GNAI1_RAT
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 03-AUG-2022, entry version 207.
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}.
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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 SASBDB; P10824; -.
DR SMR; P10824; -.
DR BioGRID; 247715; 2.
DR CORUM; P10824; -.
DR DIP; DIP-6073N; -.
DR IntAct; P10824; 4.
DR MINT; P10824; -.
DR iPTMnet; P10824; -.
DR PhosphoSitePlus; P10824; -.
DR SwissPalm; P10824; -.
DR World-2DPAGE; 0004:P10824; -.
DR jPOST; P10824; -.
DR PRIDE; P10824; -.
DR ABCD; P10824; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096.
DR GeneID; 25686; -.
DR KEGG; rno:25686; -.
DR CTD; 2770; -.
DR RGD; 2713; Gnai1.
DR GeneTree; ENSGT00940000153567; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P10824; -.
DR OMA; LWVDRGV; -.
DR OrthoDB; 754573at2759; -.
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 tissues.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0099738; C:cell cortex region; 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:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
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: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; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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
