ID   UBP29_MOUSE             Reviewed;         869 AA.
AC   Q9ES63; C6EQG1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 29 {ECO:0000305};
DE            EC=3.4.19.12 {ECO:0000269|PubMed:32457395};
DE   AltName: Full=Deubiquitinating enzyme 29;
DE   AltName: Full=Ubiquitin thioesterase 29;
DE   AltName: Full=Ubiquitin-specific-processing protease 29;
GN   Name=Usp29 {ECO:0000303|PubMed:10958632};
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 [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=10958632; DOI=10.1101/gr.10.8.1138;
RA   Kim J., Noskov V.N., Lu X., Bergmann A., Ren X., Warth T., Richardson P.,
RA   Kouprina N., Stubbs L.;
RT   "Discovery of a novel, paternally expressed ubiquitin-specific processing
RT   protease gene through comparative analysis of an imprinted region of mouse
RT   chromosome 7 and human chromosome 19q13.4.";
RL   Genome Res. 10:1138-1147(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Li J., Symer D.E.;
RT   "An active antisense promoter in mouse L1 retrotransposons has implications
RT   for fusion gene expression and epigenetic control.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=30919279; DOI=10.1007/s11427-018-9469-4;
RA   Huang Z., Khan M., Xu J., Khan T., Ma H., Khan R., Hussain H.M.J.,
RA   Jiang X., Shi Q.;
RT   "The deubiquitinating gene Usp29 is dispensable for fertility in male
RT   mice.";
RL   Sci. China Life Sci. 62:544-552(2019).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-298.
RX   PubMed=32457395; DOI=10.1038/s41422-020-0341-6;
RA   Zhang Q., Tang Z., An R., Ye L., Zhong B.;
RT   "USP29 maintains the stability of cGAS and promotes cellular antiviral
RT   responses and autoimmunity.";
RL   Cell Res. 30:914-927(2020).
CC   -!- FUNCTION: Deubiquitinase involved in innate antiviral immunity by
CC       mediating 'Lys-48'-linked deubiquitination of CGAS, thereby promoting
CC       its stabilization. {ECO:0000269|PubMed:32457395}.
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:32457395};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:32457395}. Note=Localizes to perinuclear region in
CC       response to herpes simplex virus-1 (HSV-1) infection.
CC       {ECO:0000269|PubMed:32457395}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain and testis
CC       (PubMed:30919279). Highest expression levels in adult brain, especially
CC       in the cerebral cortex and hippocampus, and in the forebrain, face, and
CC       limb buds of midgestation mouse embryos (PubMed:10958632).
CC       {ECO:0000269|PubMed:10958632, ECO:0000269|PubMed:30919279}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions.
CC       {ECO:0000269|PubMed:30919279}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; AF229257; AAG14415.1; -; mRNA.
DR   EMBL; EU233992; ACD47025.1; -; mRNA.
DR   CCDS; CCDS20784.1; -.
DR   RefSeq; NP_001277923.1; NM_001290994.1.
DR   RefSeq; NP_067298.2; NM_021323.3.
DR   AlphaFoldDB; Q9ES63; -.
DR   STRING; 10090.ENSMUSP00000143769; -.
DR   MEROPS; C19.043; -.
DR   iPTMnet; Q9ES63; -.
DR   PhosphoSitePlus; Q9ES63; -.
DR   MaxQB; Q9ES63; -.
DR   PaxDb; 10090-ENSMUSP00000062349; -.
DR   ProteomicsDB; 298459; -.
DR   Antibodypedia; 19631; 145 antibodies from 25 providers.
DR   DNASU; 57775; -.
DR   Ensembl; ENSMUST00000054055.7; ENSMUSP00000062349.7; ENSMUSG00000051527.12.
DR   Ensembl; ENSMUST00000198068.3; ENSMUSP00000143267.3; ENSMUSG00000051527.12.
DR   Ensembl; ENSMUST00000200535.6; ENSMUSP00000143769.3; ENSMUSG00000051527.12.
DR   GeneID; 57775; -.
