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Three-prime repair exonuclease 1 (EC 3.1.11.2) (3'-5' exonuclease TREX1) (DNase III)

 TREX1_HUMAN             Reviewed;         314 AA.
Q9NSU2; B2RCN9; Q8TEU2; Q9BPW1; Q9Y4X2;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
20-DEC-2017, sequence version 2.
28-MAR-2018, entry version 167.
RecName: Full=Three-prime repair exonuclease 1 {ECO:0000305};
EC=3.1.11.2;
AltName: Full=3'-5' exonuclease TREX1 {ECO:0000303|PubMed:10391904};
AltName: Full=Deoxyribonuclease III {ECO:0000303|PubMed:10393201};
Short=DNase III {ECO:0000303|PubMed:10393201};
Name=TREX1 {ECO:0000312|HGNC:HGNC:12269};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
PubMed=10393201; DOI=10.1093/emboj/18.13.3868;
Hoess M., Robins P., Naven T.J.P., Pappin D.J.C., Sgouros J.,
Lindahl T.;
"A human DNA editing enzyme homologous to the Escherichia coli
DnaQ/MutD protein.";
EMBO J. 18:3868-3875(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=10391904; DOI=10.1074/jbc.274.28.19655;
Mazur D.J., Perrino F.W.;
"Identification and expression of the TREX1 and TREX2 cDNA sequences
encoding mammalian 3'-->5' exonucleases.";
J. Biol. Chem. 274:19655-19660(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
PubMed=11278605; DOI=10.1074/jbc.M010051200;
Mazur D.J., Perrino F.W.;
"Structure and expression of the TREX1 and TREX2 3'-->5' exonuclease
genes.";
J. Biol. Chem. 276:14718-14727(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION IN CELL DEATH, IDENTIFICATION IN THE SET COMPLEX, INTERACTION
WITH NME1 AND SET, AND SUBCELLULAR LOCATION.
PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005;
Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B.,
Perrino F.W., Lieberman J.;
"The exonuclease TREX1 is in the SET complex and acts in concert with
NM23-H1 to degrade DNA during granzyme A-mediated cell death.";
Mol. Cell 23:133-142(2006).
[10]
FUNCTION IN CELL CYCLE REGULATION, AND CHARACTERIZATION OF VARIANT
AGS1 HIS-114.
PubMed=18045533; DOI=10.1016/j.cell.2007.10.017;
Yang Y.G., Lindahl T., Barnes D.E.;
"Trex1 exonuclease degrades ssDNA to prevent chronic checkpoint
activation and autoimmune disease.";
Cell 131:873-886(2007).
[11]
FUNCTION, AND CHARACTERIZATION OF VARIANTS AGS1 HIS-114; ASP-200 INS
AND ASP-201.
PubMed=17293595; DOI=10.1074/jbc.M700039200;
de Silva U., Choudhury S., Bailey S.L., Harvey S., Perrino F.W.,
Hollis T.;
"The crystal structure of TREX1 explains the 3' nucleotide specificity
and reveals a polyproline II helix for protein partnering.";
J. Biol. Chem. 282:10537-10543(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-261, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
FUNCTION IN OXIDIZED DNA DEGRADATION, AND POTENTIAL ROLE IN SLE SKIN
LESIONS.
PubMed=23993650; DOI=10.1016/j.immuni.2013.08.004;
Gehrke N., Mertens C., Zillinger T., Wenzel J., Bald T., Zahn S.,
Tueting T., Hartmann G., Barchet W.;
"Oxidative damage of DNA confers resistance to cytosolic nuclease
TREX1 degradation and potentiates STING-dependent immune sensing.";
Immunity 39:482-495(2013).
[14]
INTERACTION WITH UBQLN1, UBIQUITINATION, CHARACTERIZATION OF VARIANTS
AGS1 ALA-122; LYS-198; ASN-200 AND PRO-303, CHARACTERIZATION OF
VARIANTS SLE LEU-290 AND CYS-305, AND MUTAGENESIS OF LYS-30; LYS-66;
LYS-75; LYS-160; LYS-175; LYS-242; LYS-271 AND LYS-277.
