UBP5_SCHPO
ID UBP5_SCHPO Reviewed; 1108 AA.
AC Q09879; Q10433; Q9Y7P5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 5;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 5;
DE AltName: Full=Ubiquitin thioesterase 5;
DE AltName: Full=Ubiquitin-specific-processing protease 5;
GN Name=ubp5; ORFNames=SPCC188.08c;
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; CAB41228.1; -; Genomic_DNA.
DR PIR; T41188; T41188.
DR RefSeq; NP_588211.1; NM_001023201.2.
DR AlphaFoldDB; Q09879; -.
DR SMR; Q09879; -.
DR BioGRID; 275950; 3.
DR STRING; 4896.SPCC188.08c.1; -.
DR MEROPS; C19.A59; -.
DR iPTMnet; Q09879; -.
DR SwissPalm; Q09879; -.
DR MaxQB; Q09879; -.
DR PaxDb; Q09879; -.
DR PRIDE; Q09879; -.
DR EnsemblFungi; SPCC188.08c.1; SPCC188.08c.1:pep; SPCC188.08c.
DR GeneID; 2539385; -.
DR KEGG; spo:SPCC188.08c; -.
DR PomBase; SPCC188.08c; ubp5.
DR VEuPathDB; FungiDB:SPCC188.08c; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_1_1; -.
DR InParanoid; Q09879; -.
DR OMA; NRPLGPH; -.
DR PhylomeDB; Q09879; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SPO-8948747; Regulation of PTEN localization.
DR PRO; PR:Q09879; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:PomBase.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:PomBase.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:PomBase.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 2.60.210.10; -; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50144; MATH; 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..1108
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 5"
FT /id="PRO_0000080606"
FT DOMAIN 55..187
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 213..528
FT /note="USP"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 464
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1108 AA; 128668 MW; 5C5A57058E3839C7 CRC64;
MVTGETLVDS QKSLINNDTL LNEKLKEDFE ENVSIDVKIH EELRRALPDY EESGFQRFTW
HIKSWHELDR RAVSPQFAVG SRQFKITYFP QGTLQSAGFT SIFLEYIPSE EEKLSNKYGC
CCQFAFVISN PRKPSLSVAN SAHCRFSPEI VDWGFTQFAE LKKLLCRQAP DVPPIVEDGA
LLLTAYVRIL KDPTGVLWHS FNDYDSKIAT GYVGLKNQGA TCYMNSLLQS LYIIHAFRRI
VYQIPTDSPQ GKDSIAYALQ RCFYNLQFMN EPVSTTELTK SFGWDSLDSF MQHDVQEFNR
VLQDNLERSM RDTKVENALT NLFVGKMKSY IACVNVNFES ARSEDYWDIQ LNVKGMKNLE
DSFRSYIQVE TLEGDNCYFA DTYGFQEAKK GVIFESFPPI LHLQLKRFEY DFERDMMIKI
NDRYEFPLEF DAKAFLSPEA DQSQNCEYVL YGVLVHSGDL HNGHYYALLK TEKDGPWYKY
DDTRVTRATL REVLEENYGG DYIMHPPFRS PVKLKRFMSA YMLLYLRKDK LDELMNPVSA
DEIPEHLKEA LNPSIQLAEL RRKERLESHL YTKVQLITPE FYSEHHEFDI ADFGNAYKEE
TIPQFRIKKE AKFSEFIPIV AEKLGYPQEC MRFWYVVKRH NCTVRVESPV NELNSTMEEV
KNVWNSQGEI LRLYLEITPE NELSSSLTHQ NTGEWNAFIF VKYFDRKSQE ISGCGTLHVN
KSDEIRSICP LLCERANLPK NTPLNIYEEI KPGMVDFLRL EKTFTQSELS TGDIICFEPC
RPSALEDDIV NSGFDSALKL YDFLSNKVLV LFRPRFIDQD SIIEFEMLLD RRIKYDDLCI
ELGQKLGIGA DHIRLTTCNP LTYSAGMVVP NDSNITLYEI LYSSEEEMPS NVIFYETMDV
SLSDLDRKRL VRLRWLVDGL ANIELVEAYI NKSGDINDLF GAVCERFPDS DLRKKKVRVY
EVFESRYHRD LSLRTLIRTI NPAATLVGEV VPLDQLQLYP EEKIVQVHHF HKDIARIHGI
PFSFVIKPQE KFIDTKLRLA ARTQYPESIF SVIKFCVVDF DNNRVVYLND EDITYDVVEK
LNGTLALDRA KKDSKKPNIL DRAIQMKN
