ID AVR2_RAT STANDARD; PRT; 513 AA. AC P38444; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE ACTIVIN RECEPTOR TYPE II PRECURSOR (EC 2.7.1.-) (ACTR-II). GN ACVR2 OR ACTRII. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=TESTIS; RX MEDLINE; 93279247. RA FENG Z.M., MADIGAN M.B., CHEN C.L.C.; RT "Expression of type II activin receptor genes in the male and female RT reproductive tissues of the rat."; RL Endocrinology 132:2593-2600(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=OVARY; RX MEDLINE; 93050162. RA SHINOZAKI H., ITO I., HASEGAWA Y., NAKAMURA K., IGARASHI S., RA NAKAMURA M., MIYAMOTO K., ETO Y., IBUKI Y., MINEGISHI T.; RT "Cloning and sequencing of a rat type II activin receptor."; RL FEBS Lett. 312:53-56(1992). CC -!- FUNCTION: RECEPTOR FOR ACTIVIN A, ACTIVIN B, AND INHIBIN A. CC INVOLVED IN TRANSMEMBRANE SIGNALING. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: WITH THE CONSERVED CATALYTIC DOMAINS OF SER/THR- CC PROTEIN KINASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; L10639; AAA40674.1; -. DR EMBL; S48190; AAB23958.1; -. DR PFAM; PF00069; pkinase; 1. DR PFAM; PF01064; Activin_recp; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Receptor; Transferase; Serine/threonine-protein kinase; ATP-binding; KW Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 513 ACTIVIN RECEPTOR TYPE II. FT DOMAIN 20 135 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 136 161 POTENTIAL. FT DOMAIN 162 513 CYTOPLASMIC (POTENTIAL). FT DOMAIN 192 485 PROTEIN KINASE. FT NP_BIND 198 206 ATP (BY SIMILARITY). FT BINDING 219 219 ATP (BY SIMILARITY). FT ACT_SITE 322 322 BY SIMILARITY. FT CARBOHYD 43 43 POTENTIAL. FT CARBOHYD 66 66 POTENTIAL. FT CONFLICT 165 165 M -> K (IN REF. 2). FT CONFLICT 218 218 V -> I (IN REF. 2). FT CONFLICT 353 353 G -> A (IN REF. 2). FT CONFLICT 475 475 L -> V (IN REF. 2). SQ SEQUENCE 513 AA; 57892 MW; 7ED9352A CRC32; MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWERD RTNQTGVEPC YGDKDKRRHC FATWKNISGS IEIVKQGCWL DDINCYDRTD CIEKKDSPEV YFCCCEGNMC NEKFSYFPEM EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI AGIVICAFWV YRHHMMAYPP VLVPTQDPGP PPPSPLLGLK PLQLLEVKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG MKHENILQFI GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSGGDTHGQV GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTAADGPVDE YMLPFEEEIG QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG MAMLCETIEE CWDHDAEARL SAGCLGERIT QMQRLTNIIT TEDIVTVVTM VTNVDFPPKE SSL //