ID GB02_HUMAN STANDARD; PRT; 353 AA. AC P29777; DT 01-APR-1993 (Rel. 25, 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(O), ALPHA SUBUNIT 2. GN GNAO1. 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=91195273; PubMed=1901650; RA Tsukamoto T., Toyama R., Itoh H., Kozasa T., Matsuoka M., Kaziro Y.; RT "Structure of the human gene and two rat cDNAs encoding the alpha RT chain of GTP-binding regulatory protein Go: two different mRNAs are RT generated by alternative splicing."; RL Proc. Natl. Acad. Sci. U.S.A. 88:2974-2978(1991). 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(O) PROTEIN FUNCTION IS NOT CLEAR. CC -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA & GAMMA). CC THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING SITE. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS OF G(O) ALPHA SUBUNITS ARE CC PRODUCED BY ALTERNATIVE SPLICING OF THE SAME GENE. 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; M60162; AAA52586.1; -. DR EMBL; M60156; AAA52586.1; JOINED. DR EMBL; M60157; AAA52586.1; JOINED. DR EMBL; M60158; AAA52586.1; JOINED. DR EMBL; M60159; AAA52586.1; JOINED. DR EMBL; M60160; AAA52586.1; JOINED. DR EMBL; M60161; AAA52586.1; JOINED. DR PIR; B40436; RGHUO2. DR HSSP; P10824; 1GDD. DR MIM; 139311; -. DR INTERPRO; IPR001019; -. DR INTERPRO; IPR001408; -. DR PFAM; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. KW GTP-binding; Transducer; Multigene family; Alternative splicing; KW ADP-ribosylation; Myristate; Palmitate; Lipoprotein. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT LIPID 2 2 PALMITATE (BY SIMILARITY). FT NP_BIND 39 46 GTP (BY SIMILARITY). FT NP_BIND 200 203 GTP (BY SIMILARITY). FT NP_BIND 269 272 GTP (BY SIMILARITY). FT MOD_RES 178 178 ADP-RIBOSYL[1] (BY ACTION OF CTX). FT MOD_RES 350 350 ADP-RIBOSYL[1] (BY ACTION OF IAP). SQ SEQUENCE 353 AA; 39941 MW; 33C1C5857027D6AD CRC64; GCTLSAEERA ALERSKAIEK NLKEDGISAA KDVKLLLLGA GESGKSTIVK QMKIIHEDGF SGEDVKQYKP VVYSNTIQSL AAIVRAMDTL GIEYGDKERK ADAKMVCDVV SRMEDTEPFS AELLSAMMRL WGDSGIQECF NRSREYQLND SAKYYLDSLD RIGAADYQPT EQDILRTRVK TTGIVETHFT FKNLHFRLFD VGGQRSERKK WIHCFEDVTA IIFCVALSGY DQVLHEDETT NRMHESLKLF DSICNNKWFT DTSIILFLNK KDIFEEKIKK SPLTICFPEY TGPSAFTEAV AYIQAQYESK NKSAHKEIYS HVTCATDTNN IQFVFDAVTD VIIAKNLRGC GLY //