UBP4_CANGA
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 03-AUG-2022, entry version 103.
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 / 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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380955; CAG60481.1; -; Genomic_DNA.
DR RefSeq; XP_447544.1; XM_447544.1.
DR AlphaFoldDB; Q6FQF0; -.
DR SMR; Q6FQF0; -.
DR STRING; 5478.XP_447544.1; -.
DR MEROPS; C19.005; -.
DR EnsemblFungi; CAG60481; CAG60481; CAGL0I06765g.
DR GeneID; 2889068; -.
DR KEGG; cgr:CAGL0I06765g; -.
DR CGD; CAL0132056; CAGL0I06765g.
DR VEuPathDB; FungiDB:CAGL0I06765g; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_005922_1_0_1; -.
DR InParanoid; Q6FQF0; -.
DR OMA; KFFIDNR; -.
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:0016579; P:protein deubiquitination; IEA:InterPro.
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 Gene3D; 3.40.250.10; -; 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 Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR SUPFAM; SSF54001; SSF54001; 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
