ID GNAT1_BOVIN Reviewed; 350 AA.
AC P04695;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 207.
DE RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-1;
DE AltName: Full=Transducin alpha-1 chain;
GN Name=GNAT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2409555; DOI=10.1073/pnas.82.13.4311;
RA Medynski D.C., Sullivan K., Smith D., van Dop C., Chang F.-H.,
RA Fung B.K.-K., Seeburg P.H., Bourne H.R.;
RT "Amino acid sequence of the alpha subunit of transducin deduced from the
RT cDNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4311-4315(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2989813; DOI=10.1073/pnas.82.13.4316;
RA Yatsunami K., Khorana H.G.;
RT "GTPase of bovine rod outer segments: the amino acid sequence of the alpha
RT subunit as derived from the cDNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4316-4320(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3923359; DOI=10.1038/315242a0;
RA Tanaba T., Nukada T., Nishikawa Y., Sugimoto K., Suzuki H., Takahashi H.,
RA Noda M., Haga T., Ichiyama A., Kangawa K., Minamino N., Matsuo H., Numa S.;
RT "Primary structure of the alpha-subunit of transducin and its relationship
RT to ras proteins.";
RL Nature 315:242-245(1985).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3867352;
RA Lipkin V.M., Obukhov A.N., Bogachuk A.P., Telezhinskaya I.N.,
RA Shemyakin V.V.;
RT "Isolation and characteristics of cyanogen bromide peptides of transducin
RT alpha and beta subunits.";
RL Bioorg. Khim. 11:1481-1492(1985).
RN [5]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=1436039; DOI=10.1038/359749a0;
RA Kokame K., Fukada Y., Yoshizawa T., Takao T., Shimonishi Y.;
RT "Lipid modification at the N-terminus of photoreceptor G-protein alpha-
RT subunit.";
RL Nature 359:749-752(1992).
RN [6]
RP FUNCTION, MUTAGENESIS OF SER-43, AND SUBUNIT.
RX PubMed=21285355; DOI=10.1074/jbc.m110.166538;
RA Ramachandran S., Cerione R.A.;
RT "A dominant-negative Galpha mutant that traps a stable rhodopsin-Galpha-
RT GTP-betagamma complex.";
RL J. Biol. Chem. 286:12702-12711(2011).
RN [7]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23303210; DOI=10.1096/fj.12-225383;
RA Jastrzebska B., Orban T., Golczak M., Engel A., Palczewski K.;
RT "Asymmetry of the rhodopsin dimer in complex with transducin.";
RL FASEB J. 27:1572-1584(2013).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=28655769; DOI=10.1074/jbc.m117.797100;
RA Gao Y., Westfield G., Erickson J.W., Cerione R.A., Skiniotis G.,
RA Ramachandran S.;
RT "Isolation and structure-function characterization of a signaling-active
RT rhodopsin-G protein complex.";
RL J. Biol. Chem. 292:14280-14289(2017).
RN [9] {ECO:0007744|PDB:1TND}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 27-350 IN COMPLEX WITH GTP ANALOG,
RP AND FUNCTION.
RX PubMed=8259210; DOI=10.1038/366654a0;
RA Noel J.P., Hamm H.E., Sigler P.B.;
RT "The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma
RT S.";
RL Nature 366:654-663(1993).
RN [10] {ECO:0007744|PDB:1TAG}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-350 IN COMPLEX WITH GDP.
RX PubMed=8208289; DOI=10.1038/369621a0;
RA Lambright D.G., Noel J.P., Hamm H.E., Sigler P.B.;
RT "Structural determinants for activation of the alpha-subunit of a
RT heterotrimeric G protein.";
RL Nature 369:621-628(1994).
RN [11] {ECO:0007744|PDB:1TAD}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-350 IN COMPLEX WITH GTP ANALOG.
RX PubMed=7969474; DOI=10.1038/372276a0;
RA Sondek J., Lambright D.G., Noel J.P., Hamm H.E., Sigler P.B.;
RT "GTPase mechanism of Gproteins from the 1.7-A crystal structure of
RT transducin alpha-GDP-AIF-4.";
RL Nature 372:276-279(1994).
RN [12]
RP STRUCTURE BY NMR OF 340-350, AND INTERACTION WITH RHO.
RC TISSUE=Retina;
RX PubMed=9539726; DOI=10.1073/pnas.95.8.4270;
RA Kisselev O.G., Kao J., Ponder J.W., Fann Y.C., Gautam N., Marshall G.R.;
RT "Light-activated rhodopsin induces structural binding motif in G protein
RT alpha subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4270-4275(1998).
