ID   UBP4_CANGA              Reviewed;         887 AA.
AC   Q6FQF0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 4;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 4;
DE   AltName: Full=Ubiquitin thioesterase 4;
DE   AltName: Full=Ubiquitin-specific-processing protease 4;
GN   Name=DOA4; Synonyms=UBP4; OrderedLocusNames=CAGL0I06765g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
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: Ubiquitin thioesterase that acts at the late
CC       endosome/prevacuolar compartment to recover ubiquitin from
CC       ubiquitinated membrane proteins en route to the vacuole. Removes also
CC       ubiquitin from soluble proteins targeted to proteasomes. Is essential
CC       to maintain a normal level of free ubiquitin. Required for promoting
CC       coordination of DNA replication and avoids DNA overreplication (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- ACTIVITY REGULATION: RFU1 is an inhibitor of deubiquitination activity.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Late endosome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; CR380955; CAG60481.1; -; Genomic_DNA.
DR   RefSeq; XP_447544.1; XM_447544.1.
DR   AlphaFoldDB; Q6FQF0; -.
DR   SMR; Q6FQF0; -.
DR   STRING; 284593.Q6FQF0; -.
DR   MEROPS; C19.005; -.
DR   EnsemblFungi; CAGL0I06765g-T; CAGL0I06765g-T-p1; CAGL0I06765g.
DR   GeneID; 2889068; -.
DR   KEGG; cgr:CAGL0I06765g; -.
DR   CGD; CAL0132056; CAGL0I06765g.
DR   VEuPathDB; FungiDB:B1J91_I06765g; -.
DR   VEuPathDB; FungiDB:CAGL0I06765g; -.
DR   eggNOG; KOG1868; Eukaryota.
DR   HOGENOM; CLU_005922_1_0_1; -.
DR   InParanoid; Q6FQF0; -.
DR   OMA; SIEWERY; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:EnsemblFungi.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1904669; P:ATP export; IEA:EnsemblFungi.
DR   GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR   GO; GO:0010995; P:free ubiquitin chain depolymerization; IEA:EnsemblFungi.
DR   GO; GO:0070676; P:intralumenal vesicle formation; IEA:EnsemblFungi.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF95; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4-RELATED; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endosome; Hydrolase; Membrane; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..887
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 4"
FT                   /id="PRO_0000376819"
FT   DOMAIN          202..328
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          525..885
FT                   /note="USP"
FT   REGION          358..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        534
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT   ACT_SITE        842
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
SQ   SEQUENCE   887 AA;  101165 MW;  A9E756B4D60894BE CRC64;
     MPGIEQPVSR KNETLVKLSS LADEFVFNDE VQLNLQDVLQ ECVDTYQNYQ DEVKKIKNMD
     HTESEKVSEL CKSAYIYYKI VHNFITKVIP HLPEFEVATG PKASKLQAEL IKIYYSLFSR
     LESDKKISYI KNIIIKHMDT QENNHSVESH EQVKLSNKKL PVNRDAIEID KDSILQDIRY
     INGKRSGSGI SCSELLSLMK MKEDSLLLID VRPKLEYDAH HIKTKNIICI EPISFKESYS
     DQQIEKTSMI PSPKHEIQLF QRRSEFQYII LYTDLEEKSN FYFQQLKSLL EILLQRSFLR
     PIDDRKTKVL FLSDSLQNWI KNGGEIDKSQ EVSKIRNRSI SGSGPLLNSL SERKTIGAFP
     DINRNSTKQM PISPLPSLPG SERTVATPPN GSSTLGRINS PVTHYPKAPL INDSEFHLNI
     NNNHSPPTHL PSKDNNPLAS SMPIGSDHKP FMSPQNSLPL APKPPTLESK NYNFISDRSN
     IIDQKQNRSR SLEPQLPPIP STLIRKNSPE KTLSCNQMMD TSFTVGLENM GNSCYINCII
     QCIFATTELI KIFLNGTYAK HINKQSKLGS KGVLSHNFAK LLKDMYEENS SKKIGKKHGA
     VKTLQFKMAC ASVNSLFKDA SQQDCLEFCQ FLLDGLHEDL NQCGANPPLK ELSPEAEKMR
     ENLSLRVASS IEWERYLTTD FSIIVDLFQG QYASQLRCKV CNRTSTTYQA FSVLSVPVPS
     GKSCGLLDCF IEFTKTENLE VDEQWFCPSC KKKQPSTKKL TITRLPRNLI IHLKRFDNMM
     NKNNIFVRYP QILDLTPFWA NDSDGKLPPG ITDEIPARGQ VPPFNYRLYG AACHFGTLYG
     GHYTSYVDKG PEKGWIYFDD TVYRPVRFQN EFISPSAYVL FYHRITS
//