GNAI1_HUMAN
ID GNAI1_HUMAN Reviewed; 354 AA.
AC P63096; A8KA88; B4E2V1; C9J3A4; P04898; P11015; P31871; Q5U074; Q8TAN5;
AC Q9UGA4;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-1;
DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein;
GN Name=GNAI1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Trachea;
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].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
RX PubMed=2834384; DOI=10.1016/s0021-9258(18)68692-2;
RA Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.;
RT "Presence of three distinct molecular species of Gi protein alpha subunit.
RT Structure of rat cDNAs and human genomic DNAs.";
RL J. Biol. Chem. 263:6656-6664(1988).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-354.
RX PubMed=3110783; DOI=10.1073/pnas.84.15.5115;
RA Bray P., Carter A., Guo V., Puckett C., Kamholz J., Spiegel A.,
RA Nirenberg M.;
RT "Human cDNA clones for an alpha subunit of Gi signal-transduction
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5115-5119(1987).
RN [11]
RP PROTEIN SEQUENCE OF 91-100 AND 162-176.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH RGS10.
RX PubMed=8774883; DOI=10.1038/383175a0;
RA Hunt T.W., Fields T.A., Casey P.J., Peralta E.G.;
RT "RGS10 is a selective activator of G alpha i GTPase activity.";
RL Nature 383:175-177(1996).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17635935; DOI=10.1083/jcb.200604114;
RA Cho H., Kehrl J.H.;
RT "Localization of Gi alpha proteins in the centrosomes and at the midbody:
RT implication for their role in cell division.";
RL J. Cell Biol. 178:245-255(2007).
RN [14]
RP INTERACTION WITH CCDC88A.
RX PubMed=19211784; DOI=10.1073/pnas.0900294106;
RA Garcia-Marcos M., Ghosh P., Farquhar M.G.;
RT "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates
RT Akt signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009).
RN [15]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22327364; DOI=10.1038/ncb2440;
RA Kiyomitsu T., Cheeseman I.M.;
RT "Chromosome- and spindle-pole-derived signals generate an intrinsic code
RT for spindle position and orientation.";
RL Nat. Cell Biol. 14:311-317(2012).
RN [18]
RP DEAMIDATION AT GLN-204 (MICROBIAL INFECTION).
RX PubMed=24141704; DOI=10.1038/nsmb.2688;
RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
RA Aktories K.;
RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation
RT of Gq and Gi proteins.";
RL Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN [19]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [20]
RP INTERACTION WITH CCDC88C.
RX PubMed=26126266; DOI=10.7554/elife.07091;
RA Aznar N., Midde K.K., Dunkel Y., Lopez-Sanchez I., Pavlova Y., Marivin A.,
RA Barbazan J., Murray F., Nitsche U., Janssen K.P., Willert K., Goel A.,
RA Abal M., Garcia-Marcos M., Ghosh P.;
RT "Daple is a novel non-receptor GEF required for trimeric G protein
RT activation in Wnt signaling.";
RL Elife 4:E07091-E07091(2015).
RN [21]
RP IDENTIFICATION IN A SPINDLE ORIENTATION COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
RA Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M., Macleod G.,
RA McNeill H., Cayouette M., Angers S.;
RT "SAPCD2 controls spindle orientation and asymmetric divisions by negatively
RT regulating the Galphai-LGN-NuMA ternary complex.";
RL Dev. Cell 36:50-62(2016).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-349 IN COMPLEX WITH RGS14 AND
RP GDP, AND INTERACTION WITH RGS14.
RX PubMed=11976690; DOI=10.1038/416878a;
RA Kimple R.J., Kimple M.E., Betts L., Sondek J., Siderovski D.P.;
RT "Structural determinants for GoLoco-induced inhibition of nucleotide
RT release by Galpha subunits.";
RL Nature 416:878-881(2002).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-354 IN COMPLEX WITH GDP.
RX PubMed=16004878; DOI=10.1016/j.str.2005.04.007;
RA Johnston C.A., Willard F.S., Jezyk M.R., Fredericks Z., Bodor E.T.,
RA Jones M.B., Blaesius R., Watts V.J., Harden T.K., Sondek J., Ramer J.K.,
RA Siderovski D.P.;
RT "Structure of Galpha(i1) bound to a GDP-selective peptide provides insight
RT into guanine nucleotide exchange.";
RL Structure 13:1069-1080(2005).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 31-354, AND MUTAGENESIS OF GLU-116
RP AND GLN-147.