RN [13] {ECO:0007744|PDB:1FQJ, ECO:0007744|PDB:1FQK}
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 26-350 IN COMPLEX WITH PDE6G AND
RP RGS9.
RX PubMed=11234020; DOI=10.1038/35059138;
RA Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., Sigler P.B.;
RT "Structural determinants for regulation of phosphodiesterase by a G protein
RT at 2.0 A.";
RL Nature 409:1071-1077(2001).
RN [14] {ECO:0007744|PDB:3DQB}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 340-350 IN COMPLEX WITH RHO.
RX PubMed=18818650; DOI=10.1038/nature07330;
RA Scheerer P., Park J.H., Hildebrand P.W., Kim Y.J., Krauss N., Choe H.-W.,
RA Hofmann K.P., Ernst O.P.;
RT "Crystal structure of opsin in its G-protein-interacting conformation.";
RL Nature 455:497-502(2008).
RN [15] {ECO:0007744|PDB:3PQR}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 340-350 IN COMPLEX WITH RHO.
RX PubMed=21389988; DOI=10.1038/nature09789;
RA Choe H.W., Kim Y.J., Park J.H., Morizumi T., Pai E.F., Krauss N.,
RA Hofmann K.P., Scheerer P., Ernst O.P.;
RT "Crystal structure of metarhodopsin II.";
RL Nature 471:651-655(2011).
RN [16] {ECO:0007744|PDB:2X72}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 340-350 IN COMPLEX WITH RHO.
RX PubMed=21389983; DOI=10.1038/nature09795;
RA Standfuss J., Edwards P.C., D'Antona A., Fransen M., Xie G., Oprian D.D.,
RA Schertler G.F.;
RT "The structural basis of agonist-induced activation in constitutively
RT active rhodopsin.";
RL Nature 471:656-660(2011).
RN [17] {ECO:0007744|PDB:4BEY}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 340-350 IN COMPLEX WITH RHO.
RX PubMed=23579341; DOI=10.1038/embor.2013.44;
RA Singhal A., Ostermaier M.K., Vishnivetskiy S.A., Panneels V., Homan K.T.,
RA Tesmer J.J., Veprintsev D., Deupi X., Gurevich V.V., Schertler G.F.,
RA Standfuss J.;
RT "Insights into congenital stationary night blindness based on the structure
RT of G90D rhodopsin.";
RL EMBO Rep. 14:520-526(2013).
CC -!- FUNCTION: Functions as a signal transducer for the rod photoreceptor
CC RHO (PubMed:21285355, PubMed:23303210, PubMed:28655769,
CC PubMed:8259210). Required for normal RHO-mediated light perception by
CC the retina (By similarity). Guanine nucleotide-binding proteins (G
CC proteins) function as transducers downstream of G protein-coupled
CC receptors (GPCRs), such as the photoreceptor RHO. 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
CC (PubMed:21285355, PubMed:28655769, PubMed:8259210, PubMed:8208289,
CC PubMed:7969474). Activated RHO promotes GDP release and GTP binding
CC (PubMed:21285355, PubMed:28655769). Signaling is mediated via
CC downstream effector proteins, such as cGMP-phosphodiesterase
CC (PubMed:21285355). {ECO:0000250|UniProtKB:P11488,
CC ECO:0000269|PubMed:21285355, ECO:0000269|PubMed:28655769,
CC ECO:0000305|PubMed:23303210, ECO:0000305|PubMed:7969474,
CC ECO:0000305|PubMed:8208289, ECO:0000305|PubMed:8259210}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 subunits alpha,
CC beta and gamma (PubMed:21285355, PubMed:23303210, PubMed:28655769). The
CC alpha chain contains the guanine nucleotide binding site
CC (PubMed:21285355, PubMed:8259210, PubMed:8208289, PubMed:7969474).
CC Interacts with RHO (PubMed:21285355, PubMed:23303210, PubMed:28655769,
CC PubMed:9539726, PubMed:21389983, PubMed:23579341, PubMed:21389988,
CC PubMed:18818650). Interacts with RGS9 and PDE6G (PubMed:11234020).
CC Interacts (when myristoylated) with UNC119; interaction is required for
CC localization in sensory neurons (By similarity).
CC {ECO:0000250|UniProtKB:P11488, ECO:0000269|PubMed:11234020,
CC ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21285355,
CC ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:21389988,
CC ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:23579341,
CC ECO:0000269|PubMed:28655769, ECO:0000269|PubMed:7969474,
CC ECO:0000269|PubMed:8208289, ECO:0000269|PubMed:8259210,
CC ECO:0000269|PubMed:9539726}.
