RGA2_YEAST
ID RGA2_YEAST Reviewed; 1009 AA.
AC Q06407; D6VT11;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Rho-type GTPase-activating protein 2;
GN Name=RGA2; OrderedLocusNames=YDR379W; ORFNames=D9481.4;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: GTPase-activating protein (GAP) for CDC42 and/or RHO1.
CC -!- INTERACTION:
CC Q06407; Q12518: ENT1; NbExp=6; IntAct=EBI-15060, EBI-31494;
CC Q06407; Q05785: ENT2; NbExp=2; IntAct=EBI-15060, EBI-35928;
CC Q06407; Q06407: RGA2; NbExp=3; IntAct=EBI-15060, EBI-15060;
CC Q06407; O88339: Epn1; Xeno; NbExp=2; IntAct=EBI-15060, EBI-7066728;
CC -!- MISCELLANEOUS: Present with 254 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U28373; AAB64815.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12221.1; -; Genomic_DNA.
DR PIR; S61174; S61174.
DR RefSeq; NP_010667.1; NM_001180687.1.
DR AlphaFoldDB; Q06407; -.
DR SMR; Q06407; -.
DR BioGRID; 32438; 70.
DR DIP; DIP-2995N; -.
DR IntAct; Q06407; 9.
DR MINT; Q06407; -.
DR STRING; 4932.YDR379W; -.
DR iPTMnet; Q06407; -.
DR MaxQB; Q06407; -.
DR PaxDb; Q06407; -.
DR PRIDE; Q06407; -.
DR EnsemblFungi; YDR379W_mRNA; YDR379W; YDR379W.
DR GeneID; 851985; -.
DR KEGG; sce:YDR379W; -.
DR SGD; S000002787; RGA2.
DR VEuPathDB; FungiDB:YDR379W; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_003874_1_0_1; -.
DR InParanoid; Q06407; -.
DR OMA; CSACNNK; -.
DR BioCyc; YEAST:G3O-29928-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9013423; RAC3 GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR Reactome; R-SCE-9035034; RHOF GTPase cycle.
DR PRO; PR:Q06407; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06407; protein.
DR GO; GO:0032177; C:cellular bud neck split septin rings; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0031106; P:septin ring organization; IGI:SGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:SGD.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..1009
FT /note="Rho-type GTPase-activating protein 2"
FT /id="PRO_0000075900"
FT DOMAIN 11..68
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 69..129
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 788..1006
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 143..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1009 AA; 113291 MW; FA13BA1DF8B35D98 CRC64;
MSADPINDQS SLCVRCNKSI ASSQVYELES KKWHDQCFTC YKCDKKLNAD SDFLVLDIGT
LICYDCSDKC TNCGDKIDDT AIILPSSNEA YCSNCFRCCR CSNRIKNLKY AKTKRGLCCM
DCHEKLLRKK QLLLENQTKN SSKEDFPIKL PERSVKRPLS PTRINGKSDV STNNTAISKN
LVSSNEDQQL TPQVLVSQER DESSLNDNND NDNSKDREET SSHARTVSID DILNSTLEHD
SNSIEEQSLV DNEDYINKMG EDVTYRLLKP QRANRDSIVV KDPRIPNSNS NANRFFSIYD
KEETDKDDTD NKENEIIVNT PRNSTDKITS PLNSPMAVQM NEEVEPPHGL ALTLSEATKE
NNKSSQGIQT STSKSMNHVS PITRTDTVEM KTSTSSSTLR LSDNGSFSRP QTADNLLPHK
KVAPSPNKKL SRSFSLKSKN FVHNLKSKTS EMLDPKHPHH STSIQESDTH SGWGVSSTHT
NIRKSKAKKN PVSRGQSDST IYNTLPQHGN FTVPEFNHKK AQSSLGSISK KQNSNDTATN
RRINGSFTSS SSGHHIAMFR TPPLESGPLF KRPSLSSESA HHRSSSLQTS RSTNALLEDD
STKVDATDES ATSLEKDFYF TELTLRKLKL DVRELEGTKK KLLQDVENLR LAKERLLNDV
DNLTREKDKQ SASSRESLEQ KENIATSITV KSPSSNSDRK GSISNASPKP RFWKIFSSAK
DHQVGDLESQ QRSPNSSSGG TTNIAQKEIS SPKLIRVHDE LPSPGKVPLS PSPKRLDYTP
DGSHLYGSSL QARCAYEKST VPIIIRCCID RIEKDDIGLN MEGLYRKSGS QTLVEEIENE
FAQNNSLHSD TLSPKLNALL NQDIHAVASV LKRYLRKLPD PVLSFSIYDA LIDLVRNNQL
IERLPLNNDK FLDSPQKVTI YEMVLKSLLE IFKILPVEHQ EVLKVLAAHI GKVRRCSERN
LMNLHNLSLV FAPSLIHDFD GEKDIVDMKE RNYIVEFILG NYRDIFKQA