RX PubMed=17603074; DOI=10.1016/j.jmb.2007.05.096;
RA Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P.,
RA Kuhlman B.;
RT "Structure-based protocol for identifying mutations that enhance protein-
RT protein binding affinities.";
RL J. Mol. Biol. 371:1392-1404(2007).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=17264214; DOI=10.1073/pnas.0608599104;
RA Johnston C.A., Siderovski D.P.;
RT "Structural basis for nucleotide exchange on G alpha i subunits and
RT receptor coupling specificity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2001-2006(2007).
RN [26]
RP ERRATUM OF PUBMED:17264214, AND RETRACTION NOTICE OF PUBMED:17264214.
RX PubMed=22408789; DOI=10.1073/pnas.1200173109;
RA Johnston C.A., Siderovski D.P.;
RL Proc. Natl. Acad. Sci. U.S.A. 109:1808-1808(2012).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 32-354 IN COMPLEX WITH RGS1;
RP RGS16; GDP; MAGNESIUM AND TRANSITION STATE ANALOG, FUNCTION, INTERACTION
RP WITH GNB1; GNG2; RGS1; RGS3; RGS4; RGS6; RGS7; RGS8; RGS10; RGS12; RGS14;
RP RGS16; RGS17; RGS18 AND RGS20, AND SUBUNIT.
RX PubMed=18434541; DOI=10.1073/pnas.0801508105;
RA Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
RA Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
RA Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
RT "Structural diversity in the RGS domain and its interaction with
RT heterotrimeric G protein alpha-subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 31-354 IN COMPLEX WITH RGS14 AND
RP GDP, AND MUTAGENESIS OF GLU-116; GLN-147 AND GLU-245.
RX PubMed=21115486; DOI=10.1074/jbc.m110.190496;
RA Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M.,
RA Kuhlman B., Willard F.S., Siderovski D.P.;
RT "Structural determinants of affinity enhancement between GoLoco motifs and
RT G-protein alpha subunit mutants.";
RL J. Biol. Chem. 286:3351-3358(2011).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 25-354 IN COMPLEX WITH GPSM2 AND
RP GDP, AND INTERACTION WITH GPSM2.
RX PubMed=22952234; DOI=10.1074/jbc.m112.391607;
RA Jia M., Li J., Zhu J., Wen W., Zhang M., Wang W.;
RT "Crystal structures of the scaffolding protein LGN reveal the general
RT mechanism by which GoLoco binding motifs inhibit the release of GDP from
RT Galphai.";
RL J. Biol. Chem. 287:36766-36776(2012).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 31-354 IN COMPLEX WITH GDP AND
RP MAGNESIUM, SUBUNIT, INTERACTION WITH GNB1; GNG1 AND RGS14, AND MUTAGENESIS
RP OF GLY-42.
RX PubMed=22383884; DOI=10.1371/journal.ppat.1002553;
RA Bosch D.E., Willard F.S., Ramanujam R., Kimple A.J., Willard M.D.,
RA Naqvi N.I., Siderovski D.P.;
RT "A P-loop mutation in Galpha subunits prevents transition to the active
RT state: implications for G-protein signaling in fungal pathogenesis.";
RL PLoS Pathog. 8:E1002553-E1002553(2012).
RN [31]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 2-354 IN COMPLEX WITH
RP GNB1; GNG2 AND HHV-5 US27, INTERACTION WITH HHV-5 US27 (MICROBIAL
RP INFECTION), STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) IN COMPLEX
RP WITH HOST GNB1; CX3CL1; GNG2 AND HHV-5 US28, AND INTERACTION WITH HHV-5
RP US28 (MICROBIAL INFECTION).
RX PubMed=35061538; DOI=10.1126/sciadv.abl5442;
RA Tsutsumi N., Maeda S., Qu Q., Voegele M., Jude K.M., Suomivuori C.M.,
RA Panova O., Waghray D., Kato H.E., Velasco A., Dror R.O., Skiniotis G.,
RA Kobilka B.K., Garcia K.C.;
RT "Atypical structural snapshots of human cytomegalovirus GPCR interactions
RT with host G proteins.";
RL Sci. Adv. 8:eabl5442-eabl5442(2022).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as
CC transducers downstream of G protein-coupled receptors (GPCRs) in
CC numerous signaling cascades. The alpha chain contains the guanine
CC nucleotide binding site and alternates between an active, GTP-bound
CC state and an inactive, GDP-bound state. Signaling by an activated GPCR
CC promotes GDP release and GTP binding. The alpha subunit has a low
CC GTPase activity that converts bound GTP to GDP, thereby terminating the
CC signal. Both GDP release and GTP hydrolysis are modulated by numerous
CC regulatory proteins (PubMed:8774883, PubMed:18434541). Signaling is
CC mediated via effector proteins, such as adenylate cyclase. Inhibits
CC adenylate cyclase activity, leading to decreased intracellular cAMP
CC levels (By similarity). The inactive GDP-bound form prevents the
CC association of RGS14 with centrosomes and is required for the
CC translocation of RGS14 from the cytoplasm to the plasma membrane.
