Q24558 (EXO1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exonuclease 1
EC=3.1.-.-

Alternative name(s):
Exonuclease I
Protein tosca

Gene names

Name:	tos
Synonyms:	exo1
ORF Names:	CG10387

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	5'->3' double-stranded DNA exonuclease which may also contain a cryptic 3'->5' double-stranded DNA exonuclease activity. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for DNA mismatch repair (MMR) By similarity.
Cofactor	Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Specifically expressed in the female germline. Ref.1
Developmental stage	Maternally expressed. Accumulates in the developing oocyte. Ref.1
Sequence similarities	Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA excision DNA repair
Cellular component	Nucleus
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Endonuclease Excision nuclease Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from sequence or structural similarity. Source: UniProtKB mismatch repair Inferred from sequence or structural similarity Ref.1. Source: UniProtKB
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW double-stranded DNA specific 5'-3' exodeoxyribonuclease activity Inferred from sequence or structural similarity. Source: UniProtKB flap endonuclease activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA specific 5'-3' exodeoxyribonuclease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 732	732	Exonuclease 1		PRO_0000154043
Regions
	Region	1 – 99	99	N-domain
	Region	138 – 230	93	I-domain
Sites
	Metal binding	30	1	Magnesium 1 By similarity
	Metal binding	78	1	Magnesium 1 By similarity
	Metal binding	150	1	Magnesium 1 By similarity
	Metal binding	152	1	Magnesium 1 By similarity
	Metal binding	171	1	Magnesium 2 By similarity
	Metal binding	173	1	Magnesium 2 By similarity
	Metal binding	226	1	Magnesium 2 By similarity
Amino acid modifications
	Modified residue	431	1	Phosphoserine Ref.6
	Modified residue	433	1	Phosphoserine Ref.6
	Modified residue	443	1	Phosphothreonine Ref.6
	Modified residue	447	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	130	1	A → T in CAA61430. Ref.1
	Sequence conflict	701	1	T → I in AAK93218. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q24558 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A1AF71CDFC7813AC	FASTA	732	83,181
	10 20 30 40 50 60 MGITGLIPFV GKASSQLHLK DIRGSTVAVD TYCWLHKGVF GCAEKLARGE DTDVYIQYCL 70 80 90 100 110 120 KYVNMLLSYD IKPILVFDGQ HLPAKALTEK RRRDSRKQSK ERAAELLRLG RIEEARSHMR 130 140 150 160 170 180 RCVDVTHDMA LRLIRECRSR NVDCIVAPYE ADAQMAWLNR ADVAQYIITE DSDLTLFGAK 190 200 210 220 230 240 NIIFKLDLNG SGLLVEAEKL HLAMGCTEEK YHFDKFRRMC ILSGCDYLDS LPGIGLAKAC 250 260 270 280 290 300 KFILKTEQED MRIALKKIPS YLNMRNLEVD DDYIENFMKA EATFRHMFIY NPLERRMQRL 310 320 330 340 350 360 CALEDYETDE RYCSNAGTLL EDSEQALHLA LGNLNPFSMK RLDSWTPEKA WPTPKNVKRS 370 380 390 400 410 420 KHKSIWQTNF QSENTHTPKK ENPCALFFKK VDFVGKTLNE EIEANQRLEQ AKQTEAELFN 430 440 450 460 470 480 MYSFKAKRRR SPSREDSVDQ ERTPPPSPVH KSRHNPFAKE RTGEEANQRS PVVCENASLL 490 500 510 520 530 540 RLLSPKKASP LDGEAGVKKV DSLKRSIFAK EQVQIRSRFF ATQDEQTRLQ REHLRDTEND 550 560 570 580 590 600 DMDEQKLSSH SGHKKLRLVC KDIPGKNPIR QRCSSQISDG ETDTDTTASS LLESQDKGVP 610 620 630 640 650 660 SPLESQEDLN NSQPQIPTEG NTNSTTIRIK SLDLLLENSP EPTQESDRNN NDAIILLSDD 670 680 690 700 710 720 SCSSDQRASS TSSSSQQRQN FLPTSKRRVG LSKPSTAKKG TPKSRTNGKL GAVSQNQTKL 730 SMFGFQTKPV LK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A Drosophila gene encoding a nuclease specifically expressed in the female germline." Digilio F.A., Pannuti A., Lucchesi J., Furia M., Polito L. Dev. Biol. 178:90-100(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Canton-S.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-433; THR-443 AND SER-447, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X89021 mRNA. Translation: CAA61430.1. X89022 Genomic DNA. Translation: CAA61431.1. AE014134 Genomic DNA. Translation: AAF53687.1. AY051794 mRNA. Translation: AAK93218.1. BT058042 mRNA. Translation: ACM78484.1.
RefSeq	NP_477145.1. NM_057797.3.
UniGene	Dm.4197.
3D structure databases
ProteinModelPortal	Q24558.
SMR	Q24558. Positions 2-350.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q24558. 1 interaction.
MINT	MINT-297328.
Proteomic databases
PaxDb	Q24558.
PRIDE	Q24558.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0081131; FBpp0080675; FBgn0015553.
GeneID	35119.
KEGG	dme:Dmel_CG10387.
UCSC	CG10387-RA. d. melanogaster.
Organism-specific databases
CTD	35119.
FlyBase	FBgn0015553. tos.
Phylogenomic databases
eggNOG	COG0258.
GeneTree	ENSGT00510000047676.
InParanoid	Q24558.
KO	K10746.
OMA	LAKACKF.
OrthoDB	EOG42JM78.
PhylomeDB	Q24558.
Gene expression databases
Bgee	Q24558.
GermOnline	CG10387. Drosophila melanogaster.
Family and domain databases
InterPro	IPR020045. 5-3_exonuclease_C. IPR008918. HhH2. IPR006086. XPG-I_dom. IPR006084. XPG/Rad2. IPR019974. XPG_CS. IPR006085. XPG_DNA_repair_N. [Graphical view]
PANTHER	PTHR11081. PTHR11081. 1 hit.
Pfam	PF00867. XPG_I. 1 hit. PF00752. XPG_N. 1 hit. [Graphical view]
PRINTS	PR00853. XPGRADSUPER.
SMART	SM00279. HhH2. 1 hit. SM00484. XPGI. 1 hit. SM00485. XPGN. 1 hit. [Graphical view]
SUPFAM	SSF47807. 5_3_exo_C. 1 hit.
PROSITE	PS00841. XPG_1. 1 hit. PS00842. XPG_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	35119.
NextBio	791961.

Entry information

Entry name

EXO1_DROME

Accession

Primary (citable) accession number: Q24558
Secondary accession number(s): B9EQW7, Q24557, Q960X5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project