GPCRDB: Swiss-Prot entry

ID   GNAI3_CAVPO    STANDARD;      PRT;   353 AA.
AC   P38403;
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(k), alpha subunit (G(i) alpha-3).
GN   Name=GNAI3;
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. G(k) is the stimulatory G protein of receptor-
CC       regulated K(+) channels.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
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; D21234; BAA04766.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P38403; 4-347.
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; P38403.
DR   ProtoNet; P38403.
DR   ProtoMap; P38403.
DR   PRESAGE; P38403.
DR   DIP; P38403.
DR   ModBase; P38403.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   ADP-ribosylation; GTP-binding; Lipoprotein; Multigene family;
KW   Myristate; Transducer.
FT   INIT_MET      0      0       By similarity.
FT   NP_BIND      39     46       GTP (By similarity).
FT   NP_BIND     199    203       GTP (By similarity).
FT   NP_BIND     268    271       GTP (By similarity).
FT   MOD_RES     177    177       ADP-ribosylarginine (by cholera toxin).
FT   MOD_RES     350    350       ADP-ribosylcysteine (by pertussis toxin).
FT   LIPID         1      1       N-myristoyl glycine (By similarity).
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
//