GPCRDB: Swiss-Prot entry
ID GNAI2_MOUSE STANDARD; PRT; 354 AA.
AC P08752; Q6P1C0;
DT 01-NOV-1988 (Rel. 09, 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; Synonyms=Gnai-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=86313643; PubMed=3092218 [NCBI, ExPASy, EBI, Israel, Japan];
RA Sullivan K.A., Liao Y.-C., Alborzi A., Beiderman B., Chang F.-H.,
RA Masters S.B., Levinson A.D., Bourne H.R.;
RT "Inhibitory and stimulatory G proteins of adenylate cyclase: cDNA and
RT amino acid sequences of the alpha chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6687-6691(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6; TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 22-354.
RX MEDLINE=94224112; PubMed=8170357 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0169-328X(94)90267-4;
RA Tachibana M., Asano T., Wilcox E., Yokotani N., Rivolta M.N., Fex J.;
RT "G protein Gi2 alpha in the cochlea: cloning and selective occurrence
RT in receptor cells.";
RL Brain Res. Mol. Brain Res. 21:355-358(1994).
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 -!- 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; M13963; AAA37692.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC065159; AAH65159.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; S71213; AAB30632.2; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; B25889; RGMSI2.
DR HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P08752; 4-353.
DR Ensembl; ENSMUSG00000032562; Mus_musculus
DR MGI; MGI:95772; Gnai2.
DR GO; GO:0003924; F:GTPase activity; TAS.
DR GO; GO:0005515; F:protein binding; IPI.
DR GO; GO:0007213; P:acetylcholine receptor signaling, muscarini...; IMP.
DR GO; GO:0007193; P:G-protein signaling, adenylate cyclase inhi...; IMP.
DR GO; GO:0008016; P:regulation of heart contraction rate; IMP.
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; P08752.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P08752.
DR ProtoNet; P08752.
DR ProtoMap; P08752.
DR PRESAGE; P08752.
DR DIP; P08752.
DR ModBase; P08752.
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).
FT CONFLICT 81 81 L -> I (in Ref. 3).
FT CONFLICT 81 81 L -> M (in Ref. 2).
FT CONFLICT 86 86 A -> R (in Ref. 1).
SQ SEQUENCE 354 AA; 40340 MW; 40A7CA30EDDC3778 CRC64;
GCTVSAEDKA AAERSKMIDK NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEDGY
SEEECRQYRA VVYSNTIQSI LAIVKAMGNL QIDFADPQRA DDARQLFALS CAAEEQGMLP
EDLSGVIRRL WADHGVQACF GRSREYQLND SAAYYLNDLE RIAQSDYIPT QQDVLRTRVK
TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSAY DLVLAEDEEM
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKITQ SSLTICFPEY TGANKYDEAA
SYIQSKFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
//