ID GNAI2_HUMAN Reviewed; 355 AA. AC P04899; B3KTZ0; B4DYA0; B4E2X5; Q6B6N3; Q8IZ71; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 15-FEB-2017, entry version 195. DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-2; DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein; GN Name=GNAI2; Synonyms=GNAI2B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3100330; DOI=10.1016/0014-5793(87)81428-X; RA Didsbury J.R., Ho Y.-S., Snyderman R.; RT "Human Gi protein alpha-subunit: deduction of amino acid structure RT from a cloned cDNA."; RL FEBS Lett. 211:160-164(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3120178; DOI=10.1073/pnas.84.22.7886; RA Beals C.R., Wilson C.B., Perlmutter R.M.; RT "A small multigene family encodes Gi signal-transduction proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7886-7890(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2834384; RA Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.; RT "Presence of three distinct molecular species of Gi protein alpha RT subunit. Structure of rat cDNAs and human genomic DNAs."; RL J. Biol. Chem. 263:6656-6664(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SGI2), AND FUNCTION (ISOFORM RP SGI2). RC TISSUE=Brain; RX PubMed=17550964; DOI=10.1242/jcs.005611; RA Lopez-Aranda M.F., Acevedo M.J., Gutierrez A., Koulen P., Khan Z.U.; RT "Role of a Galphai2 protein splice variant in the formation of an RT intracellular dopamine D2 receptor pool."; RL J. Cell Sci. 120:2171-2178(2007). RN [5] 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 RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5 AND 6). RC TISSUE=Brain, Teratocarcinoma, Testis, and Uterus; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Kidney, and Mammary gland; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39. RX PubMed=2837412; DOI=10.1016/0014-5793(88)80764-6; RA Weinstein L.S., Spiegel A.M., Carter A.D.; RT "Cloning and characterization of the human gene for the alpha-subunit RT of Gi2, a GTP-binding signal transduction protein."; RL FEBS Lett. 232:333-340(1988). RN [11] RP INTERACTION WITH UNC5B. RX PubMed=12359238; DOI=10.1016/S0006-291X(02)02277-5; RA Komatsuzaki K., Dalvin S., Kinane T.B.; RT "Modulation of G(ialpha(2)) signaling by the axonal guidance molecule RT UNC5H2."; RL Biochem. Biophys. Res. Commun. 297:898-905(2002). RN [12] 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 RT midbody: implication for their role in cell division."; RL J. Cell Biol. 178:245-255(2007). RN [13] 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., RA Buerckstuemmer T., 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 [14] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [15] RP DEAMIDATION AT GLN-205 (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 RT deamidation of Gq and Gi proteins."; RL Nat. Struct. Mol. Biol. 20:1273-1280(2013). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] 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., RA Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.; RT "Global profiling of co- and post-translationally N-myristoylated RT proteomes in human cells."; RL Nat. Commun. 5:4919-4919(2014). RN [18] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25807930; DOI=10.1002/anie.201500342; RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., RA Magee A.I., Tate E.W.; RT "Multifunctional reagents for quantitative proteome-wide analysis of RT protein modification in human cells and dynamic profiling of protein RT lipidation during vertebrate development."; RL Angew. Chem. Int. Ed. 54:5948-5951(2015). RN [19] 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., RA Ayoub D., 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 CC involved as modulators or transducers in various transmembrane CC signaling systems. The G(i) proteins are involved in hormonal CC regulation of adenylate cyclase: they inhibit the cyclase in CC response to beta-adrenergic stimuli. May play a role in cell CC division. {ECO:0000269|PubMed:17635935}. CC -!- FUNCTION: Isoform sGi2: Regulates the cell surface density of CC dopamine receptors DRD2 by sequestrating them as an intracellular CC pool. {ECO:0000269|PubMed:17550964}. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and CC gamma. The alpha chain contains the guanine nucleotide binding CC site. Interacts with GPSM1. Interacts with RGS12 and RGS14 (By CC similarity). Interacts with UNC5B. {ECO:0000250, CC ECO:0000269|PubMed:12359238}. CC -!