ID   UBLH1_SCHPO             Reviewed;         222 AA.
AC   Q10171;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 1;
DE            EC=3.4.19.12;
GN   Name=uch1; ORFNames=SPAC27F1.03c;
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).
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 (By similarity).
CC       {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 C12 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93292.1; -; Genomic_DNA.
DR   PIR; T38461; T38461.
DR   RefSeq; NP_594531.1; NM_001019960.2.
DR   AlphaFoldDB; Q10171; -.
DR   SMR; Q10171; -.
DR   BioGRID; 278227; 31.
DR   STRING; 284812.Q10171; -.
DR   MEROPS; C12.A10; -.
DR   MaxQB; Q10171; -.
DR   PaxDb; 4896-SPAC27F1-03c-1; -.
DR   EnsemblFungi; SPAC27F1.03c.1; SPAC27F1.03c.1:pep; SPAC27F1.03c.
DR   GeneID; 2541733; -.
DR   KEGG; spo:SPAC27F1.03c; -.
DR   PomBase; SPAC27F1.03c; uch1.
DR   VEuPathDB; FungiDB:SPAC27F1.03c; -.
DR   eggNOG; KOG1415; Eukaryota.
DR   HOGENOM; CLU_054406_0_2_1; -.
DR   InParanoid; Q10171; -.
DR   OMA; EFTADHQ; -.
DR   PhylomeDB; Q10171; -.
DR   Reactome; R-SPO-5689603; UCH proteinases.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   PRO; PR:Q10171; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0019784; F:deNEDDylase activity; IDA:PomBase.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR   GO; GO:0000338; P:protein deneddylation; IDA:PomBase.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd09616; Peptidase_C12_UCH_L1_L3; 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   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF17; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00140; UCH_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Proteasome; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..222
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase 1"
FT                   /id="PRO_0000211074"
FT   ACT_SITE        83
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT   ACT_SITE        158
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
SQ   SEQUENCE   222 AA;  24913 MW;  218317B99BEC35B0 CRC64;
     MWRPLENTPE VLEPYLQKIG VQDASVFDLF SLEEIPEYIP RPVHALLFVF PSSGTKTIYK
     GSRILPKDSD KVLWYPQTIP NACGTIGLLH AVSNGELRRK VNENDFIKSL IRTAEGSSIE
     ERAKLIEDSK ELEALHAAFA GPPLEVEGSE EDVETDLHFI CFVKGKSKDD NHFYELDGRQ
     EGPVQHSEIE SDLLNAEVLS VIKNYIQSID SPFFSLVAIT TP
//