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Database: UniProt
Entry: A0A2K6LSH0_RHIBE
LinkDB: A0A2K6LSH0_RHIBE
Original site: A0A2K6LSH0_RHIBE 
ID   A0A2K6LSH0_RHIBE        Unreviewed;       506 AA.
AC   A0A2K6LSH0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN   Name=ACVR1B {ECO:0000313|Ensembl:ENSRBIP00000026481.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000026481.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000026481.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000026481.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|ARBA:ARBA00009605}.
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DR   AlphaFoldDB; A0A2K6LSH0; -.
DR   STRING; 61621.ENSRBIP00000026481; -.
DR   Ensembl; ENSRBIT00000050397.1; ENSRBIP00000026481.1; ENSRBIG00000037087.1.
DR   GeneTree; ENSGT00940000157032; -.
DR   Proteomes; UP000233180; Unplaced.
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-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl.
DR   GO; GO:0034711; F:inhibin binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase 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:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; 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: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:0006355; P:regulation of DNA-templated transcription; IEA:Ensembl.
DR   CDD; cd14143; STKc_TGFbR1_ACVR1b_ACVR1c; 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; 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; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF22; ACTIVIN RECEPTOR TYPE-1B; 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   Pfam; PF08515; TGF_beta_GS; 1.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        128..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          178..207
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          208..498
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   506 AA;  57328 MW;  4BD64E9608FBDE04 CRC64;
     MLSSCQASQF EEKVVPLISP LMSMSAPQFP TALLCACTSC LQANYTCETD GACMVSIFNL
     DGMEHHVRTC IPKVELVPAG KPFYCLSSED LRNTHCCYTD YCNRIDLRVP SGHLKEPEHP
     SMWGPVELVG IIAGPVFLLF LIIIIVFLVI NYHQRVYHNR QRLDMEDPSC EMCLSKDKTL
     QDLVYDLSTS GSGSGLPLFV QRTVARTIVL QEIIGKGRFG EVWRGRWRGG DVAVKIFSSR
     EERSWFREAE IYQTVMLRHE NILGFIAADN KDNGTWTQLW LVSDYHEHGS LFDYLNRYTV
     TIEGMIKLAL SAASGLAHLH MEIVGTQGKP GIAHRDLKSK NILVKKNGMC AIADLGLAVR
     HDAVTDTIDI APNQRVGTKR YMAPEVLDET INMKHFDSFK CADIYALGLV YWEIARRCNS
     GGVHEEYQLP YYDLVPSDPS IEEMRKVVCD QKLRPNIPNW WQSYEALRVM GKMMRECWYA
     NGAARLTALR IKKTLSQLSV QEDVKI
//
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