ID GBI1_XENLA STANDARD; PRT; 353 AA. AC P27044; DT 01-AUG-1992 (Rel. 23, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(I), ALPHA-1 SUBUNIT (ADENYLATE DE CYCLASE-INHIBITING G ALPHA PROTEIN). GN GNAI1. 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=90346157; PubMed=2116977; RA Olate J., Martinez S., Purcell P., Jorquera H., Codina J., RA Birnbaumer L., Allende J.E.; RT "Molecular cloning and sequence determination of four different cDNA RT species coding for alpha-subunits of G proteins from Xenopus laevis RT oocytes."; RL FEBS Lett. 268:27-31(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(I) PROTEINS ARE INVOLVED IN HORMONAL REGULATION OF CC ADENYLATE CYCLASE: THEY INHIBIT THE CYCLASE IN RESPONSE TO BETA- CC ADRENERGIC STIMULI. 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; X56089; CAA39569.1; -. DR PIR; S11045; RGXLI1. 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; 40270 MW; 6B4EE94F841B077D CRC64; GCTLSAEDKA AVERSKMIDR NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEAGY SEEECKQYKA VVYSNTIQSI IAIIRAMGRL KIDFGDPSRA DDARQLFVLA GAAEEGFMTA ELAGVIKRLW KDGGVQACFN RSREYQLNDS AAYYLNDLDR IAQNSYIPTQ QDVLRTRVKT TGIVETHFTF KDLHFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN RMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKRS PLTICYPEYP GSNTYEEAAA YIQCQFEDLN KRKDTKEIYT HFTCATDTKN VQFVFDAVTD VIIKNNLKDC GLF //