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GBG7_MOUSE
ID   GBG7_MOUSE              Reviewed;          68 AA.
AC   Q61016; Q8JZP6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;
DE   Flags: Precursor;
GN   Name=Gng7; Synonyms=Gngt7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Xiong X., Han J.;
RT   "Mouse G-protein gamma 7 cDNA.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-51.
RC   STRAIN=CF-1 / Harlan;
RX   PubMed=8858601;
RX   DOI=10.1002/(sici)1098-2795(199607)44:3<315::aid-mrd5>3.0.co;2-p;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation, and
RT   preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=12488442; DOI=10.1074/jbc.m211132200;
RA   Schwindinger W.F., Betz K.S., Giger K.E., Sabol A., Bronson S.K.,
RA   Robishaw J.D.;
RT   "Loss of G protein gamma 7 alters behavior and reduces striatal alpha(olf)
RT   level and cAMP production.";
RL   J. Biol. Chem. 278:6575-6579(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as a modulator or transducer in various transmembrane signaling
CC       systems. The beta and gamma chains are required for the GTPase
CC       activity, for replacement of GDP by GTP, and for G protein-effector
CC       interaction. Plays a role in the regulation of adenylyl cyclase
CC       signaling in certain regions of the brain. Plays a role in the
CC       formation or stabilzation of a G protein heterotrimer (G(olf) subunit
CC       alpha-beta-gamma-7) that is required for adenylyl cyclase activity in
CC       the striatum. {ECO:0000269|PubMed:12488442}.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Brain. Found in the hippocampus, striatum, midbrain
CC       and cortex. {ECO:0000269|PubMed:12488442}.
CC   -!- DISRUPTION PHENOTYPE: Mice display increased startle response but
CC       normal prepulse inhibition of the startle response. No effect on
CC       survival to weaning, fertility and mortality.
CC       {ECO:0000269|PubMed:12488442}.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; AY035844; AAK61365.1; -; mRNA.
DR   EMBL; BC034108; AAH34108.1; -; mRNA.
DR   EMBL; U38499; AAB01730.1; -; mRNA.
DR   AlphaFoldDB; Q61016; -.
DR   SMR; Q61016; -.
DR   BioGRID; 199992; 4.
DR   IntAct; Q61016; 1.
DR   STRING; 10090.ENSMUSP00000097061; -.
DR   iPTMnet; Q61016; -.
DR   PhosphoSitePlus; Q61016; -.
DR   MaxQB; Q61016; -.
DR   PaxDb; Q61016; -.
DR   PRIDE; Q61016; -.
DR   ProteomicsDB; 266778; -.
DR   Antibodypedia; 23032; 152 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000117805; ENSMUSP00000112409; ENSMUSG00000048240.
DR   Ensembl; ENSMUST00000118233; ENSMUSP00000114003; ENSMUSG00000048240.
DR   Ensembl; ENSMUST00000118465; ENSMUSP00000113798; ENSMUSG00000048240.
DR   MGI; MGI:95787; Gng7.
DR   VEuPathDB; HostDB:ENSMUSG00000048240; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01050000244858; -.
DR   HOGENOM; CLU_168377_3_1_1; -.
DR   InParanoid; Q61016; -.
DR   OMA; CDQHARS; -.
DR   PhylomeDB; Q61016; -.
DR   Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-MMU-202040; G-protein activation.
DR   Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
DR   Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-418597; G alpha (z) signalling events.
DR   Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR   Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR   Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Reactome; R-MMU-8964315; G beta:gamma signalling through BTK.
DR   Reactome; R-MMU-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-MMU-9634597; GPER1 signaling.
DR   Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   ChiTaRS; Gng7; mouse.
DR   PRO; PR:Q61016; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q61016; protein.
DR   Bgee; ENSMUSG00000048240; Expressed in caudate-putamen and 150 other tissues.
DR   ExpressionAtlas; Q61016; baseline and differential.
DR   Genevisible; Q61016; MM.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IMP:MGI.
DR   GO; GO:0045761; P:regulation of adenylate cyclase activity; IMP:UniProtKB.
DR   CDD; cd00068; GGL; 1.
DR   Gene3D; 4.10.260.10; -; 1.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   PANTHER; PTHR13809; PTHR13809; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; SSF48670; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Prenylation; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O60262"
FT   CHAIN           2..65
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-7"
FT                   /id="PRO_0000012637"
FT   PROPEP          66..68
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012638"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60262"
FT   MOD_RES         65
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           65
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   68 AA;  7480 MW;  0F07C667A29ADC07 CRC64;
     MSGTNNVAQA RKLVEQLRIE AGIERIKVSK ASSDLMGYCE QHARNDPLLV GVPASENPFK
     DKKPCIIL
 
 
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