ID GNAI1_RAT Reviewed; 354 AA. AC P10824; Q45QN2; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 215. DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-1; DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein; GN Name=Gnai1; Synonyms=Gnai-1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2820999; DOI=10.1016/s0021-9258(18)47929-x; RA Jones D.T., Reed R.R.; RT "Molecular cloning of five GTP-binding protein cDNA species from rat RT olfactory neuroepithelium."; RL J. Biol. Chem. 262:14241-14249(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=SHR, and Wistar Kyoto; RA Jackson E.K., Zhu C.; RT "Genetic similarity between spontaneously hypertensive rats and Wistar- RT Kyoto rats in the coding regions of signal transduction proteins."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP INTERACTION WITH GPSM1. RX PubMed=11121039; DOI=10.1073/pnas.97.26.14364; RA de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B., RA Siderovski D.P., Farquhar M.G.; RT "Activator of G protein signaling 3 is a guanine dissociation inhibitor for RT Galpha i subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000). RN [4] RP INTERACTION WITH RGS12 AND RGS14. RX PubMed=11387333; DOI=10.1074/jbc.m103208200; RA Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A., RA Gist Farquhar M., Siderovski D.P.; RT "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with RT guanine nucleotide dissociation inhibitor activity."; RL J. Biol. Chem. 276:29275-29281(2001). RN [5] 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 [6] RP SUBCELLULAR LOCATION, INTERACTION WITH RGS14, AND MUTAGENESIS OF GLN-204. 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 [7] 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 [8] RP INTERACTION WITH RGS14 AND RIC8A, MUTAGENESIS OF ASN-149, AND SUBCELLULAR RP LOCATION. RX PubMed=21158412; DOI=10.1021/bi101910n; RA Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.; RT "Activation of the regulator of G protein signaling 14-Galphai1-GDP RT signaling complex is regulated by resistance to inhibitors of RT cholinesterase-8A."; RL Biochemistry 50:752-762(2011). RN [9] RP INTERACTION WITH NUCB1. RX PubMed=21653697; DOI=10.1074/jbc.m110.204099; RA Garcia-Marcos M., Kietrsunthorn P.S., Wang H., Ghosh P., Farquhar M.G.; RT "G Protein binding sites on Calnuc (nucleobindin 1) and NUCB2 (nucleobindin RT 2) define a new class of G(alpha)i-regulatory motifs."; RL J. Biol. Chem. 286:28138-28149(2011). RN [10] RP MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, MUTAGENESIS OF GLY-2 AND RP CYS-3, AND SUBCELLULAR LOCATION. RX PubMed=26253820; DOI=10.1016/j.bbalip.2015.08.001; RA Alvarez R., Lopez D.J., Casas J., Llado V., Higuera M., Nagy T., RA Barcelo M., Busquets X., Escriba P.V.; RT "G protein-membrane interactions I: Galphai1 myristoyl and palmitoyl RT modifications in protein-lipid interactions and its implications in RT membrane microdomain localization."; RL Biochim. Biophys. Acta 1851:1511-1520(2015). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GDP. RX PubMed=8073283; DOI=10.1126/science.8073283; RA Coleman D.E., Berghuis A.M., Lee E., Linder M.E., Gilman A.G., Sprang S.R.; RT "Structures of active conformations of Gi alpha 1 and the mechanism of GTP RT hydrolysis."; RL Science 265:1405-1412(1994). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GNB1; GNG2 AND GDP, RP AND SUBUNIT. RX PubMed=8521505; DOI=10.1016/0092-8674(95)90220-1; RA Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A., RA Gilman A.G., Sprang S.R.; RT "The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2."; RL Cell 83:1047-1058(1995). