UBP29_MOUSE
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 03-AUG-2022, entry version 137.
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.ENSMUSP00000062349; -.
DR MEROPS; C19.043; -.
DR iPTMnet; Q9ES63; -.
DR PhosphoSitePlus; Q9ES63; -.
DR MaxQB; Q9ES63; -.
DR PaxDb; Q9ES63; -.
DR PRIDE; Q9ES63; -.
DR ProteomicsDB; 298459; -.
DR Antibodypedia; 19631; 137 antibodies from 25 providers.
DR DNASU; 57775; -.
DR Ensembl; ENSMUST00000054055; ENSMUSP00000062349; ENSMUSG00000051527.
DR Ensembl; ENSMUST00000198068; ENSMUSP00000143267; ENSMUSG00000051527.
DR Ensembl; ENSMUST00000200535; ENSMUSP00000143769; ENSMUSG00000051527.
DR GeneID; 57775; -.
DR KEGG; mmu:57775; -.
DR UCSC; uc009fcb.2; mouse.
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; YNCEMCK; -.
DR PhylomeDB; Q9ES63; -.
DR TreeFam; TF323032; -.
DR BioGRID-ORCS; 57775; 3 hits in 74 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 115 other 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:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 2.30.29.180; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033381; USP29.
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; PTHR24006:SF667; PTHR24006:SF667; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 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 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
