RFU1_YEAST
ID RFU1_YEAST Reviewed; 200 AA.
AC Q08003; D6VY74;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Regulator of free ubiquitin chains 1;
GN Name=RFU1; OrderedLocusNames=YLR073C;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH BRO1 AND DOA4.
RX PubMed=19410548; DOI=10.1016/j.cell.2009.02.028;
RA Kimura Y., Yashiroda H., Kudo T., Koitabashi S., Murata S., Kakizuka A.,
RA Tanaka K.;
RT "An inhibitor of a deubiquitinating enzyme regulates ubiquitin
RT homeostasis.";
RL Cell 137:549-559(2009).
CC -!- FUNCTION: Inhibitor of the DOA4 deubiquitinase involved in the
CC regulation of protein degradation by the proteasome and maintenance of
CC a normal level of free ubiquitin. {ECO:0000269|PubMed:19410548}.
CC -!- SUBUNIT: Interacts with BRO1 and DOA4. {ECO:0000269|PubMed:19410548}.
CC -!- INTERACTION:
CC Q08003; P48582: BRO1; NbExp=2; IntAct=EBI-2353109, EBI-3768;
CC Q08003; P32571: DOA4; NbExp=2; IntAct=EBI-2353109, EBI-19840;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RFU1 family. {ECO:0000305}.
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DR EMBL; Z73245; CAA97630.1; -; Genomic_DNA.
DR EMBL; AY558532; AAS56858.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09390.1; -; Genomic_DNA.
DR PIR; S64905; S64905.
DR RefSeq; NP_013174.1; NM_001181960.1.
DR AlphaFoldDB; Q08003; -.
DR SMR; Q08003; -.
DR BioGRID; 31347; 49.
DR IntAct; Q08003; 2.
DR MINT; Q08003; -.
DR STRING; 4932.YLR073C; -.
DR MaxQB; Q08003; -.
DR PaxDb; Q08003; -.
DR PRIDE; Q08003; -.
DR EnsemblFungi; YLR073C_mRNA; YLR073C; YLR073C.
DR GeneID; 850762; -.
DR KEGG; sce:YLR073C; -.
DR SGD; S000004063; RFU1.
DR VEuPathDB; FungiDB:YLR073C; -.
DR eggNOG; ENOG502S3ZX; Eukaryota.
DR HOGENOM; CLU_1348926_0_0_1; -.
DR InParanoid; Q08003; -.
DR OMA; LKTCVNI; -.
DR BioCyc; YEAST:G3O-32225-MON; -.
DR PRO; PR:Q08003; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q08003; protein.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:SGD.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0010992; P:ubiquitin recycling; IMP:SGD.
PE 1: Evidence at protein level;
KW Endosome; Protease inhibitor; Reference proteome; Thiol protease inhibitor.
FT CHAIN 1..200
FT /note="Regulator of free ubiquitin chains 1"
FT /id="PRO_0000247248"
SQ SEQUENCE 200 AA; 22850 MW; 1C93378ED78C41A4 CRC64;
MKSSKQLVQD AKDYRFNPAI PLRIYLKTCI GILEKAQCAF QANDLSLSFI YYFRYVDLLT
NKLSRHPELL RMDASSSSSS SYIHKREYLQ LIKLEVPAVC KIIESLRTQI DSQYSKLQTS
LANNIAKPNI NANTTPVQVE QQPLPKKSFD EYSFNQSISF FQKISNAQLN TGASSQSQAT
ARDEAYRLNY PELPRLTFST
