GBG3_HUMAN
ID GBG3_HUMAN Reviewed; 75 AA.
AC P63215; B2R4S7; P29798; Q61014;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
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 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 [MRNA].
RC TISSUE=Pituitary;
RA Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10819326; DOI=10.1093/dnares/7.2.111;
RA Hurowitz E.H., Melnyk J.M., Chen Y.J., Kouros-Mehr H., Simon M.I.,
RA Shizuya H.;
RT "Genomic characterization of the human heterotrimeric G protein alpha,
RT beta, and gamma subunit genes.";
RL DNA Res. 7:111-120(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ding J.B., Yu L., Hua Y.M., Gong R.M., Xin Y.R., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homology to bovine
RT guanine nucleotide-binding protein gamma-3 subunit mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP INTERACTION WITH SCN8A.
RX PubMed=26900580; DOI=10.1002/acn3.276;
RA Wagnon J.L., Barker B.S., Hounshell J.A., Haaxma C.A., Shealy A., Moss T.,
RA Parikh S., Messer R.D., Patel M.K., Meisler M.H.;
RT "Pathogenic mechanism of recurrent mutations of SCN8A in epileptic
RT encephalopathy.";
RL Ann. Clin. Transl. Neurol. 3:114-123(2016).
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 Interacts with SCN8A (PubMed:26900580). {ECO:0000269|PubMed:26900580}.
CC -!- INTERACTION:
CC P63215; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1046668, EBI-741158;
CC P63215; Q9UHA2: SS18L2; NbExp=3; IntAct=EBI-1046668, EBI-10962400;
CC P63215; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-1046668, EBI-10259086;
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; AF092129; AAD40371.1; -; mRNA.
DR EMBL; AF188177; AAF04567.1; -; Genomic_DNA.
DR EMBL; AF087900; AAP97199.1; -; mRNA.
DR EMBL; AF493871; AAM12585.1; -; mRNA.
DR EMBL; AK311933; BAG34874.1; -; mRNA.
DR EMBL; CH471076; EAW74082.1; -; Genomic_DNA.
DR EMBL; BC015563; AAH15563.1; -; mRNA.
DR CCDS; CCDS8032.1; -.
DR RefSeq; NP_036334.1; NM_012202.4.
DR RefSeq; XP_006718563.1; XM_006718500.2.
DR AlphaFoldDB; P63215; -.
DR SMR; P63215; -.
DR BioGRID; 109047; 28.
DR CORUM; P63215; -.
DR IntAct; P63215; 16.
DR STRING; 9606.ENSP00000294117; -.
DR iPTMnet; P63215; -.
DR PhosphoSitePlus; P63215; -.
DR BioMuta; GNG3; -.
DR DMDM; 52783596; -.
DR MassIVE; P63215; -.
DR PaxDb; P63215; -.
DR PeptideAtlas; P63215; -.
DR PRIDE; P63215; -.
DR ProteomicsDB; 57507; -.
DR Antibodypedia; 28689; 93 antibodies from 21 providers.
DR DNASU; 2785; -.
DR Ensembl; ENST00000294117.6; ENSP00000294117.5; ENSG00000162188.6.
DR GeneID; 2785; -.
DR KEGG; hsa:2785; -.
DR MANE-Select; ENST00000294117.6; ENSP00000294117.5; NM_012202.5; NP_036334.1.
DR UCSC; uc001nuv.5; human.
DR CTD; 2785; -.
DR DisGeNET; 2785; -.
DR GeneCards; GNG3; -.
DR HGNC; HGNC:4405; GNG3.
DR HPA; ENSG00000162188; Group enriched (brain, choroid plexus).
DR MIM; 608941; gene.
DR neXtProt; NX_P63215; -.
DR OpenTargets; ENSG00000162188; -.
DR PharmGKB; PA28785; -.
DR VEuPathDB; HostDB:ENSG00000162188; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_0_1_1; -.
DR InParanoid; P63215; -.
DR OMA; CEAHACD; -.
DR OrthoDB; 1581168at2759; -.
DR PhylomeDB; P63215; -.
DR TreeFam; TF319909; -.
DR PathwayCommons; P63215; -.
DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
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; P63215; -.
DR SIGNOR; P63215; -.
DR BioGRID-ORCS; 2785; 27 hits in 1069 CRISPR screens.
DR GeneWiki; GNG3; -.
DR GenomeRNAi; 2785; -.
DR Pharos; P63215; Tbio.
DR PRO; PR:P63215; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P63215; protein.
DR Bgee; ENSG00000162188; Expressed in right frontal lobe and 134 other tissues.
DR Genevisible; P63215; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809; PTHR13809; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Phosphoprotein;
KW 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_0000012617"
FT PROPEP 73..75
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012618"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
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
