ID   UBP12_SCHPO             Reviewed;         979 AA.
AC   O60079;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 12;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 12;
DE   AltName: Full=Ubiquitin thioesterase 12;
DE   AltName: Full=Ubiquitin-specific-processing protease 12;
GN   Name=ubp12; ORFNames=SPCC1494.05c;
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 SER-19; SER-37 AND SER-39, AND
RP   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; CU329672; CAA19303.1; -; Genomic_DNA.
DR   PIR; T41006; T41006.
DR   RefSeq; NP_588530.1; NM_001023518.2.
DR   AlphaFoldDB; O60079; -.
DR   SMR; O60079; -.
DR   BioGRID; 275564; 6.
DR   STRING; 284812.O60079; -.
DR   MEROPS; C19.A64; -.
DR   iPTMnet; O60079; -.
DR   MaxQB; O60079; -.
DR   PaxDb; 4896-SPCC1494-05c-1; -.
DR   EnsemblFungi; SPCC1494.05c.1; SPCC1494.05c.1:pep; SPCC1494.05c.
DR   GeneID; 2538990; -.
DR   KEGG; spo:SPCC1494.05c; -.
DR   PomBase; SPCC1494.05c; ubp12.
DR   VEuPathDB; FungiDB:SPCC1494.05c; -.
DR   eggNOG; KOG1870; Eukaryota.
DR   HOGENOM; CLU_001060_7_1_1; -.
DR   InParanoid; O60079; -.
DR   OMA; PCHAQQS; -.
DR   PhylomeDB; O60079; -.
DR   Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   PRO; PR:O60079; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA: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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 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   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 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   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..979
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase 12"
FT                   /id="PRO_0000080612"
FT   DOMAIN          51..152
FT                   /note="DUSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          311..977
FT                   /note="USP"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..746
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        935
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   979 AA;  111967 MW;  A705444BCDB437D2 CRC64;
     MDSLSESSTS SYHGKRPRSL SEESQSSSNM DDISQKSISL GDASEISKNL PSIAEQKQLI
     GELVNNQPEL ELGQVDNYIL SYSWYERLCS YLAEDGPFPG PVDQEDIADL ETGTLKPDLQ
     EEIDFTIISR DVWDLLVRWY GLKGPEFPRE TVNLGSESHP HLVVEVYPPI FSLTLLSTNA
     VDANESHKPK KISLSSKSTL EDLLEGVKYT LSLPSDQFRL WRVDTDQPLH RTIDPSSFIK
     INSKEIIDFL EKSKTLVELG MDSSCSLVAE CMINETWPVD RALRLQFLIQ QRNNQSSNEE
     QKQEKRVPGT CGLSNLGNTC YMNSALQCLT HTRELRDFFT SDEWKNQVNE SNPLGMGGQV
     ASIFASLIKS LYSPEHSSFA PRQFKATIGK FNHSFLGYGQ QDSQEFLAFL LDGLHEDLNR
     IYQKPYTSKP DLYEVDEEKI KNTAEECWRL HKLRNDSLIV DLFQGMYRST LVCPVCNTVS
     ITFDPFMDLT LPLPVKQVWS HTVTFIPADT NLTPLAIEVV LESKAATIED LVKYVAEKSG
     CSDYRKILVT ETYKGRFYRF LTQLSKSLLM EISEEDEIYL YELERPYEDG SDDILVPVYH
     ISDDSTNSAN SYMSSRDFGH PFVLQLSDNE VTDASFISEK LKLKYQQFTT LKNLKNIDSL
     ESLELGHEDE QVQKGPLDVD MDHSQTPLFE MRVFHDRFEK IPTGWNMSVS NLPLLTERDK
     KDLESTVDPL DAHSIEEEDD SEFKDVAPGS YPEPSKSNEN TKLTAKENDR LLIQGDLLVC
     EWPEKSYQFV FSVAPSSPQM GRSLWLESKT ILSDKKDDSE DSRTITLNDC LDEFEKTEQL
     GEEDPWYCPT CKEFRQASKQ MEIWRCPEIL IFHLKRFSSE RRFRDKIDDL VEFPIDNLDM
     SMRTGSYKLS EKENPKLIYE LYAVDNHYGG LGGGHYTAFA KNPDNGQFYC FDDSRVTPVC
     PEETVTSAAY LLFYRRKTS
//