ID   GBG2_MOUSE              Reviewed;          71 AA.
AC   P63213; P16874; Q3TYE8; Q61013; Q9TS47;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2;
DE   AltName: Full=G gamma-I;
DE   Flags: Precursor;
GN   Name=Gng2;
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 [GENOMIC DNA].
RX   PubMed=10191100; DOI=10.1006/geno.1999.5763;
RA   Downes G.B., Gilbert D.J., Copeland N.G., Gautam N., Jenkins N.A.;
RT   "Chromosomal mapping of five mouse G protein gamma subunits.";
RL   Genomics 57:173-176(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-52.
RC   STRAIN=CF-1 / Harlan; TISSUE=Embryo;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, and Testis;
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 (By
CC       similarity). In this context, interacts with GNB2 (By similarity). The
CC       heterodimer formed by GNB1 and GNG2 interacts with ARHGEF5 (By
CC       similarity). The heterodimer formed by GNB1 and GNG2 interacts with
CC       GRK2 (By similarity). {ECO:0000250|UniProtKB:P59768,
CC       ECO:0000250|UniProtKB:P63212}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Adrenal gland and brain.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; AF098489; AAD16272.1; -; Genomic_DNA.
DR   EMBL; AF098488; AAD16272.1; JOINED; Genomic_DNA.
DR   EMBL; AK003588; BAB22878.1; -; mRNA.
DR   EMBL; AK012405; BAB28219.1; -; mRNA.
DR   EMBL; AK036138; BAC29316.1; -; mRNA.
DR   EMBL; AK075698; BAC35896.1; -; mRNA.
DR   EMBL; AK158697; BAE34615.1; -; mRNA.
DR   EMBL; AK160396; BAE35765.1; -; mRNA.
DR   EMBL; BC021599; AAH21599.1; -; mRNA.
DR   EMBL; U38496; AAB01727.1; -; mRNA.
DR   CCDS; CCDS26840.1; -.
DR   PIR; D36204; D36204.
DR   RefSeq; NP_001033726.1; NM_001038637.1.
DR   RefSeq; NP_001272837.1; NM_001285908.1.
DR   RefSeq; NP_001272838.1; NM_001285909.1.
DR   RefSeq; NP_001272839.1; NM_001285910.1.
DR   RefSeq; NP_001272840.1; NM_001285911.1.
DR   RefSeq; NP_034445.1; NM_010315.4.
DR   PDB; 6RMV; X-ray; 1.94 A; B=1-71.
DR   PDB; 7PIV; EM; 2.86 A; G=1-71.
DR   PDB; 7Y12; EM; 3.10 A; C=1-71.
DR   PDB; 7Y15; EM; 2.90 A; C=1-71.
DR   PDB; 8IHB; EM; 2.85 A; C=3-71.
DR   PDB; 8IHF; EM; 2.97 A; C=2-71.
DR   PDB; 8IHH; EM; 3.06 A; C=2-71.
DR   PDB; 8IHI; EM; 3.11 A; C=2-71.
DR   PDB; 8IHJ; EM; 3.07 A; C=2-71.
DR   PDB; 8JSO; EM; 3.40 A; Y=1-71.
DR   PDBsum; 6RMV; -.
DR   PDBsum; 7PIV; -.
DR   PDBsum; 7Y12; -.
DR   PDBsum; 7Y15; -.
DR   PDBsum; 8IHB; -.
DR   PDBsum; 8IHF; -.
DR   PDBsum; 8IHH; -.
DR   PDBsum; 8IHI; -.
DR   PDBsum; 8IHJ; -.
DR   PDBsum; 8JSO; -.
DR   AlphaFoldDB; P63213; -.
DR   EMDB; EMD-13454; -.
DR   EMDB; EMD-33554; -.
DR   EMDB; EMD-33557; -.
DR   EMDB; EMD-35442; -.
DR   EMDB; EMD-35443; -.
DR   EMDB; EMD-35444; -.
DR   EMDB; EMD-35445; -.
DR   EMDB; EMD-35446; -.
DR   EMDB; EMD-36625; -.
DR   SMR; P63213; -.
DR   BioGRID; 199986; 20.
DR   CORUM; P63213; -.
DR   IntAct; P63213; 1.
DR   STRING; 10090.ENSMUSP00000125697; -.
DR   iPTMnet; P63213; -.
DR   PhosphoSitePlus; P63213; -.
DR   SwissPalm; P63213; -.
DR   EPD; P63213; -.
DR   jPOST; P63213; -.
DR   MaxQB; P63213; -.
DR   PaxDb; 10090-ENSMUSP00000125697; -.
DR   PeptideAtlas; P63213; -.
DR   ProteomicsDB; 271194; -.
DR   Pumba; P63213; -.
DR   TopDownProteomics; P63213; -.
DR   Antibodypedia; 198; 170 antibodies from 27 providers.
DR   DNASU; 14702; -.
DR   Ensembl; ENSMUST00000055100.14; ENSMUSP00000055256.8; ENSMUSG00000043004.14.
DR   Ensembl; ENSMUST00000159028.8; ENSMUSP00000125141.2; ENSMUSG00000043004.14.
DR   Ensembl; ENSMUST00000159073.8; ENSMUSP00000125000.2; ENSMUSG00000043004.14.
DR   Ensembl; ENSMUST00000160013.8; ENSMUSP00000125697.2; ENSMUSG00000043004.14.
DR   Ensembl; ENSMUST00000161247.2; ENSMUSP00000124725.2; ENSMUSG00000043004.14.
DR   Ensembl; ENSMUST00000162425.8; ENSMUSP00000124153.2; ENSMUSG00000043004.14.
DR   GeneID; 14702; -.
DR   KEGG; mmu:14702; -.
DR   UCSC; uc007siw.1; mouse.
DR   AGR; MGI:102705; -.
DR   CTD; 54331; -.
DR   MGI; MGI:102705; Gng2.
DR   VEuPathDB; HostDB:ENSMUSG00000043004; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01100000263497; -.
DR   HOGENOM; CLU_168377_0_1_1; -.
DR   InParanoid; P63213; -.
DR   OMA; GKQQPPM; -.
DR   OrthoDB; 2872810at2759; -.
DR   PhylomeDB; P63213; -.
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; 14702; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Gng2; mouse.
DR   PRO; PR:P63213; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P63213; Protein.
DR   Bgee; ENSMUSG00000043004; Expressed in cortical plate and 237 other cell types or tissues.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; ISS:CAFA.
DR   GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR   GO; GO:0048144; P:fibroblast proliferation; IDA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA: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:SF25; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-2; 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; P63213; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Lipoprotein; Membrane;
KW   Methylation; Prenylation; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63212"
FT   CHAIN           2..68
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-2"
FT                   /evidence="ECO:0000250|UniProtKB:P63212"
FT                   /id="PRO_0000012613"
FT   PROPEP          69..71
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000012614"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P63212"
FT   MOD_RES         68
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P63212"
FT   LIPID           68
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P63212"
FT   HELIX           10..23
FT                   /evidence="ECO:0007829|PDB:6RMV"
FT   HELIX           30..44
FT                   /evidence="ECO:0007829|PDB:6RMV"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:6RMV"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:6RMV"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:6RMV"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:7Y15"
SQ   SEQUENCE   71 AA;  7850 MW;  EDB74E4135E7A37A CRC64;
     MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP
     FREKKFFCAI L
//