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ROM1_YEAST
ID   ROM1_YEAST              Reviewed;        1155 AA.
AC   P53046; Q92326;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=RHO1 GDP-GTP exchange protein 1;
DE   AltName: Full=Protein kinase C suppressor SKC1;
GN   Name=ROM1; Synonyms=SKC1; OrderedLocusNames=YGR070W;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RA   Jacoby J.J., Kirchrath L., Heinisch J.J.;
RT   "Isolation of a novel pkc1 mutant and two of its multicopy suppressors from
RT   Saccharomyces cerevisiae.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 960.
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-1155, AND 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-155 AND THR-180, AND
RP   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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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.
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DR   EMBL; U55000; AAA99813.1; -; Genomic_DNA.
DR   EMBL; Z72855; CAA97072.1; -; Genomic_DNA.
DR   EMBL; D83171; BAA11827.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08164.2; -; Genomic_DNA.
DR   PIR; S64365; S64365.
DR   RefSeq; NP_011584.2; NM_001181199.2.
DR   AlphaFoldDB; P53046; -.
DR   SMR; P53046; -.
DR   BioGRID; 33313; 60.
DR   DIP; DIP-6270N; -.
DR   IntAct; P53046; 2.
DR   MINT; P53046; -.
DR   STRING; 4932.YGR070W; -.
DR   iPTMnet; P53046; -.
DR   PaxDb; P53046; -.
DR   PRIDE; P53046; -.
DR   EnsemblFungi; YGR070W_mRNA; YGR070W; YGR070W.
DR   GeneID; 852961; -.
DR   KEGG; sce:YGR070W; -.
DR   SGD; S000003302; ROM1.
DR   VEuPathDB; FungiDB:YGR070W; -.
DR   eggNOG; KOG4305; Eukaryota.
DR   GeneTree; ENSGT00940000176600; -.
DR   HOGENOM; CLU_001251_0_0_1; -.
DR   InParanoid; P53046; -.
DR   OMA; GEGWPIT; -.
DR   BioCyc; YEAST:G3O-30783-MON; -.
DR   PRO; PR:P53046; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53046; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:SGD.
DR   GO; GO:0090630; P:activation of GTPase activity; IGI:SGD.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IGI: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; 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   CHAIN           1..1155
FT                   /note="RHO1 GDP-GTP exchange protein 1"
FT                   /id="PRO_0000080968"
FT   DOMAIN          464..651
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          842..1137
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   REGION          100..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         180
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        214
FT                   /note="T -> P (in Ref. 1; AAA99813 and 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        250
FT                   /note="L -> V (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279..281
FT                   /note="KLS -> QLG (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="Y -> N (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="H -> Y (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557
FT                   /note="F -> L (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        844
FT                   /note="R -> C (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        852
FT                   /note="H -> S (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        897
FT                   /note="K -> N (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        959
FT                   /note="A -> T (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        960
FT                   /note="V -> A (in Ref. 2; CAA97072)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        961
FT                   /note="Q -> K (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1037
FT                   /note="N -> D (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1151
FT                   /note="E -> G (in Ref. 4; BAA11827)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1155 AA;  131420 MW;  B7289DE418BA7A64 CRC64;
     MNSNELDLRN KYFYEIFGKK RKSDTSTPTQ LFSGSKVQTN INEISITNDE DEDSTEDENK
     ASLKDYTLGH DTGARYRIAP DCSSHQLKAS PVLHISTNLN SSPQSFTGDQ ISPTNKKISI
     NDSTRQDKGN SCTTTSSPSQ KRSNVLLPHV RKHSSPSLLS FSKNSGSHMG DPNQLSTPPT
     PKSAGHTMEL HSSFNGKHSS SSTSSLFALE SLKTQNRRSS NSSNHSSQYR RHTNQHQRHH
     SRSKSSPVSL TEISMIKGTP LVYPALLSLI AIKFKQTIKL STHKKMGLLY RDSFTGKQAI
     DTLCLIIGSL DRNLGMLIGK SLEAQKLFHD VLYDHGVRDS VLEIYELSSE SIFMAHQSQS
     STSIANTFSS SSSSVNSLRT KTEIYGVFVP LTHCYSSTCS LEKLCYSISC PNRLQQQANL
     HLKLGGGLKR NISLALDKED DERISWTNSV PKSVWESLSK QQIKRQEAIY ELFTTEKKFV
     KSLEIIRDTF MKKLLETNII PSDVRINFVK HVFAHINEIY SVNREFLKAL AQRQSLSPIC
     PGIADIFLQY LPFFDPFLSY IASRPYAKYL IETQRSVNPN FARFDDEVSN SSLRHGIDSF
     LSQGVSRPGR YSLLVREIIH FSDPVTDKDD LQMLMKVQDL LKDLMKRIDR ASGAAQDRYD
     VKVLKQKILF KNEYVNLGLN NEKRKIKHEG LLSRKDVNKT DASFSGDIQF YLLDNMLLFL
     KSKAVNKWHQ HTVFQRPIPL PLLFICPAED MPPIKRYVTE NPNCSAGVLL PQYQTSNPKN
     AIVFAYYGTK QQYQVTLYAP QPAGLQTLIE KVKQEQKRLL DETKHITFKQ MVGQFFHSYI
     NTNRVNDVLI CHAGKILLVA TNMGLFVLNY ATSINQKPVH LLHKISISQI SVLEEYKVMI
     LLIDKKLYGC PLDVIDDAEN ADFLFRKNSK VLFKYVAMFK DGFCNGKRII MIAHHFLHAV
     QLLIVNPLIF DFNSGNFKKN LKAGLVDFSV DSEPLSFSFL ENKICIGCKK NIKILNVPEV
     CDKNGFKMRE LLNLHDNKVL ANMYKETFKV VSMFPIKNST FACFPELCFF LNKQGKREET
     KGCFHWEGEP EQFACSYPYI VAINSNFIEI RHIENGELVR CVLGNKIRML KSYAKKILYC
     YEDPQGFEII ELLNF
 
 
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