ID   OTUBL_DROME             Reviewed;         262 AA.
AC   Q9VL00;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Ubiquitin thioesterase otubain-like;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96DC9};
DE   AltName: Full=Ubiquitin-specific-processing protease otubain-like;
DE            Short=Deubiquitinating enzyme otubain-like;
GN   ORFNames=CG4968;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Possible hydrolase that can remove conjugated ubiquitin from
CC       proteins in vitro and may therefore play an important regulatory role
CC       at the level of protein turnover by preventing degradation.
CC       {ECO:0000250}.
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:Q96DC9};
CC   -!- SIMILARITY: Belongs to the peptidase C65 family. {ECO:0000305}.
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DR   EMBL; AE014134; AAF52905.1; -; Genomic_DNA.
DR   EMBL; AY061382; AAL28930.1; -; mRNA.
DR   RefSeq; NP_609375.1; NM_135531.3.
DR   AlphaFoldDB; Q9VL00; -.
DR   SMR; Q9VL00; -.
DR   BioGRID; 60470; 3.
DR   IntAct; Q9VL00; 2.
DR   STRING; 7227.FBpp0079577; -.
DR   MEROPS; C65.001; -.
DR   PaxDb; 7227-FBpp0079577; -.
DR   DNASU; 34384; -.
DR   EnsemblMetazoa; FBtr0079987; FBpp0079577; FBgn0032214.
DR   GeneID; 34384; -.
DR   KEGG; dme:Dmel_CG4968; -.
DR   UCSC; CG4968-RA; d. melanogaster.
DR   AGR; FB:FBgn0032214; -.
DR   FlyBase; FBgn0032214; CG4968.
DR   VEuPathDB; VectorBase:FBgn0032214; -.
DR   eggNOG; KOG3991; Eukaryota.
DR   GeneTree; ENSGT00390000006979; -.
DR   HOGENOM; CLU_014832_3_0_1; -.
DR   InParanoid; Q9VL00; -.
DR   OMA; KQNDGNR; -.
DR   OrthoDB; 148019at2759; -.
DR   PhylomeDB; Q9VL00; -.
DR   Reactome; R-DME-5689880; Ub-specific processing proteases.
DR   Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR   BioGRID-ORCS; 34384; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 34384; -.
DR   PRO; PR:Q9VL00; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032214; Expressed in testis and 32 other cell types or tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:FlyBase.
DR   GO; GO:1990380; F:K48-linked deubiquitinase activity; IDA:FlyBase.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0061059; P:positive regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:FlyBase.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd22763; OTUB1; 1.
DR   Gene3D; 3.30.200.60; Peptidase C65 Otubain, subdomain 1; 1.
DR   Gene3D; 1.20.1300.20; Peptidase C65 Otubain, subdomain 2; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR016615; Otubain.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR019400; Peptidase_C65_otubain.
DR   InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR   InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR   PANTHER; PTHR12931:SF15; UBIQUITIN THIOESTERASE OTUBAIN-LIKE; 1.
DR   PANTHER; PTHR12931; UBIQUITIN THIOLESTERASE PROTEIN OTUB; 1.
DR   Pfam; PF10275; Peptidase_C65; 1.
DR   PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   Genevisible; Q9VL00; DM.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..262
FT                   /note="Ubiquitin thioesterase otubain-like"
FT                   /id="PRO_0000221012"
FT   DOMAIN          64..262
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   262 AA;  30372 MW;  5F65662D161DFCD2 CRC64;
     MEPFTHNDGN RDELIIQQKR DIEKEISDTT PLVSEQLPLT CLYAEYSGDE IFTAKIQDLS
     KKYKFIRRTR PDGNCFFRAF AYSYLEYLIS NTSAYQEFKK LAEESKEKLV QLGFPSFTLE
     DFHETFMEVI QRVSPDNAGG HSTVQDELHK IFNEQGYSDY VVVYLRLITS GKLQEEADFY
     QNFIEGDLTI EAFRHLEVEP MYKESDHIHI IALCTALGAG VRVEYLDRGE GGTVKAHDFP
     EGSEPRIYLI YRPGHYDILY PN
//