ID BMR2_HUMAN STANDARD; PRT; 1038 AA. AC Q13873; Q16569; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Bone morphogenetic protein receptor type II precursor (EC 2.7.1.37) DE (BMP type II receptor) (BMPR-II). GN BMPR2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Substantia nigra; RX MEDLINE=95372334; PubMed=7644468; RA Rosenzweig B.L., Imamura T., Okadome T., Cox G.N., Yamashita H., RA ten Dijke P., Heldin C., Miyazono K.; RT "Cloning and characterization of a human type II receptor for bone RT morphogenetic proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7632-7636(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Skin fibroblast; RX MEDLINE=95403457; PubMed=7673243; RA Nohno T., Ishikawa T., Saito T., Hosokawa K., Noji S., Wosing D.H., RA Rosenbaum J.S.; RT "Identification of a human type II receptor for bone morphogenetic RT protein-4 that forms differential heteromeric complexes with bone RT morphogenetic protein type I receptors."; RL J. Biol. Chem. 270:22522-22526(1995). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95197572; PubMed=7890683; RA Kawabata M., Chytil A., Moses H.L.; RT "Cloning of a novel type II serine/threonine kinase receptor through RT interaction with the type I transforming growth factor-beta RT receptor."; RL J. Biol. Chem. 270:5625-5630(1995). CC -!- FUNCTION: BINDS TO BMP-7, BMP-2 AND, LESS EFFICIENTLY, BMP-4. CC BINDING IS WEAK BUT ENHANCED BY THE PRESENCE OF TYPE I RECEPTORS CC FOR BMPS. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- SUBUNIT: HETERODIMERIZE WITH TYPE-I RECEPTORS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN HEART AND LIVER. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC TGFB RECEPTOR SUBFAMILY. 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 EMBL; Z48923; CAA88759.1; -. DR EMBL; D50516; BAA09094.1; -. DR EMBL; U20165; AAC50105.1; -. DR HSSP; P27038; 1BTE. DR MIM; 600799; -. DR InterPro; IPR000472; Activin_rec. DR InterPro; IPR000719; Euk_pkinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF00069; pkinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Receptor; Transferase; Serine/threonine-protein kinase; ATP-binding; KW Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 1038 BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE FT II. FT DOMAIN 27 150 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 151 171 POTENTIAL. FT DOMAIN 172 1038 CYTOPLASMIC (POTENTIAL). FT DOMAIN 203 504 PROTEIN KINASE. FT NP_BIND 209 217 ATP (BY SIMILARITY). FT BINDING 230 230 ATP (BY SIMILARITY). FT ACT_SITE 333 333 BY SIMILARITY. FT DOMAIN 547 550 POLY-SER. FT DOMAIN 610 618 POLY-THR. FT DOMAIN 901 908 POLY-ASN. FT CARBOHYD 55 55 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 126 126 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 828 828 G -> R (IN REF. 1). SQ SEQUENCE 1038 AA; 115201 MW; 1389923CE574B913 CRC64; MTSSLQRPWR VPWLPWTILL VSTAAASQNQ ERLCAFKDPY QQDLGIGESR ISHENGTILC SKGSTCYGLW EKSKGDINLV KQGCWSHIGD PQECHYEECV VTTTPPSIQN GTYRFCCCST DLCNVNFTEN FPPPDTTPLS PPHSFNRDET IIIALASVSV LAVLIVALCF GYRMLTGDRK QGLHSMNMME AAASEPSLDL DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF INEKNIYRVP LMEHDNIARF IVGDERVTAD GRMEYLLVME YYPNGSLCKY LSLHTSDWVS SCRLAHSVTR GLAYLHTELP RGDHYKPAIS HRDLNSRNVL VKNDGTCVIS DFGLSMRLTG NRLVRPGEED NAAISEVGTI RYMAPEVLEG AVNLRDCESA LKQVDMYALG LIYWEIFMRC TDLFPGESVP EYQMAFQTEV GNHPTFEDMQ VLVSREKQRP KFPEAWKENS LAVRSLKETI EDCWDQDAEA RLTAQCAEER MAELMMIWER NKSVSPTVNP MSTAMQNERN LSHNRRVPKI GPYPDYSSSS YIEDSIHHTD SIVKNISSEH SMSSTPLTIG EKNRNSINYE RQQAQARIPS PETSVTSLST NTTTTNTTGL TPSTGMTTIS EMPYPDETNL HTTNVAQSIG PTPVCLQLTE EDLETNKLDP KEVDKNLKES SDENLMEHSL KQFSGPDPLS STSSSLLYPL IKLAVEATGQ QDFTQTANGQ ACLIPDVLPT QIYPLPKQQN LPKRPTSLPL NTKNSTKEPR LKFGSKHKSN LKQVETGVAK MNTINAAEPH VVTVTMNGVA GRNHSVNSHA ATTQYANGTV LSGQTTNIVT HRAQEMLQNQ FIGEDTRLNI NSSPDEHEPL LRREQQAGHD EGVLDRLVDR RERPLEGGRT NSNNNNSNPC SEQDVLAQGV PSTAADPGPS KPRRAQRPNS LDLSATNVLD GSSIQIGEST QDGKSGSGEK IKKRVKTPYS LKRWRPSTWV ISTESLDCEV NNNGSNRAVH SKSSTAVYLA EGGTATTMVS KDIGMNCL //