UBPY_CAEEL
ID UBPY_CAEEL Reviewed; 1276 AA.
AC Q09931;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase K02C4.3;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme;
DE AltName: Full=Ubiquitin thioesterase;
DE AltName: Full=Ubiquitin-specific-processing protease;
GN ORFNames=K02C4.3;
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).
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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; Z47811; CAA87786.3; -; Genomic_DNA.
DR PIR; T23236; T23236.
DR RefSeq; NP_001309441.1; NM_001322744.1.
DR AlphaFoldDB; Q09931; -.
DR STRING; 6239.K02C4.3; -.
DR MEROPS; C19.A34; -.
DR EPD; Q09931; -.
DR PaxDb; Q09931; -.
DR PeptideAtlas; Q09931; -.
DR EnsemblMetazoa; K02C4.3a.1; K02C4.3a.1; WBGene00010502.
DR GeneID; 174300; -.
DR UCSC; K02C4.3; c. elegans.
DR CTD; 174300; -.
DR WormBase; K02C4.3a; CE51326; WBGene00010502; -.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000173177; -.
DR HOGENOM; CLU_263514_0_0_1; -.
DR InParanoid; Q09931; -.
DR OMA; HKYELHA; -.
DR OrthoDB; 653530at2759; -.
DR PhylomeDB; Q09931; -.
DR PRO; PR:Q09931; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010502; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q09931; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 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; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1276
FT /note="Probable ubiquitin carboxyl-terminal hydrolase
FT K02C4.3"
FT /id="PRO_0000080685"
FT DOMAIN 168..762
FT /note="USP"
FT REGION 375..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 707
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1276 AA; 144893 MW; EB5293F0045028D4 CRC64;
MVEENETGTP GTSRTVTFHD GRKLTDAEHF VFFKVKEVIA DKVAEAEILE SIRKRSECKP
TDEQFISDII NELFYSGEPP KGRKSERFIG PLFDPEKAST ASGPMDCTDV VSYDSTHPNI
SEISKKEEVE MQSAIQQSLA SSASQNISRP TMLMSNLEDM VRNPNFSTGL YNSGNTCWLN
CLSQVLYSIP KFRSILYHCA PLSWHEQPIT NVKIENQQHA ELLMLFRGLF AELQFSEMKY
IEVGPLINMV DKLSKSSKGP STIGTQQDAT EMLTLIFDWL QRAFDAALHA QLNPEFSNVS
DEENLVISDS TTTAPNSDII GAPPGYNAAN LSLPSSSHVD PKSTLNPMYV NEKEPSSTPT
SLFGTRSKTI EVNESMDTEA ATSSNLPGNS VENHPNPAAP EVDDNKKAFC DKLKESFNNI
FSSVCYTESV AEDGTVSVKS NVRNCPQFFQ LQVTYGNLHD ALEAATFDHG LGNTASHVRN
LYDPLPAVIF FGLSRFSFNS NIESKLHDKF TFPKIIFMDR YLKCNKEQLV QLRSHRELCR
DSLSEVRAKL SGLRRYPQGN GEVRLEDSFQ TVWQAVSNFR EFVTFYLKVS QKTFFSREDA
HENTAFVGPL TPSTYQSSSD NCSSKFVKDG GKLFPTFTEG FFPGKAAFIE TLQNMLEALK
TEERDCLAEE ARLQEVIDQT YEVPELQQHK YELHAIIVHS GEANRGHYWT YKLKKSIDGL
EEWEKLNDQN ADRVDWPKVE SDSFGTGSRD APSAYMLMYV RSDAEWLVSA DKLTALEAFE
TIPPDLQEKV LQKRDEFKEK LQRFRENKEF NYQQFSVDSP TVQSTEETPS SFSWYRDELE
DIDIGDENAN PTKNDYLLNA RLDSYSVPIA PDVETSEMKR MVSQMWNQIT KIAPRKYTDS
QDLLDSNLRS VMEGESGGIN FINSRLGYDI HELRSDADND VEGVYNAFIN EYLGLVKDLH
ELQNSKFVVF VGFQLQRIHV PVLRYLLVRA MAVSELGIIS QRANNELSGM SSNSHDKGTA
MLQIALLLSH FFELGVMSAW GCRSSLENIH VILNDFKKKN SRGSEQIEVT YCAMIGARNA
RICNGLLREM AYFLESYSIF FVSQKHIEAC TVFSTITMIK LIMQHMASKT LQLIDMEFHL
SKNERRVRFE DIIREVVSSV CIIHHWSKSY SKEFQNEINL KELMGLLHLK VEFMVSLTSF
EVADPKYECL QAFKAMVVNT VMDLERASNE LDYDVLDGAV ELRELKKYFK ELQLTDVKVN
NIITSYDPII ESLVKI