CC Required for normal cytokinesis during mitosis (PubMed:17635935).
CC Required for cortical dynein-dynactin complex recruitment during
CC metaphase (PubMed:22327364). {ECO:0000250|UniProtKB:P10824,
CC ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:18434541,
CC ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:8774883}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC and gamma. Part of a spindle orientation complex at least composed of
CC GNAI1, GPSM2 and NUMA1 (PubMed:26766442). The alpha chain contains the
CC guanine nucleotide binding site. Identified in complex with the beta
CC subunit GNB1 and the gamma subunit GNG1 (PubMed:22383884). Identified
CC in complex with the beta subunit GNB1 and the gamma subunit GNG2
CC (PubMed:18434541). GTP binding causes dissociation of the heterotrimer,
CC liberating the individual subunits so that they can interact with
CC downstream effector proteins (PubMed:22383884). Interacts (GDP-bound
CC form) with GPSM1; this inhibits guanine nucleotide exchange and GTP
CC binding (By similarity). Interacts (GDP-bound form) with GPSM2 (via
CC GoLoco domains); this inhibits guanine nucleotide exchange
CC (PubMed:22952234). Interacts with RGS10; this strongly enhances GTP
CC hydrolysis (PubMed:8774883, PubMed:18434541). Interacts with RGS1 and
CC RGS16; this strongly enhances GTPase activity (PubMed:18434541).
CC Interacts with RGS4 (PubMed:18434541). Interacts with RGS12
CC (PubMed:18434541). Interacts (via active GTP- or inactive GDP-bound
CC forms) with RGS14 (via RGS and GoLoco domains) (PubMed:11976690,
CC PubMed:18434541, PubMed:21115486, PubMed:22383884). Interacts with
CC RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro)
CC (PubMed:18434541). Interacts (GDP-bound form) with RIC8A (via C-
CC terminus) (By similarity). Interacts (inactive GDP-bound form) with
CC NUCB1 (via GBA motif); the interaction leads to activation of GNAI1 (By
CC similarity). Interacts (inactive GDP-bound form) with CCDC88C/DAPLE
CC (via GBA motif); the interaction leads to activation of GNAI1
CC (PubMed:26126266). Interacts (inactive GDP-bound form) with CCDC8A/GIV
CC (via GBA motif) (PubMed:19211784). {ECO:0000250|UniProtKB:P10824,
CC ECO:0000269|PubMed:11976690, ECO:0000269|PubMed:16004878,
CC ECO:0000269|PubMed:17264214, ECO:0000269|PubMed:18434541,
CC ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:21115486,
CC ECO:0000269|PubMed:22383884, ECO:0000269|PubMed:22952234,
CC ECO:0000269|PubMed:26126266, ECO:0000269|PubMed:26766442,
CC ECO:0000269|PubMed:8774883}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC (HHV-5) US27; this interaction this interaction does not lead to the
CC catalytic activation of Gi complex and probably interferes with the
CC chemokine-Gi signaling. {ECO:0000269|PubMed:35061538}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC (HHV-5) US28; this interaction does not lead to the catalytic
CC activation of Gi complex and probably interferes with the chemokine-Gi
CC signaling. {ECO:0000269|PubMed:35061538}.
CC -!- INTERACTION:
CC P63096; P81274: GPSM2; NbExp=3; IntAct=EBI-618639, EBI-618655;
CC P63096; Q9Y4H4: GPSM3; NbExp=8; IntAct=EBI-618639, EBI-347538;
CC P63096; Q14980: NUMA1; NbExp=4; IntAct=EBI-618639, EBI-521611;
CC P63096; Q8IVA1: PCP2; NbExp=6; IntAct=EBI-618639, EBI-12250122;
CC P63096; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-618639, EBI-3918154;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm
CC {ECO:0000269|PubMed:17635935}. Cell membrane
CC {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:26766442}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:22327364}. Membrane
CC {ECO:0000250|UniProtKB:P10824}; Lipid-anchor
CC {ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805}.
