ID GBAK_RAT STANDARD; PRT; 353 AA. AC P08753; DT 01-NOV-1988 (Rel. 09, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(K), ALPHA SUBUNIT (G(I) ALPHA-3). GN GNAI3 OR GNAI-3. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88198230; PubMed=2834384; RA Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.; RT "Presence of three distinct molecular species of Gi protein alpha RT subunit. Structure of rat cDNAs and human genomic DNAs."; RL J. Biol. Chem. 263:6656-6664(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88007678; PubMed=2820999; RA Jones D.T., Reed R.R.; RT "Molecular cloning of five GTP-binding protein cDNA species from rat RT olfactory neuroepithelium."; RL J. Biol. Chem. 262:14241-14249(1987). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- FUNCTION: G(K) IS THE STIMULATORY G PROTEIN OF RECEPTOR-REGULATED CC K+ CHANNELS. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA & GAMMA). CC THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING SITE. CC -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 1 CC (G(I/O/T/Z)). 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 -------------------------------------------------------------------------- DR EMBL; J03219; AAA41224.1; -. DR EMBL; M20713; AAA40823.1; -. DR PIR; E27423; RGRTI3. DR PIR; A28154; A28154. DR HSSP; P10824; 1AS3. DR INTERPRO; IPR001019; -. DR INTERPRO; IPR001408; -. DR PFAM; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. KW GTP-binding; Transducer; ADP-ribosylation; Multigene family; KW Myristate. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT NP_BIND 39 46 GTP (BY SIMILARITY). FT NP_BIND 199 202 GTP (BY SIMILARITY). FT NP_BIND 268 271 GTP (BY SIMILARITY). FT MOD_RES 177 177 ADP-RIBOSYL[1] (BY ACTION OF CTX). FT MOD_RES 350 350 ADP-RIBOSYL[1] (BY ACTION OF IAP). SQ SEQUENCE 353 AA; 40391 MW; 8D8396349587E0F9 CRC64; GCTLSAEDKA AVERSKMIDR NLREDGEKAA KEVKLLLLGA GESGKSTIVK QMKIIHEDGY SEDECKQYKV VVYSNTIQSI IAIIRAMGRL KIDFGEAARA DDARQLFVLA GSAEEGVMTS ELAGVIKRLW RDGGVQACFS RSREYQLNDS ASYYLNDLDR ISQTNYIPTQ QDVLRTRVKT TGIVETHFTF KELYFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN RMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKRS PLTICYPEYT GSNTYEEAAA YIQCQFEDLN RRKDTKEVYT HFTCATDTKN VQFVFDAVTD VIIKNNLKEC GLY //