ID   GBAK_CAVPO     STANDARD;      PRT;   353 AA.
AC   P38403;
DT   01-OCT-1994 (Rel. 30, Created)
DT   01-OCT-1996 (Rel. 34, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   GUANINE NUCLEOTIDE-BINDING PROTEIN G(K), ALPHA SUBUNIT (G(I) ALPHA-3).
GN   GNAI3.
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.
CC   -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 1
CC       (G(I/O/T/Z)).
CC   --------------------------------------------------------------------------
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DR   EMBL; D21234; BAA04766.1; -.
DR   PIR; S28159; S28159.
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     199    202       GTP (BY SIMILARITY).
FT   NP_BIND     268    271       GTP (BY SIMILARITY).
FT   MOD_RES     177    177       ADP-RIBOSYL[1] (BY ACTION OF CTX).
FT   MOD_RES     350    350       ADP-RIBOSYL[1] (BY ACTION OF PTX).
SQ   SEQUENCE   353 AA;  40473 MW;  E54FCE05CEB97BBE CRC64;
     GCTLSAEDKA AVERSKMIDR NLREDGEKAA KEVKLLLLGA GESGKSTIVK QMKIIHEDGY
     SEEECKQYKV VVYSNTIQSI IAIIRAMGRL KIDFGEPARA DDARQLFVLA GSAEEGLMTS
     ELAGVIRRLW RDGGVQACFS RSREYQLNDS ASYYLNDLDR ISQTNYIPTQ QDVLRTRVKT
     TGIVETHFTF KDLYFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN
     RMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKRS PLTICYPEYT GSNTYEEAAA
     YIQCQFEDLN RRKDTKEIYT HFTCATDTKN VQFVFDAVTD VIIKNNLKEC GLY
//