CC Note=Localizes in the centrosomes of interphase and mitotic cells, but
CC not in centrosomes during cytokinesis. Detected at the cleavage furrow
CC or the midbody (PubMed:17635935). Localized at the plasma membrane
CC throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma
CC membrane. {ECO:0000250|UniProtKB:P10824, ECO:0000269|PubMed:17635935}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63096-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63096-2; Sequence=VSP_045215;
CC -!- PTM: Myristoylation at Gly-2 is required for membrane anchoring before
CC palmitoylation. {ECO:0000250|UniProtKB:P10824}.
CC -!- PTM: Palmitoylation at Cys-3 varies with membrane lipid composition.
CC {ECO:0000250|UniProtKB:P10824}.
CC -!- PTM: (Microbial infection) Deamidated at Gln-204 by Photorhabdus
CC asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric
CC GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby
CC activating RhoA. {ECO:0000269|PubMed:24141704}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; AF493905; AAM12619.1; -; mRNA.
DR EMBL; AF055013; AAC09361.1; -; mRNA.
DR EMBL; AL049933; CAB43212.2; -; mRNA.
DR EMBL; BT019775; AAV38580.1; -; mRNA.
DR EMBL; AK292953; BAF85642.1; -; mRNA.
DR EMBL; AK304442; BAG65263.1; -; mRNA.
DR EMBL; AC004159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471091; EAW77011.1; -; Genomic_DNA.
DR EMBL; BC026326; AAH26326.1; -; mRNA.
DR EMBL; M20596; AAA35893.1; -; Genomic_DNA.
DR EMBL; M20594; AAA35893.1; JOINED; Genomic_DNA.
DR EMBL; M20595; AAA35893.1; JOINED; Genomic_DNA.
DR EMBL; M17219; AAA52581.1; -; mRNA.
DR CCDS; CCDS5595.1; -. [P63096-1]
DR CCDS; CCDS59061.1; -. [P63096-2]
DR PIR; A28318; RGHUI1.
DR RefSeq; NP_001243343.1; NM_001256414.1. [P63096-2]
DR RefSeq; NP_002060.4; NM_002069.5. [P63096-1]
DR PDB; 1KJY; X-ray; 2.70 A; A/C=30-354.
DR PDB; 1Y3A; X-ray; 2.50 A; A/B/C/D=26-354.
DR PDB; 2G83; X-ray; 2.80 A; A/B=33-345.
DR PDB; 2GTP; X-ray; 2.55 A; A/B=32-354.
DR PDB; 2IK8; X-ray; 2.71 A; A/C=31-354.
DR PDB; 2OM2; X-ray; 2.20 A; A/C=31-354.
DR PDB; 2XNS; X-ray; 3.41 A; A/B=30-354.
DR PDB; 3ONW; X-ray; 2.38 A; A/B=31-354.
DR PDB; 3QE0; X-ray; 3.00 A; A/B/C=33-354.
DR PDB; 3QI2; X-ray; 2.80 A; A/B=31-354.
DR PDB; 3UMR; X-ray; 2.24 A; A=1-354.
DR PDB; 3UMS; X-ray; 2.60 A; A=1-354.
DR PDB; 4G5Q; X-ray; 2.90 A; A/B/C/D=25-354.
DR PDB; 5JS7; NMR; -; A=30-354.
DR PDB; 5JS8; NMR; -; A=30-354.
DR PDB; 5TDH; X-ray; 3.00 A; A/H=1-354.
DR PDB; 6CMO; EM; 4.50 A; A=1-354.
DR PDB; 6CRK; X-ray; 2.00 A; A=2-354.
DR PDB; 6DDE; EM; 3.50 A; A=1-354.
DR PDB; 6DDF; EM; 3.50 A; A=1-354.
DR PDB; 6KPF; EM; 2.90 A; A=1-354.
DR PDB; 6KPG; EM; 3.00 A; A=2-354.
DR PDB; 6LFM; EM; 3.50 A; A=2-354.
DR PDB; 6LFO; EM; 3.40 A; A=2-354.
DR PDB; 6LML; EM; 3.90 A; A=1-354.
DR PDB; 6N4B; EM; 3.00 A; A=1-354.
DR PDB; 6OMM; EM; 3.17 A; A=2-354.
DR PDB; 6OS9; EM; 3.00 A; A=1-354.
DR PDB; 6OSA; EM; 3.00 A; A=1-354.
DR PDB; 6OT0; EM; 3.90 A; A=1-354.
DR PDB; 6PB0; EM; 3.00 A; A=61-184.