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RGS4 AND GDP, AND RP INTERACTION WITH RGS4. RX PubMed=9108480; DOI=10.1016/s0092-8674(00)80204-4; RA Tesmer J.J.G., Berman D.M., Gilman A.G., Sprang S.R.; RT "Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of RT the transition state for GTP hydrolysis."; RL Cell 89:251-261(1997). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GDP. RX PubMed=9772163; DOI=10.1021/bi9810306; RA Coleman D.E., Sprang S.R.; RT "Crystal structures of the G protein Gi alpha 1 complexed with GDP and RT Mg2+: a crystallographic titration experiment."; RL Biochemistry 37:14376-14385(1998). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-346 IN COMPLEX WITH GDP AND RP MAGNESIUM. RX PubMed=9705312; DOI=10.1074/jbc.273.34.21752; RA Posner B.A., Mixon M.B., Wall M.A., Sprang S.R., Gilman A.G.; RT "The A326S mutant of Gialpha1 as an approximation of the receptor-bound RT state."; RL J. Biol. Chem. 273:21752-21758(1998). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-348 OF MUTANT ALA-329 IN RP COMPLEXES WITH MAGNESIUM; GDP AND GTP ANALOG, FUNCTION, AND MUTAGENESIS OF RP GLN-204; THR-329 AND VAL-332. RX PubMed=19703466; DOI=10.1016/j.jmb.2009.08.043; RA Kapoor N., Menon S.T., Chauhan R., Sachdev P., Sakmar T.P.; RT "Structural evidence for a sequential release mechanism for activation of RT heterotrimeric G proteins."; RL J. Mol. Biol. 393:882-897(2009). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH GDP AND GTP RP ANALOG, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH GNB1 AND RP GNG1, AND MUTAGENESIS OF GLU-43 AND LYS-345. RX PubMed=24596087; DOI=10.1074/jbc.m113.539064; RA Thaker T.M., Sarwar M., Preininger A.M., Hamm H.E., Iverson T.M.; RT "A transient interaction between the phosphate binding loop and switch I RT contributes to the allosteric network between receptor and nucleotide in RT Galphai1."; RL J. Biol. Chem. 289:11331-11341(2014). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF WILD-TYPE AND MUTANTS CYS-336 AND RP TYR-336 IN COMPLEXES WITH MAGNESIUM; GDP AND GTP ANALOG, FUNCTION, SUBUNIT, RP AND MUTAGENESIS OF PHE-189; PHE-191 AND PHE-336. RX PubMed=25037222; DOI=10.1074/jbc.m114.572875; RA Kaya A.I., Lokits A.D., Gilbert J.A., Iverson T.M., Meiler J., Hamm H.E.; RT "A conserved phenylalanine as a relay between the alpha5 helix and the GDP RT binding region of heterotrimeric Gi protein alpha subunit."; RL J. Biol. Chem. 289:24475-24487(2014). 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 (PubMed:19703466, PubMed:24596087, CC PubMed:25037222). The alpha subunit has a low GTPase activity that CC converts bound GTP to GDP, thereby terminating the signal CC (PubMed:21158412). Both GDP release and GTP hydrolysis are modulated by CC numerous regulatory proteins (PubMed:21158412). Signaling is mediated CC via effector proteins, such as adenylate cyclase. Inhibits adenylate CC cyclase activity, leading to decreased intracellular cAMP levels CC (PubMed:19703466). The inactive GDP-bound form prevents the association CC of RGS14 with centrosomes and is required for the translocation of CC RGS14 from the cytoplasm to the plasma membrane. Required for normal CC cytokinesis during mitosis (PubMed:16870394). Required for cortical CC dynein-dynactin complex recruitment during metaphase (By similarity). CC {ECO:0000250|UniProtKB:P63096, ECO:0000269|PubMed:16870394, CC ECO:0000269|PubMed:19703466, ECO:0000269|PubMed:21158412, CC