PubMed=23979357; DOI=10.1074/jbc.M113.503391;
Orebaugh C.D., Fye J.M., Harvey S., Hollis T., Wilkinson J.C.,
Perrino F.W.;
"The TREX1 C-terminal region controls cellular localization through
ubiquitination.";
J. Biol. Chem. 288:28881-28892(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
VARIANTS AGS1 HIS-114; ASP-200 INS AND ASP-201.
PubMed=16845398; DOI=10.1038/ng1845;
Crow Y.J., Hayward B.E., Parmar R., Robins P., Leitch A., Ali M.,
Black D.N., van Bokhoven H., Brunner H.G., Hamel B.C.J., Corry P.C.,
Cowan F.M., Frints S.G., Klepper J., Livingston J.H., Lynch S.A.,
Massey R.F., Meritet J.F., Michaud J.L., Ponsot G., Voit T., Lebon P.,
Bonthron D.T., Jackson A.P., Barnes D.E., Lindahl T.;
"Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 cause
Aicardi-Goutieres syndrome at the AGS1 locus.";
Nat. Genet. 38:917-920(2006).
[19]
INVOLVEMENT IN CHBL1, VARIANT AGS1 ASN-200, AND CHARACTERIZATION OF
VARIANT AGS1 ASN-200.
PubMed=17357087; DOI=10.1086/513443;
Rice G., Newman W.G., Dean J., Patrick T., Parmar R., Flintoff K.,
Robins P., Harvey S., Hollis T., O'Hara A., Herrick A.L., Bowden A.P.,
Perrino F.W., Lindahl T., Barnes D.E., Crow Y.J.;
"Heterozygous mutations in TREX1 cause familial chilblain lupus and
dominant Aicardi-Goutieres syndrome.";
Am. J. Hum. Genet. 80:811-815(2007).
[20]
VARIANTS AGS1 HIS-114; ALA-122; ASN-200; ASP-201 AND PRO-303.
PubMed=17846997; DOI=10.1086/521373;
Rice G., Patrick T., Parmar R., Taylor C.F., Aeby A., Aicardi J.,
Artuch R., Montalto S.A., Bacino C.A., Barroso B., Baxter P.,
Benko W.S., Bergmann C., Bertini E., Biancheri R., Blair E.M.,
Blau N., Bonthron D.T., Briggs T., Brueton L.A., Brunner H.G.,
Burke C.J., Carr I.M., Carvalho D.R., Chandler K.E., Christen H.J.,
Corry P.C., Cowan F.M., Cox H., D'Arrigo S., Dean J., De Laet C.,
De Praeter C., Dery C., Ferrie C.D., Flintoff K., Frints S.G.,
Garcia-Cazorla A., Gener B., Goizet C., Goutieres F., Green A.J.,
Guet A., Hamel B.C., Hayward B.E., Heiberg A., Hennekam R.C.,
Husson M., Jackson A.P., Jayatunga R., Jiang Y.H., Kant S.G., Kao A.,
King M.D., Kingston H.M., Klepper J., van der Knaap M.S.,
Kornberg A.J., Kotzot D., Kratzer W., Lacombe D., Lagae L.,
Landrieu P.G., Lanzi G., Leitch A., Lim M.J., Livingston J.H.,
Lourenco C.M., Lyall E.G., Lynch S.A., Lyons M.J., Marom D.,
McClure J.P., McWilliam R., Melancon S.B., Mewasingh L.D.,
Moutard M.L., Nischal K.K., Ostergaard J.R., Prendiville J.,
Rasmussen M., Rogers R.C., Roland D., Rosser E.M., Rostasy K.,
Roubertie A., Sanchis A., Schiffmann R., Scholl-Burgi S., Seal S.,
Shalev S.A., Corcoles C.S., Sinha G.P., Soler D., Spiegel R.,
Stephenson J.B., Tacke U., Tan T.Y., Till M., Tolmie J.L., Tomlin P.,
Vagnarelli F., Valente E.M., Van Coster R.N., Van der Aa N.,
Vanderver A., Vles J.S., Voit T., Wassmer E., Weschke B.,
Whiteford M.L., Willemsen M.A., Zankl A., Zuberi S.M., Orcesi S.,
Fazzi E., Lebon P., Crow Y.J.;
"Clinical and molecular phenotype of Aicardi-Goutieres syndrome.";
Am. J. Hum. Genet. 81:713-725(2007).
