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Rho-type GTPase-activating protein 1

 RGA1_YEAST              Reviewed;        1007 AA.
P39083; D6W2I5; P39934;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
28-MAR-2018, entry version 174.
RecName: Full=Rho-type GTPase-activating protein 1;
Name=RGA1; Synonyms=DBM1, THE1; OrderedLocusNames=YOR127W;
ORFNames=O3290, YOR3290W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
STRAIN=ATCC 204508 / S288c;
PubMed=8657111; DOI=10.1128/MCB.16.4.1376;
Chen G.-C., Zheng L., Chan C.S.M.;
"The LIM domain-containing Dbm1 GTPase-activating protein is required
for normal cellular morphogenesis in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 16:1376-1390(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7498791; DOI=10.1101/gad.9.23.2949;
Stevenson B.J., Ferguson B., de Virgilio C., Bi E., Pringle J.R.,
Ammerer G., Sprague G.F. Jr.;
"Mutation of RGA1, which encodes a putative GTPase-activating protein
for the polarity-establishment protein Cdc42p, activates the
pheromone-response pathway in the yeast Saccharomyces cerevisiae.";
Genes Dev. 9:2949-2963(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8904341;
DOI=10.1002/(SICI)1097-0061(19960315)12:3<281::AID-YEA904>3.0.CO;2-O;
Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
"Sequencing and analysis of 51 kb on the right arm of chromosome XV
from Saccharomyces cerevisiae reveals 30 open reading frames.";
Yeast 12:281-288(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9200815;
DOI=10.1002/(SICI)1097-0061(19970615)13:7<655::AID-YEA120>3.0.CO;2-I;
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
Schwager C., Paces V., Sander C., Ansorge W.;
"DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
Yeast 13:655-672(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 570-639.
STRAIN=S288c / SNY243;
PubMed=1454852; DOI=10.1073/pnas.89.23.11589;
Ramer S.W., Elledge S.J., Davis R.W.;
"Dominant genetics using a yeast genomic library under the control of
a strong inducible promoter.";
Proc. Natl. Acad. Sci. U.S.A. 89:11589-11593(1992).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278; SER-291 AND
THR-532, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: GTPase-activating protein (GAP) for CDC42 and/or RHO1.
Negative regulator of the pheromone-response pathway through the
STE20 protein kinase; acts at a step between the G-protein and the
MAP kinase module. Dominant suppressor of bud emergence defect
caused by deletion of IPL2/BEM2. Involved in the control of
polarized cell growth and proper bud site selection.
-!- INTERACTION:
P06787:CMD1; NbExp=2; IntAct=EBI-15044, EBI-3976;
Q12518:ENT1; NbExp=3; IntAct=EBI-15044, EBI-31494;
Q05785:ENT2; NbExp=2; IntAct=EBI-15044, EBI-35928;
O88339:Epn1 (xeno); NbExp=2; IntAct=EBI-15044, EBI-7066728;
P53141:MLC1; NbExp=2; IntAct=EBI-15044, EBI-10988;
P40073:SHO1; NbExp=2; IntAct=EBI-15044, EBI-18140;
-!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; U07421; AAA16875.1; -; mRNA.
EMBL; X90950; CAA62445.1; -; Genomic_DNA.
EMBL; X90518; CAA62108.1; -; Genomic_DNA.
EMBL; X94335; CAA64046.1; -; Genomic_DNA.
EMBL; Z75035; CAA99326.1; -; Genomic_DNA.
EMBL; L02617; AAA35153.1; -; Genomic_DNA.
EMBL; BK006948; DAA10901.1; -; Genomic_DNA.
PIR; S48535; S48535.
RefSeq; NP_014770.1; NM_001183546.1.
ProteinModelPortal; P39083; -.
BioGrid; 34522; 125.
DIP; DIP-1559N; -.
IntAct; P39083; 25.
MINT; P39083; -.
STRING; 4932.YOR127W; -.
iPTMnet; P39083; -.
MaxQB; P39083; -.
PaxDb; P39083; -.
PRIDE; P39083; -.
EnsemblFungi; YOR127W; YOR127W; YOR127W.
GeneID; 854294; -.
KEGG; sce:YOR127W; -.
EuPathDB; FungiDB:YOR127W; -.
SGD; S000005653; RGA1.
GeneTree; ENSGT00910000144080; -.
HOGENOM; HOG000000788; -.
InParanoid; P39083; -.
KO; K19839; -.
OMA; LICNNCT; -.
OrthoDB; EOG092C047S; -.
BioCyc; YEAST:G3O-33652-MONOMER; -.
Reactome; R-SCE-194840; Rho GTPase cycle.