ECO:0000269|PubMed:24596087, ECO:0000269|PubMed:25037222, ECO:0000305}. CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta CC and gamma. The alpha chain contains the guanine nucleotide binding site CC (PubMed:8521505, PubMed:24596087, PubMed:25037222). Part of a spindle CC orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (By CC similarity). Identified in complex with the beta subunit GNB1 and the CC gamma subunit GNG1 (PubMed:24596087). Identified in complex with the CC beta subunit GNB1 and the gamma subunit GNG2 (PubMed:8521505). GTP CC binding causes dissociation of the heterotrimer, liberating the CC individual subunits so that they can interact with downstream effector CC proteins. Interacts (GDP-bound form) with GPSM1; this inhibits guanine CC nucleotide exchange and GTP binding (PubMed:11121039). Interacts (GDP- CC bound form) with GPSM2 (via GoLoco domains); this inhibits guanine CC nucleotide exchange (By similarity). Interacts with RGS10; this CC strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16 (By CC similarity). Interacts with RGS4 (PubMed:9108480). Interacts with RGS12 CC (PubMed:11387333). Interacts (via active GTP- or inactive GDP-bound CC forms) with RGS14 (via RGS and GoLoco domains) (PubMed:11387333, CC PubMed:16870394, PubMed:17635935, PubMed:21158412). Interacts with CC RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) (By CC similarity). Interacts (GDP-bound form) with RIC8A (via C-terminus) CC (PubMed:21158412). Interacts (inactive GDP-bound form) with NUCB1 (via CC GBA motif); the interaction leads to activation of GNAI1 CC (PubMed:21653697). Interacts (inactive GDP-bound form) with CC CCDC88C/DAPLE (via GBA motif); the interaction leads to activation of CC GNAI1 (By similarity). Interacts (inactive GDP-bound form) with CC CCDC8A/GIV (via GBA motif) (PubMed:19211784). CC {ECO:0000250|UniProtKB:P63096, ECO:0000269|PubMed:11121039, CC ECO:0000269|PubMed:11387333, ECO:0000269|PubMed:16870394, CC ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:19211784, CC ECO:0000269|PubMed:21158412, ECO:0000269|PubMed:21653697, CC ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:8521505, CC ECO:0000269|PubMed:9108480}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000269|PubMed:17635935}. CC Cell membrane {ECO:0000269|PubMed:17635935, CC ECO:0000269|PubMed:21158412}; Peripheral membrane protein CC {ECO:0000305|PubMed:24596087, ECO:0000305|PubMed:25037222}; Cytoplasmic CC side {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:17635935}. Cytoplasm, cell CC cortex {ECO:0000250|UniProtKB:P63096}. Membrane CC {ECO:0000269|PubMed:26253820}; Lipid-anchor CC {ECO:0000269|PubMed:26253820}. Note=Localizes in the centrosomes of CC interphase and mitotic cells, but not in centrosomes during CC cytokinesis. Detected at the cleavage furrow or the midbody. Localized CC at the plasma membrane throughout mitosis. Colocalizes with RIC8A and CC RGS14 at the plasma membrane. {ECO:0000269|PubMed:21158412}. CC -!- PTM: Myristoylation at Gly-2 is required for membrane anchoring before CC palmitoylation. {ECO:0000269|PubMed:26253820}. CC -!- PTM: Palmitoylation at Cys-3 varies with membrane lipid composition. CC {ECO:0000269|PubMed:26253820}. 