[21]
VARIANT CHBL1 ASN-18, AND CHARACTERIZATION OF VARIANT CHBL1 ASN-18.
PubMed=17440703; DOI=10.1007/s00109-007-0199-9;
Lee-Kirsch M.A., Chowdhury D., Harvey S., Gong M., Senenko L.,
Engel K., Pfeiffer C., Hollis T., Gahr M., Perrino F.W., Lieberman J.,
Hubner N.;
"A mutation in TREX1 that impairs susceptibility to granzyme A-
mediated cell death underlies familial chilblain lupus.";
J. Mol. Med. 85:531-537(2007).
[22]
VARIANTS SLE HIS-114; VAL-158; SER-227; SER-240; PRO-247; LEU-290;
CYS-305 AND ALA-306, AND VARIANT GLY-266.
PubMed=17660818; DOI=10.1038/ng2091;
Lee-Kirsch M.A., Gong M., Chowdhury D., Senenko L., Engel K.,
Lee Y.A., de Silva U., Bailey S.L., Witte T., Vyse T.J., Kere J.,
Pfeiffer C., Harvey S., Wong A., Koskenmies S., Hummel O., Rohde K.,
Schmidt R.E., Dominiczak A.F., Gahr M., Hollis T., Perrino F.W.,
Lieberman J., Huebner N.;
"Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 are
associated with systemic lupus erythematosus.";
Nat. Genet. 39:1065-1067(2007).
[23]
INVOLVEMENT IN RVCL.
PubMed=17660820; DOI=10.1038/ng2082;
Richards A., van den Maagdenberg A.M.J.M., Jen J.C., Kavanagh D.,
Bertram P., Spitzer D., Liszewski M.K., Barilla-Labarca M.-L.,
Terwindt G.M., Kasai Y., McLellan M., Grand M.G., Vanmolkot K.R.J.,
de Vries B., Wan J., Kane M.J., Mamsa H., Schaefer R., Stam A.H.,
Haan J., de Jong P.T.V.M., Storimans C.W., van Schooneveld M.J.,
Oosterhuis J.A., Gschwendter A., Dichgans M., Kotschet K.E.,
Hodgkinson S., Hardy T.A., Delatycki M.B., Hajj-Ali R.A.,
Kothari P.H., Nelson S.F., Frants R.R., Baloh R.W., Ferrari M.D.,
Atkinson J.P.;
"C-terminal truncations in human 3'-5' DNA exonuclease TREX1 cause
autosomal dominant retinal vasculopathy with cerebral
leukodystrophy.";
Nat. Genet. 39:1068-1070(2007).
[24]
VARIANT AGS1 ASN-18.
PubMed=20799324; DOI=10.1002/ajmg.a.33620;
Haaxma C.A., Crow Y.J., van Steensel M.A., Lammens M.M., Rice G.I.,
Verbeek M.M., Willemsen M.A.;
"A de novo p.Asp18Asn mutation in TREX1 in a patient with Aicardi-
Goutieres syndrome.";
Am. J. Med. Genet. A 152:2612-2617(2010).
[25]
VARIANTS AGS1 HIS-114; LYS-198 AND HIS-200, AND VARIANT SLE HIS-200.
PubMed=20131292; DOI=10.1002/art.27367;
Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K.,
Hunger S., Borozdin W., Mah J.K., Ungerath K., Walkenhorst H.,
Richardt H.H., Buckard J., Bevot A., Siegel C., von Stuelpnagel C.,
Ikonomidou C., Thomas K., Proud V., Niemann F., Wieczorek D.,
Haeusler M., Niggemann P., Baltaci V., Conrad K., Lebon P.,
Lee-Kirsch M.A.;
"Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-
Goutieres syndrome.";
Arthritis Rheum. 62:1469-1477(2010).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10391904, ECO:0000269|PubMed:10393201,
ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:17293595,
ECO:0000269|PubMed:18045533, ECO:0000269|PubMed:23993650}.
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
direction to yield nucleoside 5'-phosphates.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 Mg(2+) per subunit. The second magnesium ion
interacts with only one residue. Substitution with Mn(2+) results
in partial activity. {ECO:0000250};
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:23979357}.
