Q91XB0 (TREX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Three prime repair exonuclease 1
EC=3.1.11.2

Alternative name(s):
3'-5' exonuclease TREX1

Gene names

Name:

Trex1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exonuclease with a preference for double stranded DNA with mismatched 3' termini. May play a role in DNA repair. Ref.1 Ref.4
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Cofactor	Magnesium. Required for activity. Substitution with Mn2+ results in partial activity.
Subunit structure	Homodimer By similarity. Ref.4
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the exonuclease superfamily. TREX family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5-8.0.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	Magnesium
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cellular response to interferon-beta Inferred from direct assay. Source: MGI
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'-5' exonuclease activity Inferred from sequence or structural similarity. Source: UniProtKB adenyl deoxyribonucleotide binding Inferred from direct assay. Source: MGI double-stranded DNA binding Inferred from direct assay. Source: MGI exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from physical interaction. Source: MGI single-stranded DNA binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 314

314

Three prime repair exonuclease 1

PRO_0000109869

Amino acid modifications

Modified residue

78

1

Phosphoserine By similarity

Modified residue

167

1

Phosphoserine By similarity

Modified residue

261

1

Phosphoserine By similarity

Modified residue

272

1

Phosphoserine Ref.5

Experimental info

Sequence conflict

53

1

H → L in AAH11133. Ref.3

Sequence conflict

269

1

R → G in AAH11133. Ref.3

Secondary structure

1

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314

Helix Strand Turn

Details...

Beta strand

12 – 23

12

Helix

25 – 27

3

Beta strand

31 – 40

10

Helix

41 – 44

4

Beta strand

65 – 70

6

Helix

79 – 85

7

Helix

89 – 94

6

Helix

102 – 113

12

Beta strand

117 – 123

7

Turn

124 – 129

6

Helix

130 – 139

10

Beta strand

141 – 143

3

Turn

146 – 149

4

Beta strand

151 – 154

4

Helix

155 – 164

10

Helix

179 – 187

9

Helix

197 – 208

12

Helix

212 – 222

11

Helix

226 – 228

3

Sequences

	Sequence		Length	Mass (Da)
	Q91XB0 [UniParc]. Last modified May 24, 2004. Version 2. Checksum: 52C4F63A23214A7F	FASTA	314	33,675
	10 20 30 40 50 60 MGSQTLPHGH MQTLIFLDLE ATGLPSSRPE VTELCLLAVH RRALENTSIS QGHPPPVPRP 70 80 90 100 110 120 PRVVDKLSLC IAPGKACSPG ASEITGLSKA ELEVQGRQRF DDNLAILLRA FLQRQPQPCC 130 140 150 160 170 180 LVAHNGDRYD FPLLQTELAR LSTPSPLDGT FCVDSIAALK ALEQASSPSG NGSRKSYSLG 190 200 210 220 230 240 SIYTRLYWQA PTDSHTAEGD VLTLLSICQW KPQALLQWVD EHARPFSTVK PMYGTPATTG 250 260 270 280 290 300 TTNLRPHAAT ATTPLATANG SPSNGRSRRP KSPPPEKVPE APSQEGLLAP LSLLTLLTLA 310 IATLYGLFLA SPGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10391904] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Spleen and Tongue.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[4]	"Excision of 3' termini by the Trex1 and TREX2 3'-->5' exonucleases. Characterization of the recombinant proteins." Mazur D.J., Perrino F.W. J. Biol. Chem. 276:17022-17029(2001) [PubMed: 11279105] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, HOMODIMERIZATION.
[5]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF151106 mRNA. Translation: AAD48775.2.
AF319574 mRNA. Translation: AAK07621.1.
AK009899 mRNA. Translation: BAB26571.2.
AK087832 mRNA. Translation: BAC40020.1.
AK171916 mRNA. Translation: BAE42731.1.
BC011133 mRNA. Translation: AAH11133.1.

IPI

IPI00128410.

RefSeq

NP_001012236.1. NM_001012236.1.
NP_035767.4. NM_011637.6.

UniGene

Mm.439964.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IOC	X-ray	2.10	A/B	1-242	[»]
2O4G	X-ray	2.35	A/B/C/D	9-245	[»]
2O4I	X-ray	3.50	A/B	9-245	[»]
2OA8	X-ray	2.10	A/B	5-234	[»]
3B6O	X-ray	2.10	A/B/C/D	9-245	[»]
3B6P	X-ray	2.30	A/B/C/D	9-245	[»]
3MXI	X-ray	2.55	A/B	1-242	[»]
3MXJ	X-ray	1.95	A/B	1-242	[»]
3MXM	X-ray	1.75	A/B	1-242	[»]

ProteinModelPortal

Q91XB0.

SMR

Q91XB0. Positions 6-234.

ModBase

Search...

Protein-protein interaction databases

STRING

Q91XB0.

PTM databases

PhosphoSite

Q91XB0.

Proteomic databases

PRIDE

Q91XB0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000061973; ENSMUSP00000050971; ENSMUSG00000049734.
ENSMUST00000112053; ENSMUSP00000107684; ENSMUSG00000049734.

GeneID

22040.

KEGG

mmu:22040.

UCSC

uc009rrr.1. mouse.

Organism-specific databases

CTD

11277.

MGI

MGI:1328317. Trex1.

Phylogenomic databases

eggNOG

maNOG19230.

GeneTree

ENSGT00390000012715.

HOGENOM

HBG282070.

HOVERGEN

HBG079278.

InParanoid

Q91XB0.

OMA

WVDAHAR.

OrthoDB

EOG4D52ZG.

PhylomeDB

Q91XB0.

Gene expression databases

ArrayExpress

Q91XB0.

CleanEx

MM_TREX1.

Genevestigator

Q91XB0.

GermOnline

ENSMUSG00000049734. Mus musculus.

Family and domain databases

InterPro

IPR006055. Exonuclease.
IPR012337. RNaseH-like_dom.
[Graphical view]

KO

K10790.

SMART

SM00479. EXOIII. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

ProtoNet

Search...

Other

NextBio

301818.

SOURCE

Search...

Entry information

Entry name

TREX1_MOUSE

Accession

Primary (citable) accession number: Q91XB0
Secondary accession number(s): Q3TAD7, Q9D6W2, Q9R1B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	December 14, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program