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Database: UniProt
Entry: A0A2I3T727_PANTR
LinkDB: A0A2I3T727_PANTR
Original site: A0A2I3T727_PANTR 
ID   A0A2I3T727_PANTR        Unreviewed;       505 AA.
AC   A0A2I3T727;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   08-MAY-2019, entry version 7.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   Name=ACVR1 {ECO:0000313|Ensembl:ENSPTRP00000085031,
GN   ECO:0000313|VGNC:VGNC:56};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000085031, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000085031, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the
RT   human genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000085031}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2018) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
CC         phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
CC         COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|SAAS:SAAS01128400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-threonine + ATP = [receptor-
CC         protein]-O-phospho-L-threonine + ADP + H(+);
CC         Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-
CC         COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30; Evidence={ECO:0000256|RuleBase:RU361271,
CC         ECO:0000256|SAAS:SAAS01128404};
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|RuleBase:RU361271};
CC       Single-pass type I membrane protein
CC       {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|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00595019}.
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DR   EMBL; AACZ04058432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPTRT00000093045; ENSPTRP00000085031; ENSPTRG00000012555.
DR   VGNC; VGNC:56; ACVR1.
DR   GeneTree; ENSGT00940000160160; -.
DR   Proteomes; UP000002277; Chromosome 2B.
DR   GO; GO:0016021; C:integral component of 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:InterPro.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR003605; GS_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002277};
KW   Kinase {ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138139};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138203};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138186};
KW   Transferase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138220};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00488859}.
FT   TRANSMEM    120    142       Helical. {ECO:0000256|RuleBase:RU361271}.
FT   DOMAIN      174    203       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      204    498       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   505 AA;  56897 MW;  97720A2521F05DCA CRC64;
     ASRTWLFTFY PLFPSPLVET KPKVSPKLYM CVCEGLSCGN EDHCEGQQCF SSLSINDGFH
     VYQKGCFQVY EQGKMTCKTP PSPGQAVECC QGDWCNRNIT AQLPTKGKSF PGTQNFHLEV
     GLIILSVVFA VCLLACLLGV ALRKFKRRNQ ERLNPRDVEY GTIEGLITTN VGDSTLADLL
     DHSCTSGSGS GLPFLVQRTV ARQITLLECV GKGRYGEVWR GSWQGENVAV KIFSSRDEKS
     WFRETELYNT VMLRHENILG FIASDMTSRH SSTQLWLITH YHEMGSLYDY LQLTTLDTVS
     CLRIVLSIAS GLAHLHIEIF GTQGKPAIAH RDLKSKNILV KKNGQCCIAD LGLAVMHSQS
     TNQLDVGNNP RVGTKRYMAP EVLDETIQVD CFDSYKRVDI WAFGLVLWEV ARRMVSNGIV
     EDYKPPFYDV VPNDPSFEDM RKVVCVDQQR PNIPNRWFSD PTLTSLAKLM KECWYQNPSA
     RLTALRIKKT LTKIDNSLDK LKTDC
//
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