OTU2_SCHPO
ID OTU2_SCHPO Reviewed; 324 AA.
AC Q9UUK3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ubiquitin thioesterase otu2;
DE EC=3.4.19.12;
DE AltName: Full=OTU domain-containing protein 2;
GN Name=otu2; ORFNames=SPAC1952.03;
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 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 [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20838651; DOI=10.1371/journal.pbio.1000471;
RA Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E.,
RA Roberts-Galbraith R.H., Gould K.L.;
RT "A global census of fission yeast deubiquitinating enzyme localization and
RT interaction networks reveals distinct compartmentalization profiles and
RT overlapping functions in endocytosis and polarity.";
RL PLoS Biol. 8:708-716(2010).
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.
CC {ECO:0000269|PubMed:20838651}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:20838651}.
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DR EMBL; CU329670; CAB52567.1; -; Genomic_DNA.
DR PIR; T37931; T37931.
DR RefSeq; NP_594806.1; NM_001020234.2.
DR AlphaFoldDB; Q9UUK3; -.
DR SMR; Q9UUK3; -.
DR BioGRID; 279011; 31.
DR STRING; 4896.SPAC1952.03.1; -.
DR MaxQB; Q9UUK3; -.
DR PaxDb; Q9UUK3; -.
DR EnsemblFungi; SPAC1952.03.1; SPAC1952.03.1:pep; SPAC1952.03.
DR GeneID; 2542554; -.
DR KEGG; spo:SPAC1952.03; -.
DR PomBase; SPAC1952.03; otu2.
DR VEuPathDB; FungiDB:SPAC1952.03; -.
DR eggNOG; KOG2606; Eukaryota.
DR HOGENOM; CLU_034963_2_0_1; -.
DR InParanoid; Q9UUK3; -.
DR OMA; TYHRHMY; -.
DR PhylomeDB; Q9UUK3; -.
DR PRO; PR:Q9UUK3; -.
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; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:PomBase.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 4: Predicted;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..324
FT /note="Ubiquitin thioesterase otu2"
FT /id="PRO_0000318138"
FT DOMAIN 185..322
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 47..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 37516 MW; 48BBB435960D4B9C CRC64;
MRCPLAYYYT QTTIPTQQKR KSKKMEELLS KQREECKELQ SKITNLRKQL KEGNKKQKRA
LQQKISQMEA DLSQKHATER QKLDKGDEET NETQQEDLLN TLLQQMEDTK ITTAEKSSVQ
SSLNTKENTP QQPKKSRNRQ KERLERRKAE MKKMSEQAEL ESEKMADLKN EEKKKFSKIL
EEAGLVAVDI PADGNCLFAS ISHQLNYHHN VKLNSQALRN KSADYVLKHC EQFEGFLLDE
ESGEVLPVSD YCNEIRNNSK WGSDIEIQAL ANSLEVPVHV YNTEGPVLKF NPSTVKFEKP
LCIAYYQHLF GLGAHYNSLL YRDN
