UBP4_VANPO
ID UBP4_VANPO Reviewed; 882 AA.
AC A7TGY3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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; ORFNames=Kpol_1032p28;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480389; EDO18435.1; -; Genomic_DNA.
DR RefSeq; XP_001646293.1; XM_001646243.1.
DR AlphaFoldDB; A7TGY3; -.
DR SMR; A7TGY3; -.
DR STRING; 436907.A7TGY3; -.
DR MEROPS; C19.005; -.
DR EnsemblFungi; EDO18435; EDO18435; Kpol_1032p28.
DR GeneID; 5546722; -.
DR KEGG; vpo:Kpol_1032p28; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_005922_1_0_1; -.
DR InParanoid; A7TGY3; -.
DR OMA; KFFIDNR; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; A7TGY3; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; PS00973; USP_2; 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..882
FT /note="Ubiquitin carboxyl-terminal hydrolase 4"
FT /id="PRO_0000376821"
FT DOMAIN 182..308
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 519..879
FT /note="USP"
FT REGION 382..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 528
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 836
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 882 AA; 100061 MW; 2C55FD7734FDE34A CRC64;
MVEVDSRKQL LYDPIVRLSG IADKFVMQDA TSSNMKVSLQ ECIDTLANYQ DECKKLKRNE
PTLSPSERYS IYESAYIYYK IIHIMVLTRI PSLPQFSSAK SSDATNEDKE LMQIYNMLVK
TLLSDEKIAQ IKSYLRANYP DKNSKGKESI VNKQLLNNEV FMLPLSGSPI SAVQLNHLIQ
MYDSSLLLID VRPRAEFDSK HIKAKSVICV EPVSFKNSFT DLEVEKKSLI TSPQKEIALF
QARDKYNYIV IYTQQSEKTQ FYMHQQLVLL DILMNKSFAK PLNEKNIKVF TLDKGFSGWV
SKKGACETTT QNGDAIYISG NTSSLNLQNL PQLSPNIGSS MDKSMRDMMS TSADFEGRTY
QLPQQQQPVF ARTPSFKNLF NKAKSSSTSS VTSSSPAPSQ LVRPQTSSMP PLEQNFTQYP
ETPKLLTQIN TNTMPLSQIS PISSRAMSPM TKNMLTQSPQ LPMKISRTTI GNGAMLDLKP
HPDSKPPGQP VPALPQLPHH MTGTYQNLNQ PKLDLDFTVG LENMGNSCYM NCIIQCLLST
HELSQIFLNN SYEKHINLNS KLGSKGVLAK YFARLVHTMY REGSFKRPLE KNKPIQPIQF
KMACGSINSL FKDNTQQDSQ EFCQFLLDGL HEDLNQCGAN PPLKELSEDA EKMREKLSMR
IASSIEWERF LTTDFSVIVD LFQGQYASQL KCKVCGCTST TYQTFSVLSV PVPHVSSCHI
LDCFNEFTKV EKLGTDELWS CPTCKKKQPS TKKLTITRLP RNLIIHLKRF DNMMNKNNVF
VKYPFLLDLT PYWANDFDGR LPPGVTDELP TRGQVPPFRY KLNAVASHVG SLYGGHYTAY
VNKGINRGWH YFDDTSYRPI KNETECITPN AYVLFYHRVY GV
