ID GNAI3_HUMAN Reviewed; 354 AA. AC P08754; P17539; Q5TZX1; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 247. DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-3; DE AltName: Full=G(i) alpha-3; GN Name=GNAI3; 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=3109953; DOI=10.1016/0014-5793(87)81228-0; RA Didsbury J.R., Snyderman R.; RT "Molecular cloning of a new human G protein. Evidence for two Gi alpha-like RT protein families."; RL FEBS Lett. 219:259-263(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. 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; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2452165; DOI=10.1016/s0021-9258(18)68706-x; RA Codina J., Olate J., Abramowitz J., Mattera R., Cook R.G., Birnbaumer L.; RT "Alpha i-3 cDNA encodes the alpha subunit of Gk, the stimulatory G protein RT of receptor-regulated K+ channels."; RL J. Biol. Chem. 263:6746-6750(1988). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3132707; DOI=10.1073/pnas.85.12.4153; RA Kim S., Ang S.L., Bloch D.B., Bloch K.D., Kawahara Y., Tolman C., Lee R., RA Seidman J.G., Neer E.J.; RT "Identification of cDNA encoding an additional alpha subunit of a human RT GTP-binding protein: expression of three alpha i subtypes in human tissues RT and cell lines."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4153-4157(1988). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-354. RX PubMed=2440724; DOI=10.1016/0014-5793(87)80900-6; RA Suki W.N., Abramowitz J., Mattera R., Codina J., Birnbaumer L.; RT "The human genome encodes at least three non-allelic G proteins with alpha RT i-type subunits."; RL FEBS Lett. 220:187-192(1987). RN [12] RP FUNCTION. RX PubMed=2535845; DOI=10.1016/s0021-9258(17)31281-4; RA Mattera R., Yatani A., Kirsch G.E., Graf R., Okabe K., Olate J., Codina J., RA Brown A.M., Birnbaumer L.; RT "Recombinant alpha i-3 subunit of G protein activates Gk-gated K+ RT channels."; RL J. Biol. Chem. 264:465-471(1989). RN [13] 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 [14] RP FUNCTION, INTERACTION WITH RGS14, AND SUBCELLULAR LOCATION. RX PubMed=16870394; DOI=10.1016/j.cellsig.2006.06.002; RA Shu F.J., Ramineni S., Amyot W., Hepler J.R.; RT "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR RT domain of RGS14 influence its dynamic subcellular localization."; RL Cell. Signal. 19:163-176(2007). RN [15] 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 [16] 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 [17] RP IDENTIFICATION IN COMPLEX WITH CCDC88A AND EGFR. RX PubMed=20462955; DOI=10.1091/mbc.e10-01-0028; RA Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., RA Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.; RT "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor RT and determines whether cells migrate or proliferate."; RL Mol. Biol. Cell 21:2338-2354(2010). RN [18] 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 [19] 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 [20] RP INTERACTION WITH CCDC88A AND INSR. RX PubMed=25187647; DOI=10.1091/mbc.e14-05-0978; RA Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., RA Kufareva I., Abagyan R., Ghosh P.; RT "Structural basis for activation of trimeric Gi proteins by multiple growth RT factor receptors via GIV/Girdin."; RL Mol. Biol. Cell 25:3654-3671(2014). RN [21] 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 [22] RP INTERACTION WITH CCDC88C, AND MUTAGENESIS OF TRP-211; PHE-215; LYS-248 AND RP TRP-258. 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 [23] 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). