ID   OTU1_SCHPO              Reviewed;         329 AA.
AC   O13974;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Putative ubiquitin thioesterase otu1;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
DE   AltName: Full=Meiotically up-regulated gene 141 protein;
DE   AltName: Full=OTU domain-containing protein 1;
GN   Name=otu1; Synonyms=mug141; ORFNames=SPAC24C9.14;
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   FUNCTION IN MEIOSIS.
RX   PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA   Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA   Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA   Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes required for
RT   critical meiotic events.";
RL   Curr. Biol. 15:2056-2062(2005).
RN   [3]
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).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC       and may therefore play an important regulatory role at the level of
CC       protein turnover by preventing degradation (By similarity). Has a role
CC       in meiosis. {ECO:0000250, ECO:0000269|PubMed:16303567}.
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; Evidence={ECO:0000250|UniProtKB:Q5VVQ6};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329670; CAB11271.1; -; Genomic_DNA.
DR   PIR; T38355; T38355.
DR   RefSeq; NP_594039.1; NM_001019464.2.
DR   AlphaFoldDB; O13974; -.
DR   SMR; O13974; -.
DR   BioGRID; 279103; 19.
DR   IntAct; O13974; 2.
DR   STRING; 284812.O13974; -.
DR   MEROPS; C85.007; -.
DR   MaxQB; O13974; -.
DR   PaxDb; 4896-SPAC24C9-14-1; -.
DR   EnsemblFungi; SPAC24C9.14.1; SPAC24C9.14.1:pep; SPAC24C9.14.
DR   GeneID; 2542649; -.
DR   KEGG; spo:SPAC24C9.14; -.
DR   PomBase; SPAC24C9.14; otu1.
DR   VEuPathDB; FungiDB:SPAC24C9.14; -.
DR   eggNOG; KOG3288; Eukaryota.
DR   HOGENOM; CLU_049327_0_0_1; -.
DR   InParanoid; O13974; -.
DR   OMA; IRKESSW; -.
DR   PhylomeDB; O13974; -.
DR   Reactome; R-SPO-5689896; Ovarian tumor domain proteases.
DR   PRO; PR:O13974; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   CDD; cd22745; OTU_OTU1; 1.
DR   CDD; cd17059; Ubl_OTU1; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR048857; OTU1_Ubl.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR   PANTHER; PTHR13312:SF0; UBIQUITIN THIOESTERASE OTU1; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF21403; OTU1_UBXL; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Meiosis; Metal-binding; Nucleus; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..329
FT                   /note="Putative ubiquitin thioesterase otu1"
FT                   /id="PRO_0000300503"
FT   DOMAIN          135..254
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ZN_FING         299..323
FT                   /note="C2H2-type"
FT   REGION          7..89
FT                   /note="UBX-like"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          85..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..146
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          193..203
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          243..247
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          272..277
FT                   /note="S2 site"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   COMPBIAS        100..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        146
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        323
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   329 AA;  35668 MW;  39356AC34E1C0813 CRC64;
     MSSLRLRLKY ENQSAVETVE ANATVGSFLD LVAAKFSLPR NSIALKFGFP PQDIPLVNSD
     VPLSTLVSSG QQILVLKNAA TSFSTNEPAK PPIPNAATKP TFPPQTEISN PPAVSHQSKN
     TSQDPPYVST PIGDIALRVM PDDNSCLFRA LSKPLGFSPY ELREIVANQV LSNPDIYSTA
     ILGKPSIEYA SWIRKETSWG GYIELSILSS HFGVEICSVD VKTGRVDSYN PQPATGQRTY
     IVYSGIHYDL AALAAVLWDT DVDVVLFDAS DVTITPYVQQ LASLLKNMHY YTDTASFSIR
     CTICGTGLVG EKDATAHALA TGHTQFGEY
//