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Protein

Three-prime repair exonuclease 1

Gene

TREX1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair (By similarity).By similarity1 Publication

Catalytic activityi

Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

Cofactori

Mg2+By similarityNote: Binds 2 Mg2+ per subunit. The second magnesium ion interacts with only one residue. Substitution with Mn2+ results in partial activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Magnesium 1By similarity
Metal bindingi18 – 181Magnesium 2By similarity
Metal bindingi20 – 201Magnesium 1By similarity
Binding sitei129 – 1291SubstrateBy similarity
Active sitei195 – 1951Proton donor/acceptorBy similarity
Metal bindingi200 – 2001Magnesium 1By similarity
Binding sitei200 – 2001SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Three-prime repair exonuclease 1 (EC:3.1.11.2)
Alternative name(s):
3'-5' exonuclease TREX1
Gene namesi
Name:TREX1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmcytosol By similarity
  • Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity

  • Note: Retained in the cytoplasm through the C-terminal region. In response to DNA damage, translocates to the nucleus where it is specifically recruited to replication foci. Translocation to the nucleus also occurs during GZMA-mediated cell death (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Three-prime repair exonuclease 1PRO_0000109867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei167 – 1671PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated, but not targeted to proteasomal degradation. Ubiquitination may be important for interaction with UBQLN1 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9BG99.
PRIDEiQ9BG99.

Interactioni

Subunit structurei

Homodimer. Interacts (via proline-rich region) with TCERG1/CA150 (via the second WW domain). Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within this complex, directly interacts with SET; this interaction does not result in TREX1 inhibition. Also interacts with NME1, but only following translocation to the nucleus. Directly interacts with UBQLN1 (via ubiquitin-like domain); the interaction may control TREX1 subcellular location (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000011063.

Structurei

3D structure databases

ProteinModelPortaliQ9BG99.
SMRiQ9BG99. Positions 4-233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 212Substrate bindingBy similarity
Regioni54 – 6310Proline-rich regionBy similarity
Regioni236 – 31580Necessary for endoplasmic reticulum localizationBy similarityAdd
BLAST
Regioni243 – 31573Interaction with UBQLN1By similarityAdd
BLAST
Regioni282 – 31534Necessary for cytoplasmic retentionBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the exonuclease superfamily. TREX family.Curated

Phylogenomic databases

eggNOGiKOG4793. Eukaryota.
ENOG4111YSP. LUCA.
HOGENOMiHOG000118119.
HOVERGENiHBG079278.
InParanoidiQ9BG99.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9BG99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRALPPGP VQTLIFLDLE ATGLPFSQPK ITELCLLAVH RYALEGLSAP
60 70 80 90 100
QGPSPTAPVP PRVLDKLSLC VAPGKVCSPA ASEITGLSTA VLAAHGRRAF
110 120 130 140 150
DADLVNLIRT FLQRQPQPWC LVAHNGDRYD FPLLRAELAL LGLASALDDA
160 170 180 190 200
FCVDSIAALK ALEPTGSSSE HGPRKSYSLG SVYTRLYGQA PPDSHTAEGD
210 220 230 240 250
VLALLSVCQW RPRALLRWVD AHAKPFSTVK PMYVITTSTG TNPRPSAVTA
260 270 280 290 300
TVPLARASDT GPNLRGDRSP KPAPSPKMCP GAPPGEGLLA PLGLLAFLTL
310
AVAMLYGLSL AMPGQ
Length:315
Mass (Da):33,132
Last modified:June 1, 2001 - v1
Checksum:i90AD66D1513DFDE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF319575 mRNA. Translation: AAK07622.1.
UniGeneiBt.7472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF319575 mRNA. Translation: AAK07622.1.
UniGeneiBt.7472.

3D structure databases

ProteinModelPortaliQ9BG99.
SMRiQ9BG99. Positions 4-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000011063.

Proteomic databases

PaxDbiQ9BG99.
PRIDEiQ9BG99.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG4793. Eukaryota.
ENOG4111YSP. LUCA.
HOGENOMiHOG000118119.
HOVERGENiHBG079278.
InParanoidiQ9BG99.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3'-->5' exonucleases."
    Mazur D.J., Perrino F.W.
    J. Biol. Chem. 274:19655-19660(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-60; 99-109 AND 161-184, FUNCTION, HOMODIMERIZATION.
    Tissue: Thymus.

Entry informationi

Entry nameiTREX1_BOVIN
AccessioniPrimary (citable) accession number: Q9BG99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.