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=27864364; DOI=10.1074/jbc.m116.764431; RA Parag-Sharma K., Leyme A., DiGiacomo V., Marivin A., Broselid S., RA Garcia-Marcos M.; RT "Membrane recruitment of the non-receptor protein GIV/Girdin (Galpha- RT interacting, Vesicle-associated Protein/Girdin) is sufficient for RT activating heterotrimeric G protein signaling."; RL J. Biol. Chem. 291:27098-27111(2016). RN [25] RP INTERACTION WITH PLCD4, AND MUTAGENESIS OF LYS-35; LEU-36; LEU-37; LEU-39; RP GLY-42; ILE-184; TRP-211; PHE-215; VAL-218; LEU-249; SER-252; ASN-256; RP LYS-257; TRP-258 AND PHE-259. RX PubMed=30194280; DOI=10.1074/jbc.ra118.003580; RA Maziarz M., Broselid S., DiGiacomo V., Park J.C., Luebbers A., RA Garcia-Navarrete L., Blanco-Canosa J.B., Baillie G.S., Garcia-Marcos M.; RT "A biochemical and genetic discovery pipeline identifies PLCdelta4b as a RT nonreceptor activator of heterotrimeric G-proteins."; RL J. Biol. Chem. 293:16964-16983(2018). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-350 IN COMPLEX WITH GDP AND RP RGS10, FUNCTION, AND INTERACTION WITH RGS8 AND RGS10. 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 [27] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 4-350 IN COMPLEX WITH RGS2; RP MAGNESIUM AND GDP, LACK OF INTERACTION WITH RGS2, INTERACTION WITH RGS16, RP AND FUNCTION. RX PubMed=19478087; DOI=10.1074/jbc.m109.024711; RA Kimple A.J., Soundararajan M., Hutsell S.Q., Roos A.K., Urban D.J., RA Setola V., Temple B.R., Roth B.L., Knapp S., Willard F.S., Siderovski D.P.; RT "Structural determinants of G-protein alpha subunit selectivity by RT regulator of G-protein signaling 2 (RGS2)."; RL J. Biol. Chem. 284:19402-19411(2009). RN [28] 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 [29] RP VARIANT ARCND1 ARG-40, AND INVOLVEMENT IN ARCND1. RX PubMed=22560091; DOI=10.1016/j.ajhg.2012.04.002; RA Rieder M.J., Green G.E., Park S.S., Stamper B.D., Gordon C.T., RA Johnson J.M., Cunniff C.M., Smith J.D., Emery S.B., Lyonnet S., Amiel J., RA Holder M., Heggie A.A., Bamshad M.J., Nickerson D.A., Cox T.C., Hing A.V., RA Horst J.A., Cunningham M.L.; RT "A human homeotic transformation resulting from mutations in PLCB4 and RT GNAI3 causes auriculocondylar syndrome."; RL Am. J. Hum. Genet. 90:907-914(2012). RN [30] RP ERRATUM OF PUBMED:22560091. RA Rieder M.J., Green G.E., Park S.S., Stamper B.D., Gordon C.T., RA Johnson J.M., Cunniff C.M., Smith J.D., Emery S.B., Lyonnet S., Amiel J., RA Holder M., Heggie A.A., Bamshad M.J., Nickerson D.A., Cox T.C., Hing A.V., RA Horst J.A., Cunningham M.L.; RL Am. J. Hum. Genet. 90:1116-1116(2012). RN [31] RP VARIANT ARCND1 ARG-47, AND INVOLVEMENT IN ARCND1. RX PubMed=23315542; DOI=10.1136/jmedgenet-2012-101331; RA Gordon C.T., Vuillot A., Marlin S., Gerkes E., Henderson A., Al-Kindy A., RA Holder-Espinasse M., Park S.S., Omarjee A., Sanchis-Borja M., Bdira E.B., RA Oufadem M., Sikkema-Raddatz B., Stewart A., Palmer R., McGowan R., RA Petit F., Delobel B., Speicher M.R., Aurora P., Kilner D., Pellerin P., RA Simon M., Bonnefont J.P., Tobias E.S., Garcia-Minaur S., RA Bitner-Glindzicz M., Lindholm P., Meijer B.A., Abadie V., Denoyelle F., RA Vazquez M.P., Rotky-Fast C., Couloigner V., Pierrot S., Manach Y., RA Breton S., Hendriks Y.M., Munnich A., Jakobsen L., Kroisel P., Lin A., RA Kaban L.B., Basel-Vanagaite L., Wilson L., Cunningham M.L., Lyonnet S., RA Amiel J.; RT "Heterogeneity of mutational mechanisms and modes of inheritance in RT auriculocondylar syndrome."; RL J. Med. Genet. 50:174-186(2013). RN [32] RP VARIANT ARCND1 ASN-47. RX PubMed=34789173; DOI=10.1186/s12884-021-04238-x; RA Liu X., Sun W., Wang J., Chu G., He R., Zhang B., Zhao Y.; RT "Prenatal diagnosis of auriculocondylar syndrome with a novel missense RT variant of GNAI3: a case report."; RL BMC Pregnancy Childbirth 21:780-780(2021). RN [33] RP VARIANTS ARCND1 SER-45 AND ASN-47. RX PubMed=35170830; DOI=10.1002/humu.24349; RA Vegas N., Demir Z., Gordon C.T., Breton S., Romanelli Tavares V.L., RA Moisset H., Zechi-Ceide R., Kokitsu-Nakata N.M., Kido Y., Marlin S., RA Gherbi Halem S., Meerschaut I., Callewaert B., Chung B., Revencu N., RA Lehalle D., Petit F., Propst E.J., Papsin B.C., Phillips J.H., Jakobsen L., RA Le Tanno P., Thevenon J., McGaughran J., Gerkes E.H., Leoni C., Kroisel P., RA Tan T.Y., Henderson A., Terhal P., Basel-Salmon L., Alkindy A., White S.M., RA Passos-Bueno M.R., Pingault V., De Pontual L., Amiel J.; RT "Further delineation of auriculocondylar syndrome based on 14 novel cases RT and reassessment of 25 published cases."; RL Hum. Mutat. 