U17PE_MOUSE
ID U17PE_MOUSE Reviewed; 540 AA.
AC Q7M764; D3YU85;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein E;
DE Short=USP17-E;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 17-like protein 2;
DE AltName: Full=Deubiquitinating protein 3;
DE Short=DUB-3;
DE AltName: Full=Deubiquitinating protein 6;
DE AltName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 2;
DE AltName: Full=Ubiquitin thioesterase 17-like protein 2;
DE AltName: Full=Ubiquitin-specific-processing protease 17-like protein 2;
GN Name=Usp17le; Synonyms=Dub3, Dub6, Usp17, Usp17l2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [2]
RP IDENTIFICATION.
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
RN [3]
RP FUNCTION.
RX PubMed=20228808; DOI=10.1038/ncb2041;
RA Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L.,
RA French D.M., Dixit V.M.;
RT "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing
RT Cdc25A.";
RL Nat. Cell Biol. 12:400-406(2010).
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:20228808}.
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 -!- SUBUNIT: Interacts with SUDS3; the interaction is direct.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD66057.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC110621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000117; CAD66057.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS85368.1; -.
DR AlphaFoldDB; Q7M764; -.
DR SMR; Q7M764; -.
DR STRING; 10090.ENSMUSP00000051716; -.
DR MEROPS; C19.082; -.
DR PaxDb; Q7M764; -.
DR PRIDE; Q7M764; -.
DR UCSC; uc029wnn.1; mouse.
DR MGI; MGI:107697; Usp17le.
DR eggNOG; KOG1865; Eukaryota.
DR InParanoid; Q7M764; -.
DR PhylomeDB; Q7M764; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9648002; RAS processing.
DR PRO; PR:Q7M764; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7M764; protein.
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; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071586; P:CAAX-box protein processing; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0031064; P:negative regulation of histone deacetylation; ISS:UniProtKB.
DR GO; GO:0010955; P:negative regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; ISS:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IDA:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0050691; P:regulation of defense response to virus by host; ISS:UniProtKB.
DR GO; GO:0110030; P:regulation of G2/MI transition of meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:1900027; P:regulation of ruffle assembly; ISS:UniProtKB.
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 Apoptosis; Cell cycle; Endoplasmic reticulum; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..540
FT /note="Ubiquitin carboxyl-terminal hydrolase 17-like
FT protein E"
FT /id="PRO_5000095963"
FT DOMAIN 85..382
FT /note="USP"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 540 AA; 60219 MW; C71382D289659704 CRC64;
MVVSLSFPEE TGGENLPSAP LEDSSKFFEE VFGDMVFARS FPEADPALSS PDAPELHQDE
AQVVEELTTN GKHSLSWESP QGPGCGLQNT GNSCYLNAAL QCLTHTPPLA DYMLSQEHSQ
TCCSPEGCKM CAMEAHVTQS LLHSHSGDVM KPSQILTSAF HKHQQEDAHE FLMFTLETMH
ESCLQVHRQS DPTPQDTSPI HDIFGGWWRS QIKCLHCQGT SHTFDPFLDV PLDISSAQSV
NQALWDTGKS EELLGENAYY CGRCRQKMPA SKTLHVHIAP KVLLLVLKRF SAFTGNKLDR
KVSYPEFLDL KPYLSEPTGG PLPYALYAVL VHDGATSNSG HYFCCVKAGH GKWYKMDDTK
VTRCDVTSVL NENAYVLFYV QQTDLKQVSI DMPEGRVHEV LDPKYQLKKS RRKKRKKQCH
CTDDAGEACE NREKRAKKET SLGEGKVPQE VNHEKAGQKH GNTKLVPQEQ NHQRAGQNLR
NTEVELDLPV DAIVIHQPRS TANWGTDAPD KENQPWHNGD RLLTSQGLMS PGQLCSQGGR