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; M17527; AAA40825.1; -; mRNA. DR EMBL; DQ120469; AAZ23808.1; -; mRNA. DR EMBL; DQ120470; AAZ23809.1; -; mRNA. DR PIR; A35377; A35377. DR PIR; C27423; RGRTI1. DR RefSeq; NP_037277.1; NM_013145.1. DR PDB; 1AGR; X-ray; 2.80 A; A/D=2-354. DR PDB; 1AS0; X-ray; 2.00 A; A=2-354. DR PDB; 1AS2; X-ray; 2.80 A; A=2-354. DR PDB; 1AS3; X-ray; 2.40 A; A=2-354. DR PDB; 1BH2; X-ray; 2.10 A; A=32-346. DR PDB; 1BOF; X-ray; 2.20 A; A=2-354. DR PDB; 1CIP; X-ray; 1.50 A; A=2-354. DR PDB; 1FQJ; X-ray; 2.02 A; A/D=220-299. DR PDB; 1FQK; X-ray; 2.30 A; A/C=220-299. DR PDB; 1GDD; X-ray; 2.20 A; A=2-354. DR PDB; 1GFI; X-ray; 2.20 A; A=2-354. DR PDB; 1GG2; X-ray; 2.40 A; A=2-354. DR PDB; 1GIA; X-ray; 2.00 A; A=2-354. DR PDB; 1GIL; X-ray; 2.30 A; A=2-354. DR PDB; 1GIT; X-ray; 2.60 A; A=2-354. DR PDB; 1GP2; X-ray; 2.30 A; A=2-354. DR PDB; 1SHZ; X-ray; 2.85 A; A/D=22-48, A/D=185-353. DR PDB; 1SVK; X-ray; 2.00 A; A=2-354. DR PDB; 1SVS; X-ray; 1.50 A; A=2-354. DR PDB; 2BCJ; X-ray; 3.06 A; Q=1-28. DR PDB; 2RGN; X-ray; 3.50 A; A/D=1-28. DR PDB; 2ZJY; X-ray; 2.80 A; A=1-354. DR PDB; 2ZJZ; X-ray; 2.60 A; A/B=1-354. DR PDB; 3AH8; X-ray; 2.90 A; A=2-28. DR PDB; 3D7M; X-ray; 2.90 A; A=1-354. DR PDB; 3FFA; X-ray; 2.30 A; A=1-354. DR PDB; 3FFB; X-ray; 2.57 A; A=1-354. DR PDB; 3V00; X-ray; 2.90 A; A/B/C=220-298. DR PDB; 4N0D; X-ray; 1.55 A; A=1-354. DR PDB; 4N0E; X-ray; 2.10 A; A=1-354. DR PDB; 4PAM; X-ray; 2.10 A; A=1-354. DR PDB; 4PAN; X-ray; 2.40 A; A=1-354. DR PDB; 4PAO; X-ray; 2.00 A; A=1-354. DR PDB; 4PAQ; X-ray; 2.00 A; A=1-354. DR PDB; 5KDL; X-ray; 2.67 A; A/B=1-354. DR PDB; 5KDO; X-ray; 1.90 A; A=1-354. DR PDB; 6M8H; X-ray; 2.07 A; A=1-354. DR PDB; 6TYL; X-ray; 3.30 A; B/G=1-354. DR PDB; 6UKT; EM; 3.87 A; B=32-354. DR PDB; 6VMS; EM; 3.80 A; A=1-354. DR PDB; 7S0F; EM; 2.96 A; A=1-354. DR PDB; 7S0G; EM; 3.86 A; A=1-343. DR PDBsum; 1AGR; -. DR PDBsum; 1AS0; -. DR PDBsum; 1AS2; -. DR PDBsum; 1AS3; -. DR PDBsum; 1BH2; -. DR PDBsum; 1BOF; -. DR PDBsum; 1CIP; -. DR PDBsum; 1FQJ; -. DR PDBsum; 1FQK; -. DR PDBsum; 1GDD; -. DR PDBsum; 1GFI; -. DR PDBsum; 1GG2; -. DR PDBsum; 1GIA; -. DR PDBsum; 1GIL; -. DR PDBsum; 1GIT; -. DR PDBsum; 1GP2; -. DR PDBsum; 1SHZ; -. DR PDBsum; 1SVK; -. DR PDBsum; 1SVS; -. DR PDBsum; 2BCJ; -. DR PDBsum; 2RGN; -. DR PDBsum; 2ZJY; -. DR PDBsum; 2ZJZ; -. DR PDBsum; 3AH8; -. DR PDBsum; 3D7M; -. DR PDBsum; 3FFA; -. DR PDBsum; 3FFB; -. DR PDBsum; 3V00; -. DR PDBsum; 4N0D; -. DR PDBsum; 4N0E; -. DR PDBsum; 4PAM; -. DR PDBsum; 4PAN; -. DR PDBsum; 4PAO; -. DR PDBsum; 4PAQ; -. DR PDBsum; 5KDL; -. DR PDBsum; 5KDO; -. DR PDBsum; 6M8H; -. DR PDBsum; 6TYL; -. DR PDBsum; 6UKT; -. DR PDBsum; 6VMS; -. DR PDBsum; 7S0F; -. DR PDBsum; 7S0G; -. DR AlphaFoldDB; P10824; -. DR EMDB; EMD-20812; -. DR EMDB; EMD-21243; -. DR EMDB; EMD-24789; -. DR SASBDB; P10824; -. DR SMR; P10824; -. DR BioGRID; 247715; 2. DR CORUM; P10824; -. DR DIP; DIP-6073N; -. DR IntAct; P10824; 5. DR MINT; P10824; -. DR STRING; 10116.ENSRNOP00000074036; -. DR iPTMnet; P10824; -. DR PhosphoSitePlus; P10824; -. DR SwissPalm; P10824; -. DR jPOST; P10824; -. DR ABCD; P10824; 1 sequenced antibody. DR Ensembl; ENSRNOT00000091004.2; ENSRNOP00000074036.1; ENSRNOG00000057096.2. DR Ensembl; ENSRNOT00055037843; ENSRNOP00055030885; ENSRNOG00055021986. DR Ensembl; ENSRNOT00060021730; ENSRNOP00060017197; ENSRNOG00060012765. DR Ensembl; ENSRNOT00065028267; ENSRNOP00065022342; ENSRNOG00065016882. DR GeneID; 25686; -. DR KEGG; rno:25686; -. DR AGR; RGD:2713; -. DR CTD; 2770; -. DR RGD; 2713; Gnai1. DR GeneTree; ENSGT00940000153567; -. DR HOGENOM; CLU_014184_6_0_1; -. DR InParanoid; P10824; -. DR OMA; QVIWADA; -. DR OrthoDB; 2897309at2759; -. DR PhylomeDB; P10824; -. DR Reactome; R-RNO-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12. DR Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion. DR Reactome; R-RNO-418594; G alpha (i) signalling events. DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling. DR SABIO-RK; P10824; -. DR EvolutionaryTrace; P10824; -. DR PRO; PR:P10824; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000057096; Expressed in cerebellum and 18 other cell types or tissues. