ID GBGT2_MOUSE Reviewed; 69 AA.
AC Q61017; Q9CWL5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2;
DE AltName: Full=G gamma-C;
DE AltName: Full=G-gamma-8;
DE Flags: Precursor;
GN Name=Gngt2; Synonyms=Gng8, Gngt8;
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;
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 [MRNA] OF 20-54.
RC STRAIN=CF-1 / Harlan; TISSUE=Retina;
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).
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; AK010554; BAB27023.1; -; mRNA.
DR EMBL; U38500; AAB01731.1; -; mRNA.
DR CCDS; CCDS25284.1; -.
DR RefSeq; NP_001033753.2; NM_001038664.2.
DR RefSeq; NP_001271322.1; NM_001284393.1.
DR RefSeq; NP_001271326.1; NM_001284397.1.
DR RefSeq; NP_075610.1; NM_023121.2.
DR RefSeq; XP_006532294.1; XM_006532231.3.
DR RefSeq; XP_011247039.1; XM_011248737.1.
DR RefSeq; XP_017169763.1; XM_017314274.1.
DR AlphaFoldDB; Q61017; -.
DR SMR; Q61017; -.
DR CORUM; Q61017; -.
DR STRING; 10090.ENSMUSP00000047586; -.
DR PhosphoSitePlus; Q61017; -.
DR EPD; Q61017; -.
DR MaxQB; Q61017; -.
DR PaxDb; 10090-ENSMUSP00000047586; -.
DR ProteomicsDB; 272937; -.
DR Antibodypedia; 30361; 108 antibodies from 22 providers.
DR DNASU; 14710; -.
DR Ensembl; ENSMUST00000036088.11; ENSMUSP00000047586.5; ENSMUSG00000038811.14.
DR Ensembl; ENSMUST00000100532.10; ENSMUSP00000098101.4; ENSMUSG00000038811.14.
DR Ensembl; ENSMUST00000107708.2; ENSMUSP00000103336.2; ENSMUSG00000038811.14.
DR Ensembl; ENSMUST00000107709.8; ENSMUSP00000103337.2; ENSMUSG00000038811.14.
DR Ensembl; ENSMUST00000107711.8; ENSMUSP00000103339.2; ENSMUSG00000038811.14.
DR Ensembl; ENSMUST00000107712.8; ENSMUSP00000103340.2; ENSMUSG00000038811.14.
DR Ensembl; ENSMUST00000107714.9; ENSMUSP00000103342.3; ENSMUSG00000038811.14.
DR GeneID; 14710; -.
DR KEGG; mmu:14710; -.
DR UCSC; uc007lau.1; mouse.
DR AGR; MGI:893584; -.
DR CTD; 2793; -.
DR MGI; MGI:893584; Gngt2.
DR VEuPathDB; HostDB:ENSMUSG00000038811; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01100000263525; -.
DR HOGENOM; CLU_168377_2_1_1; -.
DR InParanoid; Q61017; -.
DR OMA; SWLEIAW; -.
DR OrthoDB; 5344095at2759; -.
DR PhylomeDB; Q61017; -.
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; 14710; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Gngt2; mouse.
DR PRO; PR:Q61017; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61017; Protein.
DR Bgee; ENSMUSG00000038811; Expressed in retinal neural layer and 134 other cell types or tissues.
DR ExpressionAtlas; Q61017; baseline and differential.
DR Genevisible; Q61017; 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:0003924; F:GTPase activity; IEA:Ensembl.
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:SF28; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-T2; 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.
PE 3: Inferred from homology;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW Reference proteome; Transducer.
FT CHAIN 1..66
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-T2"
FT /id="PRO_0000012647"
FT PROPEP 67..69
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012648"
FT MOD_RES 66
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 66
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 69 AA; 7802 MW; 80A9586CD56BB304 CRC64;
MAQDLSEKEL LRMEVEQLKK EVKNPRDLIS KTGKEIKDYV EAQAGTDPLL KGIPEDKNPF
KEKGTCVLS
//
