UBP7_DROME
ID UBP7_DROME Reviewed; 1129 AA.
AC Q9VYQ8; B5RJQ7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q93009};
DE AltName: Full=Ubiquitin thioesterase 7;
DE AltName: Full=Ubiquitin-specific-processing protease 7;
DE Short=Deubiquitinating enzyme 7;
GN Name=Usp7; ORFNames=CG1490;
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;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Hydrolase that deubiquitinates target proteins.
CC {ECO:0000250|UniProtKB:Q93009}.
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:Q93009};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93009}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48134.1; -; Genomic_DNA.
DR EMBL; BT044531; ACH95305.1; -; mRNA.
DR RefSeq; NP_572779.2; NM_132551.3.
DR AlphaFoldDB; Q9VYQ8; -.
DR SMR; Q9VYQ8; -.
DR BioGRID; 58574; 18.
DR IntAct; Q9VYQ8; 2.
DR STRING; 7227.FBpp0073474; -.
DR MEROPS; C19.A52; -.
DR iPTMnet; Q9VYQ8; -.
DR PaxDb; Q9VYQ8; -.
DR PRIDE; Q9VYQ8; -.
DR EnsemblMetazoa; FBtr0073641; FBpp0073474; FBgn0030366.
DR GeneID; 32169; -.
DR KEGG; dme:Dmel_CG1490; -.
DR CTD; 7874; -.
DR FlyBase; FBgn0030366; Usp7.
DR VEuPathDB; VectorBase:FBgn0030366; -.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000156053; -.
DR InParanoid; Q9VYQ8; -.
DR OMA; KMKGTCL; -.
DR OrthoDB; 77113at2759; -.
DR PhylomeDB; Q9VYQ8; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DME-6804757; Regulation of TP53 Degradation.
DR Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DME-8948747; Regulation of PTEN localization.
DR SignaLink; Q9VYQ8; -.
DR BioGRID-ORCS; 32169; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Usp7; fly.
DR GenomeRNAi; 32169; -.
DR PRO; PR:Q9VYQ8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030366; Expressed in wing disc and 28 other tissues.
DR ExpressionAtlas; Q9VYQ8; baseline and differential.
DR Genevisible; Q9VYQ8; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IGI:FlyBase.
DR GO; GO:0016578; P:histone deubiquitination; IDA:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IGI:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 2.60.210.10; -; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1129
FT /note="Ubiquitin carboxyl-terminal hydrolase 7"
FT /id="PRO_0000268011"
FT DOMAIN 101..222
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 241..548
FT /note="USP"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 490
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1129 AA; 130446 MW; 41F7D1B654579258 CRC64;
MEIETDQSIE AMDTQDTQEV EILTSDLQQT QQQRNSPPQL PKFKNLIQPQ LHAVGAVTQL
PSENGNMPPQ QLLADSSSTS FGDGEAMGID DESKEDQFRS ETTFSFTVEN VVQLKSQRLS
PPVYVRMLPW RIMVIPNDRA LGFFLQCNGE NDSPTWSCNA IAELRLKCHK PDAQPFTRAR
IKHLFYSKEN DYGYSNFITW QELKDSEKSY VHNNSITLEV HVVADAPHGV LWDSKKHTGY
VGLKNQGATC YMNSLLQTLY FTNSLRLSVY RIPTEADDSS KSVGLSLQRV FHELQFGDRP
VGTKKLTKSF GWETLDSFMQ HDVQEFLRVL LDKLESKMKG TILEGTIPGL FEGKMSSYIK
CKNVDYNSTR YETFYDIQLN IKDKKNIYES FQDYVAPETL EGDNKYDAGV HGLQEASKGV
IFTSFPPVLH LHLMRFQYDP VTDSSIKYND RFEFYEHINL DRYLAESENT LADYVLHAVL
VHSGDNHGGH YVVFINPKAD GRWFKFDDDV VSSCRKQEAI EQNYGGMDDE ISFHAKCSNA
YMLVYIRQSE LDRVLGDITE SEISSDLVER LDLEKRIEMA RRKERGEANT YVSVHVILEE
NFEEQHKRRL FDLEKVHPRV FRIKQNQTVD ELVDLFVRGF GVSRQRMRMW NLCTAQTQKF
SHFDFVAEGS RTIEQISTSQ KPWVIWLQLA WTDVPGPLPP FNPKTESLLF LKYYDPRNKR
LNYIGCTQQP HTRRLIDLVP DVNSKLGFEP DTELTIYDEY ADKKLVNLNE PIESALFIPQ
DHLQGHILIF ERENVDAKLD LPTVGDYFLD LVYRIEIIFS DKCNPNEPDF TLELSNRYNY
DQLANAVAER LNTDPQKLQF FMCINNYKET AGNAVPYTFK GTIKDLVSYT KQSSTKRIFY
QRLSLSIHEL DNKKQFKCVW VSSDLKDEKE LVLYPNKNDT VKGLLEEAAK KISFAENSRR
KLRLLKISNH KIVAVCKDDI PLDTLLKSNE SITTAQGAQK TFRIEEVPAE DMQLAENEFL
IPVAHFSKEL YNSFGIPFLT KARQGEPYGA LKQRIQRRLN VQDKEWENYK FCVISMGHNA
DVNDNTPVDL EVYRSWTSGQ LPFFGLDHIN KSRKRSSLNF SEKAIKIYN
