UBP1_SCHPO
ID UBP1_SCHPO Reviewed; 849 AA.
AC Q9USM5;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 1;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 1;
DE AltName: Full=Ubiquitin thioesterase 1;
DE AltName: Full=Ubiquitin-specific-processing protease 1;
GN Name=ubp1; ORFNames=SPCC16A11.12c;
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 -!- 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; CU329672; CAB53084.1; -; Genomic_DNA.
DR PIR; T41085; T41085.
DR RefSeq; NP_587999.1; NM_001022990.2.
DR AlphaFoldDB; Q9USM5; -.
DR BioGRID; 275798; 1.
DR STRING; 4896.SPCC16A11.12c.1; -.
DR MEROPS; C19.A55; -.
DR iPTMnet; Q9USM5; -.
DR MaxQB; Q9USM5; -.
DR PaxDb; Q9USM5; -.
DR PRIDE; Q9USM5; -.
DR EnsemblFungi; SPCC16A11.12c.1; SPCC16A11.12c.1:pep; SPCC16A11.12c.
DR GeneID; 2539228; -.
DR KEGG; spo:SPCC16A11.12c; -.
DR PomBase; SPCC16A11.12c; ubp1.
DR VEuPathDB; FungiDB:SPCC16A11.12c; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; Q9USM5; -.
DR OMA; SGTCNEA; -.
DR PhylomeDB; Q9USM5; -.
DR Reactome; R-SPO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR PRO; PR:Q9USM5; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 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..849
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 1"
FT /id="PRO_0000080602"
FT DOMAIN 20..120
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 279..848
FT /note="USP"
FT ACT_SITE 288
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 849 AA; 98656 MW; C8118042229BA9CB CRC64;
MASTATQNAS TRYSQIWIDQ PASLPFQDSI NLIKEDKEKW KKEKTAFLID YDWFEGYVDF
IYGEGDNPGP ITQWRLLDEK NELKHSLEES IDYSIVSASL WHMLVEWFGL EGLAIERKVL
LVGLAAEQKP FVDIYPINFT LHVLFDPING ENTSYSPLYQ IDEPYHSDEP YAFSFSRSDT
LRSLYKQVME AFQISDGTSF RLWYLNKSNL SSRFVSLSEF NDQPAIALLS EYAVCMTIFE
IDIADGSLLL EFQHPNGEWL SDSITKEQNL TINKEIGLCG LYNLGNSCYM NSALQCMIHT
HELTKYFLSD SYEKDINYNN PLGMMGKVAL SYASLLKMIH HTADMHSVSP SSFKFIIGEF
NTYFSGYRQQ DSQEFIAFFL DGLHEDLNRI QIKPYFERPD LFDEHPLHVQ RVANQCWDIH
TKRNDSIIVQ LFQGMYKSTL ECSICYQKST AFDPFMYLTL PLPTSAKWRH KVVYVPPFGT
QSPVELYLEL LMESTVIQMK FQATEKLQKM GLECGELTAC DIYRGKVYKV LKNKDKISKK
IHKWDHVVLY GSTANGLTIP IVHGCKRPAM PGSYQSNDVF GFPLQLNVRS RNVLTNDLVK
EIVELYRVYA GIDVAIGTLQ LGLKRMESKA GKWECIKEIE VKRFEIVEEE EIVIDDKTVI
MCLWNDQQYE KLFYNCEWIF EKIQFHMESI TLEDCLLEFS KPEQLDLQDS WYCPGCKAFR
PATKRLEIWR LPKILVIHLN RFSGHGGDLR RRRKRRDLVV YPVFDLNLKQ FLSPFIKDHE
WLSSQKSMLY DLYAVDNHHG FMSNGHYTAY ARDASSQTFF KFDDTAICEI DPEDIVTSSA
YVLFYRAKN
