ID   B1APZ0_HUMAN            Unreviewed;        75 AA.
AC   B1APZ0; A0A024R3R8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 147.
DE   RecName: Full=Guanine nucleotide-binding protein subunit gamma {ECO:0000256|RuleBase:RU004973};
GN   Name=GNG4 {ECO:0000313|EMBL:EAW70030.1};
GN   ORFNames=hCG_23460 {ECO:0000313|EMBL:EAW70030.1};
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 {ECO:0000313|EMBL:BAG34724.1};
RN   [1] {ECO:0000313|EMBL:EAW70030.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW70030.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton 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   [3] {ECO:0000313|EMBL:BAG34724.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU004973}.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma.
CC       {ECO:0000256|RuleBase:RU004973}.
CC   -!- INTERACTION:
CC       B1APZ0; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-10175453, EBI-1105213;
CC       B1APZ0; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10175453, EBI-739895;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342,
CC       ECO:0000256|RuleBase:RU004973}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU004973};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342,
CC       ECO:0000256|RuleBase:RU004973}.
CC   -!- SIMILARITY: Belongs to the G protein gamma family.
CC       {ECO:0000256|ARBA:ARBA00007431, ECO:0000256|RuleBase:RU004973}.
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; AK311781; BAG34724.1; -; mRNA.
DR   EMBL; CH471098; EAW70030.1; -; Genomic_DNA.
DR   RefSeq; NP_001092191.1; NM_001098721.2.
DR   RefSeq; NP_001092192.1; NM_001098722.2.
DR   RefSeq; NP_004476.1; NM_004485.4.
DR   RefSeq; XP_006711824.1; XM_006711761.3.
DR   RefSeq; XP_011542469.1; XM_011544167.2.
DR   RefSeq; XP_047274040.1; XM_047418084.1.
DR   RefSeq; XP_054192062.1; XM_054336087.1.
DR   RefSeq; XP_054192063.1; XM_054336088.1.
DR   RefSeq; XP_054192064.1; XM_054336089.1.
DR   AlphaFoldDB; B1APZ0; -.
DR   SMR; B1APZ0; -.
DR   IntAct; B1APZ0; 2.
DR   Antibodypedia; 34696; 95 antibodies from 25 providers.
DR   DNASU; 2786; -.
DR   GeneID; 2786; -.
DR   KEGG; hsa:2786; -.
DR   ClinPGx; PA28786; -.
DR   CTD; 2786; -.
DR   DisGeNET; 2786; -.
DR   VEuPathDB; HostDB:ENSG00000168243; -.
DR   HOGENOM; CLU_168377_0_1_1; -.
DR   OMA; TFACFRG; -.
DR   OrthoDB; 6264244at2759; -.
DR   BioGRID-ORCS; 2786; 13 hits in 1146 CRISPR screens.
DR   ChiTaRS; GNG4; human.
DR   ExpressionAtlas; B1APZ0; baseline and differential.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00068; GGL; 1.
DR   FunFam; 4.10.260.10:FF:000001; Guanine nucleotide-binding protein subunit gamma; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   InterPro; IPR001770; G-protein_gamma.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
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   1: Evidence at protein level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU004973};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU004973};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004973};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU004973}.
FT   DOMAIN          9..75
FT                   /note="G protein gamma"
FT                   /evidence="ECO:0000259|PROSITE:PS50058"
SQ   SEQUENCE   75 AA;  8389 MW;  42FAEF4728F83FF5 CRC64;
     MKEGMSNNST TSISQARKAV EQLKMEACMD RVKVSQAAAD LLAYCEAHVR EDPLIIPVPA
     SENPFREKKF FCTIL
//