ID GBT2_BOVIN STANDARD; PRT; 353 AA. AC P04696; DT 13-AUG-1987 (Rel. 05, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(T), ALPHA-2 SUBUNIT (TRANSDUCIN DE ALPHA-2 CHAIN). GN GNAT2. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85142187; PubMed=3856323; RA Lochrie M.A., Hurley J.B., Simon M.I.; RT "Sequence of the alpha subunit of photoreceptor G protein: homologies RT between transducin, ras, and elongation factors."; RL Science 228:96-99(1985). RN [2] RP IDENTIFICATION OF TOXIN-CATALYZED ADP-RIBOSYLATION SITE. RX MEDLINE=84212501; PubMed=6586721; RA Navon S., Fung B.K.-K.; RT "Characterization of transducin from bovine retinal rod outer RT segments. Mechanism and effects of cholera toxin-catalyzed ADP- RT ribosylation."; RL J. Biol. Chem. 259:6686-6693(1984). CC -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE CC INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE CC SIGNALING SYSTEMS. CC -!- FUNCTION: TRANSDUCIN IS AN AMPLIFIER AND ONE OF THE TRANSDUCERS OF CC A VISUAL IMPULSE THAT PERFORMS THE COUPLING BETWEEN RHODOPSIN AND CC CGMP-PHOSPHODIESTERASE. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA & GAMMA). CC THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING SITE. CC -!- TISSUE SPECIFICITY: OUTER SEGMENTS. 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; M11116; AAA30790.1; -. DR PIR; A94279; RGBOT2. 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; Vision; Multigene family; ADP-ribosylation; 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; 40012 MW; C5CD424F69D582BD CRC64; GSGASAEDKE LAKRSKELEK KLQEDADKEA KTVKLLLLGA GESGKSTIVK QMKIIHQDGY SPEECLEYKA IIYGNVLQSI LAIIRAMPTL GIDYAEVSCV DNGRQLNNLA DSIEEGTMPP ELVEVIRKLW KDGGVQACFD RAAEYQLNDS ASYYLNQLDR ITAPDYLPNE QDVLRSRVKT TGIIETKFSV KDLNFRMFDV GGQRSERKKW IHCFEGVTCI IFCAALSAYD MVLVEDDEVN RMHESLHLFN SICNHKFFAA TSIVLFLNKK DLFEEKIKKV HLSICFPEYD GNNSYEDAGN YIKSQFLDLN MRKDVKEIYS HMTCATDTQN VKFVFDAVTD IIIKENLKDC GLF //