OTU1_DROME
ID OTU1_DROME Reviewed; 347 AA.
AC Q9VRJ9; Q8T9H3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ubiquitin thioesterase OTU1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN ORFNames=CG4603;
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=Ovary;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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. {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:Q5VVQ6};
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DR EMBL; AE014296; AAF50796.1; -; Genomic_DNA.
DR EMBL; AY069295; AAL39440.1; -; mRNA.
DR RefSeq; NP_001261436.1; NM_001274507.1.
DR RefSeq; NP_647951.2; NM_139694.4.
DR AlphaFoldDB; Q9VRJ9; -.
DR SMR; Q9VRJ9; -.
DR BioGRID; 64071; 8.
DR IntAct; Q9VRJ9; 3.
DR STRING; 7227.FBpp0304189; -.
DR MEROPS; C85.007; -.
DR PaxDb; Q9VRJ9; -.
DR DNASU; 38603; -.
DR EnsemblMetazoa; FBtr0077164; FBpp0076867; FBgn0035593.
DR EnsemblMetazoa; FBtr0331804; FBpp0304189; FBgn0035593.
DR GeneID; 38603; -.
DR KEGG; dme:Dmel_CG4603; -.
DR UCSC; CG4603-RA; d. melanogaster.
DR FlyBase; FBgn0035593; CG4603.
DR VEuPathDB; VectorBase:FBgn0035593; -.
DR eggNOG; KOG3288; Eukaryota.
DR GeneTree; ENSGT00390000009989; -.
DR HOGENOM; CLU_049327_1_1_1; -.
DR InParanoid; Q9VRJ9; -.
DR OMA; NEEYCDW; -.
DR OrthoDB; 1327072at2759; -.
DR PhylomeDB; Q9VRJ9; -.
DR Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR BioGRID-ORCS; 38603; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38603; -.
DR PRO; PR:Q9VRJ9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035593; Expressed in testis and 11 other tissues.
DR ExpressionAtlas; Q9VRJ9; baseline and differential.
DR Genevisible; Q9VRJ9; DM.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:FlyBase.
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:0016579; P:protein deubiquitination; ISS:FlyBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR039138; OTU1_2_3.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13312; PTHR13312; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..347
FT /note="Ubiquitin thioesterase OTU1"
FT /id="PRO_0000282362"
FT DOMAIN 5..87
FT /note="Ubiquitin-like"
FT DOMAIN 150..274
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 317..341
FT /note="C2H2-type"
FT REGION 8..89
FT /note="UBX-like"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 155..161
FT /note="Cys-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 213..223
FT /note="Variable-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 263..267
FT /note="His-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 290..295
FT /note="S2 site"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 158
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 267
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 341
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT CONFLICT 87
FT /note="A -> S (in Ref. 3; AAL39440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 37823 MW; F8AFA9C679DD77E4 CRC64;
MTGSFSVKLK SKKGQFIVND LNEHTTLGEL KTKIVQATDI EATQLHVLVG YPPKPLDLSQ
QQEQRALKAV GINSGETLIV EEKAAPAPAA PVPGGTTVED DEALARRLQA EEEAQLLQET
AGGPVAQAAD YQLPVAPTES GPNGDFNGIL LKKVVPADNS CLFTSIRFVL NGKVDNEGSE
MMRHIIAQEV AADPQSYNDA VLGKSNAEYC AWIQKADSWG GAIEVSILSN YYGIEIDVVD
IQNAIINRFG EDKNFGLRVF LLFDGIHYDP LYMETSPSAA PATIFPVEEL GVYQQAEQLA
NEAQSSRQYT NVDKFTLRCM QCDVRLVGQV QAQEHAKQTG HKNFGEI
