ID GB01_MOUSE STANDARD; PRT; 353 AA. AC P18872; DT 01-NOV-1990 (Rel. 16, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(O), ALPHA SUBUNIT 1. GN GNAO OR GNA0. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN, AND SPERMATID; RX MEDLINE=90370808; PubMed=1697681; RA Strathmann M., Wilkie T.M., Simon M.I.; RT "Alternative splicing produces transcripts encoding two forms of the RT alpha subunit of GTP-binding protein Go."; RL Proc. Natl. Acad. Sci. U.S.A. 87:6477-6481(1990). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- FUNCTION: THE G(O) PROTEIN FUNCTION IS NOT CLEAR. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA & GAMMA). CC THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING SITE. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; 1 (SHOWN HERE) AND 2 (AC CC P18873); ARE PRODUCED BY ALTERNATIVE SPLICING. 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; M36777; AAA37645.1; -. DR PIR; A36038; RGMSO1. DR HSSP; P10824; 1GDD. DR MGD; MGI:95775; Gnao. DR INTERPRO; IPR001019; -. DR INTERPRO; IPR001408; -. DR PFAM; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. KW GTP-binding; Transducer; Multigene family; Alternative splicing; KW ADP-ribosylation; Myristate; Palmitate; Lipoprotein. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT LIPID 2 2 PALMITATE (BY SIMILARITY). FT NP_BIND 39 46 GTP (BY SIMILARITY). FT NP_BIND 200 203 GTP (BY SIMILARITY). FT NP_BIND 269 272 GTP (BY SIMILARITY). FT MOD_RES 178 178 ADP-RIBOSYL[1] (BY ACTION OF CTX). FT MOD_RES 350 350 ADP-RIBOSYL[1] (BY ACTION OF IAP). SQ SEQUENCE 353 AA; 39953 MW; 9CE471097205B8A2 CRC64; GCTLSAEERA ALERSKAIEK NLKEDGISAA KDVKLLLLGA GESGKSTIVK QMKIIHEDGF SGEDVKQYKP VVYSNTIQSL AAIVRAMDTL GVEYGDKERK TDSKMVCDVV SRMEDTEPFS AELLSAMMRL WGDSGIQECF NRSREYQLND SAKYYLDSLD RIGAGDYQPT EQDILRTRVK TTGIVETHFT FKNLHFRLFD VGGQRSERKK WIHCFEDVTA IIFCVALSGY DQVLHEDETT NRMHESLMLF DSICNNKFFI DTSIILFLNK KDLFGEKIKK SPLTICFPEY PGSNTYEDAA AYIQTQFESK NRSPNKEIYC HMTCATDTNN IQVVFDAVTD IIIANNLRGC GLY //