ID   GBG3_MOUSE              Reviewed;          75 AA.
AC   P63216; P29798; Q61014;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3;
DE   Flags: Precursor;
GN   Name=Gng3; Synonyms=Gngt3;
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.
RC   TISSUE=Brain;
RX   PubMed=7488078; DOI=10.1006/bbrc.1995.2600;
RA   Kalyanaraman S., Kalyanaraman V., Gautam N.;
RT   "A brain-specific G protein gamma subunit.";
RL   Biochem. Biophys. Res. Commun. 216:126-132(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9790771; DOI=10.1006/geno.1998.5508;
RA   Downes G.B., Copeland N.G., Jenkins N.A., Gautam N.;
RT   "Structure and mapping of the G protein gamma3 subunit gene and a
RT   divergently transcribed novel gene, Gng3lg.";
RL   Genomics 53:220-230(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 1-17 AND 25-31, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-68.
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; SER-9; THR-10 AND SER-12,
RP   AND 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.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC       Forms a complex with GNAO1 and GNB1. Interacts with SCN8A.
CC       {ECO:0000250|UniProtKB:P63215}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in brain. Low levels in
CC       testis.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; AF069953; AAC83941.1; -; Genomic_DNA.
DR   EMBL; AK004459; BAB23313.1; -; mRNA.
DR   EMBL; AK032646; BAC27969.1; -; mRNA.
DR   EMBL; BC029680; AAH29680.1; -; mRNA.
DR   EMBL; U38497; AAB01728.1; -; mRNA.
DR   CCDS; CCDS29550.1; -.
DR   PIR; JC4340; JC4340.
DR   RefSeq; NP_034446.1; NM_010316.3.
DR   AlphaFoldDB; P63216; -.
DR   SMR; P63216; -.
DR   BioGRID; 199988; 8.
DR   IntAct; P63216; 1.
DR   STRING; 10090.ENSMUSP00000093978; -.
DR   iPTMnet; P63216; -.
DR   PhosphoSitePlus; P63216; -.
DR   SwissPalm; P63216; -.
DR   MaxQB; P63216; -.
DR   PaxDb; 10090-ENSMUSP00000093978; -.
DR   PeptideAtlas; P63216; -.
DR   ProteomicsDB; 267768; -.
DR   Antibodypedia; 28689; 100 antibodies from 21 providers.
DR   DNASU; 14704; -.
DR   Ensembl; ENSMUST00000096259.6; ENSMUSP00000093978.5; ENSMUSG00000071658.6.
DR   GeneID; 14704; -.
DR   KEGG; mmu:14704; -.
DR   UCSC; uc008gnh.1; mouse.
DR   AGR; MGI:102704; -.
DR   CTD; 2785; -.
DR   MGI; MGI:102704; Gng3.
DR   VEuPathDB; HostDB:ENSMUSG00000071658; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01100000263497; -.
DR   HOGENOM; CLU_168377_0_1_1; -.
DR   InParanoid; P63216; -.
DR   OMA; NAHACED; -.
DR   PhylomeDB; P63216; -.
DR   TreeFam; TF319909; -.
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   BioGRID-ORCS; 14704; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Gng3; mouse.
DR   PRO; PR:P63216; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P63216; Protein.
DR   Bgee; ENSMUSG00000071658; Expressed in perirhinal cortex and 180 other cell types or tissues.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; ISA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; ISA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   CDD; cd00068; GGL; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   PANTHER; PTHR13809:SF11; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-3; 1.
DR   PANTHER; PTHR13809; GUANINE NUCLEOTIDE-BINDING PROTEIN GAMMA SUBUNIT; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
DR   Genevisible; P63216; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Lipoprotein; Membrane;
KW   Methylation; Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT   CHAIN           1..72
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-3"
FT                   /id="PRO_0000012619"
FT   PROPEP          73..75
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012620"
FT   MOD_RES         5
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         10
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         72
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           72
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   75 AA;  8305 MW;  35CC03965FE69A9D CRC64;
     MKGETPVNST MSIGQARKMV EQLKIEASLC RIKVSKAAAD LMTYCDAHAC EDPLITPVPT
     SENPFREKKF FCALL
//