ID GBI_HELTI STANDARD; PRT; 353 AA. AC P51876; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(I), ALPHA SUBUNIT (ADENYLATE DE CYCLASE-INHIBITING G ALPHA PROTEIN). OS Helisoma trivolvis (Snail). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Pulmonata; Basommatophora; OC Planorbidae; Helisoma. OX NCBI_TaxID=27815; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=OREGON RED; TISSUE=CENTRAL GANGLION; RX MEDLINE=94138304; PubMed=7508312; RA Durgerian S., Bahls F., Richmond J., Doyle R.T., Larson D.D., RA Haydon P.G.; RT "Roles for arachidonic acid and GTP-binding proteins in synaptic RT transmission."; RL J. Physiol. (Paris) 87:123-137(1993). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. 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; L18922; AAC41538.1; -. 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 (BY SIMILARITY). FT MOD_RES 350 350 ADP-RIBOSYL[1] (BY ACTION OF IAP) FT (BY SIMILARITY). SQ SEQUENCE 353 AA; 40412 MW; 19878620EECFA76A CRC64; GCVTSQEDKA AVERSKQIDK SLRMDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEKGY SQEECLQYNP VVYSNAIQSM IAIIKAMGQL KIQFGHPDRA EEARQFFALA GHADEGEMSQ ELSGIMKRLW KDVGVQECFS RSREYQLNDS AEYYLNALDR ISAPGYIPTE QDVLRTRVKT TGIVETHFTF KDLHFKMFDV GGQRSERKKW IHCFEGVTAI IFIVAMSEYD LTLAEDQEMN RMMESMKLFD SICNNKWFTE TSIILFLNKK DLFEEKIKKS PLTICFPEYT GANTYEEAAA YIQLQFENLN KKKDTKEIYS HFTCATDTNN VQFVFDAVTD VIIKNNLKDC GLF //