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   27-MAR-2024, entry version 155.
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; 10090-ENSMUSP00000068997; -.
DR   DNASU; 13531; -.
DR   Ensembl; ENSMUST00000067695.8; ENSMUSP00000068997.8; ENSMUSG00000054568.8.
DR   GeneID; 13531; -.
DR   KEGG; mmu:13531; -.
DR   UCSC; uc009iwz.2; mouse.
DR   AGR; MGI:107699; -.
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; 227085at2759; -.
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 76 CRISPR screens.
DR   PRO; PR:Q61068; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q61068; Protein.
DR   Bgee; ENSMUSG00000054568; Expressed in cleaving embryo and 5 other cell types or tissues.
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:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
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.
DR   Genevisible; Q61068; MM.
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
//