BMR1B_CHICK
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 03-AUG-2022, entry version 149.
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.ENSGALP00000019925; -.
DR PaxDb; Q05438; -.
DR GeneID; 396030; -.
DR KEGG; gga:396030; -.
DR CTD; 658; -.
DR VEuPathDB; HostDB:geneid_396030; -.
DR eggNOG; KOG2052; Eukaryota.
DR InParanoid; Q05438; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; Q05438; -.
DR BRENDA; 2.7.10.2; 1306.
DR PRO; PR:Q05438; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0044214; C:spanning component of plasma membrane; TAS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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: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: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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:AgBase.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR Gene3D; 2.10.60.10; -; 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; PTHR23255; 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; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 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
