ID GBAZ_HUMAN STANDARD; PRT; 354 AA. AC P19086; DT 01-NOV-1990 (Rel. 16, 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). GN GNAZ. 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=88203641; PubMed=3129724; RA Fong H.K.W., Yoshimoto K.K., Eversole-Cire P., Simon M.I.; RT "Identification of a GTP-binding protein alpha subunit that lacks an RT apparent ADP-ribosylation site for pertussis toxin."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3066-3070(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90330667; PubMed=2115889; RA Matsuoka M., Itoh H., Kaziro Y.; RT "Characterization of the human gene for Gx alpha, a pertussis toxin- RT insensitive regulatory GTP-binding protein."; RL J. Biol. Chem. 265:13215-13220(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=91346834; PubMed=1908722; RA Gagnon A.W., Manning D.R., Catani L., Gewirtz A., Poncz M., RA Brass L.F.; RT "Identification of Gz alpha as a pertussis toxin-insensitive G protein RT in human platelets and megakaryocytes."; RL Blood 78:1247-1253(1991). 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; J03260; AAA52580.1; -. DR EMBL; D90150; BAA14180.1; -. DR PIR; A36628; RGHUGX. DR PIR; A61179; A61179. DR HSSP; P10824; 1AS3. DR MIM; 139160; -. DR INTERPRO; IPR001019; -. DR INTERPRO; IPR001408; -. DR PFAM; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. 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). FT CONFLICT 131 131 W -> Y (IN REF. 3). FT CONFLICT 229 229 G -> A (IN REF. 2). FT CONFLICT 272 272 D -> N (IN REF. 3). ZM 3HGE ZC 3H-label(metabolic)..SDS-PAGE SQ SEQUENCE 354 AA; 40792 MW; 3863241237E7C6CC CRC64; GCRQSSEEKE AARRSRRIDR HLRSESQRQR REIKLLLLGT SNSGKSTIVK QMKIIHSGGF NLEACKEYKP LIIYNAIDSL TRIIRALAAL RIDFHNPDRA YDAVQLFALT GPAESKGEIT PELLGVMRRL WADPGAQACF SRSSEYHLED NAAYYLNDLE RIAAADYIPT VEDILRSRDM TTGIVENKFT FKELTFKMVD VGGQRSERKK WIHCFEGVTA IIFCVELSGY DLKLYEDNQT SRMAESLRLF DSICNNNWFI NTSLILFLNK KDLLAEKIRR IPLTICFPEY KGQNTYEEAA VYIQRQFEDL NRNKETKEIY SHFTCATDTS NIQFVFDAVT DVIIQNNLKY IGLC //