ID   UBP2_KLULA              Reviewed;        1220 AA.
AC   O42726; Q6CPT4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 2;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 2;
DE   AltName: Full=Ubiquitin thioesterase 2;
DE   AltName: Full=Ubiquitin-specific-processing protease 2;
GN   Name=UBP2; OrderedLocusNames=KLLA0E02376g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-539 / JBD100;
RX   PubMed=10953877; DOI=10.1007/s002940000129;
RA   Winkler A.A., Korstanje R., Zonneveld B.J.M., Hooykaas P.J.J.,
RA   Steensma H.Y.;
RT   "Isolation and characterization of KIUBP2, a ubiquitin hydrolase gene of
RT   Kluyveromyces lactis that can suppress a ts-mutation in CBF2, a gene
RT   encoding a centromeric protein of Saccharomyces cerevisiae.";
RL   Curr. Genet. 38:17-22(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: Has an ATP-independent isopeptidase activity, cleaving at the
CC       C-terminus of the ubiquitin moiety in natural or engineered linear
CC       fusion proteins, irrespective of their size or the presence of an N-
CC       terminal extension to ubiquitin. {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   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; AF022776; AAB94074.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99142.1; -; Genomic_DNA.
DR   PIR; T30529; T30529.
DR   RefSeq; XP_454055.1; XM_454055.1.
DR   AlphaFoldDB; O42726; -.
DR   STRING; 28985.XP_454055.1; -.
DR   MEROPS; C19.A56; -.
DR   EnsemblFungi; CAG99142; CAG99142; KLLA0_E02377g.
DR   GeneID; 2894270; -.
DR   KEGG; kla:KLLA0_E02377g; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003155_1_0_1; -.
DR   InParanoid; O42726; -.
DR   OMA; CDIKVDV; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:EnsemblFungi.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:EnsemblFungi.
DR   GO; GO:0010992; P:ubiquitin recycling; IEA:EnsemblFungi.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR025305; UCH_repeat_domain.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF13446; RPT; 3.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; SSF54001; 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   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1220
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 2"
FT                   /id="PRO_0000080587"
FT   DOMAIN          698..1202
FT                   /note="USP"
FT   ACT_SITE        707
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        1153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   CONFLICT        646..650
FT                   /note="KWSHG -> EMESR (in Ref. 1; AAB94074)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1009..1022
FT                   /note="KSIEPLPFGETLYM -> QVYRAATFRRKRCTW (in Ref. 1;
FT                   AAB94074)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1220 AA;  141120 MW;  7362B30C368B4A47 CRC64;
     MMASQEPALE LNGEQRDSVS ETAEVLRSKS LESFSDLVDD GKTLLYGDIS KSFPFKTCDR
     ILDDIRISPW FLKKFGSSVM KQPMLQYSRE RQQLQPWNLV HLIDQVNLRS RYDYDSMTCP
     GKNTISVMFA LLVDPNFTPN DFDDIDKFPE YFFHLKITVK RRSYLENFNR HVGITHYHVL
     EPESLHPFDK RDIFIMEEKD CRLVDQSIFV SADTNKLILV EIIKPEFNSE NLAEYRTAKI
     EERYKNACQE FDLLNPDDIP SQAECLKTLF MIFKNPLQRK SANSEFKIIS RDSVALNSQI
     NTDWLTTMFD FSLQKTAVED NVQSGEEYKP PDLVDYITDF KVRGIREAYT RKSMEVVLIG
     KQSMLLENEL GTEKKTVAKC FSNQHFSASH TWWFNILNHQ HIEPFPYDIN YHFINLSVAF
     KYIDKDIIKN YETQIALDQE NISHYFDALQ YVTNAKGSYQ LIAYCGKQDV VGYEDLNNAL
     QVFGLDPTDI DASLLDANTM IEYYNSHLLR SSDNQRKDLR NALRVLGKYL GSQKMLFLVE
     YEPYYNVQQA YTLLKVDETV DDDIIQTAYT INIADAPGLK KDYDRAIFTI ALDRRSIFLL
     NVLTDECPEF AQYYNCTDIS YDEALNIIEI DMNASDDVIL EVFQKKWSHG IMTGPDYLLK
     LKMALQNIGF TRNSKLINHF LDTGIVDVSC LPVATWPAGI NNVGNTCYLN SLLQFFFTIK
     PLRDFILNYD DDSAKLLDAS EYHSRRRIGG REVSKQEELR SVQFVYHLRD LFNDMIHTNS
     RCVTPTKELV YLAFAPSNVE VEFGDDTVAQ KELIDLTTDV VEDPTDTTRH LASCDDDIIM
     CQSPVALPEH KTSSEAGTQQ YSVQVAKISA DQLENTLEIG RQQDVTECIG NVLAQLEIAS
     EPLSLEDDLE QNDLVKQLFY GRIKQDLIPV NDEASVRTKY ERFLSLLVNT GDHPKDIYDA
     LDFYFQNDYL NLEEYGDVKR TVSISELPAV LQIQIQRVYY DREKFMPFKS IEPLPFGETL
     YMDRYMATED PKLLAEIQQN AELKQKLQDL KQRQRKLLSQ NEIGLTLKSS LIETKKFLQS
     GTLKAHDIDA DNIPSSIAYI DILINNIDEE LKSLFNKITD LETTISQQFS EFKHIGYSLF
     AVFIHRGEAS YGHYWVYIKD HTKNGIWRKY NDDSVTEVPQ SEVFNFTEGN TATPYFLVYV
     REGQEQETIE PLKRILQQQE