ID   AVR2B_BOVIN             Reviewed;         512 AA.
AC   Q95126;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   22-JUL-2008, entry version 68.
DE   RecName: Full=Activin receptor type-2B;
DE            EC=2.7.11.30;
DE   AltName: Full=Activin receptor type IIB;
DE            Short=ACTR-IIB;
DE   Flags: Precursor;
GN   Name=ACVR2B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Corpus luteum, and Pituitary;
RX   MEDLINE=97307690; PubMed=9165032; DOI=10.1210/en.138.6.2425;
RA   Ethier J.-F., Lussier J.G., Silversides D.W.;
RT   "Bovine activin receptor type IIB messenger ribonucleic acid displays
RT   alternative splicing involving a sequence homologous to Src-homology 3
RT   domain binding sites.";
RL   Endocrinology 138:2425-2434(1997).
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC       of two type II and two type I transmembrane serine/threonine
CC       kinases. Type II receptors phosphorylate and activate type I
CC       receptors which autophosphorylate, then bind and activate SMAD
CC       transcriptional regulators. Receptor for activin A, activin B and
CC       inhibin A.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U57707; AAC02647.1; -; mRNA.
DR   RefSeq; NP_776920.1; -.
DR   UniGene; Bt.4990; -.
DR   HSSP; P27038; 1BTE.
DR   SMR; Q95126; 24-117.
DR   Ensembl; ENSBTAG00000018105; Bos taurus.
DR   GeneID; 282131; -.
DR   KEGG; bta:282131; -.
DR   HOVERGEN; Q95126; -.
DR   InterPro; IPR000333; Activin_II_recpt.
DR   InterPro; IPR015768; Activin_II_recpt_C.
DR   InterPro; IPR000472; Activin_rcpt.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_bd_CS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   PANTHER; PTHR23255:SF10; Activin_II_recpt_C; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Nucleotide-binding; Receptor;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    512       Activin receptor type-2B.
FT                                /FTId=PRO_0000024403.
FT   TOPO_DOM     19    137       Extracellular (Potential).
FT   TRANSMEM    138    158       Potential.
FT   TOPO_DOM    159    512       Cytoplasmic (Potential).
FT   DOMAIN      190    480       Protein kinase.
FT   NP_BIND     196    204       ATP (By similarity).
FT   ACT_SITE    321    321       Proton acceptor (By similarity).
FT   BINDING     217    217       ATP (By similarity).
FT   CARBOHYD     42     42       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     65     65       N-linked (GlcNAc...) (Potential).
FT   DISULFID     29     59       By similarity.
FT   DISULFID     49     77       By similarity.
FT   DISULFID     84    103       By similarity.
FT   DISULFID     90    102       By similarity.
FT   DISULFID    104    109       By similarity.
SQ   SEQUENCE   512 AA;  57569 MW;  D8E14D465B3EEF04 CRC64;
     MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GERDKRLHCY
     ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG
     GPEVTYEPPP TAPTLLTVLA YSLLPVGGLS LIALLAFWMY RHRKPPYGHA DIHEDPGPPP
     PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK
     HENLLQFIAA EKRGSSLEAE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
     LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG
     TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ
     HPSLEELQEV VVHKKMRPAI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL
     IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI
//