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0031749; F:D2 dopamine receptor binding; ISO:RGD. DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB. DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IPI:RGD. 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; IDA:UniProtKB. DR GO; GO:0032794; F:GTPase activating protein binding; IDA:RGD. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; 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; ISS:UniProtKB. DR GO; GO:1904322; P:cellular response to forskolin; IMP:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0050805; P:negative regulation of synaptic transmission; IMP:RGD. DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB. DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; IMP:UniProtKB. DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS: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:SF359; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; 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 World-2DPAGE; 0004:P10824; -. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Cell membrane; Cytoplasm; KW Cytoskeleton; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Mitosis; Myristate; Nucleotide-binding; Nucleus; Palmitate; KW Reference proteome; Transducer; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:26253820" FT CHAIN 2..354 FT /note="Guanine nucleotide-binding protein G(i) subunit FT alpha-1" FT /id="PRO_0000203673" 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:1AS0, ECO:0007744|PDB:1BH2, FT ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, FT ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, FT ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:25037222, FT ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, FT ECO:0007744|PDB:4PAO" FT BINDING 150..151 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, FT ECO:0007744|PDB:1GIL, ECO:0007744|PDB:4N0D" FT BINDING 175..178 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, FT ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, FT ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, FT ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:19703466, FT ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, FT ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO" FT BINDING 200..204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, FT ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, FT ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, FT ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ" FT BINDING 269..272 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, FT ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, FT ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, FT ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ" FT BINDING 326 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1GIA, FT ECO:0007744|PDB:1GIL, ECO:0007744|PDB:3FFA, FT ECO:0007744|PDB:4N0D, ECO:0007744|PDB:4PAO, FT ECO:0007744|PDB:4PAQ" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:26253820" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:26253820" FT MUTAGEN 2 FT /note="G->A: Abolishes