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   27-MAR-2024, entry version 167.
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; 19.
DR   IntAct; Q9VYQ8; 2.
DR   STRING; 7227.FBpp0073474; -.
DR   MEROPS; C19.A52; -.
DR   iPTMnet; Q9VYQ8; -.
DR   PaxDb; 7227-FBpp0073474; -.
DR   EnsemblMetazoa; FBtr0073641; FBpp0073474; FBgn0030366.
DR   GeneID; 32169; -.
DR   KEGG; dme:Dmel_CG1490; -.
DR   AGR; FB:FBgn0030366; -.
DR   CTD; 7874; -.
DR   FlyBase; FBgn0030366; Usp7.
DR   VEuPathDB; VectorBase:FBgn0030366; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   GeneTree; ENSGT00940000156053; -.
DR   InParanoid; Q9VYQ8; -.
DR   OMA; HTAHHRF; -.
DR   OrthoDB; 51419at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q9VYQ8; baseline and differential.
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:0035331; P:negative regulation of hippo signaling; IGI:FlyBase.
DR   GO; GO:0031453; P:positive regulation of heterochromatin formation; IGI:FlyBase.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR   CDD; cd03772; MATH_HAUSP; 1.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
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; Cysteine proteinases; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q9VYQ8; DM.
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
//