UBLH1_SCHPO
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 03-AUG-2022, entry version 142.
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; 4896.SPAC27F1.03c.1; -.
DR MEROPS; C12.A10; -.
DR MaxQB; Q10171; -.
DR PaxDb; Q10171; -.
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; YVCFVKG; -.
DR PhylomeDB; Q10171; -.
DR Reactome; R-SPO-5689603; UCH proteinases.
DR Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
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:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.532.10; -; 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; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 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
