ID   GBG12_MOUSE             Reviewed;          72 AA.
AC   Q9DAS9; Q544P3;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;
DE   Flags: Precursor;
GN   Name=Gng12;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cecum, Colon, Lung, Mammary gland, Placenta, and Sympathetic
RC   ganglion;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; TYR-42 AND SER-49, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, 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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; AK005561; BAB24121.1; -; mRNA.
DR   EMBL; AK033422; BAC28280.1; -; mRNA.
DR   EMBL; AK148765; BAE28660.1; -; mRNA.
DR   EMBL; AK159872; BAE35445.1; -; mRNA.
DR   EMBL; AK162342; BAE36863.1; -; mRNA.
DR   EMBL; AK166035; BAE38536.1; -; mRNA.
DR   EMBL; AK166299; BAE38688.1; -; mRNA.
DR   EMBL; BC040685; AAH40685.1; -; mRNA.
DR   CCDS; CCDS39502.1; -.
DR   RefSeq; NP_001171027.1; NM_001177556.1.
DR   RefSeq; NP_001171028.1; NM_001177557.1.
DR   RefSeq; NP_001171029.1; NM_001177558.1.
DR   RefSeq; NP_001171030.1; NM_001177559.1.
DR   RefSeq; NP_001171031.1; NM_001177560.1.
DR   RefSeq; NP_079554.1; NM_025278.5.
DR   RefSeq; XP_006505605.1; XM_006505542.3.
DR   AlphaFoldDB; Q9DAS9; -.
DR   SMR; Q9DAS9; -.
DR   BioGRID; 199985; 17.
DR   IntAct; Q9DAS9; 4.
DR   STRING; 10090.ENSMUSP00000046557; -.
DR   iPTMnet; Q9DAS9; -.
DR   PhosphoSitePlus; Q9DAS9; -.
DR   EPD; Q9DAS9; -.
DR   jPOST; Q9DAS9; -.
DR   MaxQB; Q9DAS9; -.
DR   PaxDb; 10090-ENSMUSP00000109863; -.
DR   PeptideAtlas; Q9DAS9; -.
DR   ProteomicsDB; 273418; -.
DR   Pumba; Q9DAS9; -.
DR   TopDownProteomics; Q9DAS9; -.
DR   Antibodypedia; 33413; 86 antibodies from 22 providers.
DR   DNASU; 14701; -.
DR   Ensembl; ENSMUST00000043148.13; ENSMUSP00000046557.7; ENSMUSG00000036402.14.
DR   Ensembl; ENSMUST00000114222.4; ENSMUSP00000109860.2; ENSMUSG00000036402.14.
DR   Ensembl; ENSMUST00000114224.8; ENSMUSP00000109862.2; ENSMUSG00000036402.14.
DR   Ensembl; ENSMUST00000114225.8; ENSMUSP00000109863.2; ENSMUSG00000036402.14.
DR   Ensembl; ENSMUST00000114226.8; ENSMUSP00000109864.2; ENSMUSG00000036402.14.
DR   Ensembl; ENSMUST00000114227.8; ENSMUSP00000109865.2; ENSMUSG00000036402.14.
DR   Ensembl; ENSMUST00000114228.8; ENSMUSP00000109866.2; ENSMUSG00000036402.14.
DR   GeneID; 14701; -.
DR   KEGG; mmu:14701; -.
DR   UCSC; uc009cew.2; mouse.
DR   AGR; MGI:1336171; -.
DR   CTD; 55970; -.
DR   MGI; MGI:1336171; Gng12.
DR   VEuPathDB; HostDB:ENSMUSG00000036402; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01100000263497; -.
DR   HOGENOM; CLU_168377_3_1_1; -.
DR   InParanoid; Q9DAS9; -.
DR   OMA; EKKSCAV; -.
DR   OrthoDB; 2872810at2759; -.
DR   PhylomeDB; Q9DAS9; -.
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; 14701; 6 hits in 77 CRISPR screens.
DR   ChiTaRS; Gng12; mouse.
DR   PRO; PR:Q9DAS9; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9DAS9; Protein.
DR   Bgee; ENSMUSG00000036402; Expressed in gastrula and 272 other cell types or tissues.
DR   ExpressionAtlas; Q9DAS9; baseline and differential.
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:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:SF9; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-12; 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; Q9DAS9; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q28024"
FT   CHAIN           2..69
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-12"
FT                   /id="PRO_0000012669"
FT   PROPEP          70..72
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012670"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28024"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         42
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         69
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           69
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   72 AA;  7997 MW;  A4D56F3BD697E7B4 CRC64;
     MSSKTASTNS IAQARRTVQQ LRLEASIERI KVSKASADLM SYCEEHARSD PLLMGIPTSE
     NPFKDKKTCI IL
//