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