DR PDB; 6PB1; EM; 2.80 A; A=61-184.
DR PDB; 6PT0; EM; 3.20 A; A=1-354.
DR PDB; 6QNO; EM; 4.38 A; A=1-354.
DR PDB; 6VU8; EM; 4.14 A; B=2-354.
DR PDB; 6XBJ; EM; 3.88 A; A=1-354.
DR PDB; 6XBK; EM; 3.24 A; A=1-354.
DR PDB; 6XBL; EM; 3.90 A; A=1-354.
DR PDB; 6XBM; EM; 3.15 A; A=1-354.
DR PDB; 7CMU; EM; 3.00 A; A=1-354.
DR PDB; 7CMV; EM; 2.70 A; A=1-354.
DR PDB; 7DB6; EM; 3.30 A; A=1-354.
DR PDB; 7DW9; EM; 2.60 A; A=1-19, A=61-181, A=229-242.
DR PDB; 7E2X; EM; 3.00 A; A=1-354.
DR PDB; 7E2Y; EM; 3.00 A; A=1-354.
DR PDB; 7E2Z; EM; 3.10 A; A=1-354.
DR PDB; 7E32; EM; 2.90 A; A=1-354.
DR PDB; 7E33; EM; 2.90 A; A=1-354.
DR PDB; 7E9G; EM; 3.50 A; A=1-354.
DR PDB; 7EB2; EM; 3.50 A; A=1-354.
DR PDB; 7EJX; EM; 2.40 A; A=1-354.
DR PDB; 7EO2; EM; 2.89 A; B=1-354.
DR PDB; 7EO4; EM; 2.86 A; B=1-354.
DR PDB; 7EVY; EM; 2.98 A; A=1-354.
DR PDB; 7EVZ; EM; 3.07 A; A=1-354.
DR PDB; 7EW0; EM; 3.42 A; A=1-354.
DR PDB; 7EW1; EM; 3.40 A; D=1-354.
DR PDB; 7EW2; EM; 3.10 A; A=1-354.
DR PDB; 7EW3; EM; 3.10 A; A=1-354.
DR PDB; 7EW4; EM; 3.20 A; A=1-354.
DR PDB; 7EW7; EM; 3.27 A; A=1-354.
DR PDB; 7EXD; EM; 3.40 A; A=1-354.
DR PDB; 7EZH; EM; 3.20 A; A=1-354.
DR PDB; 7EZK; EM; 3.10 A; A=4-19, A=61-181, A=229-242.
DR PDB; 7EZM; EM; 2.90 A; A=2-30.
DR PDB; 7F1Q; EM; 2.90 A; A=1-354.
DR PDB; 7F1R; EM; 3.00 A; A=1-354.
DR PDB; 7F1S; EM; 2.80 A; A=1-354.
DR PDB; 7F4D; EM; 3.00 A; A=4-19, A=61-181, A=229-242.
DR PDB; 7F4F; EM; 2.90 A; A=1-19, A=61-181, A=229-242.
DR PDB; 7F4H; EM; 2.70 A; A=4-19, A=61-181, A=229-242.
DR PDB; 7F4I; EM; 3.10 A; A=1-19, A=61-181, A=229-242.
DR PDB; 7JHJ; EM; 3.20 A; A=2-354.
DR PDB; 7JVR; EM; 2.80 A; A=1-354.
DR PDB; 7L0P; EM; 4.10 A; A=1-354.
DR PDB; 7L0Q; EM; 4.30 A; A=1-354.
DR PDB; 7L0R; EM; 4.20 A; A=1-354.
DR PDB; 7L0S; EM; 4.50 A; A=1-354.
DR PDB; 7MTS; EM; 3.20 A; C=1-354.
DR PDB; 7NA7; EM; 2.70 A; A=1-354.
DR PDB; 7NA8; EM; 2.70 A; A=1-354.
DR PDB; 7O7F; EM; 3.15 A; A=1-354.
DR PDB; 7P02; EM; 2.87 A; A=229-242.
DR PDB; 7RKM; EM; 3.50 A; A=2-354.
DR PDB; 7RKN; EM; 3.60 A; A=2-354.
DR PDB; 7RKX; EM; 3.10 A; A=2-354.
DR PDB; 7RKY; EM; 3.80 A; A=2-354.
DR PDB; 7S8M; EM; 2.54 A; B=1-354.
DR PDB; 7S8O; EM; 2.58 A; B=1-354.
DR PDB; 7T6S; EM; 3.00 A; A=2-354.
