(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 197.
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;
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 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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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). {ECO:0000250|UniProtKB:P63096,
CC       ECO:0000269|PubMed:11121039, ECO:0000269|PubMed:11387333,
CC       ECO:0000269|PubMed:16870394, ECO:0000269|PubMed:17635935,
CC       ECO:0000269|PubMed:21158412, ECO:0000269|PubMed:25037222,
CC       ECO:0000269|PubMed:8521505, 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}.
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; 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   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; 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   SMR; P10824; -.
DR   BioGrid; 247715; 2.
DR   CORUM; P10824; -.
DR   DIP; DIP-6073N; -.
DR   IntAct; P10824; 2.
DR   MINT; P10824; -.
DR   iPTMnet; P10824; -.
DR   PhosphoSitePlus; P10824; -.
DR   SwissPalm; P10824; -.
DR   World-2DPAGE; 0004:P10824; -.
DR   jPOST; P10824; -.
DR   PRIDE; P10824; -.
DR   Ensembl; ENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096.
DR   GeneID; 25686; -.
DR   KEGG; rno:25686; -.
DR   CTD; 2770; -.
DR   RGD; 2713; Gnai1.
DR   GeneTree; ENSGT00940000153567; -.
DR   HOGENOM; HOG000038730; -.
DR   InParanoid; P10824; -.
DR   KO; K04630; -.
DR   OMA; QVIWADA; -.
DR   OrthoDB; 754573at2759; -.
DR   PhylomeDB; P10824; -.
DR   Reactome; R-RNO-112043; PLC beta mediated events.
DR   Reactome; R-RNO-170670; Adenylate cyclase inhibitory pathway.
DR   Reactome; R-RNO-202040; G-protein activation.
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-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
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 9 organ(s), highest expression level in brain.
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   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;
DR   PRODOM; P10824.
DR   SWISS-2DPAGE; P10824.
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   NP_BIND         43..48
FT                   /note="GTP"
FT                   /evidence="ECO:0000244|PDB:1AS0, ECO:0000244|PDB:1BH2,
FT                   ECO:0000244|PDB:1GIA, ECO:0000244|PDB:1GIL,
FT                   ECO:0000244|PDB:3FFA, ECO:0000244|PDB:4N0D,
FT                   ECO:0000244|PDB:4PAO, ECO:0000244|PDB:4PAQ"
FT   NP_BIND         150..151
FT                   /note="GTP"
FT                   /evidence="ECO:0000244|PDB:1AS0, ECO:0000244|PDB:1BH2,
FT                   ECO:0000244|PDB:1GIL, ECO:0000244|PDB:4N0D"
FT   NP_BIND         175..178
FT                   /note="GTP"
FT                   /evidence="ECO:0000244|PDB:1AS0, ECO:0000244|PDB:1BH2,
FT                   ECO:0000244|PDB:1GIA, ECO:0000244|PDB:1GIL,
FT                   ECO:0000244|PDB:3FFA, ECO:0000244|PDB:4N0D,
FT                   ECO:0000244|PDB:4PAO, ECO:0000244|PDB:4PAQ"
FT   NP_BIND         200..204
FT                   /note="GTP"
FT                   /evidence="ECO:0000244|PDB:1AS0, ECO:0000244|PDB:1BH2,
FT                   ECO:0000244|PDB:1GIA, ECO:0000244|PDB:1GIL,
FT                   ECO:0000244|PDB:3FFA, ECO:0000244|PDB:4N0D,
FT                   ECO:0000244|PDB:4PAO, ECO:0000244|PDB:4PAQ"
FT   NP_BIND         269..272
FT                   /note="GTP"
FT                   /evidence="ECO:0000244|PDB:1AS0, ECO:0000244|PDB:1BH2,
FT                   ECO:0000244|PDB:1GIA, ECO:0000244|PDB:1GIL,
FT                   ECO:0000244|PDB:3FFA, ECO:0000244|PDB:4N0D,
FT                   ECO:0000244|PDB:4PAO, ECO:0000244|PDB:4PAQ"
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   METAL           47
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000244|PDB:1BH2, ECO:0000244|PDB:4PAO,
FT                   ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312"
FT   METAL           181
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000244|PDB:1BH2, ECO:0000244|PDB:4PAO,
FT                   ECO:0000269|PubMed:19703466, ECO:0000269|PubMed:25037222,
FT                   ECO:0000269|PubMed:9705312"
FT   BINDING         326
FT                   /note="GTP; via amide nitrogen"
FT                   /evidence="ECO:0000244|PDB:1AS0, ECO:0000244|PDB:1GIA,
FT                   ECO:0000244|PDB:1GIL, ECO:0000244|PDB:3FFA,
FT                   ECO:0000244|PDB:4N0D, ECO:0000244|PDB:4PAO,
FT                   ECO:0000244|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:0000244|PDB:5KDO"
FT   STRAND          33..39
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           46..57
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           63..68
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           70..91
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           100..110
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           111..116
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           121..132
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           134..140
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           141..145
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           152..156
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           159..162
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   STRAND          164..166
FT                   /evidence="ECO:0000244|PDB:2ZJY"
FT   HELIX           171..175
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   STRAND          183..191
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   STRAND          194..201
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           205..214
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   STRAND          219..226
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           227..231
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   STRAND          237..241
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           242..254
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           257..259
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   STRAND          262..269
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           271..278
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           283..285
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           296..308
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   TURN            314..316
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   STRAND          319..323
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           329..346
FT                   /evidence="ECO:0000244|PDB:1CIP"
FT   HELIX           348..350
FT                   /evidence="ECO:0000244|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
//

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