ID GBT2_HUMAN STANDARD; PRT; 353 AA. AC P19087; DT 01-NOV-1990 (Rel. 16, 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92038044; PubMed=1936270; RA Kubo M., Hirano T., Kakinuma M.; RT "Molecular cloning and sequence analysis of cDNA and genomic DNA for RT the human cone transducin alpha subunit."; RL FEBS Lett. 291:245-248(1991). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=RETINA; RX MEDLINE=90380379; PubMed=2534964; RA Lerea C.L., Bunt-Milam A.H., Hurley J.B.; RT "Alpha transducin is present in blue-, green-, and red-sensitive cone RT photoreceptors in the human retina."; RL Neuron 3:367-376(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=94010942; PubMed=8406495; RA Morris A.T., Fong S.; RT "Characterization of the gene encoding human cone transducin alpha- RT subunit (GNAT2)."; RL Genomics 17:442-448(1993). 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; D10384; BAA01211.1; -. DR EMBL; D10377; BAA01211.1; JOINED. DR EMBL; D10378; BAA01211.1; JOINED. DR EMBL; D10379; BAA01211.1; JOINED. DR EMBL; D10380; BAA01211.1; JOINED. DR EMBL; D10381; BAA01211.1; JOINED. DR EMBL; D10382; BAA01211.1; JOINED. DR EMBL; D10383; BAA01211.1; JOINED. DR EMBL; Z18859; CAA79310.1; -. DR PIR; S18303; RGHUT2. DR HSSP; P04896; 1AZT. DR MIM; 139340; -. 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). FT CONFLICT 105 106 QL -> HV (IN REF. 2). SQ SEQUENCE 353 AA; 40044 MW; 942620F6CDFA3F54 CRC64; GSGASAEDKE LAKRSKELEK KLQEDADKEA KTVKLLLLGA GESGKSTIVK QMKIIHQDGY SPEECLEFKA IIYGNVLQSI LAIIRAMTTL GIDYAEPSCA DDGRQLNNLA DSIEEGTMPP ELVEVIRRLW KDGGVQACFE RAAEYQLNDS ASYYLNQLER ITDPEYLPSE QDVLRSRVKT TGIIETKFSV KDLNFRMFDV GGQRSERKKW IHCFEGVTCI IFCAALSAYD MVLVEDDEVN RMHESLHLFN SICNHKFFAA TSIVLFLNKK DLFEEKIKKV HLSICFPEYD GNNSYDDAGN YIKSQFLDLN MRKDVKEIYS HMTCATDTQN VKFVFDAVTD IIIKENLKDC GLF //