ID GB0_XENLA STANDARD; PRT; 353 AA. AC P10825; DT 01-JUL-1989 (Rel. 11, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(O), ALPHA SUBUNIT. GN GNA0. OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=OOCYTE; RX MEDLINE=89171257; PubMed=2494063; RA Olate J., Jorquera H., Purcell P., Codina J., Birnbaumer L., RA Allende J.E.; RT "Molecular cloning and sequence determination of a cDNA coding for the RT alpha-subunit of a Go-type protein of Xenopus laevis oocytes."; RL FEBS Lett. 244:188-192(1989). RN [2] RP REVISIONS. RA Olate J., Jorquera H., Purcell P., Codina J., Birnbaumer L., RA Allende J.E.; RL FEBS Lett. 267:316-316(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 -!- 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; X14636; CAA32784.1; -. DR PIR; S02785; RGXLOA. DR HSSP; P04896; 1AZT. 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; ADP-ribosylation; KW 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; 40332 MW; 60DD9D84DFE606BD CRC64; GCTLSAEERA ALERSKQIEK NLKEDGVTAA KDVKLLLLGA GESGKSTIVK QMKIIHEDGF SGEDVKQYKP VVYSNTIQSL AAIVRAMDTL GIEYGDKERR ADAKMVCDVV SRMEDTEPYS PELLSAMVRL WADSGIQECF NRSREYQLND SAKYYLDSLD RIGAPDYQPT EQDILRTRVK TTGIVETHFT FKNLHFRLFD VGGQRSERKK WWHCFEDVTA IIFCVALTGY DQVLHEDETT NRMHESLKLF DSICNNKWFT DTSIILFLNK KDIFQEKIKS SPLTICFPEY TGPNSFTEAV AHTQHQYESR NKSENKEIYT HITCATDTQN IQFVFDAVTD VIIAYNLRGC GLY //