GBG7_HUMAN
ID GBG7_HUMAN Reviewed; 68 AA.
AC O60262; B2R496;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;
DE Flags: Precursor;
GN Name=GNG7; Synonyms=GNGT7;
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].
RX PubMed=9600093; DOI=10.1006/bbrc.1998.8581;
RA Shibata K., Mori M., Tanaka S., Kitano S., Akiyoshi T.;
RT "Identification and cloning of human G-protein gamma 7, down-regulated in
RT pancreatic cancer.";
RL Biochem. Biophys. Res. Commun. 246:205-209(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=18219292; DOI=10.1038/sj.bjc.6604124;
RA Ohta M., Mimori K., Fukuyoshi Y., Kita Y., Motoyama K., Yamashita K.,
RA Ishii H., Inoue H., Mori M.;
RT "Clinical significance of the reduced expression of G protein gamma 7
RT (GNG7) in oesophageal cancer.";
RL Br. J. Cancer 98:410-417(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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. Plays a role in the regulation of adenylyl cyclase
CC signaling in certain regions of the brain. Plays a role in the
CC formation or stabilzation of a G protein heterotrimer (G(olf) subunit
CC alpha-beta-gamma-7) that is required for adenylyl cyclase activity in
CC the striatum (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC -!- INTERACTION:
CC O60262; Q9H8Y8: GORASP2; NbExp=6; IntAct=EBI-717760, EBI-739467;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues. Down-regulated
CC in pancreatic and esophageal cancer. {ECO:0000269|PubMed:18219292}.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB010414; BAA28348.1; -; mRNA.
DR EMBL; AF493874; AAM12588.1; -; mRNA.
DR EMBL; AK311750; BAG34693.1; -; mRNA.
DR EMBL; AC005512; AAC32595.1; -; Genomic_DNA.
DR EMBL; BC014466; AAH14466.1; -; mRNA.
DR EMBL; BC053630; AAH53630.1; -; mRNA.
DR CCDS; CCDS12091.1; -.
DR PIR; JW0050; JW0050.
DR RefSeq; NP_443079.1; NM_052847.2.
DR RefSeq; XP_016882095.1; XM_017026606.1.
DR AlphaFoldDB; O60262; -.
DR SMR; O60262; -.
DR BioGRID; 109050; 16.
DR CORUM; O60262; -.
DR IntAct; O60262; 9.
DR STRING; 9606.ENSP00000371594; -.
DR iPTMnet; O60262; -.
DR PhosphoSitePlus; O60262; -.
DR BioMuta; GNG7; -.
DR EPD; O60262; -.
DR jPOST; O60262; -.
DR MassIVE; O60262; -.
DR MaxQB; O60262; -.
DR PaxDb; O60262; -.
DR PeptideAtlas; O60262; -.
DR PRIDE; O60262; -.
DR ProteomicsDB; 49296; -.
DR Antibodypedia; 23032; 152 antibodies from 23 providers.
DR DNASU; 2788; -.
DR Ensembl; ENST00000382159.8; ENSP00000371594.2; ENSG00000176533.13.
DR GeneID; 2788; -.
DR KEGG; hsa:2788; -.
DR MANE-Select; ENST00000382159.8; ENSP00000371594.2; NM_052847.3; NP_443079.1.
DR UCSC; uc002lwd.3; human.
DR CTD; 2788; -.
DR DisGeNET; 2788; -.
DR GeneCards; GNG7; -.
DR HGNC; HGNC:4410; GNG7.
DR HPA; ENSG00000176533; Tissue enriched (brain).
DR MIM; 604430; gene.
DR neXtProt; NX_O60262; -.
DR OpenTargets; ENSG00000176533; -.
DR PharmGKB; PA28789; -.
DR VEuPathDB; HostDB:ENSG00000176533; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244858; -.
DR HOGENOM; CLU_168377_3_1_1; -.
DR InParanoid; O60262; -.
DR OMA; CDQHARS; -.
DR PhylomeDB; O60262; -.
DR TreeFam; TF319909; -.
DR PathwayCommons; O60262; -.
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; O60262; -.
DR BioGRID-ORCS; 2788; 12 hits in 1069 CRISPR screens.
DR ChiTaRS; GNG7; human.
DR GeneWiki; GNG7; -.
DR GenomeRNAi; 2788; -.
DR Pharos; O60262; Tbio.
DR PRO; PR:O60262; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60262; protein.
DR Bgee; ENSG00000176533; Expressed in nucleus accumbens and 191 other tissues.
DR ExpressionAtlas; O60262; baseline and differential.
DR Genevisible; O60262; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
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 Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW Prenylation; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..65
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-7"
FT /id="PRO_0000012635"
FT PROPEP 66..68
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012636"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 65
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 65
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 68 AA; 7522 MW; 704133C7BEC7FD72 CRC64;
MSATNNIAQA RKLVEQLRIE AGIERIKVSK AASDLMSYCE QHARNDPLLV GVPASENPFK
DKKPCIIL
