ID   RFU1_CANGA              Reviewed;         203 AA.
AC   Q6FKA3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Regulator of free ubiquitin chains 1;
GN   Name=RFU1; OrderedLocusNames=CAGL0L13156g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RFU1 family. {ECO:0000305}.
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DR   EMBL; CR380958; CAG62315.1; -; Genomic_DNA.
DR   RefSeq; XP_449341.1; XM_449341.1.
DR   AlphaFoldDB; Q6FKA3; -.
DR   SMR; Q6FKA3; -.
DR   STRING; 5478.XP_449341.1; -.
DR   EnsemblFungi; CAG62315; CAG62315; CAGL0L13156g.
DR   GeneID; 2890591; -.
DR   KEGG; cgr:CAGL0L13156g; -.
DR   CGD; CAL0135822; CAGL0L13156g.
DR   VEuPathDB; FungiDB:CAGL0L13156g; -.
DR   eggNOG; ENOG502S3ZX; Eukaryota.
DR   HOGENOM; CLU_1348926_0_0_1; -.
DR   InParanoid; Q6FKA3; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProt.
DR   GO; GO:0010992; P:ubiquitin recycling; IEA:EnsemblFungi.
DR   InterPro; IPR015063; USP8_dimer.
DR   Pfam; PF08969; USP8_dimer; 1.
PE   3: Inferred from homology;
KW   Endosome; Protease inhibitor; Reference proteome; Thiol protease inhibitor.
FT   CHAIN           1..203
FT                   /note="Regulator of free ubiquitin chains 1"
FT                   /id="PRO_0000376813"
SQ   SEQUENCE   203 AA;  23706 MW;  39F786E409293996 CRC64;
     MKSTQQLGQE AREFEFNPNI PLHLYLKTCV TLLNNASECF QRGDKSLSYF YYFRYVDLCT
     NKLPNHPTIR STSTGLDNDS KLYVQEYKQL LRLEVPHILK IMEELKTELD AMYERHKVSL
     ANNIASPISY KHNNRMDALL HDYYTERGCT GHSMQHKTSL HKNENFNERI NLMKDSFMGR
     APNGSQEVRN VSNTFYPDLP TLS