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Database: UniProt
Entry: A0A218U9E3_9PASE
LinkDB: A0A218U9E3_9PASE
Original site: A0A218U9E3_9PASE 
ID   A0A218U9E3_9PASE        Unreviewed;       453 AA.
AC   A0A218U9E3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   31-JUL-2019, entry version 8.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   Name=ACVR1B {ECO:0000313|EMBL:OWK50295.1};
GN   ORFNames=RLOC_00001576 {ECO:0000313|EMBL:OWK50295.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea;
OC   Estrildidae; Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK50295.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK50295.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK50295.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata
RT   domestica.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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|SAAS:SAAS01128404};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OWK50295.1}.
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DR   EMBL; MUZQ01000571; OWK50295.1; -; Genomic_DNA.
DR   Ensembl; ENSLSDT00000000993; ENSLSDP00000000854; ENSLSDG00000000687.
DR   Ensembl; ENSLSDT00000001005; ENSLSDP00000000864; ENSLSDG00000000687.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0048179; C:activin receptor complex; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0048185; F:activin binding; IEA:Ensembl.
DR   GO; GO:0016361; F:activin receptor activity, type I; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0034711; F:inhibin binding; IEA:Ensembl.
DR   GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:1901165; P:positive regulation of trophoblast cell migration; IEA:Ensembl.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
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:RU000304,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000197619};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:OWK50295.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00138186};
KW   Transferase {ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00138220,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00488859,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     75     97       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      125    154       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      155    445       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   453 AA;  51476 MW;  DEC3F331A7D457B5 CRC64;
     MVSVFNLDGV KHHVRTCIPE AKLIPAGKPF YCLSSEDLRN THCCYSDFCN KIDLMVPSGH
     LKDNEPPSSW GPVELVAVIA GPVFLVFVVM IIVVFVFHHH QRVYHNRQRL DMEDPSCEMC
     LSKDKTLQDL VYDLSTSGSG SGLPLFVQRT VARTIVLQEI IGKGRFGEVW RGRWRGGDVA
     VKIFSSREER SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD
     YLNRYTVTIE GMIKLALSAA SGLAHLHMEI VGTQGKPGIA HRDLKSKNIL VKKNGTCAIA
     DLGLAVRHDS VTDTIDIAPN QRVGTKRYMA PEVLDETINM KHFDSFKCAD IYALGLVYWE
     IARRCNAGGI HEEYQLPYYD LVPSDPSIEE MRKVVCDQKL RPNIPNWWQS YEALRVMGKM
     MRECWYANGA ARLTALRIKK TLSQLSVQED VKI
//
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