UniProt: A0A3B4H1S2

Database: UniProt
Entry: A0A3B4H1S2_9CICH

LinkDB:  A0A3B4H1S2_9CICH 
Original site:  A0A3B4H1S2_9CICH

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
All databases (20)   

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ID   A0A3B4H1S2_9CICH        Unreviewed;       521 AA.
AC   A0A3B4H1S2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   Name=ACVR2A {ECO:0000313|Ensembl:ENSPNYP00000029592.1};
GN   Synonyms=acvr2a {ECO:0000313|RefSeq:XP_005738721.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000029592.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000029592.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005738721.1}
RP   IDENTIFICATION.
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:ARBA00036790};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674;
CC         Evidence={ECO:0000256|ARBA:ARBA00036790};
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:ARBA00036287};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881;
CC         Evidence={ECO:0000256|ARBA:ARBA00036287};
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_005738721.1; XM_005738664.1.
DR   AlphaFoldDB; A0A3B4H1S2; -.
DR   STRING; 303518.ENSPNYP00000029592; -.
DR   Ensembl; ENSPNYT00000030309.1; ENSPNYP00000029592.1; ENSPNYG00000022291.1.
DR   GeneID; 102199573; -.
DR   CTD; 92; -.
DR   GeneTree; ENSGT00940000157233; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000261460; Unplaced.
DR   Proteomes; UP000695023; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF64; ACTIVIN RECEPTOR TYPE-2A; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00220; S_TKc; 1.
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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|RuleBase:RU361271};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000695023};
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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..521
FT                   /note="Serine/threonine-protein kinase receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041073921"
FT   TRANSMEM        148..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361271"
FT   DOMAIN          200..497
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   521 AA;  58673 MW;  740E5F6CF91E4BB6 CRC64;
     MGDATKLAFA VFLISCSSGA ILGRSETQEC AYYNSSWEKE RTNRSGIEPC YGEKDKRRHC
     FATWKNVSGT VEIVKQGCWL DDVNCYDSNE CVERKESPDV FFCCCEGNMC NERFLYAPEA
     PPQSDPHHST AYTTSNPFSQ KPQLFSTLLY SLVPIIGLAA VVLFSFWMWR HHKLAYPAAL
     VPTHDPGPSP PSPILGHKPL QLIEVKARGR FGCVWKAQLL NEYMAVKIFP IQDKLSWQNE
     YEIYSVSGMK HENILHFIGA EKRNNNLDLE LWLITAYHDK GSLTDYLKAN VVSWNELCHI
     AQSAARGLAY LHEDIPGHKD GHKPSIAHRD IKSKNVLLKN NLTACIADFG LALKFEAGKS
     AGDTHGQVGT RRYMAPEVLE GAINFQRDSF LRIDMYAFGL VLWELASRCT AADGPVDEYM
     LPFEEEVGQH PSLEDMQEVV VHKKLRPCLR DCWQKHTGLA MLCETIEDCW DHEAEARLSA
     GCVEERIGQM QRQAPVIGPE EIVTVVTMVT NVDLPPKESS L
//

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