TREX2_MOUSE
ID TREX2_MOUSE Reviewed; 236 AA.
AC Q9R1A9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Three prime repair exonuclease 2;
DE EC=3.1.11.2;
DE AltName: Full=3'-5' exonuclease TREX2;
GN Name=Trex2;
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 FUNCTION.
RX PubMed=10391904; DOI=10.1074/jbc.274.28.19655;
RA Mazur D.J., Perrino F.W.;
RT "Identification and expression of the TREX1 and TREX2 cDNA sequences
RT encoding mammalian 3'-->5' exonucleases.";
RL J. Biol. Chem. 274:19655-19660(1999).
CC -!- FUNCTION: Exonuclease with a preference for double-stranded DNA with
CC mismatched 3' termini. May play a role in DNA repair.
CC {ECO:0000269|PubMed:10391904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) per subunit. The second magnesium ion interacts
CC with only one residue. Substitution with Mn(2+) results in partial
CC activity. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the exonuclease superfamily. TREX family.
CC {ECO:0000305}.
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DR EMBL; AF151108; AAD48777.1; -; mRNA.
DR CCDS; CCDS30201.1; -.
DR RefSeq; NP_036037.1; NM_011907.4.
DR PDB; 6A45; X-ray; 1.90 A; A/B=1-236.
DR PDB; 6A46; X-ray; 2.00 A; A/B=1-236.
DR PDB; 6A47; X-ray; 1.90 A; A/B=1-236.
DR PDB; 6A4B; X-ray; 2.70 A; A/B/C/D/E/F=1-236.
DR PDBsum; 6A45; -.
DR PDBsum; 6A46; -.
DR PDBsum; 6A47; -.
DR PDBsum; 6A4B; -.
DR AlphaFoldDB; Q9R1A9; -.
DR SMR; Q9R1A9; -.
DR BioGRID; 204898; 1.
DR STRING; 10090.ENSMUSP00000033738; -.
DR iPTMnet; Q9R1A9; -.
DR PhosphoSitePlus; Q9R1A9; -.
DR PaxDb; Q9R1A9; -.
DR PRIDE; Q9R1A9; -.
DR ProteomicsDB; 298214; -.
DR Antibodypedia; 30811; 138 antibodies from 28 providers.
DR DNASU; 24102; -.
DR Ensembl; ENSMUST00000033738; ENSMUSP00000033738; ENSMUSG00000031372.
DR GeneID; 24102; -.
DR KEGG; mmu:24102; -.
DR UCSC; uc009tlt.2; mouse.
DR CTD; 11219; -.
DR MGI; MGI:1346343; Trex2.
DR VEuPathDB; HostDB:ENSMUSG00000031372; -.
DR eggNOG; KOG4793; Eukaryota.
DR GeneTree; ENSGT00390000012715; -.
DR HOGENOM; CLU_067419_1_0_1; -.
DR InParanoid; Q9R1A9; -.
DR OMA; CKGYSLG; -.
DR OrthoDB; 1365966at2759; -.
DR PhylomeDB; Q9R1A9; -.
DR TreeFam; TF323333; -.
DR BioGRID-ORCS; 24102; 2 hits in 109 CRISPR screens.
DR PRO; PR:Q9R1A9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R1A9; protein.
DR Bgee; ENSMUSG00000031372; Expressed in esophagus and 18 other tissues.
DR ExpressionAtlas; Q9R1A9; baseline and differential.
DR Genevisible; Q9R1A9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR040393; TREX1/2.
DR InterPro; IPR034926; TREX2.
DR PANTHER; PTHR13058; PTHR13058; 1.
DR PANTHER; PTHR13058:SF24; PTHR13058:SF24; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..236
FT /note="Three prime repair exonuclease 2"
FT /id="PRO_0000109871"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 16..17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6A47"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:6A47"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:6A47"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6A47"
FT TURN 117..122
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:6A47"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6A47"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:6A47"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6A46"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:6A47"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6A47"
SQ SEQUENCE 236 AA; 25955 MW; 695CF4126AB06676 CRC64;
MSEPPRAETF VFLDLEATGL PNMDPEIAEI SLFAVHRSSL ENPERDDSGS LVLPRVLDKL
TLCMCPERPF TAKASEITGL SSESLMHCGK AGFNGAVVRT LQGFLSRQEG PICLVAHNGF
DYDFPLLCTE LQRLGAHLPQ DTVCLDTLPA LRGLDRAHSH GTRAQGRKSY SLASLFHRYF
QAEPSAAHSA EGDVHTLLLI FLHRAPELLA WADEQARSWA HIEPMYVPPD GPSLEA