DR PDB; 7T6T; EM; 3.20 A; A=2-354.
DR PDB; 7T6U; EM; 2.90 A; A=2-354.
DR PDB; 7T6V; EM; 3.10 A; A=2-354.
DR PDB; 7TUZ; EM; 3.12 A; A=1-354.
DR PDB; 7VDH; EM; 2.90 A; A=1-354.
DR PDB; 7VDL; EM; 3.22 A; A=1-354.
DR PDB; 7VDM; EM; 2.98 A; A=1-354.
DR PDB; 7VGX; EM; 3.20 A; A=2-354.
DR PDB; 7VGY; EM; 3.10 A; B=2-354.
DR PDB; 7VGZ; EM; 3.30 A; C=2-354.
DR PDB; 7VH0; EM; 3.46 A; B=2-354.
DR PDB; 7VKT; EM; 2.90 A; B=1-354.
DR PDB; 7VL8; EM; 2.90 A; A=1-354.
DR PDB; 7VL9; EM; 2.60 A; A=1-354.
DR PDB; 7VLA; EM; 2.70 A; A=1-354.
DR PDB; 7VUG; EM; 3.20 A; A=2-354.
DR PDB; 7VUY; EM; 2.84 A; A=1-354.
DR PDB; 7VUZ; EM; 2.89 A; A=1-354.
DR PDB; 7VV3; EM; 2.97 A; A=1-354.
DR PDB; 7VV5; EM; 2.76 A; A=1-354.
DR PDB; 7WF7; EM; 3.40 A; B=1-354.
DR PDB; 7WVU; EM; 3.30 A; A=1-354.
DR PDBsum; 1KJY; -.
DR PDBsum; 1Y3A; -.
DR PDBsum; 2G83; -.
DR PDBsum; 2GTP; -.
DR PDBsum; 2IK8; -.
DR PDBsum; 2OM2; -.
DR PDBsum; 2XNS; -.
DR PDBsum; 3ONW; -.
DR PDBsum; 3QE0; -.
DR PDBsum; 3QI2; -.
DR PDBsum; 3UMR; -.
DR PDBsum; 3UMS; -.
DR PDBsum; 4G5Q; -.
DR PDBsum; 5JS7; -.
DR PDBsum; 5JS8; -.
DR PDBsum; 5TDH; -.
DR PDBsum; 6CMO; -.
DR PDBsum; 6CRK; -.
DR PDBsum; 6DDE; -.
DR PDBsum; 6DDF; -.
DR PDBsum; 6KPF; -.
DR PDBsum; 6KPG; -.
DR PDBsum; 6LFM; -.
DR PDBsum; 6LFO; -.
DR PDBsum; 6LML; -.
DR PDBsum; 6N4B; -.
DR PDBsum; 6OMM; -.
DR PDBsum; 6OS9; -.
DR PDBsum; 6OSA; -.
DR PDBsum; 6OT0; -.
DR PDBsum; 6PB0; -.
DR PDBsum; 6PB1; -.
DR PDBsum; 6PT0; -.
DR PDBsum; 6QNO; -.
DR PDBsum; 6VU8; -.
DR PDBsum; 6XBJ; -.
DR PDBsum; 6XBK; -.
DR PDBsum; 6XBL; -.
DR PDBsum; 6XBM; -.
DR PDBsum; 7CMU; -.
DR PDBsum; 7CMV; -.
DR PDBsum; 7DB6; -.
DR PDBsum; 7DW9; -.
DR PDBsum; 7E2X; -.
DR PDBsum; 7E2Y; -.
DR PDBsum; 7E2Z; -.
DR PDBsum; 7E32; -.
DR PDBsum; 7E33; -.
DR PDBsum; 7E9G; -.
DR PDBsum; 7EB2; -.
DR PDBsum; 7EJX; -.
DR PDBsum; 7EO2; -.
DR PDBsum; 7EO4; -.
DR PDBsum; 7EVY; -.
DR PDBsum; 7EVZ; -.
DR PDBsum; 7EW0; -.
DR PDBsum; 7EW1; -.
DR PDBsum; 7EW2; -.
DR PDBsum; 7EW3; -.
DR PDBsum; 7EW4; -.
DR PDBsum; 7EW7; -.
DR PDBsum; 7EXD; -.
DR PDBsum; 7EZH; -.
DR PDBsum; 7EZK; -.
DR PDBsum; 7EZM; -.
DR PDBsum; 7F1Q; -.
DR PDBsum; 7F1R; -.
DR PDBsum; 7F1S; -.
