, ECO:0000269|PubMed:30364975, ECO:0000269|PubMed:34910520}.
|
Mus musculus (Mouse)
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.