CC -!- INTERACTION:
CC P04695; Q28181: CNGB1; NbExp=4; IntAct=EBI-7052221, EBI-6979031;
CC P04695; P02699: RHO; NbExp=3; IntAct=EBI-7052221, EBI-8592832;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000269|PubMed:23303210}. Membrane
CC {ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:28655769}; Peripheral
CC membrane protein {ECO:0000269|PubMed:23303210,
CC ECO:0000269|PubMed:28655769}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P20612}. Note=Localizes mainly in the outer
CC segment in the dark-adapted state, whereas is translocated to the inner
CC part of the photoreceptors in the light-adapted state. During dark-
CC adapted conditions, in the presence of UNC119 mislocalizes from the
CC outer segment to the inner part of rod photoreceptors which leads to
CC decreased photoreceptor damage caused by light.
CC {ECO:0000250|UniProtKB:P20612}.
CC -!- TISSUE SPECIFICITY: Rod.
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DR EMBL; K03253; AAA30787.1; -; mRNA.
DR EMBL; K03254; AAA30791.1; -; mRNA.
DR EMBL; X02440; CAA26285.1; -; mRNA.
DR PIR; A22244; RGBOT1.
DR RefSeq; NP_851365.1; NM_181022.2.
DR RefSeq; XP_010815966.1; XM_010817664.2.
DR PDB; 1AQG; NMR; -; A=340-350.
DR PDB; 1FQJ; X-ray; 2.02 A; A/D=26-215, A/D=295-350.
DR PDB; 1FQK; X-ray; 2.30 A; A/C=26-215, A/C=295-350.
DR PDB; 1GOT; X-ray; 2.00 A; A=1-350.
DR PDB; 1LVZ; NMR; -; A=340-350.
DR PDB; 1TAD; X-ray; 1.70 A; A/B/C=27-350.
DR PDB; 1TAG; X-ray; 1.80 A; A=27-350.
DR PDB; 1TND; X-ray; 2.20 A; A/B/C=27-350.
DR PDB; 2X72; X-ray; 3.00 A; B=340-350.
DR PDB; 3DQB; X-ray; 3.20 A; B=340-350.
DR PDB; 3PQR; X-ray; 2.85 A; B=340-350.
DR PDB; 3V00; X-ray; 2.90 A; A/B/C=1-215, A/B/C=295-350.
DR PDB; 4BEY; X-ray; 2.90 A; B=340-350.
DR PDB; 4J4Q; X-ray; 2.65 A; B=340-350.
DR PDB; 6OY9; EM; 3.90 A; A=1-350.
DR PDB; 6OYA; EM; 3.30 A; A=1-350.
DR PDB; 7JSN; EM; 3.20 A; E/F=1-350.
DR PDBsum; 1AQG; -.
DR PDBsum; 1FQJ; -.
DR PDBsum; 1FQK; -.
DR PDBsum; 1GOT; -.
DR PDBsum; 1LVZ; -.
DR PDBsum; 1TAD; -.
DR PDBsum; 1TAG; -.
DR PDBsum; 1TND; -.
DR PDBsum; 2X72; -.
DR PDBsum; 3DQB; -.
DR PDBsum; 3PQR; -.
DR PDBsum; 3V00; -.
DR PDBsum; 4BEY; -.
DR PDBsum; 4J4Q; -.
DR PDBsum; 6OY9; -.
DR PDBsum; 6OYA; -.
DR PDBsum; 7JSN; -.
DR AlphaFoldDB; P04695; -.
DR EMDB; EMD-22458; -.
DR SMR; P04695; -.
DR BioGRID; 159108; 1.
DR CORUM; P04695; -.
DR DIP; DIP-29226N; -.
DR IntAct; P04695; 5.
DR MINT; P04695; -.
DR STRING; 9913.ENSBTAP00000023990; -.
DR iPTMnet; P04695; -.
DR PaxDb; 9913-ENSBTAP00000023990; -.
DR Ensembl; ENSBTAT00000023990.5; ENSBTAP00000023990.4; ENSBTAG00000018020.5.
DR GeneID; 281794; -.
DR KEGG; bta:281794; -.
DR CTD; 2779; -.
DR VEuPathDB; HostDB:ENSBTAG00000018020; -.
DR VGNC; VGNC:29454; GNAT1.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000160395; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P04695; -.
DR OMA; EFIVIIY; -.
