UBP7_CAEEL
ID UBP7_CAEEL Reviewed; 1135 AA.
AC Q7JKC3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q93009};
DE AltName: Full=Deubiquitinating enzyme 7;
DE AltName: Full=Ubiquitin thioesterase 7;
DE AltName: Full=Ubiquitin-specific-processing protease 7;
GN Name=math-33 {ECO:0000312|WormBase:H19N07.2c};
GN Synonyms=usp-7 {ECO:0000312|WormBase:H19N07.2c};
GN ORFNames=H19N07.2 {ECO:0000312|WormBase:H19N07.2c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32338603; DOI=10.7554/elife.56731;
RA Manage K.I., Rogers A.K., Wallis D.C., Uebel C.J., Anderson D.C.,
RA Nguyen D.A.H., Arca K., Brown K.C., Cordeiro Rodrigues R.J.,
RA de Albuquerque B.F.M., Ketting R.F., Montgomery T.A., Phillips C.M.;
RT "A Tudor domain protein, SIMR-1, promotes siRNA production at piRNA-
RT targeted mRNAs in C. elegans.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Hydrolase that deubiquitinates target proteins. May play a
CC role in regulating the levels of endogenous siRNA biogenesis
CC (PubMed:32338603). {ECO:0000250|UniProtKB:Q93009,
CC ECO:0000269|PubMed:32338603}.
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:0000269|PubMed:32338603}.
CC Note=Localizes to the nucleus of germ cells.
CC {ECO:0000269|PubMed:32338603}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; BX284605; CAE54910.1; -; Genomic_DNA.
DR RefSeq; NP_001024012.1; NM_001028841.3.
DR AlphaFoldDB; Q7JKC3; -.
DR SMR; Q7JKC3; -.
DR BioGRID; 44565; 5.
DR STRING; 6239.H19N07.2k; -.
DR MEROPS; C19.A54; -.
DR iPTMnet; Q7JKC3; -.
DR PaxDb; Q7JKC3; -.
DR PRIDE; Q7JKC3; -.
DR EnsemblMetazoa; H19N07.2c.1; H19N07.2c.1; WBGene00010406.
DR GeneID; 179538; -.
DR UCSC; H19N07.2a; c. elegans.
DR CTD; 179538; -.
DR WormBase; H19N07.2c; CE36180; WBGene00010406; math-33.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000174573; -.
DR InParanoid; Q7JKC3; -.
DR PhylomeDB; Q7JKC3; -.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-CEL-8948747; Regulation of PTEN localization.
DR PRO; PR:Q7JKC3; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010406; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q7JKC3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:WormBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:WormBase.
DR GO; GO:0031581; P:hemidesmosome assembly; IGI:WormBase.
DR GO; GO:0051661; P:maintenance of centrosome location; IMP:WormBase.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:WormBase.
DR GO; GO:0016579; P:protein deubiquitination; IDA:WormBase.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
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 3: Inferred from homology;
KW Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1135
FT /note="Ubiquitin carboxyl-terminal hydrolase 7"
FT /id="PRO_0000268010"
FT DOMAIN 31..172
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 193..503
FT /note="USP"
FT ACT_SITE 202
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 442
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1135 AA; 131597 MW; C4B24A58E9EEFAEB CRC64;
MQCSPDPEDL LIVPTHDIPS YDESLDPFGP EGHLSLDIDC FSKFMSRSDN RIMSKPIIVR
GIPWRILAIC RNQQGSRHSM NSRVNRSNFN FGFFLQCNND ELLQKRGMWR CYGTAVLEVL
NADGPSIQKK IHHSFHNTEV DWGFSNYDQY DTLCNPKDGY VVNDTIKLRC RFTADVPTGA
NYMWDSKRHT GCIGLRNQGA TCYMNSILQS FYFTTGFRRA VYNMDVGTEP NESNIVLAMQ
RVFYELQMAS EAVETNSLTR AFGWDKLDAF NQHDVQEFCR VLLDNLETKM KGTSEEKSIP
NLFRGNMKSY IKCLDVDYES SRTESFYDVQ LNVLGMDSLE RAFEAYTTSE ILDDENKYDA
GDHGLQRAEK GVKFVELPPI LHVQLMRFQY CGVEQKINER FSFPEKMNLA SCCELGPMLT
EEDCVYSLHA VLVHSGEFHG GHYVTYINVN LHESAVDPTS SAKWCKFDDD VVSRTTTDDA
IVSNFGGEKT MNSSAYMLVY VRDNAIDQFL APIPDSQIPQ SVSRTFEMER LHRNREKKKL
EEEQLCMGIV LVTPDIVASN HSFDLVDQSI VHDSIPHETV WKHMFTAELY QFVHDRLFEK
SAMQKIDMFD SDDEARQARR DNLRRIKSKK FNFRLWRMTD SYSLERTTQK LTSRLRPSEF
IDCKTDTRLD TLLSQDFETI YVEFSNNIER PLCEYDTARD LLFFVKYYDT MTDKFTIIGH
TMFDCHKRFN LYRSMLCEMI GLPADTELKY YMEHAASYLE LVDLTQNYSI GRLVEEQDGG
ILVVEKVETS TSTQNAKQKM NELFLDVEVE FVQSFYNKKP EEEPFEQFVK RICLDDKLFT
VAEEIGARLN VDPKKVLIWT RVSGSRFEPF FDDYMLNTCK GLMTRPVHDP RAYKRYRVQY
AIMPFDIDEI SKHRIQTKLF WQLPNGHVEE LTLFPLKEGT VIDIINEAKR YYPFVEGGSG
KFRLLQIGAP PLSNQRVYQI YGENTLISDL DQRTMYKLVS SQALHCRLEE VPIDELDMSP
GEFLCPVVHF DREPTKLFGL SFVIKIRNNE LMTEVRDRLR RKLNDVSDAD FAKYKFALLS
RDKLQLCRTI EFNNGEKVNL ADMANQTTGV PQVYIGLDHK SPIQHSSEAA IRILN
