ID   UBP2_SCHPO              Reviewed;        1141 AA.
AC   Q9P3U0;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 2;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 2;
DE   AltName: Full=Ubiquitin thioesterase 2;
DE   AltName: Full=Ubiquitin-specific-processing protease 2;
GN   Name=ubp2; ORFNames=SPAC328.06;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112; SER-113; THR-115;
RP   THR-721 AND SER-722, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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; CU329670; CAB96001.1; -; Genomic_DNA.
DR   RefSeq; NP_594208.1; NM_001019631.2.
DR   AlphaFoldDB; Q9P3U0; -.
DR   BioGRID; 278537; 152.
DR   STRING; 284812.Q9P3U0; -.
DR   MEROPS; C19.A56; -.
DR   iPTMnet; Q9P3U0; -.
DR   MaxQB; Q9P3U0; -.
DR   PaxDb; 4896-SPAC328-06-1; -.
DR   EnsemblFungi; SPAC328.06.1; SPAC328.06.1:pep; SPAC328.06.
DR   GeneID; 2542059; -.
DR   KEGG; spo:SPAC328.06; -.
DR   PomBase; SPAC328.06; ubp2.
DR   VEuPathDB; FungiDB:SPAC328.06; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003155_0_0_1; -.
DR   InParanoid; Q9P3U0; -.
DR   OMA; HHLVYKS; -.
DR   PhylomeDB; Q9P3U0; -.
DR   PRO; PR:Q9P3U0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061578; F:K63-linked deubiquitinase activity; IDA:PomBase.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IDA:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:PomBase.
DR   CDD; cd02666; Peptidase_C19J; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR025305; UCH_repeat_domain.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF13446; RPT; 4.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1141
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase 2"
FT                   /id="PRO_0000080603"
FT   DOMAIN          614..1124
FT                   /note="USP"
FT   REGION          748..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        623
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        1076
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         112
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         115
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         721
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         722
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1141 AA;  130297 MW;  1499E32DB6CB26CB CRC64;
     MATVKNLRIG KSPNRLIQDL DVFDSPSAGW NDPWSPHSSR YHWQLHSNLG ESAVFDENDF
     WCVCQKTRKH LHVKVRRDRG KPLIEEPEEN YGIKDRIPVY YEEEELPEPH VTSPTKSEFA
     TTSTCMKWSS KTTKSEIEVE WRDSYLDANC IKEIIDSRRP SFASLLTKKS SSHQGSSHSS
     QPSLFTTFTS LELFLRNVLV HNDQRAISAA PEGTFERHVG KGRQIQSLMK SLLFEYHHEN
     VNYVPTIADA PLTDEQKLNL YLARNELIVL ANHFRDTKED PAIVANPFPV RLARPALINA
     FGVPNYDSVV PMYTTVFRDN SASLPDDPAF IALGITNDYP DSFVRYFYEE QKKNDEANVR
     VYADALAHIY NLRKSSFLRD LIAADRKNGI VSSDVIQAAY SSLGLEAEVG PDYRYSQEKI
     FEAFHSALLR KPEFARAIRN DLETIGYARK SSEILNYVLS TEQAFYTVNE AYQWLGIKSN
     TEDAMVASVA LVKFEDDSDK AIEAVKWIAE ERNSSILYDF LASQGRPSNK KPKEVPMDED
     LAYNTLGVQD RALSDDVLIN VYGFAVEDHP EQSDTLRAAL KCIGEVRNSR LITHYLEHGN
     LDIPPEVSSL DTPIGLENTG NLCYLNSLIQ YYFIIKPLRN AILDIDENKD LNMIENKEAV
     KKVGGRIVTR IEFLRALQFT YELRKLFIEL ITSKSSSVHP SSVLTYLALI PLTLDQVKSG
     TSSVMDLSSS RELSNLNERS ITIDPRAEEQ AQGLEQEQGQ DEAKSPAEQS SSVNLIDFPM
     ANTNGESQTQ PHYFEVSEEE INSSMDLGRQ QDVLECIDHV LFQLEASLGR ISNSEDRLGS
     DNDLIRRLFS GKLKQTLNDA SQGVRSNYEI FSHLIVDLFE EKQTLYDALD GVFETVNIDM
     GSETAQRSLC ITELPIILQL QIQRVQFDRT TGQPFKSNAF VEFGKELSMD RYVEDTDGKM
     APLLQRYWDL KREIINLQKR QQLLLTTNSN LMSSVDTLSI LSKWAAQQQD SRLPINPKLP
     DILQEEINNV VAEVDMLKKQ EASLKEERTH LFDNYISHSY DLLAVFVHRG QASFGHYWTY
     IHDFENNVYR KYNDEYVTVV DESEIFADTT GNNANPYMLT YIRKEYRHII ECVHREHNLL
     L
//