ID GBAZ_MOUSE STANDARD; PRT; 352 AA. AC O70443; O70442; Q61637; DT 01-OCT-2000 (Rel. 40, Created) DT 01-OCT-2000 (Rel. 40, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(Z), ALPHA SUBUNIT (G(X) ALPHA DE CHAIN) (FRAGMENT). GN GNAZ. 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. RC STRAIN=C57BL/6; RA Matthaei K.I., Mellick A.M., Hendry I.A.; RT "Partial genomic sequence of the mouse GTP binding protein Gz alpha."; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 206-266 FROM N.A. RC STRAIN=BALB/C; TISSUE=PANCREATIC ISLETS; RX MEDLINE=94283273; PubMed=8013366; RA Zigman J.M., Westermark G.T., LaMendola J., Steiner D.F.; RT "Expression of cone transducin, Gz alpha, and other G-protein alpha- RT subunit messenger ribonucleic acids in pancreatic islets."; RL Endocrinology 135:31-37(1994). 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 -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. 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; AF056973; AAC13569.1; -. DR EMBL; AF056972; AAC13568.1; -. DR EMBL; L17074; AAC37651.1; -. DR MGD; MGI:95780; Gnaz. DR HSSP; P10824; 1AS3. DR INTERPRO; IPR001019; -. DR PFAM; PF00503; G-alpha; 1. DR PROSITE; PS00017; ATP_GTP_A; UNKNOWN_1. KW GTP-binding; Transducer; ADP-ribosylation; Multigene family; KW Lipoprotein; Palmitate; Myristate; Membrane. FT INIT_MET 0 0 PROBABLE. 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) (BY FT SIMILARITY). FT CONFLICT 209 209 K -> R (IN REF. 2). FT NON_TER 352 352 SQ SEQUENCE 352 AA; 40502 MW; E4104B31E877F2E5 CRC64; GCRQSSEEKE AARRSRRIDR HLRSESQRQR REIKLLLLGT SNSGKSTIVK QMKIIHSGGF NLDACKEYKP LIIYNAIDSL TRIIRALAAL KIDFHNPDRA YDAVQLFALT GPAESKGEIT PELLGVMRRL WADPGAQACF GRSSEYHLED NAAYYLNDLE RIAAPDYIPT VEDILRSRDM TTGIVENKFT FKELTFKMVD VGGQRSERKK WIHCFEGVTA IIFCVELSGY DLKLYEDNQT SRMAESLRLF DSICNNNWFI NTSLILFLNK KDLLAEKIRR IPLSVCFPEY KGQNTYEEAA VYIQRQFEDL NRNKETKEIY SHFTCATDTS NIQFVFDAVT DVIIQNNLKY IG //