myristoylation and palmitoylation." FT /evidence="ECO:0000269|PubMed:26253820" FT MUTAGEN 3 FT /note="C->S: Abolishes palmitoylation." FT /evidence="ECO:0000269|PubMed:26253820" FT MUTAGEN 43 FT /note="E->A: Mildly impairs receptor binding; mildly FT decreases basal and receptor-stimulated GDP exchange." FT /evidence="ECO:0000269|PubMed:24596087" FT MUTAGEN 149 FT /note="N->I: Inhibits interaction with RGS14. Does not FT inhibit interaction with RIC8A." FT /evidence="ECO:0000269|PubMed:21158412" FT MUTAGEN 189 FT /note="F->Y: Increases basal GDP exchange rate; no effect FT on receptor-stimulated GDP exchange." FT /evidence="ECO:0000269|PubMed:25037222" FT MUTAGEN 191 FT /note="F->Y: No effect on basal GDP exchange rate; mildly FT decreases receptor-stimulated GDP exchange." FT /evidence="ECO:0000269|PubMed:25037222" FT MUTAGEN 204 FT /note="Q->L: Expected to have lost GTPase activity; FT inhibits the forskolin-mediated increase of cellular cAMP FT levels. Does not inhibit interaction with RGS14 at FT centrosomes." FT /evidence="ECO:0000269|PubMed:17635935, FT ECO:0000269|PubMed:19703466" FT MUTAGEN 329 FT /note="T->A: Increases basal GDP exchange rate and inhibits FT the forskolin-mediated increase of cellular cAMP levels." FT /evidence="ECO:0000269|PubMed:19703466" FT MUTAGEN 332 FT /note="V->A: Increases basal GDP exchange rate." FT /evidence="ECO:0000269|PubMed:19703466" FT MUTAGEN 336 FT /note="F->A,C: Increases basal GDP exchange rate; mildly FT decreases receptor-stimulated GDP exchange." FT /evidence="ECO:0000269|PubMed:25037222" FT MUTAGEN 336 FT /note="F->Y: Strongly increases basal GDP exchange rate; FT mildly decreases receptor-stimulated GDP exchange." FT /evidence="ECO:0000269|PubMed:25037222" FT MUTAGEN 345 FT /note="K->L: Mildly impairs receptor binding; mildly FT decreases basal and receptor-stimulated GDP exchange." FT /evidence="ECO:0000269|PubMed:24596087" FT HELIX 8..31 FT /evidence="ECO:0007829|PDB:5KDO" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 63..68 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 70..91 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 100..110 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 111..116 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 134..140 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 141..145 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 152..156 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 159..162 FT /evidence="ECO:0007829|PDB:1CIP" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:2ZJY" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:1CIP" FT STRAND 183..191 FT /evidence="ECO:0007829|PDB:1CIP" FT STRAND 194..201 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 205..214 FT /evidence="ECO:0007829|PDB:1CIP" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:1CIP" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 242..254 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:1CIP" FT STRAND 262..269 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 271..278 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 296..308 FT /evidence="ECO:0007829|PDB:1CIP" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:1CIP" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 329..346 FT /evidence="ECO:0007829|PDB:1CIP" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:4N0E" SQ SEQUENCE 354 AA; 40345 MW; 99E9D11B485C2DE3 CRC64; MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDAAR 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 //