43:582-594(2022). CC -!- FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G CC proteins) function as transducers downstream of G protein-coupled CC receptors (GPCRs) in numerous signaling cascades. The alpha chain CC contains the guanine nucleotide binding site and alternates between an CC active, GTP-bound state and an inactive, GDP-bound state. Signaling by CC an activated GPCR promotes GDP release and GTP binding. The alpha CC subunit has a low GTPase activity that converts bound GTP to GDP, CC thereby terminating the signal. Both GDP release and GTP hydrolysis are CC modulated by numerous regulatory proteins (PubMed:8774883, CC PubMed:18434541, PubMed:19478087). Signaling is mediated via effector CC proteins, such as adenylate cyclase. Inhibits adenylate cyclase CC activity, leading to decreased intracellular cAMP levels CC (PubMed:19478087). Stimulates the activity of receptor-regulated K(+) CC channels (PubMed:2535845). The active GTP-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. May CC play a role in cell division (PubMed:17635935). CC {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:18434541, CC ECO:0000269|PubMed:2535845, ECO:0000269|PubMed:8774883}. CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta CC and gamma. The alpha subunit contains the guanine nucleotide binding CC site. GTP binding causes dissociation of the heterotrimer, liberating CC the individual subunits so that they can interact with downstream CC effector proteins. Forms a complex with CCDC88A/GIV and EGFR which CC leads to enhanced EGFR signaling and triggering of cell migration; CC ligand stimulation is required for recruitment of GNAI3 to the complex CC (PubMed:20462955). Interacts (inactive GDP-bound form) with CCDC88A/GIV CC (via GBA motif); the interaction leads to activation of GNAI3 CC (PubMed:19211784, PubMed:20462955). Interacts (inactive GDP-bound form) CC with CCDC88C/DAPLE (via GBA motif); the interaction leads to activation CC of GNAI3 (PubMed:26126266). Interacts (inactive GDP-bound form) with CC NUCB1 (via GBA motif) and NUCB2 (via GBA motif); the interaction leads CC to activation of GNAI3 (By similarity). Interacts (inactive GDP-bound CC form) with PLCD4 (via GBA motif); the interaction leads to activation CC of GNAI3 (PubMed:30194280). Interacts with INSR; the interaction is CC probably mediated by CCDC88A/GIV (PubMed:25187647). Interacts with CC GPSM1 (By similarity). Interacts (GDP-bound form) with GPSM2 (via CC GoLoco domains) (PubMed:22952234). Does not interact with RGS2 CC (PubMed:19478087). Interacts with RGS8 and RGS10; this strongly CC enhances the intrinsic GTPase activity (PubMed:8774883, CC PubMed:18434541). Interacts with RGS16; this strongly enhances the CC intrinsic GTPase activity (PubMed:19478087). Interacts with RGS12 (By CC similarity). Interacts (via active GTP- or inactive GDP-bound form) CC with RGS14 (By similarity). {ECO:0000250|UniProtKB:P08753, CC ECO:0000250|UniProtKB:Q9DC51, ECO:0000269|PubMed:18434541, CC ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:19478087, CC ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:22952234, CC ECO:0000269|PubMed:25187647, ECO:0000269|PubMed:26126266, CC ECO:0000269|PubMed:30194280, ECO:0000305}. CC -!- INTERACTION: CC P08754; P81274: GPSM2; NbExp=3; IntAct=EBI-357563, EBI-618655; CC P08754; Q9Y4H4: GPSM3; NbExp=8; IntAct=EBI-357563, EBI-347538; CC P08754; Q8IVA1: PCP2; NbExp=9; IntAct=EBI-357563, EBI-12250122; CC P08754; Q9UPV7: PHF24; NbExp=3; IntAct=EBI-357563, EBI-17717171; CC P08754; O43566: RGS14; NbExp=4; IntAct=EBI-357563, EBI-750603; CC P08754; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-357563, EBI-3918154; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. Cell CC membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:27864364}; CC Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:17635935}. CC Note=Localizes in the centrosomes of interphase and mitotic cells. CC Detected at the cleavage furrow and/or the midbody. CC {ECO:0000269|PubMed:17635935}. 