GPCRDB: Swiss-Prot entry

ID   GNAI3_RAT      STANDARD;      PRT;   353 AA.
AC   P08753;
DT   01-NOV-1988 (Rel. 09, Created)
DT   01-OCT-1994 (Rel. 30, 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; Synonyms=Gnai-3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 
OC   Muridae; Murinae; Rattus. 
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=88198230; PubMed=2834384 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.;
RT   "Presence of three distinct molecular species of Gi protein alpha
RT   subunit. Structure of rat cDNAs and human genomic DNAs.";
RL   J. Biol. Chem. 263:6656-6664(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=88007678; PubMed=2820999 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Jones D.T., Reed R.R.;
RT   "Molecular cloning of five GTP-binding protein cDNA species from rat
RT   olfactory neuroepithelium.";
RL   J. Biol. Chem. 262:14241-14249(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 110-124.
RX   PubMed=2159473 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Linder M.E., Ewald D.A., Miller R.J., Gilman A.G.;
RT   "Purification and characterization of Go alpha and three types of Gi
RT   alpha after expression in Escherichia coli.";
RL   J. Biol. Chem. 265:8243-8251(1990).
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   -!- 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; J03219; AAA41224.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; M20713; AAA40823.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; E27423; RGRTI3.
DR   HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P08753; 4-347.
DR   Ensembl; ENSRNOG00000019465; Rattus_norvegicus
DR   RGD; 2714; Gnai3.
DR   GO; GO:0042588; C:zymogen granule; IDA.
DR   GO; GO:0006906; P:vesicle fusion; IDA.
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   CMR; P08753.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P08753.
DR   ProtoNet; P08753.
DR   ProtoMap; P08753.
DR   PRESAGE; P08753.
DR   DIP; P08753.
DR   ModBase; P08753.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   ADP-ribosylation; Direct protein sequencing; GTP-binding; Lipoprotein;
KW   Multigene family; Myristate; Palmitate; 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).
FT   LIPID         2      2       S-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   353 AA;  40391 MW;  8D8396349587E0F9 CRC64;
     GCTLSAEDKA AVERSKMIDR NLREDGEKAA KEVKLLLLGA GESGKSTIVK QMKIIHEDGY
     SEDECKQYKV VVYSNTIQSI IAIIRAMGRL KIDFGEAARA DDARQLFVLA GSAEEGVMTS
     ELAGVIKRLW RDGGVQACFS RSREYQLNDS ASYYLNDLDR ISQTNYIPTQ QDVLRTRVKT
     TGIVETHFTF KELYFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN
     RMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKRS PLTICYPEYT GSNTYEEAAA
     YIQCQFEDLN RRKDTKEVYT HFTCATDTKN VQFVFDAVTD VIIKNNLKEC GLY
//