-!- INTERACTION:
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-16746122, EBI-10172290;
P60409-2:KRTAP10-7; NbExp=3; IntAct=EBI-16746122, EBI-10695388;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Endoplasmic
reticulum membrane; Peripheral membrane protein. Note=Retained in
the cytoplasm through the C-terminal region (By similarity). 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.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=3;
IsoId=Q9NSU2-3; Sequence=Displayed;
Name=1;
IsoId=Q9NSU2-1; Sequence=VSP_059279;
Name=2;
IsoId=Q9NSU2-2; Sequence=VSP_010445;
-!- TISSUE SPECIFICITY: Detected in thymus, spleen, liver, brain,
heart, small intestine and colon. {ECO:0000269|PubMed:10393201,
ECO:0000269|PubMed:11278605}.
-!- INDUCTION: Induced by cytosolic DNA. Induced by inflammatory
stimuli such as IFN-alpha and IFN-gamma in B cells and also by LPS
and viral and bacterial DNA (via TLR9) in dendritic cells and
macrophages (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated, but not targeted to proteasomal degradation.
Ubiquitination may be important for interaction with UBQLN1.
{ECO:0000269|PubMed:23979357}.
-!- DISEASE: Aicardi-Goutieres syndrome 1 (AGS1) [MIM:225750]: A form
of Aicardi-Goutieres syndrome, a genetically heterogeneous disease
characterized by cerebral atrophy, leukoencephalopathy,
intracranial calcifications, chronic cerebrospinal fluid (CSF)
lymphocytosis, increased CSF alpha-interferon, and negative
serologic investigations for common prenatal infection. Clinical
features as thrombocytopenia, hepatosplenomegaly and elevated
hepatic transaminases along with intermittent fever may
erroneously suggest an infective process. Severe neurological
dysfunctions manifest in infancy as progressive microcephaly,
spasticity, dystonic posturing and profound psychomotor
retardation. Death often occurs in early childhood.
{ECO:0000269|PubMed:16845398, ECO:0000269|PubMed:17293595,
ECO:0000269|PubMed:17357087, ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:18045533, ECO:0000269|PubMed:20131292,
ECO:0000269|PubMed:20799324, ECO:0000269|PubMed:23979357}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A
chronic, relapsing, inflammatory, and often febrile multisystemic
disorder of connective tissue, characterized principally by
involvement of the skin, joints, kidneys and serosal membranes. It
is of unknown etiology, but is thought to represent a failure of
the regulatory mechanisms of the autoimmune system. The disease is
marked by a wide range of system dysfunctions, an elevated
erythrocyte sedimentation rate, and the formation of LE cells in
the blood or bone marrow. {ECO:0000269|PubMed:17660818,
ECO:0000269|PubMed:20131292, ECO:0000269|PubMed:23979357}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry. Enhanced immune
sensing of oxidized DNA may be involved in the phototoxicity
experienced by SLE patients. Exposure to UV-light produces DNA
oxidative damage. Oxidized DNA being a poor TREX1 substrate, it
accumulates in skin, leading to enhanced auto-immune reactivity
and eventually skin lesions (PubMed:23993650).
{ECO:0000269|PubMed:23993650}.
-!- DISEASE: Chilblain lupus 1 (CHBL1) [MIM:610448]: A rare cutaneous
form of lupus erythematosus. Affected individuals present with
painful bluish-red papular or nodular lesions of the skin in acral
locations precipitated by cold and wet exposure at temperatures
less than 10 degrees centigrade. {ECO:0000269|PubMed:17357087,
ECO:0000269|PubMed:17440703}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Vasculopathy, retinal, with cerebral leukodystrophy
(RVCL) [MIM:192315]: A microvascular endotheliopathy resulting in
central nervous system degeneration and retinopathy, with
progressive loss of vision, stroke, motor impairment, and
cognitive decline. The ocular manifestations are characterized by
telangiectasias, microaneurysms and retinal capillary obliteration
starting in the macula. Diseased cerebral white matter has
prominent small infarcts that often coalesce to pseudotumors.
{ECO:0000269|PubMed:17660820}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the exonuclease superfamily. TREX family.
{ECO:0000305}.
