ID GNAI2_MOUSE Reviewed; 355 AA. AC P08752; Q3TXK7; Q6P1C0; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 5. DT 27-MAR-2024, entry version 212. 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=Gnai-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3092218; DOI=10.1073/pnas.83.18.6687; RA Sullivan K.A., Liao Y.-C., Alborzi A., Beiderman B., Chang F.-H., RA Masters S.B., Levinson A.D., Bourne H.R.; RT "Inhibitory and stimulatory G proteins of adenylate cyclase: cDNA and amino RT acid sequences of the alpha chains."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6687-6691(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-355. RX PubMed=8170357; DOI=10.1016/0169-328x(94)90267-4; RA Tachibana M., Asano T., Wilcox E., Yokotani N., Rivolta M.N., Fex J.; RT "G protein Gi2 alpha in the cochlea: cloning and selective occurrence in RT receptor cells."; RL Brain Res. Mol. Brain Res. 21:355-358(1994). RN [5] RP PROTEIN SEQUENCE OF 36-46; 55-67; 146-162; 182-193; 199-206; 250-258; RP 279-296 AND 319-331, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved CC as modulators or transducers in various transmembrane signaling CC systems. The G(i) proteins are involved in hormonal regulation of CC adenylate cyclase: they inhibit the cyclase in response to beta- CC adrenergic stimuli. May play a role in cell division. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The CC alpha chain contains the guanine nucleotide binding site. In this CC context, interacts with GNB2 (By similarity). Interacts with UNC5B (By CC similarity). Interacts with GPSM1 (By similarity). Interacts with RGS12 CC and RGS14 (By similarity). Interacts (inactive GDP-bound form) with CC NUCB1 (via GBA motif); the interaction leads to activation of GNAI3 (By CC similarity). Interacts (inactive GDP-bound form) with CCDC88C/DAPLE CC (via GBA motif) (By similarity). Interacts (inactive GDP-bound form) CC with CCDC8A/GIV (via GBA motif) (By similarity). Interacts with CXCR1 CC and CXCR2 (By similarity). {ECO:0000250|UniProtKB:P04897, CC ECO:0000250|UniProtKB:P04899}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome {ECO:0000250}. Cell membrane CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P04899}; Lipid-anchor CC {ECO:0000250|UniProtKB:P04899}. Note=Localizes in the centrosomes of CC interphase and mitotic cells. Detected at the cleavage furrow and/or CC the midbody (By similarity). {ECO:0000250}. 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; M13963; AAA37692.1; -; mRNA. DR EMBL; AK157998; BAE34308.1; -; mRNA. DR EMBL; AK159222; BAE34909.1; -; mRNA. DR EMBL; AK167388; BAE39478.1; -; mRNA. DR EMBL; BC065159; AAH65159.1; -; mRNA. DR EMBL; S71213; AAB30632.2; -; mRNA. DR CCDS; CCDS23502.1; -. DR PIR; B25889; RGMSI2. DR RefSeq; NP_032164.2; NM_008138.4. DR RefSeq; XP_006511700.1; XM_006511637.2. DR AlphaFoldDB; P08752; -. DR SMR; P08752; -. DR BioGRID; 199967; 45. DR CORUM; P08752; -. DR DIP; DIP-605N; -. DR IntAct; P08752; 6. DR STRING; 10090.ENSMUSP00000057543; -. DR GlyGen; P08752; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P08752; -. DR PhosphoSitePlus; P08752; -. DR SwissPalm; P08752; -. DR EPD; P08752; -. DR jPOST; P08752; -. DR MaxQB; P08752; -. DR PaxDb; 10090-ENSMUSP00000057543; -. DR PeptideAtlas; P08752; -. DR ProteomicsDB; 267639; -. DR Pumba; P08752; -. DR Antibodypedia; 2180; 344 antibodies from 35 providers. DR DNASU; 14678; -. DR Ensembl; ENSMUST00000055704.12; ENSMUSP00000057543.7; ENSMUSG00000032562.14. DR Ensembl; ENSMUST00000192615.6; ENSMUSP00000142326.2; ENSMUSG00000032562.14. DR GeneID; 14678; -. DR KEGG; mmu:14678; -. DR UCSC; uc009rml.1; mouse. DR AGR; MGI:95772; -. DR CTD; 2771; -. DR MGI; MGI:95772; Gnai2. DR VEuPathDB; HostDB:ENSMUSG00000032562; -. DR eggNOG; KOG0082; Eukaryota. DR GeneTree; ENSGT00940000155125; -. DR HOGENOM; CLU_014184_6_0_1; -. DR InParanoid; P08752; -. DR OMA; GMGCTVS; -. DR OrthoDB; 2897309at2759; -. DR PhylomeDB; P08752; -. DR TreeFam; TF300673; -. DR Reactome; R-MMU-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12. DR Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR BioGRID-ORCS; 14678; 3 hits in 81 CRISPR screens. DR ChiTaRS; Gnai2; mouse. DR PRO; PR:P08752; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; P08752; Protein. DR Bgee; ENSMUSG00000032562; Expressed in ileal epithelium and 291 other cell types or tissues. DR ExpressionAtlas; P08752; baseline and differential. DR GO; GO:0044297; C:cell body; IDA:MGI. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030425; C:dendrite; IDA:MGI. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; ISA:MGI. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:MGI. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; ISS:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; IPI:MGI. DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IMP:MGI. DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; ISO:MGI. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:MGI. DR GO; GO:0140199; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; ISO:MGI. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:MGI. DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; ISO:MGI. DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI. DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:MGI. DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:MGI. DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI. DR GO; GO:0035810; P:positive regulation of urine volume; ISO:MGI. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI. DR CDD; cd00066; G-alpha; 1. DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR PANTHER; PTHR10218:SF73; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-2; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. DR SMART; SM00275; G_alpha; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1. DR PROSITE; PS51882; G_ALPHA; 1. DR Genevisible; P08752; MM. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cell membrane; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; GTP-binding; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Myristate; Nucleotide-binding; Palmitate; KW Reference proteome; Transducer. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P04899" FT CHAIN 2..355 FT /note="Guanine nucleotide-binding protein G(i) subunit FT alpha-2" FT /id="PRO_0000203681" FT DOMAIN 32..355 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 174..182 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 197..206 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 266..273 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 325..330 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT BINDING 40..47 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 176..182 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 182 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 201..205 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 270..273 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 327 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250|UniProtKB:P04899" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CONFLICT 82 FT /note="M -> I (in Ref. 4; AAB30632)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="M -> L (in Ref. 1; AAA37692)" FT /evidence="ECO:0000305" FT CONFLICT 87 FT /note="A -> R (in Ref. 1; AAA37692)" FT /evidence="ECO:0000305" SQ SEQUENCE 355 AA; 40489 MW; 90AC64AFA713493E CRC64; MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPQR ADDARQLFAL SCAAEEQGML PEDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT QSSLTICFPE YTGANKYDEA ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF //