ID   UBLH2_SCHPO             Reviewed;         300 AA.
AC   Q9UUB6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 2;
DE            EC=3.4.19.12;
GN   Name=uch2; ORFNames=SPBC409.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, INTERACTION WITH RPN10, AND SUBCELLULAR LOCATION.
RX   PubMed=15533439; DOI=10.1016/j.jmb.2004.09.057;
RA   Stone M., Hartmann-Petersen R., Seeger M., Bech-Otschir D., Wallace M.,
RA   Gordon C.;
RT   "Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S
RT   proteasome in fission yeast.";
RL   J. Mol. Biol. 344:697-706(2004).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10872838; DOI=10.1006/bbrc.2000.2767;
RA   Li T., Naqvi N.I., Yang H., Teo T.S.;
RT   "Identification of a 26S proteasome-associated UCH in fission yeast.";
RL   Biochem. Biophys. Res. Commun. 272:270-275(2000).
CC   -!- FUNCTION: Ubiquitin-protein hydrolase is involved both in the
CC       processing of ubiquitin precursors and of ubiquitinated proteins. This
CC       enzyme is a thiol protease that recognizes and hydrolyzes a peptide
CC       bond at the C-terminal glycine of ubiquitin.
CC       {ECO:0000269|PubMed:15533439}.
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   -!- SUBUNIT: Component of the 26S proteasome. Interacts with rpn10.
CC       {ECO:0000269|PubMed:15533439}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10872838,
CC       ECO:0000269|PubMed:15533439}.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB52608.1; -; Genomic_DNA.
DR   PIR; T40434; T40434.
DR   RefSeq; NP_595456.1; NM_001021366.3.
DR   AlphaFoldDB; Q9UUB6; -.
DR   SMR; Q9UUB6; -.
DR   BioGRID; 277472; 67.
DR   ComplexPortal; CPX-9077; 26S proteasome complex.
DR   FunCoup; Q9UUB6; 946.
DR   IntAct; Q9UUB6; 1.
DR   STRING; 284812.Q9UUB6; -.
DR   MEROPS; C12.009; -.
DR   iPTMnet; Q9UUB6; -.
DR   PaxDb; 284812-Q9UUB6; -.
DR   GeneID; 2540956; -.
DR   KEGG; spo:2540956; -.
DR   PomBase; SPBC409.06; uch2.
DR   VEuPathDB; FungiDB:SPBC409.06; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_1_0_1; -.
DR   InParanoid; Q9UUB6; -.
DR   OMA; YIQYEIQ; -.
DR   PhylomeDB; Q9UUB6; -.
DR   Reactome; R-SPO-5689603; UCH proteinases.
DR   PRO; PR:Q9UUB6; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0034399; C:nuclear periphery; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000502; C:proteasome complex; HDA:PomBase.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IGI:PomBase.
DR   GO; GO:0019784; F:deNEDDylase activity; IDA:PomBase.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR   GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IGI:PomBase.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; NAS:ComplexPortal.
DR   GO; GO:0000338; P:protein deneddylation; IDA:PomBase.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR   FunFam; 3.40.532.10:FF:000003; Ubiquitin carboxyl-terminal hydrolase; 1.
DR   Gene3D; 1.20.58.860; -; 1.
DR   Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR   InterPro; IPR041507; UCH_C.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS52048; UCH_DOMAIN; 1.
DR   PROSITE; PS52049; ULD; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..300
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 2"
FT                   /id="PRO_0000234561"
FT   DOMAIN          2..220
FT                   /note="UCH catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01393"
FT   DOMAIN          261..290
FT                   /note="ULD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01394"
FT   ACT_SITE        83
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01393"
FT   ACT_SITE        159
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01393"
FT   SITE            77
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01393"
FT   SITE            174
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01393"
SQ   SEQUENCE   300 AA;  34196 MW;  93B13076EF2EDB80 CRC64;
     MSWTTIESDA GVFTDLIENL GVKDVEVDEL YSLDVDSLRQ FPDIYGIIFL FKWNSKVDKP
     DGTMDYDSMD NIFFAKQVIN NACATQALLS VLLNHSDEID LGTTLSEFKD FSKTLPPELK
     GEALGNSEHI RCCHNSFARS DPFISEEVRA ATDEDEVYHF IAYTNINNVF YELDGLQAAP
     INHGSCTKEE FAEKAVSVIQ ARIANYDPAE IRFNLMVICK DKKASLLTRE DLTDEEKAAS
     IAVEDEKRLR WKRENQLRRH NFVGLFVELS KLLVKDRIDK NTWNSTLETA KAKYASQKRP
//