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 -!- DISEASE: Auriculocondylar syndrome 1 (ARCND1) [MIM:602483]: An CC autosomal dominant form of auriculocondylar syndrome, a craniofacial CC malformation syndrome characterized by variable mandibular anomalies, CC including mild to severe micrognathia, temporomandibular joint CC ankylosis, cleft palate, and a characteristic ear malformation that CC consists of separation of the lobule from the external ear, giving the CC appearance of a question mark (question-mark ear). Other frequently CC described features include prominent cheeks, cupped and posteriorly CC rotated ears, preauricular tags, and microstomia. Glossoptosis, CC masticatory abnormalities, orthodontic problems, and malocclusion occur CC in a majority of affected subjects. {ECO:0000269|PubMed:22560091, CC ECO:0000269|PubMed:23315542, ECO:0000269|PubMed:34789173, CC ECO:0000269|PubMed:35170830}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; M27543; AAA52579.1; -; mRNA. DR EMBL; J03005; AAA52557.1; -; mRNA. DR EMBL; M20604; AAA35895.1; -; Genomic_DNA. DR EMBL; M20597; AAA35895.1; JOINED; Genomic_DNA. DR EMBL; M20598; AAA35895.1; JOINED; Genomic_DNA. DR EMBL; M20599; AAA35895.1; JOINED; Genomic_DNA. DR EMBL; M20600; AAA35895.1; JOINED; Genomic_DNA. DR EMBL; M20601; AAA35895.1; JOINED; Genomic_DNA. DR EMBL; M20602; AAA35895.1; JOINED; Genomic_DNA. DR EMBL; M20603; AAA35895.1; JOINED; Genomic_DNA. DR EMBL; J03198; AAA35896.1; -; mRNA. DR EMBL; J03238; AAA35939.1; -; mRNA. DR EMBL; AF493907; AAM12621.1; -; mRNA. DR EMBL; BT019973; AAV38776.1; -; mRNA. DR EMBL; BT019974; AAV38777.1; -; mRNA. DR EMBL; AK312252; BAG35184.1; -; mRNA. DR EMBL; CH471122; EAW56393.1; -; Genomic_DNA. DR EMBL; BC025285; AAH25285.1; -; mRNA. DR CCDS; CCDS802.1; -. DR PIR; S02348; RGHUI3. DR RefSeq; NP_006487.1; NM_006496.3. DR PDB; 2IHB; X-ray; 2.71 A; A=32-354. DR PDB; 2ODE; X-ray; 1.90 A; A/C=4-350. DR PDB; 2V4Z; X-ray; 2.80 A; A=4-350. DR PDB; 4G5O; X-ray; 2.90 A; A/B/C/D=25-354. DR PDB; 4G5R; X-ray; 3.48 A; A/B/C/D=25-354. DR PDB; 4G5S; X-ray; 3.62 A; A/B/C/D=25-354. DR PDB; 7E9H; EM; 4.00 A; A=1-354. DR PDB; 7KH0; EM; 2.80 A; A=2-19. DR PDB; 7RA3; EM; 3.24 A; A=1-19. DR PDB; 7RGP; EM; 2.90 A; A=4-19. DR PDB; 7T10; EM; 2.50 A; A=1-354. DR PDB; 7T11; EM; 2.70 A; A=1-354. DR PDB; 7X6I; EM; 3.93 A; E/F/G/H=1-354. DR PDB; 8GVX; EM; 3.91 A; E/F/G/H=1-354. DR PDB; 8JD6; EM; 3.40 A; A=1-354. DR PDBsum; 2IHB; -. DR PDBsum; 2ODE; -. DR PDBsum; 2V4Z; -. DR PDBsum; 4G5O; -. DR PDBsum; 4G5R; -. DR PDBsum; 4G5S; -. DR PDBsum; 7E9H; -. DR PDBsum; 7KH0; -. DR PDBsum; 7RA3; -. DR PDBsum; 7RGP; -. DR PDBsum; 7T10; -. DR PDBsum; 7T11; -. DR PDBsum; 7X6I; -. DR PDBsum; 8GVX; -. DR PDBsum; 8JD6; -. DR AlphaFoldDB; P08754; -. DR BMRB; P08754; -. DR EMDB; EMD-22872; -. DR EMDB; EMD-24334; -. DR EMDB; EMD-24453; -. DR EMDB; EMD-25586; -. DR EMDB; EMD-25587; -. DR EMDB; EMD-31032; -. DR EMDB; EMD-36177; -. DR SMR; P08754; -. DR BioGRID; 109035; 220. DR IntAct; P08754; 87. DR MINT; P08754; -. DR STRING; 9606.ENSP00000358867; -. DR BindingDB; P08754; -. DR ChEMBL; CHEMBL4221; -. DR GlyCosmos; P08754; 3 sites, 1 glycan. DR GlyGen; P08754; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P08754; -. DR PhosphoSitePlus; P08754; -. DR SwissPalm; P08754; -. DR BioMuta; GNAI3; -. DR DMDM; 120996; -. DR CPTAC; CPTAC-1245; -. DR CPTAC; CPTAC-1246; -. DR EPD; P08754; -. DR jPOST; P08754; -. DR MassIVE; P08754; -. DR PaxDb; 9606-ENSP00000358867; -. DR PeptideAtlas; P08754; -. DR PRIDE; P08754; -. DR ProteomicsDB; 52164; -. DR Pumba; P08754; -. DR Antibodypedia; 20068; 277 antibodies from 33 providers. DR DNASU; 2773; -. DR Ensembl; ENST00000369851.7; ENSP00000358867.4; ENSG00000065135.12. DR GeneID; 2773; -. DR KEGG; hsa:2773; -. DR MANE-Select; ENST00000369851.7; ENSP00000358867.4; NM_006496.4; NP_006487.1. DR