-!- CAUTION: The gene for this protein is either identical to or
adjacent to that of ATRIP. Some of the mRNAs that encode ATRIP
also encode TREX1 in another reading frame. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD48774.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL82504.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/trex1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ243797; CAB50866.1; -; mRNA.
EMBL; AF151105; AAD48774.2; ALT_INIT; mRNA.
EMBL; AF319566; AAK07613.1; -; mRNA.
EMBL; AF319567; AAK07614.1; -; mRNA.
EMBL; AF319568; AAK07615.1; -; mRNA.
EMBL; AF319569; AAK07616.1; -; mRNA.
EMBL; AK315196; BAG37636.1; -; mRNA.
EMBL; AL137745; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF483777; AAL82504.1; ALT_INIT; Genomic_DNA.
EMBL; BC023630; AAH23630.1; -; mRNA.
CCDS; CCDS2769.1; -. [Q9NSU2-3]
CCDS; CCDS59451.1; -. [Q9NSU2-2]
PIR; T46299; T46299.
RefSeq; NP_009179.2; NM_007248.3. [Q9NSU2-2]
RefSeq; NP_057465.1; NM_016381.5. [Q9NSU2-1]
RefSeq; NP_338599.1; NM_033629.4. [Q9NSU2-3]
UniGene; Hs.707026; -.
UniGene; Hs.713742; -.
UniGene; Hs.744646; -.
ProteinModelPortal; Q9NSU2; -.
SMR; Q9NSU2; -.
BioGrid; 116433; 12.
IntAct; Q9NSU2; 5.
STRING; 9606.ENSP00000390478; -.
iPTMnet; Q9NSU2; -.
PhosphoSitePlus; Q9NSU2; -.
DMDM; 47606216; -.
EPD; Q9NSU2; -.
PaxDb; Q9NSU2; -.
PeptideAtlas; Q9NSU2; -.
PRIDE; Q9NSU2; -.
DNASU; 11277; -.
Ensembl; ENST00000444177; ENSP00000415972; ENSG00000213689. [Q9NSU2-2]
Ensembl; ENST00000625293; ENSP00000486676; ENSG00000213689. [Q9NSU2-1]
Ensembl; ENST00000629913; ENSP00000486444; ENSG00000213689. [Q9NSU2-3]
GeneID; 11277; -.
KEGG; hsa:11277; -.
UCSC; uc031rzp.2; human. [Q9NSU2-3]
CTD; 11277; -.
DisGeNET; 11277; -.
EuPathDB; HostDB:ENSG00000213689.10; -.
EuPathDB; HostDB:ENSG00000282827.1; -.
GeneCards; TREX1; -.
GeneReviews; TREX1; -.
HGNC; HGNC:12269; TREX1.
HPA; HPA035437; -.
MalaCards; TREX1; -.
MIM; 152700; phenotype.
MIM; 192315; phenotype.
MIM; 225750; phenotype.
MIM; 606609; gene.
MIM; 610448; phenotype.
neXtProt; NX_Q9NSU2; -.
OpenTargets; ENSG00000213689; -.
Orphanet; 51; Aicardi-Goutieres syndrome.
Orphanet; 3421; Cerebroretinal vasculopathy.
Orphanet; 90280; Chilblain lupus.
Orphanet; 71291; Hereditary vascular retinopathy.
Orphanet; 63261; HERNS syndrome.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA36949; -.
eggNOG; KOG4793; Eukaryota.
eggNOG; ENOG4111YSP; LUCA.
GeneTree; ENSGT00390000012715; -.
HOGENOM; HOG000118119; -.
HOVERGEN; HBG079278; -.
InParanoid; Q9NSU2; -.
KO; K10790; -.
OMA; LLSICQW; -.
OrthoDB; EOG091G0LSM; -.
PhylomeDB; Q9NSU2; -.
TreeFam; TF323333; -.
Reactome; R-HSA-3248023; Regulation by TREX1.
Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
ChiTaRS; TREX1; human.
GeneWiki; TREX1; -.
GenomeRNAi; 11277; -.
PRO; PR:Q9NSU2; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000213689; -.
CleanEx; HS_TREX1; -.
ExpressionAtlas; Q9NSU2; baseline.
Genevisible; Q9NSU2; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005635; C:nuclear envelope; NAS:UniProtKB.
GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; ISS:UniProtKB.
GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; TAS:UniProtKB.
GO; GO:0032405; F:MutLalpha complex binding; IDA:MGI.
GO; GO:0032407; F:MutSalpha complex binding; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; TAS:UniProtKB.
GO; GO:0006259; P:DNA metabolic process; ISS:UniProtKB.
GO; GO:0006310; P:DNA recombination; NAS:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
GO; GO:0006298; P:mismatch repair; NAS:UniProtKB.
GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
SMART; SM00479; EXOIII; 1.
SUPFAM; SSF53098; SSF53098; 1.
1: Evidence at protein level;
Aicardi-Goutieres syndrome; Alternative splicing; Complete proteome;
Cytoplasm; Disease mutation; Endoplasmic reticulum; Exonuclease;
Hydrolase; Magnesium; Membrane; Metal-binding; Neurodegeneration;
Nuclease; Nucleus; Phosphoprotein; Reference proteome;
Systemic lupus erythematosus; Ubl conjugation.
CHAIN 1 314 Three-prime repair exonuclease 1.
/FTId=PRO_0000109868.
REGION 20 21 Substrate binding. {ECO:0000250}.
REGION 54 63 Proline-rich region. {ECO:0000250}.
REGION 236 314 Necessary for endoplasmic reticulum
localization. {ECO:0000250}.
REGION 243 314 Interaction with UBQLN1.
{ECO:0000269|PubMed:23979357}.
REGION 281 314 Necessary for cytoplasmic retention.
{ECO:0000250}.
ACT_SITE 195 195 Proton donor/acceptor. {ECO:0000250}.
METAL 18 18 Magnesium 1. {ECO:0000250}.
METAL 18 18 Magnesium 2. {ECO:0000250}.
METAL 20 20 Magnesium 1. {ECO:0000250}.
METAL 200 200 Magnesium 1. {ECO:0000250}.
BINDING 129 129 Substrate. {ECO:0000250}.
BINDING 200 200 Substrate. {ECO:0000250}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 10 Missing (in isoform 2).
{ECO:0000303|PubMed:10393201}.
/FTId=VSP_010445.
VAR_SEQ 1 1 M -> MGPGARRQGRIVQGRPEMCFCPPPTPLPPLRILTLG
THTPTPCSSPGSAAGTYPTM (in isoform 1).
{ECO:0000303|PubMed:11278605}.
/FTId=VSP_059279.
VARIANT 18 18 D -> N (in CHBL1 and AGS1; loss of
function; dbSNP:rs121908117).
{ECO:0000269|PubMed:17440703,
ECO:0000269|PubMed:20799324}.
/FTId=VAR_037948.
VARIANT 114 114 R -> H (in AGS1 and SLE; primary
fibroblasts from an AGS1 patient carrying
H-169 show defective G1/S transition and
chronic G2/M DNA damage checkpoint
activation; strongly reduces activity;
dbSNP:rs72556554).
{ECO:0000269|PubMed:16845398,
ECO:0000269|PubMed:17293595,
ECO:0000269|PubMed:17660818,
ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:18045533,
ECO:0000269|PubMed:20131292}.
/FTId=VAR_028319.
VARIANT 122 122 V -> A (in AGS1; increases ubiquitination
levels; no effect on exonuclease
activity; dbSNP:rs79993407).
{ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:23979357}.
/FTId=VAR_070899.
VARIANT 158 158 A -> V (in SLE; dbSNP:rs762011967).
{ECO:0000269|PubMed:17660818}.
/FTId=VAR_037949.
VARIANT 198 198 E -> K (in AGS1; increases ubiquitination
levels; no effect on exonuclease
activity). {ECO:0000269|PubMed:20131292,
ECO:0000269|PubMed:23979357}.
/FTId=VAR_070900.
VARIANT 200 200 D -> DD (in AGS1; heterozygous compound
with H-169; loss of activity).
{ECO:0000269|PubMed:16845398,
ECO:0000269|PubMed:17293595}.
/FTId=VAR_028320.
VARIANT 200 200 D -> H (in AGS1 and SLE).
{ECO:0000269|PubMed:20131292}.
/FTId=VAR_070901.
VARIANT 200 200 D -> N (in AGS1; autosomal dominant form;
no effect on dsDNA exonuclease activity;
abolishes ssDNA exonuclease activity;
dbSNP:rs78846775).
