U17PA_MOUSE
ID U17PA_MOUSE Reviewed; 526 AA.
AC Q61068;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein A;
DE Short=USP17-A;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 1;
DE AltName: Full=Ubiquitin carboxyl-terminal hydrolase DUB-1;
DE AltName: Full=Ubiquitin thioesterase DUB-1;
DE AltName: Full=Ubiquitin-specific-processing protease DUB-1;
GN Name=Usp17la; Synonyms=Dub-1, Dub1;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=8756639; DOI=10.1128/mcb.16.9.4808;
RA Zhu Y., Pless M., Inhorn R., Mathey-Prevot B., D'Andrea A.D.;
RT "The murine DUB-1 gene is specifically induced by the betac subunit of
RT interleukin-3 receptor.";
RL Mol. Cell. Biol. 16:4808-4817(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND
RP MUTAGENESIS OF CYS-60.
RX PubMed=8622927; DOI=10.1073/pnas.93.8.3275;
RA Zhu Y., Carroll M., Papa F.R., Hochstrasser M., D'Andrea A.D.;
RT "DUB-1, a deubiquitinating enzyme with growth-suppressing activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3275-3279(1996).
RN [3]
RP FUNCTION, INTERACTION WITH DNAH5, AND UBIQUITINATION.
RX PubMed=18980247; DOI=10.1002/jcb.21961;
RA Lee M.Y., Ajjappala B.S., Kim M.S., Oh Y.K., Baek K.H.;
RT "DUB-1, a fate determinant of dynein heavy chain in B-lymphocytes, is
RT regulated by the ubiquitin-proteasome pathway.";
RL J. Cell. Biochem. 105:1420-1429(2008).
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes. Has
CC deubiquitinating enzyme activity for DNAH5, suggesting a role in the
CC regulation of DNAH5 degradation by the ubiquitin-proteasome pathway.
CC Has growth-suppressing activity; induces arrest in G1 phase upon
CC controlled expression. {ECO:0000269|PubMed:18980247,
CC ECO:0000269|PubMed:8622927}.
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:8622927};
CC -!- TISSUE SPECIFICITY: Expressed in hematopoietic progenitor cell lines
CC Ba/F3 and FDCP1. Not detected in brain, lung, liver, kidney, thymus,
CC spleen and bone marrow. {ECO:0000269|PubMed:8756639}.
CC -!- INDUCTION: Up-regulated by IL3, IL5 and CSF2.
CC {ECO:0000269|PubMed:8622927, ECO:0000269|PubMed:8756639}.
CC -!- PTM: Polyubiquitinated; ubiquitination leads to its subsequent
CC degradation. {ECO:0000269|PubMed:18980247}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; U41636; AAC52532.1; -; mRNA.
DR CCDS; CCDS21629.1; -.
DR PIR; JC6133; JC6133.
DR RefSeq; NP_031913.1; NM_007887.2.
DR AlphaFoldDB; Q61068; -.
DR SMR; Q61068; -.
DR BioGRID; 199337; 1.
DR STRING; 10090.ENSMUSP00000068997; -.
DR MEROPS; C19.031; -.
DR PaxDb; Q61068; -.
DR PRIDE; Q61068; -.
DR DNASU; 13531; -.
DR Ensembl; ENSMUST00000067695; ENSMUSP00000068997; ENSMUSG00000054568.
DR GeneID; 13531; -.
DR KEGG; mmu:13531; -.
DR UCSC; uc009iwz.2; mouse.
DR CTD; 13531; -.
DR MGI; MGI:107699; Usp17la.
DR VEuPathDB; HostDB:ENSMUSG00000054568; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000162665; -.
DR HOGENOM; CLU_008279_10_0_1; -.
DR InParanoid; Q61068; -.
DR OMA; CKLCAME; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; Q61068; -.
DR TreeFam; TF315281; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 13531; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q61068; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61068; protein.
DR Bgee; ENSMUSG00000054568; Expressed in cleaving embryo and 3 other tissues.
DR Genevisible; Q61068; MM.
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; IDA:MGI.
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 Hydrolase; Protease; Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..526
FT /note="Ubiquitin carboxyl-terminal hydrolase 17-like
FT protein A"
FT /id="PRO_0000080683"
FT DOMAIN 51..348
FT /note="USP"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /note="Nucleophile"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MUTAGEN 60
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8622927"
SQ SEQUENCE 526 AA; 59073 MW; 263AA7B7579694EA CRC64;
MVVALSFPEA DPALSSPDAP ELHQDEAQVV EELTVNGKHS LSWESPQGPG CGLQNTGNSC
YLNAALQCLT HTPPLADYML SQEHSQTCCS PEGCKLCAME ALVTQSLLHS HSGDVMKPSH
ILTSAFHKHQ QEDAHEFLMF TLETMHESCL QVHRQSKPTS EDSSPIHDIF GGWWRSQIKC
LLCQGTSDTY DRFLDIPLDI SSAQSVKQAL WDTEKSEELC GDNAYYCGKC RQKMPASKTL
HVHIAPKVLM VVLNRFSAFT GNKLDRKVSY PEFLDLKPYL SEPTGGPLPY ALYAVLVHDG
ATSHSGHYFC CVKAGHGKWY KMDDTKVTRC DVTSVLNENA YVLFYVQQAN LKQVSIDMPE
GRINEVLDPE YQLKKSRRKK HKKKSPFTED LGEPCENRDK RAIKETSLGK GKVLQEVNHK
KAGQKHGNTK LMPQKQNHQK AGQNLRNTEV ELDLPADAIV IHQPRSTANW GRDSPDKENQ
PLHNADRLLT SQGPVNTWQL CRQEGRRRSK KGQNKNKQGQ RLLLVC
