A8JR14 (APLF_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aprataxin and PNK-like factor
EC=4.2.99.18

Alternative name(s):
Apurinic-apyrimidinic endonuclease APLF

Gene names

ORF Names:

CG6171

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	255 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Ref.4
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. Ref.4
Sequence similarities	Belongs to the APLF family. Contains 2 PBZ-type zinc fingers.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	3'-5' exonuclease activity Inferred from direct assay Ref.4. Source: UniProtKB DNA-(apurinic or apyrimidinic site) lyase activity Inferred from direct assay Ref.4. Source: UniProtKB endodeoxyribonuclease activity Inferred from direct assay Ref.4. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform B (identifier: A8JR14-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform A (identifier: A8JR14-2)

The sequence of this isoform differs from the canonical sequence as follows:
     186-187: FN → CK
     188-255: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 255	255	Aprataxin and PNK-like factor		PRO_0000385300
Regions
	Zinc finger	121 – 142	22	PBZ-type 1
	Zinc finger	161 – 182	22	PBZ-type 2
	Compositional bias	206 – 255	50	Asp-rich
Natural variations
	Alternative sequence	186 – 187	2	FN → CK in isoform A.		VSP_038137
	Alternative sequence	188 – 255	68	Missing in isoform A.		VSP_038138

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 1CB1AC10524D57F3	FASTA	255	28,006
	10 20 30 40 50 60 MSATDASTAD SGAKRKSSED ITHNCNANFG AENGLRKRVK SEEPVASIKD ETNPEVPMKI 70 80 90 100 110 120 KAEPVENADE PTSTTPAIKI KAEPADNGNS PAAAMVKTEP TNSNAQDAAD ESTVSSSSIR 130 140 150 160 170 180 TSCRFGIRCY RRNPAHRSAE AHPGDQDYRR PNFPAPPLGT PACPFGNACY RRNPVHFQDY 190 200 210 220 230 240 SHPADFNSAQ NIRNRLRQRR AQRQNDDDSG TDEEDEPFGG DNDRDADYRP GADINEDEDD 250 ELEFDSQPIS GDDYD
	Isoform A [UniParc]. Checksum: 7C196DF08C487378	FASTA	187	20,158
	10 20 30 40 50 60 MSATDASTAD SGAKRKSSED ITHNCNANFG AENGLRKRVK SEEPVASIKD ETNPEVPMKI 70 80 90 100 110 120 KAEPVENADE PTSTTPAIKI KAEPADNGNS PAAAMVKTEP TNSNAQDAAD ESTVSSSSIR 130 140 150 160 170 180 TSCRFGIRCY RRNPAHRSAE AHPGDQDYRR PNFPAPPLGT PACPFGNACY RRNPVHFQDY SHPADCK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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, ALTERNATIVE SPLICING. Strain: Berkeley.
[3]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Strain: Berkeley. Tissue: Embryo.
[4]	"A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses." Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A. EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: ABW08680.1. AE014297 Genomic DNA. Translation: AAF55184.1. BT004895 mRNA. Translation: AAO47873.1.
RefSeq	NP_001097801.1. NM_001104331.2. NP_650455.1. NM_142198.3.
UniGene	Dm.31310.
3D structure databases
ProteinModelPortal	A8JR14.
SMR	A8JR14. Positions 103-182.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-986200.
Proteomic databases
PaxDb	A8JR14.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0112926; FBpp0111839; FBgn0026737.
GeneID	41872.
KEGG	dme:Dmel_CG6171.
UCSC	CG6171-RA. d. melanogaster. CG6171-RB. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0026737. CG6171.
Phylogenomic databases
eggNOG	NOG85452.
GeneTree	ENSGT00390000010591.
InParanoid	Q9VF76.
OrthoDB	EOG459ZXG.
PhylomeDB	A8JR14.
Family and domain databases
InterPro	IPR019406. Znf_C2H2_APLF-like. [Graphical view]
Pfam	PF10283. zf-CCHH. 2 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	41872.
NextBio	826032.

Entry information

Entry name

APLF_DROME

Accession

Primary (citable) accession number: A8JR14
Secondary accession number(s): Q9VF76

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	December 4, 2007
Last modified:	May 29, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project