{ECO:0000269|PubMed:17357087,
ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:23979357}.
/FTId=VAR_032940.
VARIANT 201 201 V -> D (in AGS1; reduces activity by 75%;
dbSNP:rs78408272).
{ECO:0000269|PubMed:16845398,
ECO:0000269|PubMed:17293595,
ECO:0000269|PubMed:17846997}.
/FTId=VAR_028321.
VARIANT 227 227 G -> S (in SLE; associated in cis with P-
302; dbSNP:rs113107733).
{ECO:0000269|PubMed:17660818}.
/FTId=VAR_037950.
VARIANT 240 240 R -> S (in SLE; dbSNP:rs72556555).
{ECO:0000269|PubMed:17660818}.
/FTId=VAR_037951.
VARIANT 247 247 A -> P (in SLE; associated in cis with S-
282; dbSNP:rs112741962).
{ECO:0000269|PubMed:17660818}.
/FTId=VAR_037952.
VARIANT 266 266 E -> G (in dbSNP:rs55999987).
{ECO:0000269|PubMed:17660818}.
/FTId=VAR_037953.
VARIANT 290 290 P -> L (in SLE; increases ubiquitination
levels; no effect on exonuclease
activity; dbSNP:rs148833270).
{ECO:0000269|PubMed:17660818,
ECO:0000269|PubMed:23979357}.
/FTId=VAR_037954.
VARIANT 303 303 T -> P (in AGS1; decreases ubiquitination
levels; decreases colocalization with
UBQLN1; no effect on exonuclease
activity; dbSNP:rs76224909).
{ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:23979357}.
/FTId=VAR_070902.
VARIANT 305 305 Y -> C (in SLE; decreases ubiquitination
levels; decreases colocalization with
UBQLN1; no effect on exonuclease
activity; dbSNP:rs370504038).
{ECO:0000269|PubMed:17660818,
ECO:0000269|PubMed:23979357}.
/FTId=VAR_037955.
VARIANT 306 306 G -> A (in SLE; dbSNP:rs780022923).
{ECO:0000269|PubMed:17660818}.
/FTId=VAR_037956.
MUTAGEN 30 30 K->R: Reduces ubiquitination.
{ECO:0000269|PubMed:23979357}.
MUTAGEN 66 66 K->R: No effect on ubiquitination.
{ECO:0000269|PubMed:23979357}.
MUTAGEN 75 75 K->R: Reduces ubiquitination.
{ECO:0000269|PubMed:23979357}.
MUTAGEN 160 160 K->R: Reduces ubiquitination.
{ECO:0000269|PubMed:23979357}.
MUTAGEN 175 175 K->R: Reduces ubiquitination.
{ECO:0000269|PubMed:23979357}.
MUTAGEN 242 242 K->R: Reduces ubiquitination.
{ECO:0000269|PubMed:23979357}.
MUTAGEN 271 271 K->R: Reduces ubiquitination. Strongly
reduces ubiquitination; when associated
with R-277.
{ECO:0000269|PubMed:23979357}.
MUTAGEN 277 277 K->R: Reduces ubiquitination. Strongly
reduces ubiquitination; when associated
with R-271.
{ECO:0000269|PubMed:23979357}.
CONFLICT 265 265 G -> R (in Ref. 1; CAB50866).
{ECO:0000305}.
SEQUENCE 314 AA; 33212 MW; EE8F63B6496D72F4 CRC64;
MGSQALPPGP MQTLIFFDME ATGLPFSQPK VTELCLLAVH RCALESPPTS QGPPPTVPPP
PRVVDKLSLC VAPGKACSPA ASEITGLSTA VLAAHGRQCF DDNLANLLLA FLRRQPQPWC
LVAHNGDRYD FPLLQAELAM LGLTSALDGA FCVDSITALK ALERASSPSE HGPRKSYSLG
SIYTRLYGQS PPDSHTAEGD VLALLSICQW RPQALLRWVD AHARPFGTIR PMYGVTASAR
TKPRPSAVTT TAHLATTRNT SPSLGESRGT KDLPPVKDPG ALSREGLLAP LGLLAILTLA
VATLYGLSLA TPGE


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