ID A0A8I6A0G0_RAT Unreviewed; 550 AA. AC A0A8I6A0G0; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 27-MAR-2024, entry version 10. DE RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271}; DE EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271}; GN Name=Bmpr1b {ECO:0000313|Ensembl:ENSRNOP00000086028.1, GN ECO:0000313|RGD:1595863}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000086028.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000086028.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000086028.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000086028.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000086028.1}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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:0000256|ARBA:ARBA00023945}; 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:0000256|ARBA:ARBA00023948, CC ECO:0000256|RuleBase:RU361271}; 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|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479, 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|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSRNOT00000114929.1; ENSRNOP00000086028.1; ENSRNOG00000016289.8. DR AGR; RGD:1595863; -. DR RGD; 1595863; Bmpr1b. DR GeneTree; ENSGT00940000155919; -. DR Proteomes; UP000002494; Chromosome 2. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; ISO:RGD. DR GO; GO:0036122; F:BMP binding; ISO:RGD. DR GO; GO:0098821; F:BMP receptor activity; ISO:RGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD. DR GO; GO:0046332; F:SMAD binding; ISO:RGD. DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; ISO:RGD. DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISO:RGD. DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD. DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD. DR GO; GO:0060348; P:bone development; ISO:RGD. DR GO; GO:0043010; P:camera-type eye development; ISO:RGD. DR GO; GO:0001502; P:cartilage condensation; ISO:RGD. DR GO; GO:0030154; P:cell differentiation; ISO:RGD. DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD. DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD. DR GO; GO:0021953; P:central nervous system neuron differentiation; ISO:RGD. DR GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD. DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD. DR GO; GO:0001654; P:eye development; ISO:RGD. DR GO; GO:0006954; P:inflammatory response; ISO:RGD. DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD. DR GO; GO:0001550; P:ovarian cumulus expansion; ISO:RGD. DR GO; GO:0042698; P:ovulation cycle; ISO:RGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:RGD. DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD. DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:RGD. 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 PRINTS; PR00653; ACTIVIN2R. 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|RuleBase:RU361271}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361271}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361271}; KW Membrane {ECO:0000256|RuleBase:RU361271}; KW Metal-binding {ECO:0000256|RuleBase:RU361271}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU361271}; Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transferase {ECO:0000256|RuleBase:RU361271}; KW Transmembrane {ECO:0000256|RuleBase:RU361271}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361271}. FT TRANSMEM 175..196 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361271" FT DOMAIN 222..251 FT /note="GS" FT /evidence="ECO:0000259|PROSITE:PS51256" FT DOMAIN 252..542 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 279 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 550 AA; 62217 MW; 15BB2A6DEA8830D2 CRC64; MCDLGAFITL RRRSSMAKNF PPPSPSSNCS GIFLLSLWDN SLEKFVDNML LRSSGKLNVG TKKEDGESTA PTARPKVLRC KCHHHCPEDS VNNICSTDGY CFTMIEEDDS GTPVVTSGCL GLEGSDFQCR DTPIPHQRRS IECCTERNEC NKDLHPTLPP LKDRDFVDGP IHHKALLISV TVCSLLLVLI ILFCYFRYKR QEARPRYSIG LEQDETYIPP GESLRDLIEQ SQSSGSGSGL PLLVQRTIAK QIQMVKQIGK GRYGEVWMGK WRGEKVAVKV FFTTEEASWF RETEIYQTVL MRHENILGFI AADIKGTGSW TQLYLITDYH ENGSLYDYLK STTLDAKSML KLAYSSVSGL CHLHTEIFST QGKPAIAHRD LKSKNILVKK NGTCCIADLG LAVKFISDTN EVDIPPNTRV GTKRYMPPEV LDESLNRTHF QSYIMADMYS FGLILWEIAR RCVSGGIVEE YQLPYHDLVP SDPSYEDMRE IVCMKKLRPS FPNRWSSDEC LRQMGKLMTE CWAHNPASRL TALRVKKTLA KMSESQDIKL //