OTUBL_DROME
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 03-AUG-2022, entry version 139.
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; 2.
DR IntAct; Q9VL00; 2.
DR STRING; 7227.FBpp0079577; -.
DR MEROPS; C65.001; -.
DR PaxDb; Q9VL00; -.
DR PRIDE; Q9VL00; -.
DR DNASU; 34384; -.
DR EnsemblMetazoa; FBtr0079987; FBpp0079577; FBgn0032214.
DR GeneID; 34384; -.
DR KEGG; dme:Dmel_CG4968; -.
DR UCSC; CG4968-RA; d. melanogaster.
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; VRVRYMD; -.
DR OrthoDB; 1257066at2759; -.
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 tissues.
DR Genevisible; Q9VL00; DM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:FlyBase.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:FlyBase.
DR Gene3D; 1.20.1300.20; -; 1.
DR Gene3D; 3.30.200.60; -; 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; PTHR12931; 1.
DR Pfam; PF10275; Peptidase_C65; 1.
DR PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
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
