UBP4_ASHGO
ID UBP4_ASHGO Reviewed; 852 AA.
AC Q754R5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=AFR007W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53378.2; -; Genomic_DNA.
DR RefSeq; NP_985554.2; NM_210908.2.
DR AlphaFoldDB; Q754R5; -.
DR SMR; Q754R5; -.
DR STRING; 33169.AAS53378; -.
DR MEROPS; C19.005; -.
DR EnsemblFungi; AAS53378; AAS53378; AGOS_AFR007W.
DR GeneID; 4621793; -.
DR KEGG; ago:AGOS_AFR007W; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_005922_1_0_1; -.
DR InParanoid; Q754R5; -.
DR OMA; KFFIDNR; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
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..852
FT /note="Ubiquitin carboxyl-terminal hydrolase 4"
FT /id="PRO_0000376818"
FT DOMAIN 172..296
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 488..849
FT /note="USP"
FT REGION 369..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 497
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 806
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 852 AA; 96523 MW; 770745A86B229FAD CRC64;
MPHIQESRVW CRSISQLSHL AEQFVTENGT ESTDMKLLLQ QCVDTLSNYQ DECKKIKSVS
KPVPSKELYD LYETAYVYFK IVSLIVLNKI PKLEEYARAK SDAVDRTGKQ LLEIYNMLVN
RLVKDDRIAE IKRFVKENSR RDPEAKNEQI GVESGKSIPA TLLRNLLMGP SASGTVLLVD
VRPRLDFMRC HIKSSSIICI EPVSFKESYT DIDLGKKSMI TSPDAEIALF QDRDKFDYIV
VYTQDSEKNK HNVQQQQLLV DLLINRSFEK ALDRTKVFIL AGGFSEWSNA HPDFCVSSQG
DSVYLNGDTS GLSLQLMPQT TPQKQYNNMF QTMLSGPTDV HGIIRNPHNF PTQQKSKLKR
VPSFRDYFRS SSSSSNINER PGSVPPQLSN GSTIYPETPK LMTNDEYMKS LPQLSPITAR
AITSPSRALS AVGVSKSSAS NSISSLLANS GSASPMKPPD TPLPFTDSIK TLGQQNLTVA
VSNLNFSVGL VNCGNSCYMS CIIQCLLGTQ ELCTMFLNNS YQNHINLNSR LGSKGLLARY
FSQLIHQMYQ YGKDIRKKMG NEKTAVIPTQ FKIACGSINS SFKDNTQQDC QEFCQFLLDG
LHEDLNQCGN NPPLKELSEE AEKMREMMPM RLASAIEWER YLTTDFSVIV DLFQGQYASQ
LQCKVCQRTS TTYQPFSVLS VPVPSTRTCT LTDCFTEFTK IETLEQEEQW SCPSCKKRQP
STKKITITRL PRNLIIHLKR FDNMLNKNNV FVSYPSVLDL TAFWANDYDK KVTNNNVELP
SRGQVPPFNY QLYGIACHDG TLRAGHYTAY VNKGAVLGWC YYDDTNWRQI RSAREYITQN
AYVLFYHRIH ST