Reactome; R-SCE-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
PRO; PR:P39083; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0032177; C:cellular bud neck split septin rings; IDA:SGD.
GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007015; P:actin filament organization; IMP:SGD.
GO; GO:0007118; P:budding cell apical bud growth; IPI:SGD.
GO; GO:0007119; P:budding cell isotropic bud growth; IPI:SGD.
GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IPI:SGD.
GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IGI:SGD.
GO; GO:0007124; P:pseudohyphal growth; IPI:SGD.
GO; GO:0031106; P:septin ring organization; IGI:SGD.
Gene3D; 1.10.555.10; -; 1.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR001781; Znf_LIM.
Pfam; PF00412; LIM; 1.
Pfam; PF00620; RhoGAP; 1.
SMART; SM00132; LIM; 2.
SMART; SM00324; RhoGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS00478; LIM_DOMAIN_1; 1.
PROSITE; PS50023; LIM_DOMAIN_2; 2.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
Complete proteome; GTPase activation; LIM domain; Metal-binding;
Pheromone response; Phosphoprotein; Reference proteome; Repeat; Zinc.
CHAIN 1 1007 Rho-type GTPase-activating protein 1.
/FTId=PRO_0000075899.
DOMAIN 13 66 LIM zinc-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 70 122 LIM zinc-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 791 1006 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
MOD_RES 278 278 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 532 532 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
VARIANT 866 866 V -> A.
VARIANT 898 898 K -> R.
VARIANT 926 926 S -> G.
MUTAGEN 37 37 C->S: Bipolar budding.
{ECO:0000269|PubMed:8657111}.
MUTAGEN 40 40 C->S: Bipolar budding.
{ECO:0000269|PubMed:8657111}.
MUTAGEN 98 98 C->S: Bipolar budding.
{ECO:0000269|PubMed:8657111}.
MUTAGEN 101 101 C->S: Bipolar budding.
{ECO:0000269|PubMed:8657111}.
CONFLICT 457 457 D -> E (in Ref. 2; CAA62445).
{ECO:0000305}.
CONFLICT 507 507 T -> P (in Ref. 2; CAA62445).
{ECO:0000305}.
SEQUENCE 1007 AA; 112832 MW; C805411B57553791 CRC64;
MASTAPNEQF PSCVRCKEFI TTGHAYELGC DRWHTHCFAC YKCEKPLSCE SDFLVLGTGA
LICFDCSDSC KNCGKKIDDL AIILSSSNEA YCSDCFKCCK CGENIADLRY AKTKRGLFCL
SCHEKLLAKR KYYEEKKRRL KKNLPSLPTP VIDNGHTDEV SASAVLPEKT FSRPASLVNE
IPSGSEPSKD IETNSSDIVP HFITGYNDSD DNSGSSKFGS NVSIDVIGPE ENSTEHVNDD
VKEEAEAPSA NMSLNVATDP TLSCKEPPSH SRNLLNKTPL RNSSGQYLAK SPSSYRQGII
VNDSLEESDQ IDPPNNSSRN ASELLTSVLH SPVSVNMKNP KGSNTDIFNT GEISQMDPSL
SRKVLNNIVE ETNALQRPVV EVVKEDRSVP DLAGVQQEQA EKYSYSNNSG KGRKISRSLS
RRSKDLMINL KSRATGKQDS NVKLSPASKV TSRRSQDLMR DNDSHTGLDT PNSNSTSLDI
LVNNQKSLNY KRFTDNGTLR VTSGKETALE EQKNHSFKSP SPIDHLLQSP ATPSNVSMYR
TPPLDSSLTF DRRNGSSYSN QNYSIPSWQK TPKTQLENSD NFEEQKETLY ENSESRNDPS
LDKEIVTAEH YLKQLKINLK ELESQREELM KEITEMKSMK EALRRHIESY NSEKNKLYLD
SNELSNNPPM INEISLGESP PVKHVATASS VARSSVKPKF WKFFSSAKPQ TEQSIQGVST
NNTNSIVKSA PVLLSAPSSG SNSGRLEISP PVLQNPNEFS DVRLVPIEND ANMGQSKDGE
EYLDGSNLYG SSLVARCNYE NNEIPMILSV CIDFIESDEE NMRSEGIYRK SGSQLVIEEI
EKQFSAWKVQ QNTETPNILT EQDLNVVTGV LKRYLRKLPN PIFTFQIYEP LMRLVKSKKM
MENLPFVGGK LSLEAKNSDT YMSSKSALKN ILEDLPREHY RVLRVLSEHI EKVTRYSHWN
RMTLYNLALV FAPGLIRDFS GEKDIIDMKE RNYIVAFIFG NYKDILT


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