- INTERACTION: CC P32302:CXCR5; NbExp=5; IntAct=EBI-353997, EBI-2835269; CC Q9Y4H4:GPSM3; NbExp=3; IntAct=EBI-353997, EBI-347538; CC Q15323:KRT31; NbExp=3; IntAct=EBI-353997, EBI-948001; CC Q6A162:KRT40; NbExp=3; IntAct=EBI-353997, EBI-10171697; CC P60410:KRTAP10-8; NbExp=3; IntAct=EBI-353997, EBI-10171774; CC Q99750:MDFI; NbExp=5; IntAct=EBI-353997, EBI-724076; CC P14598:NCF1; NbExp=2; IntAct=EBI-353997, EBI-395044; CC P19878:NCF2; NbExp=4; IntAct=EBI-353997, EBI-489611; CC Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-353997, EBI-945833; CC O76081-6:RGS20; NbExp=3; IntAct=EBI-353997, EBI-10178530; CC Q15654:TRIP6; NbExp=3; IntAct=EBI-353997, EBI-742327; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:17635935}. Cell membrane CC {ECO:0000269|PubMed:17635935}. Membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000305}. Note=Localizes in the centrosomes of CC interphase and mitotic cells. Detected at the cleavage furrow CC and/or the midbody. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=P04899-1; Sequence=Displayed; CC Name=2; CC IsoId=P04899-2; Sequence=VSP_017497; CC Name=3; CC IsoId=P04899-3; Sequence=VSP_043473; CC Note=No experimental confirmation available.; CC Name=sGi2; Synonyms=sGalphai2; CC IsoId=P04899-4; Sequence=VSP_043903; CC Name=5; CC IsoId=P04899-5; Sequence=VSP_054789; CC Note=No experimental confirmation available.; CC Name=6; CC IsoId=P04899-6; Sequence=VSP_054788; CC Note=No experimental confirmation available.; CC -!- PTM: (Microbial infection) Deamidated at Gln-205 by Photorhabdus CC asymbiotica toxin PAU_02230, blocking GTP hydrolysis of CC heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) CC proteins, thereby activating RhoA. {ECO:0000269|PubMed:24141704}. CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily. CC {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; X04828; CAA28512.1; -; mRNA. DR EMBL; J03004; AAA52556.1; ALT_SEQ; mRNA. DR EMBL; M20593; AAA35894.1; -; Genomic_DNA. DR EMBL; M20586; AAA35894.1; JOINED; Genomic_DNA. DR EMBL; M20587; AAA35894.1; JOINED; Genomic_DNA. DR EMBL; M20588; AAA35894.1; JOINED; Genomic_DNA. DR EMBL; M20589; AAA35894.1; JOINED; Genomic_DNA. DR EMBL; M20590; AAA35894.1; JOINED; Genomic_DNA. DR EMBL; M20591; AAA35894.1; JOINED; Genomic_DNA. DR EMBL; M20592; AAA35894.1; JOINED; Genomic_DNA. DR EMBL; AY677118; AAT78421.1; -; mRNA. DR EMBL; AF493906; AAM12620.1; -; mRNA. DR EMBL; AK096299; BAG53252.1; -; mRNA. DR EMBL; AK096595; BAG53334.1; -; mRNA. DR EMBL; AK302330; BAG63662.1; -; mRNA. DR EMBL; AK304473; BAG65287.1; -; mRNA. DR EMBL; AC002077; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U73166; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U73169; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW65053.1; -; Genomic_DNA. DR EMBL; CH471055; EAW65055.1; -; Genomic_DNA. DR EMBL; CH471055; EAW65056.1; -; Genomic_DNA. DR EMBL; BC012138; AAH12138.1; -; mRNA. DR EMBL; BC016995; AAH16995.1; -; mRNA. DR EMBL; X07854; CAA30703.1; -; Genomic_DNA. DR CCDS; CCDS2813.1; -. [P04899-1] DR CCDS; CCDS54587.1; -. [P04899-3] DR CCDS; CCDS63642.1; -. [P04899-5] DR CCDS; CCDS63644.1; -. [P04899-6] DR PIR; S02319; RGHUI2. DR RefSeq; NP_001159897.1; NM_001166425.1. [P04899-3] DR RefSeq; NP_001269546.1; NM_001282617.1. [P04899-6] DR RefSeq; NP_001269547.1; NM_001282618.1. DR RefSeq; NP_001269548.1; NM_001282619.1. [P04899-2] DR RefSeq; NP_001269549.1; NM_001282620.1. [P04899-5] DR RefSeq; NP_002061.1; NM_002070.3. [P04899-1] DR UniGene; Hs.77269; -. DR ProteinModelPortal; P04899; -. DR SMR; P04899; -. DR BioGrid; 109033; 117. DR DIP; DIP-602N; -. DR IntAct; P04899; 42. DR MINT; MINT-7901704; -. DR STRING; 9606.ENSP00000312999; -. DR iPTMnet; P04899; -. DR PhosphoSitePlus; P04899; -. DR SwissPalm; P04899; -. DR DMDM; 121023; -. DR EPD; P04899; -. DR MaxQB; P04899; -. DR PaxDb; P04899; -. DR PeptideAtlas; P04899; -. DR PRIDE; P04899; -. DR DNASU; 2771; -. DR Ensembl; ENST00000266027; ENSP00000266027; ENSG00000114353. [P04899-6] DR Ensembl; ENST00000313601; ENSP00000312999; ENSG00000114353. [P04899-1] DR Ensembl; ENST00000422163; ENSP00000406871; ENSG00000114353. [P04899-5] DR Ensembl; ENST00000440628; ENSP00000395736; ENSG00000114353. [P04899-6] DR Ensembl; ENST00000451956; ENSP00000406369; ENSG00000114353. [P04899-3] DR GeneID; 2771; -. DR KEGG; hsa:2771; -. DR UCSC; uc003cyp.3; human. [P04899-1] DR CTD; 2771; -. DR DisGeNET; 2771; -. DR GeneCards; GNAI2; -. DR H-InvDB; HIX0003320; -. DR HGNC; HGNC:4385; GNAI2. DR HPA; HPA007704; -. DR MalaCards; GNAI2; -. DR MIM; 139360; gene. DR neXtProt; NX_P04899; -. DR OpenTargets; ENSG00000114353; -. DR PharmGKB; PA24347; -. DR eggNOG; KOG0082; Eukaryota. DR eggNOG; ENOG410XNVQ; LUCA. DR GeneTree; ENSGT00760000118851; -. DR HOGENOM; HOG000038730; -. DR HOVERGEN; HBG063184; -. DR InParanoid; P04899; -. DR KO; K04630; -. DR OMA; YSGANKY; -. DR OrthoDB; EOG090B0813; -. DR PhylomeDB; P04899; -. DR TreeFam; TF300673; -. DR Reactome; R-HSA-112043; PLC beta mediated events. DR Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-HSA-202040; G-protein activation. 