DR   KEGG; mmu:57775; -.
DR   UCSC; uc009fcb.2; mouse.
DR   AGR; MGI:1888998; -.
DR   CTD; 57663; -.
DR   MGI; MGI:1888998; Usp29.
DR   VEuPathDB; HostDB:ENSMUSG00000051527; -.
DR   eggNOG; KOG1868; Eukaryota.
DR   GeneTree; ENSGT00940000161929; -.
DR   HOGENOM; CLU_012557_0_0_1; -.
DR   InParanoid; Q9ES63; -.
DR   OMA; YIPKYLS; -.
DR   PhylomeDB; Q9ES63; -.
DR   TreeFam; TF323032; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 57775; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Usp29; mouse.
DR   PRO; PR:Q9ES63; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9ES63; Protein.
DR   Bgee; ENSMUSG00000051527; Expressed in ventromedial nucleus of hypothalamus and 118 other cell types or tissues.
DR   ExpressionAtlas; Q9ES63; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02257; Peptidase_C19; 1.
DR   CDD; cd13312; PH_USP37_like; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR032069; USP37-like_PH.
DR   InterPro; IPR038093; USP37-like_PH_sf.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF16674; UCH_N; 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   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Immunity; Innate immunity; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..869
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 29"
FT                   /id="PRO_0000080661"
FT   DOMAIN          289..826
FT                   /note="USP"
FT   REGION          104..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093,
FT                   ECO:0000305|PubMed:32457395"
FT   ACT_SITE        781
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MUTAGEN         298
FT                   /note="C->A: Impaired ability to mediate deubiquitination
FT                   of CGAS."
FT                   /evidence="ECO:0000269|PubMed:32457395"
FT   CONFLICT        568
FT                   /note="L -> S (in Ref. 1; AAG14415)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   869 AA;  97823 MW;  4B661AD187BCA966 CRC64;
     MAHLKINGLV QIRSTNRSKH TRASQWKEAV IEIVERKQKV NLVVSFKLEE RRRVFQLGDN
     VTGVVVSGEL GLYHLDLTLR DDTSLLIDKL SSADVEHLKS FLDSSTPCES QQPMEPMSSQ
     DDLESSDPFC GEHQEAACGS LNTTPESGTP LSRKMPLSMS NTTGGQKRGE KQGRKRKTEP
     SSSSAEVNKD IPKENTPDQK KKSRRYYSRN RGGKAEKAVT LREQEKRSNW KLEPAFNSKS
     YGRANLDGTI LPIATCSDDR DVSIFGLEII THNGVQSLPD PYLNQLKREG FPNLGNTCYM
     NSILQSVFGI PTFAKDLLTQ GIPWEKVSYD DLIMPLSQLL VLKDIRDVEI KGELLTSVKK
     SISTVADTFS GNEQNDAHEF LSLCLDQLKL NMEKVNAMWD TERRNTCAGS AGTKRFVCPV
     GANFEFELHS SIICEGCGEA TIKTEVSNYL SIDLHHGTKT HPLSIQKSFD LFFTPEKIEH
     NCEKCKNKNS VLKYTLRRLP RVLIVHLKRY QVTTDLLPVK SEQPVEISKY LNISSHCHEN
     RKLPFPLANT SPDVSQGMMP GIFNQSMLSK KVISESCDPM VLQVGSSVDA EIQSFQIMYE
     DEDASEEQQQ RGLESGSMLE PELVKTENRI LRQKTSLATD SMMGDGYSFL PMLCEPLSIQ
     DPGLAEMGLQ EVPENPEFKN YEKINIYGKS DGRTNTELSK LYQNHGSRIK GLFLPASLAS
     VSSQEDPEKD LSRSPELQED DPHSFAFGSD DSKDGEMGDD LQNYRLVSVV SHFGSSPNSG
     HYVSDVYDFQ KQAWLLYSDV QVFESSDPSI QENRLNSGYI FFYMHNEIFE ELLKKASECK
     VLSTSKEEKR DIDYFSTLLN GLTYILEEF
//