DR PDBsum; 7F4D; -.
DR PDBsum; 7F4F; -.
DR PDBsum; 7F4H; -.
DR PDBsum; 7F4I; -.
DR PDBsum; 7JHJ; -.
DR PDBsum; 7JVR; -.
DR PDBsum; 7L0P; -.
DR PDBsum; 7L0Q; -.
DR PDBsum; 7L0R; -.
DR PDBsum; 7L0S; -.
DR PDBsum; 7MTS; -.
DR PDBsum; 7NA7; -.
DR PDBsum; 7NA8; -.
DR PDBsum; 7O7F; -.
DR PDBsum; 7P02; -.
DR PDBsum; 7RKM; -.
DR PDBsum; 7RKN; -.
DR PDBsum; 7RKX; -.
DR PDBsum; 7RKY; -.
DR PDBsum; 7S8M; -.
DR PDBsum; 7S8O; -.
DR PDBsum; 7T6S; -.
DR PDBsum; 7T6T; -.
DR PDBsum; 7T6U; -.
DR PDBsum; 7T6V; -.
DR PDBsum; 7TUZ; -.
DR PDBsum; 7VDH; -.
DR PDBsum; 7VDL; -.
DR PDBsum; 7VDM; -.
DR PDBsum; 7VGX; -.
DR PDBsum; 7VGY; -.
DR PDBsum; 7VGZ; -.
DR PDBsum; 7VH0; -.
DR PDBsum; 7VKT; -.
DR PDBsum; 7VL8; -.
DR PDBsum; 7VL9; -.
DR PDBsum; 7VLA; -.
DR PDBsum; 7VUG; -.
DR PDBsum; 7VUY; -.
DR PDBsum; 7VUZ; -.
DR PDBsum; 7VV3; -.
DR PDBsum; 7VV5; -.
DR PDBsum; 7WF7; -.
DR PDBsum; 7WVU; -.
DR AlphaFoldDB; P63096; -.
DR SMR; P63096; -.
DR BioGRID; 109032; 137.
DR CORUM; P63096; -.
DR ELM; P63096; -.
DR IntAct; P63096; 64.
DR MINT; P63096; -.
DR STRING; 9606.ENSP00000343027; -.
DR BindingDB; P63096; -.
DR ChEMBL; CHEMBL4741; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB04444; Tetrafluoroaluminate Ion.
DR GlyGen; P63096; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P63096; -.
DR PhosphoSitePlus; P63096; -.
DR SwissPalm; P63096; -.
DR BioMuta; GNAI1; -.
DR DMDM; 52000964; -.
DR CPTAC; CPTAC-1243; -.
DR CPTAC; CPTAC-1244; -.
DR EPD; P63096; -.
DR jPOST; P63096; -.
DR MassIVE; P63096; -.
DR MaxQB; P63096; -.
DR PaxDb; P63096; -.
DR PeptideAtlas; P63096; -.
DR PRIDE; P63096; -.
DR ProteomicsDB; 57475; -. [P63096-1]
DR ProteomicsDB; 5853; -.
DR ABCD; P63096; 2 sequenced antibodies.
DR Antibodypedia; 15099; 301 antibodies from 37 providers.
DR DNASU; 2770; -.
DR Ensembl; ENST00000351004.8; ENSP00000343027.3; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000442586.2; ENSP00000391439.2; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000457358.7; ENSP00000410572.2; ENSG00000127955.17. [P63096-2]
DR Ensembl; ENST00000648098.1; ENSP00000497717.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000648306.1; ENSP00000497773.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000648412.1; ENSP00000497051.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000648476.1; ENSP00000497179.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000648663.1; ENSP00000497379.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000648832.1; ENSP00000497765.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000648877.1; ENSP00000497760.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000648953.1; ENSP00000496800.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000649225.1; ENSP00000496829.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000649267.1; ENSP00000497315.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000649487.1; ENSP00000498091.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000649796.2; ENSP00000497260.1; ENSG00000127955.17. [P63096-1]
DR Ensembl; ENST00000649855.1; ENSP00000497754.1; ENSG00000127955.17. [P63096-1]
DR GeneID; 2770; -.
DR KEGG; hsa:2770; -.
DR MANE-Select; ENST00000649796.2; ENSP00000497260.1; NM_002069.6; NP_002060.4.
DR UCSC; uc003uhb.2; human. [P63096-1]
DR CTD; 2770; -.
DR DisGeNET; 2770; -.
DR GeneCards; GNAI1; -.
DR HGNC; HGNC:4384; GNAI1.
