UBP7_CAEBR
ID UBP7_CAEBR Reviewed; 1129 AA.
AC Q60MK8; A8Y4P5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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:CBG23105};
GN ORFNames=CBG23105 {ECO:0000312|WormBase:CBG23105};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601533; CAP39865.3; -; Genomic_DNA.
DR RefSeq; XP_002636444.1; XM_002636398.1.
DR AlphaFoldDB; Q60MK8; -.
DR SMR; Q60MK8; -.
DR STRING; 6238.CBG23105; -.
DR GeneID; 8578439; -.
DR KEGG; cbr:CBG_23105; -.
DR CTD; 8578439; -.
DR WormBase; CBG23105; CBP46576; WBGene00041522; Cbr-math-33.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_0_1_1; -.
DR InParanoid; Q60MK8; -.
DR OMA; QFLPCET; -.
DR OrthoDB; 77113at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
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 3: Inferred from homology;
KW Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1129
FT /note="Ubiquitin carboxyl-terminal hydrolase 7"
FT /id="PRO_0000268009"
FT DOMAIN 29..169
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 190..500
FT /note="USP"
FT ACT_SITE 199
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1129 AA; 130838 MW; 0230AA8BC1806610 CRC64;
MCSPDPEDMH ILTNDIPSFD KSLDPYGPEG HLALDIERFS SFMNKPDSRI MSKPVIVRGI
PWRILAICRH QQNNRQVATS RSRNNYNFGF FLQCNNDDLL QKRGMWRCYG QATLEVLNAN
GPPIQKKIHH SFHNTEVDWG FSNYDQYDTL TSPKDGYVID DVIRLRCRFT ADVPTGANYM
WDSKKHTGCI GLRNQGATCY MNSILQSFYF TTGFRRAVYN MEVGTEPNES NIVLAMQRVF
YELQMSSEAV ETNSLTRAFG WDKLDAFNQH DVQEFCRVLL DNLETKMKGT SEEKSIPNLF
RGNMKSYIKC LDVDYESSRT ESFYDVQLNV LGMDSLERAF DAYTTPETLD DDNKYDAGDH
GLQRAEKGVK FVELPPVLHV QLMRFQYCGV EQKINERFSF PEKMNLSNCC ELGPMLNEED
CVYSLHAVLV HSGEFHGGHY VTYINVNLHE SAVDPTATAK WCKFDDDVVS RTTTDDAIVS
NFGGEKAMNS SAYMLVYVRD NAIDQVLAPI PDTQIPQSVS RTFEMERMHR NREKKKQEEE
QMCMSITLVT PDILATNHSF DLIEPVTITD VLPHETVYKH MVTAELYQFV QEKLFEKSTL
PKVDMFDSDD ETRMKRKEIL RRLKTKKFGF RLWRMTDSYT VDKPQKMASR LRPSDFIEYS
IDTRLDHTLS HDTETIYVEH SQFLQPLNEY LPTRDILFFL KYYDAITDKF TIIGHVTLDS
HKRLNLYRMT FCDLLGLPKD TELKYYIEHA PNHVEQIDDP NRSTISRLVD DQDGAIVIVE
KADPTAKKDA KTKMIELYND VEFEFSQQFY SKMPNEEPFE LFTKRFCLEQ KLTDVTEFIG
SELNVDPRNV MLWTRVSGSR FEPNFDDYAV TGIQCKYLTL RTLHDPRQHK KYSVSYAIFP
FPVNEVHTTR MFVRLYRQMP NGNVEELNLF PPKDGTVTDL IAEAKRYYPS VEGGSGKFRL
LQIGTSPLNN QRVFQIYNEN TAIVDLDQRP VYKQQAQHTL NCRIEEIPHD ELDVAQGEFF
CPVVHYDREP TKLFGVSFVI KIRNGELMTD VRDRLRRKLP DVSDAEFAKY KFALLSRDKL
CRNIEFNAGE KVNLMDMANQ TTGVPQVYIG LDHKSPSQHS NEAAIRILN
