GPCRDB: Swiss-Prot entry
ID GNAI2_CAVPO STANDARD; PRT; 354 AA.
AC P38402;
DT 01-OCT-1994 (Rel. 30, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Guanine nucleotide-binding protein G(i), alpha-2 subunit (Adenylate
DE cyclase-inhibiting G alpha protein).
GN Name=GNAI2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC Hystricognathi; Caviidae; Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hartley; TISSUE=Lung;
RX MEDLINE=93129640; PubMed=1482697 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0167-4889(92)90009-Z;
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. The G(i) proteins are involved in hormonal
CC regulation of adenylate cyclase: they inhibit the cyclase in
CC response to beta-adrenergic stimuli.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC gamma. The alpha chain contains the guanine nucleotide binding
CC site. Interacts with UNC5B (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Most abundant in the
CC lung and in the spleen.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
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 as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; D21233; BAA04765.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P38402; 4-353.
DR InterPro; IPR001019; Gprotein_alpha.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00503; G-alpha; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR ProDom; PD000281; Gprotein_alpha; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P38402.
DR ProtoNet; P38402.
DR ProtoMap; P38402.
DR PRESAGE; P38402.
DR DIP; P38402.
DR ModBase; P38402.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW ADP-ribosylation; GTP-binding; Lipoprotein; Multigene family;
KW Myristate; Palmitate; Transducer.
FT INIT_MET 0 0 By similarity.
FT NP_BIND 39 46 GTP (By similarity).
FT NP_BIND 200 204 GTP (By similarity).
FT NP_BIND 269 272 GTP (By similarity).
FT MOD_RES 178 178 ADP-ribosylarginine (by cholera toxin).
FT MOD_RES 351 351 ADP-ribosylcysteine (by pertussis toxin).
FT LIPID 1 1 N-myristoyl glycine (By similarity).
FT LIPID 2 2 S-palmitoyl cysteine (By similarity).
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
//