ID   BMR1B_CHICK             Reviewed;         502 AA.
AC   Q05438;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Bone morphogenetic protein receptor type-1B;
DE            Short=BMP type-1B receptor;
DE            Short=BMPR-1B;
DE            EC=2.7.11.30 {ECO:0000250|UniProtKB:P36898};
DE   AltName: Full=Activin receptor-like kinase 6;
DE            Short=ALK-6;
DE   AltName: Full=RPK-1;
DE   AltName: Full=Serine/threonine-protein kinase receptor R6;
DE            Short=SKR6;
DE   Flags: Precursor;
GN   Name=BMPR1B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8400359; DOI=10.3109/10425179309020827;
RA   Yamazaki Y., Saito T., Nohno T.;
RT   "A new receptor protein kinase from chick embryo related to type II
RT   receptor for TGF-beta.";
RL   DNA Seq. 3:297-302(1993).
RN   [2]
RP   MUTAGENESIS OF ILE-200 AND ARG-486, AND FUNCTION.
RX   PubMed=14523231; DOI=10.1073/pnas.2133476100;
RA   Lehmann K., Seemann P., Stricker S., Sammar M., Meyer B., Suering K.,
RA   Majewski F., Tinschert S., Grzeschik K.-H., Mueller D., Knaus P.,
RA   Nuernberg P., Mundlos S.;
RT   "Mutations in bone morphogenetic protein receptor 1B cause brachydactyly
RT   type A2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=24129431; DOI=10.1038/ejhg.2013.222;
RA   Graul-Neumann L.M., Deichsel A., Wille U., Kakar N., Koll R., Bassir C.,
RA   Ahmad J., Cormier-Daire V., Mundlos S., Kubisch C., Borck G., Klopocki E.,
RA   Mueller T.D., Doelken S.C., Seemann P.;
RT   "Homozygous missense and nonsense mutations in BMPR1B cause acromesomelic
RT   chondrodysplasia-type Grebe.";
RL   Eur. J. Hum. Genet. 22:726-733(2014).
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting of two
CC       type II and two type I transmembrane serine/threonine kinases. Type II
CC       receptors phosphorylate and activate type I receptors which
CC       autophosphorylate, then bind and activate SMAD transcription (By
CC       similarity). Positively regulates chondrocyte differentiation
CC       (PubMed:24129431, PubMed:14523231). {ECO:0000250|UniProtKB:P36898,
CC       ECO:0000269|PubMed:24129431}.
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:0000250|UniProtKB:P36898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881;
CC         Evidence={ECO:0000250|UniProtKB:P36898};
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:0000250|UniProtKB:P36898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674;
CC         Evidence={ECO:0000250|UniProtKB:P36898};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36898};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P36898}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR   EMBL; D13432; BAA02694.1; -; mRNA.
DR   PIR; A56683; A56683.
DR   RefSeq; NP_990463.1; NM_205132.1.
DR   AlphaFoldDB; Q05438; -.
DR   SMR; Q05438; -.
DR   DIP; DIP-5822N; -.
DR   STRING; 9031.ENSGALP00000036862; -.
DR   GlyCosmos; Q05438; 1 site, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000019925; -.
DR   GeneID; 396030; -.
DR   KEGG; gga:396030; -.
DR   CTD; 658; -.
DR   VEuPathDB; HostDB:geneid_396030; -.
DR   eggNOG; KOG2052; Eukaryota.
DR   InParanoid; Q05438; -.
DR   PhylomeDB; Q05438; -.
DR   BRENDA; 2.7.10.2; 1306.
DR   PRO; PR:Q05438; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR   GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001502; P:cartilage condensation; NAS:UniProtKB.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0002063; P:chondrocyte development; IMP:AgBase.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR   GO; GO:0060350; P:endochondral bone morphogenesis; IMP:AgBase.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
DR   GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IMP:AgBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0061036; P:positive regulation of cartilage development; IMP:AgBase.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:AgBase.
DR   GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR   CDD; cd14219; STKc_BMPR1b; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF62; BONE MORPHOGENETIC PROTEIN 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; PF07714; PK_Tyr_Ser-Thr; 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   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Chondrogenesis; Disulfide bond; Glycoprotein;
KW   Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..502
FT                   /note="Bone morphogenetic protein receptor type-1B"
FT                   /id="PRO_0000024414"
FT   TOPO_DOM        14..126
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..502
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          174..203
FT                   /note="GS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT   DOMAIN          204..494
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         210..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..53
FT                   /evidence="ECO:0000250|UniProtKB:P36898"
FT   DISULFID        34..38
FT                   /evidence="ECO:0000250|UniProtKB:P36898"
FT   DISULFID        47..71
FT                   /evidence="ECO:0000250|UniProtKB:P36898"
FT   DISULFID        81..95
FT                   /evidence="ECO:0000250|UniProtKB:P36898"
FT   DISULFID        96..102
FT                   /evidence="ECO:0000250|UniProtKB:P36898"
FT   MUTAGEN         200
FT                   /note="I->K: Loss of positive regulation of chondrocyte
FT                   differentiation."
FT                   /evidence="ECO:0000269|PubMed:14523231"
FT   MUTAGEN         486
FT                   /note="R->W: Strongly decreases positive regulation of
FT                   chondrocyte differentiation."
FT                   /evidence="ECO:0000269|PubMed:14523231"
SQ   SEQUENCE   502 AA;  56766 MW;  D5D93CCEBF2A0680 CRC64;
     MPLLSSSKLS MESRKEDSEG TAPAPPQKKL SCQCHHHCPE DSVNSTCSTD GYCFTIIEED
     DSGGHLVTKG CLGLEGSDFQ CRDTPIPHQR RSIECCTGQD YCNKHLHPTL PPLKNRDFAE
     GNIHHKALLI SVTVCSILLV LIIIFCYFRY KRQEARPRYS IGLEQDETYI PPGESLKDLI
     EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS
     WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDTKG
     MLKLAYSSVS GLCHLHTGIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD
     TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEI ARRCVSGGIV
     EEYQLPYHDL VPSDPSYEDM REIVCIKRLR PSFPNRWSSD ECLRQMGKLM MECWAHNPAS
     RLTALRVKKT LAKMSESQDI KL
//