UCSC; uc001dxz.4; human. DR AGR; HGNC:4387; -. DR CTD; 2773; -. DR DisGeNET; 2773; -. DR GeneCards; GNAI3; -. DR HGNC; HGNC:4387; GNAI3. DR HPA; ENSG00000065135; Low tissue specificity. DR MalaCards; GNAI3; -. DR MIM; 139370; gene. DR MIM; 602483; phenotype. DR neXtProt; NX_P08754; -. DR OpenTargets; ENSG00000065135; -. DR Orphanet; 137888; Auriculocondylar syndrome. DR PharmGKB; PA173; -. DR VEuPathDB; HostDB:ENSG00000065135; -. DR eggNOG; KOG0082; Eukaryota. DR GeneTree; ENSGT00940000153567; -. DR HOGENOM; CLU_014184_6_0_1; -. DR InParanoid; P08754; -. DR OMA; ICYPEYC; -. DR OrthoDB; 2897309at2759; -. DR PhylomeDB; P08754; -. DR TreeFam; TF300673; -. DR PathwayCommons; P08754; -. DR Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12. 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-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; P08754; -. DR SIGNOR; P08754; -. DR BioGRID-ORCS; 2773; 14 hits in 1155 CRISPR screens. DR ChiTaRS; GNAI3; human. DR EvolutionaryTrace; P08754; -. DR GeneWiki; GNAI3; -. DR GenomeRNAi; 2773; -. DR Pharos; P08754; Tbio. DR PRO; PR:P08754; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P08754; Protein. DR Bgee; ENSG00000065135; Expressed in esophagus squamous epithelium and 209 other cell types or tissues. 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:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. 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:0019003; F:GDP binding; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0007212; P:dopamine receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB. DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc. DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:UniProtKB. 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:SF230; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-3; 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; P08754; HS. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Cell cycle; Cell division; Cell membrane; KW Cytoplasm; Cytoskeleton; Disease variant; GTP-binding; Lipoprotein; KW Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding; KW Palmitate; Reference proteome; Transducer. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:25255805" FT CHAIN 2..354 FT /note="Guanine nucleotide-binding protein G(i) subunit FT alpha-3" FT /id="PRO_0000203692" 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:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, FT ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, FT ECO:0007744|PDB:4G5R, ECO:0007744|PDB:4G5S" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:19478087, FT ECO:0007744|PDB:2V4Z" FT BINDING 150..151 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, FT ECO:0007744|PDB:4G5R, ECO:0007744|PDB:4G5S" FT BINDING 175..181 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, FT ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, FT ECO:0007744|PDB:4G5R, ECO:0007744|PDB:4G5S" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:19478087, FT ECO:0007744|PDB:2V4Z" FT BINDING 200..204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:19478087, FT ECO:0007744|PDB:2V4Z" FT BINDING 269..272 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, FT ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, FT ECO:0007744|PDB:4G5R, ECO:0007744|PDB:4G5S" FT BINDING 326 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, FT ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, FT ECO:0007744|PDB:4G5R" 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:25255805" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT VARIANT 40 FT /note="G -> R (in ARCND1; likely pathogenic; FT dbSNP:rs387907178)" FT /evidence="ECO:0000269|PubMed:22560091" FT /id="VAR_068558" FT VARIANT 45 FT /note="G -> S (in ARCND1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:35170830" FT /id="VAR_088775" FT VARIANT 47 FT /note="S -> N (in ARCND1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:34789173, FT ECO:0000269|PubMed:35170830" FT /id="VAR_088776" FT VARIANT 47 FT /note="S -> R (in ARCND1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:23315542" FT /id="VAR_088777" FT MUTAGEN 35 FT /note="K->A: Decreased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 36 FT /note="L->A: Increased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 37 FT /note="L->A: No effect on binding to PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 39 FT /note="L->A: Decreased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 42 FT /note="G->R: Decreased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 184 FT /note="I->A: No effect on binding to PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 211 FT /note="W->A: Decreased affinity for CCDC88C and PLCD4." FT /evidence="ECO:0000269|PubMed:26126266, FT ECO:0000269|PubMed:30194280" FT MUTAGEN 215 FT /note="F->A: Decreased affinity for CCDC88C and PLCD4." FT /evidence="ECO:0000269|PubMed:26126266, FT ECO:0000269|PubMed:30194280" FT MUTAGEN 218 FT /note="V->A: No effect on binding to PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 248 FT /note="K->M: No effect on binding to CCDC88C." FT /evidence="ECO:0000269|PubMed:26126266" FT MUTAGEN 249 FT /note="L->H: Decreased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 249 FT /note="L->V: No effect on binding to PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 252 FT /note="S->A: Increased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 252 FT /note="S->D: Decreased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 256 FT /note="N->A: Decreased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 256 FT /note="N->E: Decreased affinity for PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 257 FT /note="K->A: No effect on binding to PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT MUTAGEN 258 FT /note="W->F: Increased affinity for PLCD4. No effect on FT binding to CCDC88C." FT /evidence="ECO:0000269|PubMed:26126266, FT ECO:0000269|PubMed:30194280" FT MUTAGEN 259 FT /note="F->A: No effect on binding to PLCD4." FT /evidence="ECO:0000269|PubMed:30194280" FT CONFLICT 21 FT /note="R -> C (in Ref. 11; no nucleotide entry)" FT /evidence="ECO:0000305" FT HELIX 7..31 FT /evidence="ECO:0007829|PDB:7T10" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:7T10" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 63..68 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 70..91 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 100..110 FT /evidence="ECO:0007829|PDB:2ODE" FT TURN 111..116 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 121..131 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 134..141 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 152..157 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 159..162 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 183..191 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 194..201 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 205..214 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 242..254 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 262..269 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 271..278 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:8JD6" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 296..308 FT /evidence="ECO:0007829|PDB:2ODE" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:2ODE" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 329..346 FT /evidence="ECO:0007829|PDB:2ODE" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:8JD6" SQ SEQUENCE 354 AA; 40532 MW; EAB6B4DD3646BC01 CRC64; MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV KQMKIIHEDG YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR ADDARQLFVL AGSAEEGVMT PELAGVIKRL WRDGGVQACF SRSREYQLND SASYYLNDLD RISQSNYIPT QQDVLRTRVK TTGIVETHFT FKDLYFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF DSICNNKWFT ETSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA AYIQCQFEDL NRRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKE CGLY //