U17PD_MOUSE
ID U17PD_MOUSE Reviewed; 545 AA.
AC G5E8G2; Q923V2; Q923V3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein D {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000269|PubMed:11468161};
DE AltName: Full=Deubiquitinating enzyme 2A {ECO:0000303|PubMed:11468161};
GN Name=Usp17ld {ECO:0000312|MGI:MGI:3051372};
GN Synonyms=Dub2a {ECO:0000303|PubMed:11468161, ECO:0000312|MGI:MGI:3051372};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAK77003.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-60.
RC STRAIN=129 {ECO:0000312|EMBL:AAK84135.1}, and
RC 129/W {ECO:0000312|EMBL:AAK77003.1};
RX PubMed=11468161; DOI=10.1182/blood.v98.3.636;
RA Baek K.H., Mondoux M.A., Jaster R., Fire-Levin E., D'Andrea A.D.;
RT "DUB-2A, a new member of the DUB subfamily of hematopoietic
RT deubiquitinating enzymes.";
RL Blood 98:636-642(2001).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:EDL16653.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes that
CC may include cell proliferation, progression through the cell cycle,
CC apoptosis, cell migration, and the cellular response to viral
CC infection. {ECO:0000269|PubMed:11468161}.
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:0000269|PubMed:11468161};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6R6M4}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6R6M4}.
CC -!- TISSUE SPECIFICITY: Detected in T-cell, myeloid, and embryonic stem
CC cell lines. {ECO:0000269|PubMed:11468161}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF393637; AAK84135.1; -; Genomic_DNA.
DR EMBL; AF393638; AAK77003.1; -; mRNA.
DR EMBL; AC108410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL16653.1; -; Genomic_DNA.
DR CCDS; CCDS21567.1; -.
DR RefSeq; NP_001001559.2; NM_001001559.2.
DR AlphaFoldDB; G5E8G2; -.
DR SMR; G5E8G2; -.
DR STRING; 10090.ENSMUSP00000073107; -.
DR MEROPS; C19.032; -.
DR MEROPS; C19.086; -.
DR iPTMnet; G5E8G2; -.
DR PhosphoSitePlus; G5E8G2; -.
DR MaxQB; G5E8G2; -.
DR PaxDb; G5E8G2; -.
DR PRIDE; G5E8G2; -.
DR DNASU; 384701; -.
DR Ensembl; ENSMUST00000073394; ENSMUSP00000073107; ENSMUSG00000057321.
DR GeneID; 384701; -.
DR KEGG; mmu:384701; -.
DR UCSC; uc009itk.1; mouse.
DR CTD; 384701; -.
DR MGI; MGI:3051372; Usp17ld.
DR VEuPathDB; HostDB:ENSMUSG00000057321; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000162665; -.
DR HOGENOM; CLU_008279_10_0_1; -.
DR InParanoid; G5E8G2; -.
DR OMA; HDSKDTT; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; G5E8G2; -.
DR TreeFam; TF315281; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 384701; 1 hit in 51 CRISPR screens.
DR PRO; PR:G5E8G2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; G5E8G2; protein.
DR Bgee; ENSMUSG00000057321; Expressed in animal zygote and 1 other tissue.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Nucleus; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..545
FT /note="Ubiquitin carboxyl-terminal hydrolase 17-like
FT protein D"
FT /id="PRO_0000438105"
FT DOMAIN 51..348
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 367..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035,
FT ECO:0000305|PubMed:11468161"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT MUTAGEN 60
FT /note="C->S: Loss of deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:11468161"
FT CONFLICT 259
FT /note="F -> S (in Ref. 1; AAK84135)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="V -> C (in Ref. 1; AAK84135)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="L -> S (in Ref. 1; AAK84135)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="Q -> L (in Ref. 1; AAK77003/AAK84135)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="K -> N (in Ref. 1; AAK84135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 61450 MW; 2FFDF08BE0F2E88D CRC64;
MVVSLSFPEA DPALSSPGAQ QLHQDEAQVV VELTANDKPS LSWECPQGPG CGLQNTGNSC
YLNAALQCLT HTPPLADYML SQEYSQTCCS PEGCKMCAME AHVTQSLLHS HSGDVMKPSQ
ILTSAFHKHQ QEDAHEFLMF TLETMHESCL QVHRQSEPTS EDSSPIHDIF GGLWRSQIKC
LHCQGTSDTY DRFLDVPLDI SSAQSVNQAL WDTEKSEELR GENAYYCGRC RQKMPASKTL
HIHSAPKVLL LVLKRFSAFM GNKLDRKVSY PEFLDLKPYL SQPTGGPLPY ALYAVLVHEG
ATCHSGHYFS YVKAGHGKWY KMDDTKVTSC DVTSVLNENA YVLFYVQQTD LKEVSIDMPE
GRIHEVLDPE YQLKKSRRKK HKKKSPCTED VGEPSKNREK KATKETSLGE GKVLQEKNHK
KAGQKHENTK LVPQEQNHQK LGQKHRNNEI LPQEQNHQKT GQSLRNTEGE LDLPADAIVI
HLPRSIANWG RDTPDKVNQP WHNADRLLTS QDLVNTGQLC RQEGRRRSKK GKNKNKQGQK
LLLVR