DR HPA; ENSG00000127955; Low tissue specificity.
DR MIM; 139310; gene.
DR neXtProt; NX_P63096; -.
DR OpenTargets; ENSG00000127955; -.
DR PharmGKB; PA172; -.
DR VEuPathDB; HostDB:ENSG00000127955; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000153567; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P63096; -.
DR OMA; LWVDRGV; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P63096; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; P63096; -.
DR Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
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 SignaLink; P63096; -.
DR SIGNOR; P63096; -.
DR BioGRID-ORCS; 2770; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; GNAI1; human.
DR EvolutionaryTrace; P63096; -.
DR GeneWiki; GNAI1; -.
DR GenomeRNAi; 2770; -.
DR Pharos; P63096; Tbio.
DR PRO; PR:P63096; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P63096; protein.
DR Bgee; ENSG00000127955; Expressed in corpus callosum and 199 other tissues.
DR ExpressionAtlas; P63096; baseline and differential.
DR Genevisible; P63096; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0099738; C:cell cortex region; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISS:UniProtKB.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB.
DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0043434; P:response to peptide hormone; ISS:BHF-UCL.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00608; -.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; Cell cycle;
KW Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Host-virus interaction;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Mitosis; Myristate;
KW Nucleotide-binding; Nucleus; Palmitate; Reference proteome; Transducer;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20213681,
FT ECO:0000269|PubMed:25255805"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-1"
FT /id="PRO_0000203671"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 173..181
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 196..205
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 265..272
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 43..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21115486,
FT ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A,
FT ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP,
FT ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2,
FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW,
FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2,
FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS,
FT ECO:0007744|PDB:4G5Q"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18434541,
FT ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0"
FT BINDING 151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1KJY, ECO:0007744|PDB:2OM2,
FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW,
FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2,
FT ECO:0007744|PDB:4G5Q"
FT BINDING 175..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A,
FT ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP,
FT ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2,
FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW,
FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2,
FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS,
FT ECO:0007744|PDB:4G5Q"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18434541,
FT ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0"
FT BINDING 200..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21115486"
FT BINDING 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21115486,
FT ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A,
FT ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP,
FT ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2,
FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW,
FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2,
FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS,
FT ECO:0007744|PDB:4G5Q"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83,
FT ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8,
FT ECO:0007744|PDB:2OM2, ECO:0007744|PDB:3ONW,
FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2,
FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS,
FT ECO:0007744|PDB:4G5Q"
FT MOD_RES 178
FT /note="ADP-ribosylarginine; by cholera toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 204
FT /note="Deamidated glutamine; by Photorhabdus PAU_02230"
FT /evidence="ECO:0000269|PubMed:24141704"
FT MOD_RES 351
FT /note="ADP-ribosylcysteine; by pertussis toxin"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681,
FT ECO:0000269|PubMed:25255805"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045215"
FT MUTAGEN 42
FT /note="G->R: Abolishes switch to an activated conformation
FT and dissociation from beta and gamma subunits upon GTP
FT binding. Abolishes interaction with RGS family members."
FT /evidence="ECO:0000269|PubMed:22383884"
FT MUTAGEN 116
FT /note="E->L: Enhances interaction (inactive GDP-bound) with
FT RGS14."
FT /evidence="ECO:0000269|PubMed:17603074,
FT ECO:0000269|PubMed:21115486"
FT MUTAGEN 147
FT /note="Q->L: Enhances interaction (inactive GDP-bound) with
FT RGS14."
FT /evidence="ECO:0000269|PubMed:17603074,
FT ECO:0000269|PubMed:21115486"
FT MUTAGEN 245
FT /note="E->L: Enhances interaction (inactive GDP-bound) with
FT RGS14."
FT /evidence="ECO:0000269|PubMed:21115486"
FT CONFLICT 138
FT /note="A -> G (in Ref. 3; CAB43212)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="T -> A (in Ref. 8; AAH26326)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="H -> Y (in Ref. 4; AAV38580)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> M (in Ref. 4; AAV38580)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="P -> Q (in Ref. 8; AAH26326)"
FT /evidence="ECO:0000305"
FT HELIX 7..31
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:7S8M"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 70..91
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:4G5Q"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2G83"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:7JVR"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3UMS"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6PT0"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:7F1S"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:7EW3"
FT HELIX 329..346
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:3UMR"
SQ SEQUENCE 354 AA; 40361 MW; 9F88311B46E62DE3 CRC64;
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG
YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR ADDARQLFVL AGAAEEGFMT
AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK
TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
