ID GBT1_MOUSE STANDARD; PRT; 349 AA. AC P20612; DT 01-FEB-1991 (Rel. 17, 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(T), ALPHA-1 SUBUNIT (TRANSDUCIN DE ALPHA-1 CHAIN). GN GNAT1 OR GNAT-1. 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. RX MEDLINE=89214143; PubMed=2708360; RA Raport C.J., Dere B., Hurley J.B.; RT "Characterization of the mouse rod transducin alpha subunit gene."; RL J. Biol. Chem. 264:7122-7128(1989). RN [2] RP SEQUENCE OF 123-316 FROM N.A. RC STRAIN=CF-1 / HARLAN; TISSUE=RETINA; RX MEDLINE=97011591; PubMed=8858601; RA Williams C.J., Schultz R.M., Kopf G.S.; RT "G protein gene expression during mouse oocyte growth and maturation, RT and preimplantation embryo development."; RL Mol. Reprod. Dev. 44:315-323(1996). 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: ROD. 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; M25513; AAA40473.1; -. DR EMBL; M25506; AAA40473.1; JOINED. DR EMBL; M25507; AAA40473.1; JOINED. DR EMBL; M25508; AAA40473.1; JOINED. DR EMBL; M25509; AAA40473.1; JOINED. DR EMBL; M25510; AAA40473.1; JOINED. DR EMBL; M25511; AAA40473.1; JOINED. DR EMBL; M25512; AAA40473.1; JOINED. DR EMBL; U38504; AAB01735.1; -. DR PIR; A33352; RGMST1. DR HSSP; P04695; 1TND. DR MGD; MGI:95778; Gnat1. 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 35 42 GTP (BY SIMILARITY). FT NP_BIND 195 198 GTP (BY SIMILARITY). FT NP_BIND 264 267 GTP (BY SIMILARITY). FT MOD_RES 173 173 ADP-RIBOSYL[1] (BY ACTION OF CTX). FT MOD_RES 346 346 ADP-RIBOSYL[1] (BY ACTION OF IAP). SQ SEQUENCE 349 AA; 39835 MW; 57A59D03DAEDBC03 CRC64; GAGASAEEKH SRELEKKLKE DAEKDARTVK LLLLGAGESG KSTIVKQMKI IHQDGYSLEE CLEFIAIIYG NTLQSILAIV RAMTTLNIQY GDSARQDDAR KLMHMADTIE EGTMPKEMSD IIQRLWKDSG IQACFDRASE YQLNDSAGYY LSDLERLVTP GYVPTEQDVL RSRVKTTGII ETQFSFKDLN FRMFDVGGQR SERKKWIHCF EGVTCIIFIA ALSAYDMVLV EDDEVNRMHE SLHLFNSICN HRYFATTSIV LFLNKKDVFS EKIKKAHLSI CFPDYDGPNT YEDAGNYIKV QFLELNMRRD VKEIYSHMTC ATDTQNVKFV FDAVTDIIIK ENLKDCGLF //