UCHL_DROME
ID UCHL_DROME Reviewed; 227 AA.
AC P35122; Q4PIX7; Q9TWA0; Q9V417;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase;
DE EC=3.4.19.12;
DE AltName: Full=Ubiquitin thioesterase;
GN Name=Uch; Synonyms=ubc-D; ORFNames=CG4265;
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 [GENOMIC DNA].
RX PubMed=1426603; DOI=10.1042/bst0200631;
RA Wilkinson K.D., Deshpande S., Larsen C.N.;
RT "Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal
RT hydrolases.";
RL Biochem. Soc. Trans. 20:631-637(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Oregon-R;
RX PubMed=7683284; DOI=10.1006/dbio.1993.1125;
RA Zhang N., Wilkinson K., Bownes M.;
RT "Cloning and analysis of expression of a ubiquitin carboxyl terminal
RT hydrolase expressed during oogenesis in Drosophila melanogaster.";
RL Dev. Biol. 157:214-223(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
CC -!- FUNCTION: Ubiquitin-protein hydrolase is involved both in the
CC processing of ubiquitin precursors and of ubiquitinated proteins. This
CC enzyme is a thiol protease that recognizes and hydrolyzes a peptide
CC bond at the C-terminal glycine of ubiquitin.
CC {ECO:0000269|PubMed:7683284}.
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 -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:7683284}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR EMBL; S60346; AAA15411.1; -; Genomic_DNA.
DR EMBL; X69678; CAA49358.1; -; mRNA.
DR EMBL; X69679; CAA49359.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51291.1; -; Genomic_DNA.
DR EMBL; AF145600; AAD38575.1; -; mRNA.
DR PIR; S33956; S33956.
DR RefSeq; NP_001188681.1; NM_001201752.2.
DR RefSeq; NP_476940.1; NM_057592.4.
DR AlphaFoldDB; P35122; -.
DR SMR; P35122; -.
DR BioGRID; 59626; 66.
DR STRING; 7227.FBpp0077516; -.
DR MEROPS; C12.008; -.
DR PaxDb; P35122; -.
DR PRIDE; P35122; -.
DR DNASU; 33397; -.
DR EnsemblMetazoa; FBtr0077844; FBpp0077516; FBgn0010288.
DR EnsemblMetazoa; FBtr0303459; FBpp0292511; FBgn0010288.
DR GeneID; 33397; -.
DR KEGG; dme:Dmel_CG4265; -.
DR CTD; 33397; -.
DR FlyBase; FBgn0010288; Uch.
DR VEuPathDB; VectorBase:FBgn0010288; -.
DR eggNOG; KOG1415; Eukaryota.
DR GeneTree; ENSGT00940000172624; -.
DR InParanoid; P35122; -.
DR OMA; YVCFVKG; -.
DR OrthoDB; 1013351at2759; -.
DR PhylomeDB; P35122; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DME-8951664; Neddylation.
DR BioGRID-ORCS; 33397; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33397; -.
DR PRO; PR:P35122; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010288; Expressed in secondary oocyte and 25 other tissues.
DR ExpressionAtlas; P35122; baseline and differential.
DR Genevisible; P35122; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00140; UCH_1; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..227
FT /note="Ubiquitin carboxyl-terminal hydrolase"
FT /id="PRO_0000211072"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT SITE 179
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="G -> A (in Ref. 2; AAA15411/CAA49358/CAA49359)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="E -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25850 MW; 298A025569C3D409 CRC64;
MLTWTPLESN PEVLTKYIHK LGVSPAWSVT DVIGLEDDTL EWIPRPVKAF ILLFPCSETY
EKHRAEEHDR IKEVEEQHPE DLFYMRQFTH NACGTVALIH SVANNKEVDI DRGVLKDFLE
KTASLSPEER GRALEKDEKF TADHEALAQE GQTNAANHEK VIHHFIALVN KEGTLYELDG
RKSFPIKHGP TSEETFVKDA AKVCKEFMAR DPNEVRFTVL ALTAAQQ