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-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR SignaLink; P04899; -. DR SIGNOR; P04899; -. DR ChiTaRS; GNAI2; human. DR GeneWiki; GNAI2; -. DR GenomeRNAi; 2771; -. DR PRO; PR:P04899; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000114353; -. DR CleanEx; HS_GNAI2; -. DR ExpressionAtlas; P04899; baseline and differential. DR Genevisible; P04899; HS. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central. DR GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; TAS:Reactome. DR GO; GO:0003924; F:GTPase activity; TAS:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004871; F:signal transducer activity; IBA:GO_Central. DR GO; GO:0000186; P:activation of MAPKK activity; IEA:Ensembl. DR GO; GO:0001973; P:adenosine receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007193; P:adenylate cyclase-inhibiting 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:0008283; P:cell proliferation; IEA:Ensembl. DR GO; GO:0007213; P:G-protein coupled acetylcholine receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central. DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl. DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc. DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0006457; P:protein folding; TAS:Reactome. DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00066; G-alpha; 1. DR Gene3D; 1.10.400.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. 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; 2. PE 1: Evidence at protein level; KW ADP-ribosylation; Alternative splicing; Cell cycle; Cell division; KW Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; KW GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Myristate; Nucleotide-binding; Palmitate; Reference proteome; KW Transducer. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895, FT ECO:0000269|PubMed:22223895, FT ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:25807930}. FT CHAIN 2 355 Guanine nucleotide-binding protein G(i) FT subunit alpha-2. FT /FTId=PRO_0000203679. FT NP_BIND 40 47 GTP. {ECO:0000250|UniProtKB:P63096}. FT NP_BIND 176 182 GTP. {ECO:0000250}. FT NP_BIND 201 205 GTP. {ECO:0000250|UniProtKB:P63096}. FT NP_BIND 270 273 GTP. {ECO:0000250|UniProtKB:P63096}. FT METAL 47 47 Magnesium. {ECO:0000250}. FT METAL 182 182 Magnesium. {ECO:0000250}. FT BINDING 327 327 GTP; via amide nitrogen. {ECO:0000250}. FT MOD_RES 179 179 ADP-ribosylarginine; by cholera toxin. FT {ECO:0000250}. FT MOD_RES 205 205 Deamidated glutamine; by Photorhabdus FT PAU_02230. {ECO:0000269|PubMed:24141704}. FT MOD_RES 352 352 ADP-ribosylcysteine; by pertussis toxin. FT {ECO:0000250}. FT LIPID 2 2 N-myristoyl glycine. FT {ECO:0000269|PubMed:22223895, FT ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:25807930}. FT LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}. FT VAR_SEQ 1 52 Missing (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054788. FT VAR_SEQ 1 39 MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL FT -> MEYAGHLPASSAQGTILACTSCT (in isoform FT 2). {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_017497. FT VAR_SEQ 1 39 MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL FT -> MR (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043473. FT VAR_SEQ 1 39 MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL FT -> MTEGVKTLGWTKQKGGCHWGRSE (in isoform FT 5). {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054789. FT VAR_SEQ 332 355 NVQFVFDAVTDVIIKNNLKDCGLF -> SRKLFRETYLKLS FT GPDQHPHPSPAPAPPLSSDSVP (in isoform sGi2). FT {ECO:0000303|PubMed:17550964}. FT /FTId=VSP_043903. SQ SEQUENCE 355 AA; 40451 MW; BE6D6FF720CF3DCC CRC64; MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPSR ADDARQLFAL SCTAEEQGVL PDDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYDEA ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF //