ID   ULP2_SCHPO              Reviewed;         638 AA.
AC   O13769;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   02-SEP-2026, entry version 132.
DE   RecName: Full=Ubiquitin-like-specific protease 2;
DE            EC=3.4.22.-;
GN   Name=ulp2; ORFNames=SPAC17A5.07c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   GENE NAME.
RA   Watts F.;
RL   Submitted (MAR-2001) to UniProtKB.
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, AND IDENTIFICATION BY
RP   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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11507.2; -; Genomic_DNA.
DR   PIR; T37822; T37822.
DR   RefSeq; NP_593475.2; NM_001018908.3.
DR   AlphaFoldDB; O13769; -.
DR   SMR; O13769; -.
DR   BioGRID; 278737; 109.
DR   FunCoup; O13769; 201.
DR   STRING; 284812.O13769; -.
DR   MEROPS; C48.A09; -.
DR   iPTMnet; O13769; -.
DR   PaxDb; 284812-O13769; -.
DR   GeneID; 2542268; -.
DR   KEGG; spo:2542268; -.
DR   PomBase; SPAC17A5.07c; ulp2.
DR   VEuPathDB; FungiDB:SPAC17A5.07c; -.
DR   eggNOG; KOG0779; Eukaryota.
DR   HOGENOM; CLU_417467_0_0_1; -.
DR   InParanoid; O13769; -.
DR   OMA; FHAKVPQ; -.
DR   PRO; PR:O13769; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016929; F:deSUMOylase activity; IDA:PomBase.
DR   GO; GO:0070139; F:SUMO-specific endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0016926; P:protein desumoylation; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:2000765; P:regulation of cytoplasmic translation; EXP:PomBase.
DR   Gene3D; 1.10.418.20; -; 1.
DR   Gene3D; 3.30.310.130; Ubiquitin-related; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003653; Peptidase_C48_C.
DR   InterPro; IPR051947; Sentrin-specific_protease.
DR   PANTHER; PTHR46896:SF3; FI06413P-RELATED; 1.
DR   PANTHER; PTHR46896; SENTRIN-SPECIFIC PROTEASE; 1.
DR   Pfam; PF02902; Peptidase_C48; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50600; ULP_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..638
FT                   /note="Ubiquitin-like-specific protease 2"
FT                   /id="PRO_0000101734"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..12
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..264
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..631
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        494
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000250"
FT   MOD_RES         526
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   638 AA;  71917 MW;  0F83228A45C50020 CRC64;
     MRDSKDALDD KSGSFTSLLP PFGKQRGTSP NDAIPIKSPL ERLANSVTSP EKPTVRTAIQ
     KDSPRRKQID DDQTPPKHLK RSFQNVTVVS PRKKKTIDVV ELPFTKGGYG GFYDPRPGCL
     KFTTHEINVS YTDTSIPVIH IPVQLLKRCC WLQGWRDNLV ESPVHAIHLT LKNRDMKRIT
     IGDSASLLFL YNPLHVESAR AGLDLLDQSD FSLTSPSSAK EFKQLLTLKQ STIIPRTPQK
     TVRSIVKQTS SPHSSKMPKH SLPSSPTPFN SNSGDSLLSR IKNSNQSSSE RPTANNGAQE
     QNQSSSSAGN TSNDFSTLCS QGSDKTLLSD ASCTTILVYP FSGTNSIAIT NTDLTRLNEG
     EFLNDTIVDF YLRYLYCKLQ TQNPSLANDT HIFNTFFYNR LTSKDKDGKR LGHRGVRKWT
     QKVDLFHKKY IIVPINETFH WYLAIICNID RLMPVDTKLE EQDEIVMSSV EQPSASKTRQ
     AELTSNSPAI LIFDSLANLH KGALNYLREY LLEEAFERKN VHLKSTDIRG FHAKVPQQSN
     FSDCGIYALH FVELFLETPE QVIANTLDKS LRRTDAKNFD QQWNLQKINT MRCDLKGLIR
     RLSTEWSSNN ERQSLSSGSN DEEDKENDDD LAILPITN
//