ID GBI2_CAVPO STANDARD; PRT; 354 AA. AC P38402; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE GUANINE NUCLEOTIDE-BINDING PROTEIN G(I), ALPHA-2 SUBUNIT (ADENYLATE DE CYCLASE-INHIBITING G ALPHA PROTEIN). GN GNAI2. OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HARTLEY; TISSUE=LUNG; RX MEDLINE=93129640; PubMed=1482697; RA Sakanaka C., Izumi T., Nakamura M., Honda Z.-I., Watanabe T., RA Minami M., Mutoh H., Bito H., Seyama Y., Ui M., Shimizu T.; RT "Three types of Gi alpha protein of the guinea-pig lung: cDNA cloning RT and analysis of their tissue distribution."; RL Biochim. Biophys. Acta 1175:61-66(1992). 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(I) PROTEINS ARE INVOLVED IN HORMONAL REGULATION OF CC ADENYLATE CYCLASE: THEY INHIBIT THE CYCLASE IN RESPONSE TO BETA- CC ADRENERGIC STIMULI. 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: UBIQUITOUSLY EXPRESSED. MOST ABUNDANT IN THE CC LUNG AND IN THE SPLEEN. 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; D21233; BAA04765.1; -. DR PIR; S28158; S28158. DR HSSP; P10824; 1AS3. 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 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 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 351 351 ADP-RIBOSYL[1] (BY ACTION OF PTX). SQ SEQUENCE 354 AA; 40408 MW; D6C151413CC5EB91 CRC64; GCTVSAEDKA AAERSKMIDK NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEDGY SEEECRQYRA VVYSNTIQSI MAIVKAMGNL QIDFADPLRA DDARQLFALS CTAEEQGMLP EDLSGVIRRL WADHGVQACF SRSREYQLND SAAYYLNDLD RIAQSDYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSAY DLVLAEDEEM NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKITH SPLTICFPEY TGANKYDEAA SYIQSKFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF //