UniProt: A0A2Y9TAV5

Database: UniProt
Entry: A0A2Y9TAV5_PHYMC

LinkDB:  A0A2Y9TAV5_PHYMC 
Original site:  A0A2Y9TAV5_PHYMC

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Ontology (14)   
   GO (14)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG GENES (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (2)   
All databases (30)   

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ID   A0A2Y9TAV5_PHYMC        Unreviewed;       512 AA.
AC   A0A2Y9TAV5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   Name=ACVR2B {ECO:0000313|RefSeq:XP_023988026.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023988026.1};
RN   [1] {ECO:0000313|RefSeq:XP_023988026.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023988026.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC         seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC         Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30; Evidence={ECO:0000256|ARBA:ARBA00023945};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC         L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC         COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|ARBA:ARBA00023948,
CC         ECO:0000256|RuleBase:RU361271};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}.
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DR   RefSeq; XP_023988026.1; XM_024132258.3.
DR   AlphaFoldDB; A0A2Y9TAV5; -.
DR   STRING; 9755.ENSPCTP00005029848; -.
DR   Ensembl; ENSPCTT00005032813; ENSPCTP00005029848; ENSPCTG00005021275.
DR   KEGG; pcad:102991507; -.
DR   Proteomes; UP000248484; Chromosome 18.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0016362; F:activin receptor activity, type II; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR   CDD; cd14140; STKc_ACVR2b; 1.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF70; ACTIVIN RECEPTOR TYPE-2B; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361271};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Kinase {ECO:0000256|RuleBase:RU361271};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|RuleBase:RU361271};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361271};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU361271};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU361271};
KW   Transmembrane {ECO:0000256|RuleBase:RU361271};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361271}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..512
FT                   /note="Serine/threonine-protein kinase receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015856939"
FT   TRANSMEM        138..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361271"
FT   DOMAIN          190..480
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   512 AA;  57666 MW;  B367E92E09E64837 CRC64;
     MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY
     ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG
     GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP
     PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK
     HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
     LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG
     TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ
     HPSLEELQEV VVHKKMRPAI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL
     IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI
//

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