DR TreeFam; TF300673; -.
DR Reactome; R-BTA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR EvolutionaryTrace; P04695; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000018020; Expressed in retina and 89 other cell types or tissues.
DR GO; GO:0097648; C:G protein-coupled receptor complex; IDA:CAFA.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:UniProtKB.
DR GO; GO:0000035; F:acyl binding; IDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:CAFA.
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:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0007602; P:phototransduction; NAS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00066; G-alpha; 1.
DR DisProt; DP00273; -.
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:SF67; GUANINE NUCLEOTIDE-BINDING PROTEIN G(T) 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Direct protein sequencing; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sensory transduction; Transducer; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..350
FT /note="Guanine nucleotide-binding protein G(t) subunit
FT alpha-1"
FT /id="PRO_0000203735"
FT DOMAIN 28..350
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..44
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 169..177
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 192..201
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 261..268
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 320..325
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 340..350
FT /note="Interaction with RHO"
FT /evidence="ECO:0000269|PubMed:18818650,
FT ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:21389988,
FT ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:9539726"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:7969474,
FT ECO:0000269|PubMed:8208289, ECO:0000269|PubMed:8259210,
FT ECO:0007744|PDB:1FQJ, ECO:0007744|PDB:1FQK,
FT ECO:0007744|PDB:1GOT, ECO:0007744|PDB:1TAD,
FT ECO:0007744|PDB:1TAG, ECO:0007744|PDB:1TND,
FT ECO:0007744|PDB:3V00"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:7969474,
FT ECO:0000269|PubMed:8208289, ECO:0000269|PubMed:8259210,
FT ECO:0007744|PDB:1FQJ, ECO:0007744|PDB:1FQK,
FT ECO:0007744|PDB:1GOT, ECO:0007744|PDB:1TAD,
FT ECO:0007744|PDB:1TAG, ECO:0007744|PDB:1TND,
FT ECO:0007744|PDB:3V00"
FT BINDING 171..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:7969474,
FT ECO:0000269|PubMed:8208289, ECO:0000269|PubMed:8259210,
FT ECO:0007744|PDB:1FQJ, ECO:0007744|PDB:1FQK,
FT ECO:0007744|PDB:1GOT, ECO:0007744|PDB:1TAD,
FT ECO:0007744|PDB:1TAG, ECO:0007744|PDB:1TND,
FT ECO:0007744|PDB:3V00"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:8259210,
FT ECO:0007744|PDB:1TND"
FT BINDING 265..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:7969474,
FT ECO:0000269|PubMed:8208289, ECO:0000269|PubMed:8259210,
FT ECO:0007744|PDB:1GOT, ECO:0007744|PDB:1TAD,
FT ECO:0007744|PDB:1TAG, ECO:0007744|PDB:1TND"
FT BINDING 322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:8259210,
FT ECO:0007744|PDB:1TND"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11488"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:1436039"
FT MUTAGEN 43
FT /note="S->N: Facilitated GDP-GTP exchange, increasing the
FT levels of the activated GTP-bound form."
FT /evidence="ECO:0000269|PubMed:21285355"
FT HELIX 7..27
FT /evidence="ECO:0007829|PDB:1GOT"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1TAD"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6OYA"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 59..86
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1TAD"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3V00"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:1TAD"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1TAD"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:1TAD"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1TAD"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:1TAD"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1TAD"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6OYA"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:1TAD"
FT TURN 308..312
FT /evidence="ECO:0007829|PDB:1TAD"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 325..341
FT /evidence="ECO:0007829|PDB:1TAD"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1AQG"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:1AQG"
SQ SEQUENCE 350 AA; 39966 MW; 36F0B4630EFBD7DF CRC64;
MGAGASAEEK HSRELEKKLK EDAEKDARTV KLLLLGAGES GKSTIVKQMK IIHQDGYSLE
ECLEFIAIIY GNTLQSILAI VRAMTTLNIQ YGDSARQDDA RKLMHMADTI EEGTMPKEMS
DIIQRLWKDS GIQACFDRAS EYQLNDSAGY YLSDLERLVT PGYVPTEQDV LRSRVKTTGI
IETQFSFKDL NFRMFDVGGQ RSERKKWIHC FEGVTCIIFI AALSAYDMVL VEDDEVNRMH
ESLHLFNSIC NHRYFATTSI VLFLNKKDVF SEKIKKAHLS ICFPDYNGPN TYEDAGNYIK
VQFLELNMRR DVKEIYSHMT CATDTQNVKF VFDAVTDIII KENLKDCGLF
//
