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 27-MAR-2024, entry version 103. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSMUSP00000147776; -. DR MEROPS; C19.082; -. DR PaxDb; 10090-ENSMUSP00000051716; -. DR UCSC; uc029wnn.1; mouse. DR AGR; MGI:107697; -. 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:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI. 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: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; ISS:UniProtKB. 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; IBA:GO_Central. 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 CDD; cd02661; Peptidase_C19E; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. 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 PANTHER; PTHR24006:SF651; INACTIVE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 17-LIKE PROTEIN 4-RELATED; 1. DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR Pfam; PF00443; UCH; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 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 //