ID   GBGT2_HUMAN             Reviewed;          69 AA.
AC   O14610; B2R746; D3DTW5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 185.
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   AltName: Full=G-gamma-9;
DE   AltName: Full=Guanine nucleotide binding protein gamma transducing activity polypeptide 2;
DE   Flags: Precursor;
GN   Name=GNGT2; Synonyms=GNG8, GNG9, GNGT8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Retina;
RX   PubMed=9286705; DOI=10.1006/geno.1997.4814;
RA   Ong O.C., Hu K., Rong H., Lee R.H., Fung B.K.-K.;
RT   "Gene structure and chromosome localization of the G gamma c subunit of
RT   human cone G-protein (GNGT2).";
RL   Genomics 44:101-109(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11714923; DOI=10.1110/ps.ps.26401;
RA   Cook L.A., Schey K.L., Cleator J.H., Wilcox M.D., Dingus J.,
RA   Hildebrandt J.D.;
RT   "Identification of a region in G protein gamma subunits conserved across
RT   species but hypervariable among subunit isoforms.";
RL   Protein Sci. 10:2548-2555(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
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   -!- TISSUE SPECIFICITY: Retinal cones.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; AF001160; AAB70039.1; -; Genomic_DNA.
DR   EMBL; AF001159; AAB70039.1; JOINED; Genomic_DNA.
DR   EMBL; AF365870; AAK53384.1; -; mRNA.
DR   EMBL; AF493876; AAM12590.1; -; mRNA.
DR   EMBL; AK312839; BAG35693.1; -; mRNA.
DR   EMBL; CH471109; EAW94688.1; -; Genomic_DNA.
DR   EMBL; CH471109; EAW94689.1; -; Genomic_DNA.
DR   EMBL; BC008663; AAH08663.1; -; mRNA.
DR   CCDS; CCDS11545.1; -.
DR   RefSeq; NP_001185683.1; NM_001198754.1.
DR   RefSeq; NP_001185684.1; NM_001198755.1.
DR   RefSeq; NP_001185685.1; NM_001198756.1.
DR   RefSeq; NP_113686.1; NM_031498.2.
DR   AlphaFoldDB; O14610; -.
DR   SMR; O14610; -.
DR   BioGRID; 109055; 6.
DR   STRING; 9606.ENSP00000421710; -.
DR   TCDB; 8.A.92.1.1; the g-protein AlphaBetaGama complex (gpc) family.
DR   iPTMnet; O14610; -.
DR   PhosphoSitePlus; O14610; -.
DR   BioMuta; GNGT2; -.
DR   MassIVE; O14610; -.
DR   MaxQB; O14610; -.
DR   PaxDb; 9606-ENSP00000426022; -.
DR   PeptideAtlas; O14610; -.
DR   ProteomicsDB; 48115; -.
DR   Antibodypedia; 30361; 108 antibodies from 22 providers.
DR   DNASU; 2793; -.
DR   Ensembl; ENST00000300406.6; ENSP00000300406.2; ENSG00000167083.7.
DR   Ensembl; ENST00000507680.6; ENSP00000421710.1; ENSG00000167083.7.
DR   Ensembl; ENST00000511277.5; ENSP00000426022.1; ENSG00000167083.7.
DR   Ensembl; ENST00000511673.1; ENSP00000422879.1; ENSG00000167083.7.
DR   Ensembl; ENST00000515635.5; ENSP00000423924.1; ENSG00000167083.7.
DR   GeneID; 2793; -.
DR   KEGG; hsa:2793; -.
DR   MANE-Select; ENST00000507680.6; ENSP00000421710.1; NM_001198754.2; NP_001185683.1.
DR   UCSC; uc002ioo.3; human.
DR   AGR; HGNC:4412; -.
DR   CTD; 2793; -.
DR   DisGeNET; 2793; -.
DR   GeneCards; GNGT2; -.
DR   HGNC; HGNC:4412; GNGT2.
DR   HPA; ENSG00000167083; Tissue enriched (retina).
DR   MIM; 139391; gene.
DR   neXtProt; NX_O14610; -.
DR   OpenTargets; ENSG00000167083; -.
DR   PharmGKB; PA28791; -.
DR   VEuPathDB; HostDB:ENSG00000167083; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01100000263525; -.
DR   HOGENOM; CLU_168377_2_1_1; -.
DR   InParanoid; O14610; -.
DR   OMA; SWLEIAW; -.
DR   OrthoDB; 5344095at2759; -.
DR   PhylomeDB; O14610; -.
DR   TreeFam; TF319909; -.
DR   PathwayCommons; O14610; -.
DR   Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-HSA-202040; G-protein activation.
DR   Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor.
DR   Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-HSA-4086398; Ca2+ pathway.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR   Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-418597; G alpha (z) signalling events.
DR   Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR   Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR   Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Reactome; R-HSA-8964315; G beta:gamma signalling through BTK.
DR   Reactome; R-HSA-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-HSA-9634597; GPER1 signaling.
DR   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   SignaLink; O14610; -.
DR   BioGRID-ORCS; 2793; 13 hits in 1145 CRISPR screens.
DR   GeneWiki; GNGT2; -.
DR   GenomeRNAi; 2793; -.
DR   Pharos; O14610; Tbio.
DR   PRO; PR:O14610; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O14610; Protein.
DR   Bgee; ENSG00000167083; Expressed in granulocyte and 117 other cell types or tissues.
DR   ExpressionAtlas; O14610; baseline and differential.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:MGI.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007602; P:phototransduction; NAS:UniProtKB.
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.
DR   Genevisible; O14610; HS.
PE   2: Evidence at transcript level;
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_0000012645"
FT   PROPEP          67..69
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012646"
FT   MOD_RES         66
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           66
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         11
FT                   /note="L -> F (in dbSNP:rs9895097)"
FT                   /id="VAR_049271"
SQ   SEQUENCE   69 AA;  7747 MW;  7ABD417F097F719B CRC64;
     MAQDLSEKDL LKMEVEQLKK EVKNTRIPIS KAGKEIKEYV EAQAGNDPFL KGIPEDKNPF
     KEKGGCLIS
//