ROM2_YEAST
ID ROM2_YEAST Reviewed; 1356 AA.
AC P51862;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=RHO1 GDP-GTP exchange protein 2;
GN Name=ROM2; OrderedLocusNames=YLR371W; ORFNames=L8039.3;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 CHARACTERIZATION.
RX PubMed=8641285; DOI=10.1002/j.1460-2075.1996.tb00573.x;
RA Ozaki K., Tanaka K., Imamura H., Hihara T., Kameyama T., Nonaka H.,
RA Hirano H., Matsuura Y., Takai Y.;
RT "Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small
RT GTP binding protein in Saccharomyces cerevisiae.";
RL EMBO J. 15:2196-2207(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-193 AND SER-223, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-223; SER-566 AND
RP SER-628, AND IDENTIFICATION BY 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Stimulates the exchange of RHO1 GDP-bound form into GTP-bound
CC form.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U19103; AAB67564.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09674.1; -; Genomic_DNA.
DR PIR; S51389; S51389.
DR RefSeq; NP_013475.1; NM_001182260.1.
DR AlphaFoldDB; P51862; -.
DR SMR; P51862; -.
DR BioGRID; 31631; 808.
DR DIP; DIP-4663N; -.
DR IntAct; P51862; 16.
DR MINT; P51862; -.
DR STRING; 4932.YLR371W; -.
DR iPTMnet; P51862; -.
DR MaxQB; P51862; -.
DR PaxDb; P51862; -.
DR PRIDE; P51862; -.
DR EnsemblFungi; YLR371W_mRNA; YLR371W; YLR371W.
DR GeneID; 851086; -.
DR KEGG; sce:YLR371W; -.
DR SGD; S000004363; ROM2.
DR VEuPathDB; FungiDB:YLR371W; -.
DR eggNOG; KOG4305; Eukaryota.
DR GeneTree; ENSGT00940000176600; -.
DR HOGENOM; CLU_001251_6_1_1; -.
DR InParanoid; P51862; -.
DR OMA; PYFARFD; -.
DR BioCyc; YEAST:G3O-32440-MON; -.
DR PRO; PR:P51862; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P51862; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IGI:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:SGD.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1356
FT /note="RHO1 GDP-GTP exchange protein 2"
FT /id="PRO_0000080969"
FT DOMAIN 659..846
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1034..1336
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 74..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1356 AA; 152596 MW; 5FBC542114E7BC92 CRC64;
MSETNVDSLG DRNDIYSQIF GVERRPDSFA TFDSDSHGDI SSQLLPNRIE NIQNLNVLLS
EDIANDIIIA KQRRRSGVEA AIDDSDIPNN EMKGKSSNYI LSQQTNIKEV PDTQSLSSAD
NTPVSSPKKA RDATSSHPIV HAKSMSHIYS TSNSASRQAK HYNDHPLPPM SPRNEVYQKN
KSTTAFVPKR KPSLPQLALA GLKKQSSFST GSASTTPTQA RKSPLQGFGF FSRPSSKDLH
EQHQHHQHIQ HNNINNHNNN NTNNNGAHYQ VGSSNSNYPQ HSHSISSRSM SLNSSTLKNI
ASSFQSKTSN SRKATQKYDI TSNPFSDPHH HHHHHHSSNS HSSLNNVHGS GNSSSVMGSS
SNIGLGLKTR VSSTSLALKR YTSVSGTSLS SPRRSSMTPL SASRPVMSAS SKKPQVYPAL
LSRVATKFKS SIQLGEHKKD GLVYRDAFTG QQAVDVICAI IRTSDRNLAL LFGRSLDAQK
LFHDVVYEHR LRDSPHEVYE FTDNSRFTGT GSTNAHDPLM LLPNSSSFNS GNHSYPNSGM
VPSSSTSSLN SDQATLTGSR LHMSSSLSQQ KNPAAIHNVN GVFTLLAECY SPTCTRDALC
YSISCPRRLE QQARLNLKPN GGLKRNISMA LDDDDEEKPS WTSSVSKEDW ENLPKKEIKR
QEAIYEVYIT EKNFVKSLEI TRDTFMKTLA ETNIISADIR KNFIKHVFAH INDIYSVNRR
FLKALTDRQR SSPVVRGIGD IVLRFIPFFE PFVSYVASRP YAKYLIETQR SVNPYFARFD
DDMMSSSLRH GIDSFLSQGV SRPGRYMLLV KEIMKSTDPE KDKSDYEDLS KAMDALRDFM
KRIDQASGAA QDRHDVKLLK QKILFKNEYV NLGLNDERRK IKHEGILSRK ELSKSDGTVV
GDIQFYLLDN MLLFLKAKAV NKWHQHKVFQ RPIPLPLLFA CPGEDMPALR KYIGDHPDCS
GTVIQPEYNT SNPKNAITFL YYGAKQRYQV TLYAAQYAGL QTLLEKIKQG QAAIISKTEM
FNVTKMSDRF FDYTNKINSV TSCDGGRKLL IATNSGLYMS NIKRQQNKDH RHKSSAFFST
PIQLVQRNNI TQIAVLEEFK SIILLIDKKL YSCPLSLIEA EGNGTSFFKK HHKELINHVS
FFAEGDCNGK RLIVTAHSSS HSIKYFEHEH PLLAEKNGSG SGNKKSLKKK ITEVIFDSEP
VSISFLKANL CIGCKKGFQI VSISQNAHES LLDPADTSLE FALRDTLKPM AIYRVGNMFL
LCYTEFAFFV NNQGWRKKES HIIHWEGEPQ KFAIWYPYIL AFDSNFIEIR KIETGELIRC
VLADKIRLLQ TSTQEILYCY EDYRGYDTVA SLDFWG
