OTUBL_CAEEL
ID OTUBL_CAEEL Reviewed; 284 AA.
AC Q9XVR6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ubiquitin thioesterase otubain-like;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96DC9};
DE AltName: Full=Deubiquitinating enzyme otubain-like;
DE AltName: Full=Ubiquitin-specific-processing protease otubain-like;
GN Name=otub-1; ORFNames=C25D7.8;
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.
RX PubMed=19211026; DOI=10.1016/j.jmb.2008.12.085;
RA Wang T., Yin L., Cooper E.M., Lai M.-Y., Dickey S., Pickart C.M.,
RA Fushman D., Wilkinson K.D., Cohen R.E., Wolberger C.;
RT "Evidence for bidentate substrate binding as the basis for the K48 linkage
RT specificity of otubain 1.";
RL J. Mol. Biol. 386:1011-1023(2009).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC and plays an important regulatory role at the level of protein turnover
CC by preventing degradation. Specifically cleaves 'Lys-48'-linked
CC polyubiquitin. {ECO:0000269|PubMed:19211026}.
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:Q96DC9};
CC -!- INTERACTION:
CC Q9XVR6; P61088: UBE2N; Xeno; NbExp=2; IntAct=EBI-316044, EBI-1052908;
CC -!- SIMILARITY: Belongs to the peptidase C65 family. {ECO:0000305}.
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DR EMBL; Z81039; CAB02772.1; -; Genomic_DNA.
DR PIR; T19448; T19448.
DR RefSeq; NP_506709.1; NM_074308.4.
DR PDB; 4DHI; X-ray; 1.80 A; B=1-284.
DR PDB; 4DHJ; X-ray; 2.35 A; A/E/I/L=1-284.
DR PDB; 4DHZ; X-ray; 3.11 A; A=42-284.
DR PDB; 4LDT; X-ray; 1.90 A; A=42-284.
DR PDBsum; 4DHI; -.
DR PDBsum; 4DHJ; -.
DR PDBsum; 4DHZ; -.
DR PDBsum; 4LDT; -.
DR AlphaFoldDB; Q9XVR6; -.
DR SMR; Q9XVR6; -.
DR BioGRID; 533138; 2.
DR DIP; DIP-26135N; -.
DR IntAct; Q9XVR6; 3.
DR STRING; 6239.C25D7.8; -.
DR MEROPS; C65.A01; -.
DR EPD; Q9XVR6; -.
DR PaxDb; Q9XVR6; -.
DR PeptideAtlas; Q9XVR6; -.
DR EnsemblMetazoa; C25D7.8.1; C25D7.8.1; WBGene00007718.
DR GeneID; 3565820; -.
DR UCSC; C25D7.8; c. elegans.
DR CTD; 3565820; -.
DR WormBase; C25D7.8; CE08394; WBGene00007718; otub-1.
DR eggNOG; KOG3991; Eukaryota.
DR GeneTree; ENSGT00390000006979; -.
DR HOGENOM; CLU_014832_3_0_1; -.
DR InParanoid; Q9XVR6; -.
DR OMA; EDFHGTF; -.
DR OrthoDB; 1257066at2759; -.
DR PhylomeDB; Q9XVR6; -.
DR Reactome; R-CEL-5689896; Ovarian tumor domain proteases.
DR SignaLink; Q9XVR6; -.
DR PRO; PR:Q9XVR6; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007718; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:WormBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:WormBase.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:WormBase.
DR Gene3D; 1.20.1300.20; -; 1.
DR Gene3D; 3.30.200.60; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR016615; Otubain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR019400; Peptidase_C65_otubain.
DR InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR PANTHER; PTHR12931; PTHR12931; 1.
DR Pfam; PF10275; Peptidase_C65; 1.
DR PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..284
FT /note="Ubiquitin thioesterase otubain-like"
FT /id="PRO_0000221013"
FT DOMAIN 77..274
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ACT_SITE 85
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 245
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 267
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4DHJ"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4DHJ"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:4DHI"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4LDT"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:4DHI"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 129..147
FT /evidence="ECO:0007829|PDB:4DHI"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4DHZ"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 163..183
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:4DHI"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:4DHI"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4DHI"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:4DHI"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:4DHI"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:4DHI"
SQ SEQUENCE 284 AA; 32293 MW; 262500E41F8FA23C CRC64;
MANEPQKSDD NGQAAEAVVT DDEIVLQDQQ LKTIEDEQKS VPLVATLAPF SILCAEYDNE
TSAAFLSKAT ELSEVYGEIR YIRGDGNCFY RAILVGLIEI MLKDRARLEK FIASSRDWTR
TLVELGFPDW TCTDFCDFFI EFLEKIHSGV HTEEAVYTIL NDDGSANYIL MFFRLITSAF
LKQNSEEYAP FIDEGMTVAQ YCEQEIEPMW KDADHLAINS LIKAAGTRVR IEYMDRTAAP
NGGWHYDIPS DDQQIAPEIT LLYRPGHYDV IYKKDSTEAS EIEN
