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A8JR14

- APLF_DROME

UniProt

A8JR14 - APLF_DROME

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Protein
Aprataxin and PNK-like factor
Gene
CG6171
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro.1 Publication

Catalytic activityi

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 14222PBZ-type 1
Add
BLAST
Zinc fingeri161 – 18222PBZ-type 2
Add
BLAST

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: UniProtKB
  2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
  3. endodeoxyribonuclease activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: GOC
  2. nucleic acid phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aprataxin and PNK-like factor (EC:4.2.99.18)
Alternative name(s):
Apurinic-apyrimidinic endonuclease APLF
Gene namesi
ORF Names:CG6171
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0026737. CG6171.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 255255Aprataxin and PNK-like factor
PRO_0000385300Add
BLAST

Proteomic databases

PaxDbiA8JR14.

Interactioni

Protein-protein interaction databases

BioGridi66935. 10 interactions.
MINTiMINT-986200.

Structurei

3D structure databases

ProteinModelPortaliA8JR14.
SMRiA8JR14. Positions 103-182.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi206 – 25550Asp-rich
Add
BLAST

Sequence similaritiesi

Belongs to the APLF family.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG85452.
GeneTreeiENSGT00390000010591.
InParanoidiQ9VF76.
OMAiSEDITHN.
OrthoDBiEOG73805W.
PhylomeDBiA8JR14.

Family and domain databases

InterProiIPR019406. Znf_C2H2_APLF-like.
[Graphical view]
PfamiPF10283. zf-CCHH. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform B (identifier: A8JR14-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSATDASTAD SGAKRKSSED ITHNCNANFG AENGLRKRVK SEEPVASIKD    50
ETNPEVPMKI KAEPVENADE PTSTTPAIKI KAEPADNGNS PAAAMVKTEP 100
TNSNAQDAAD ESTVSSSSIR TSCRFGIRCY RRNPAHRSAE AHPGDQDYRR 150
PNFPAPPLGT PACPFGNACY RRNPVHFQDY SHPADFNSAQ NIRNRLRQRR 200
AQRQNDDDSG TDEEDEPFGG DNDRDADYRP GADINEDEDD ELEFDSQPIS 250
GDDYD 255

Note: No experimental confirmation available.

Length:255
Mass (Da):28,006
Last modified:December 4, 2007 - v1
Checksum:i1CB1AC10524D57F3
GO
Isoform A (identifier: A8JR14-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:187
Mass (Da):20,158
Checksum:i7C196DF08C487378
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei186 – 1872FN → CK in isoform A.
VSP_038137
Alternative sequencei188 – 25568Missing in isoform A.
VSP_038138Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: ABW08680.1.
AE014297 Genomic DNA. Translation: AAF55184.1.
BT004895 mRNA. Translation: AAO47873.1.
RefSeqiNP_001097801.1. NM_001104331.2. [A8JR14-1]
NP_650455.1. NM_142198.3. [A8JR14-2]
UniGeneiDm.31310.

Genome annotation databases

EnsemblMetazoaiFBtr0112926; FBpp0111839; FBgn0026737. [A8JR14-1]
GeneIDi41872.
KEGGidme:Dmel_CG6171.
UCSCiCG6171-RA. d. melanogaster.
CG6171-RB. d. melanogaster. [A8JR14-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: ABW08680.1 .
AE014297 Genomic DNA. Translation: AAF55184.1 .
BT004895 mRNA. Translation: AAO47873.1 .
RefSeqi NP_001097801.1. NM_001104331.2. [A8JR14-1 ]
NP_650455.1. NM_142198.3. [A8JR14-2 ]
UniGenei Dm.31310.

3D structure databases

ProteinModelPortali A8JR14.
SMRi A8JR14. Positions 103-182.
ModBasei Search...

Protein-protein interaction databases

BioGridi 66935. 10 interactions.
MINTi MINT-986200.

Proteomic databases

PaxDbi A8JR14.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0112926 ; FBpp0111839 ; FBgn0026737 . [A8JR14-1 ]
GeneIDi 41872.
KEGGi dme:Dmel_CG6171.
UCSCi CG6171-RA. d. melanogaster.
CG6171-RB. d. melanogaster. [A8JR14-1 ]

Organism-specific databases

FlyBasei FBgn0026737. CG6171.

Phylogenomic databases

eggNOGi NOG85452.
GeneTreei ENSGT00390000010591.
InParanoidi Q9VF76.
OMAi SEDITHN.
OrthoDBi EOG73805W.
PhylomeDBi A8JR14.

Miscellaneous databases

GenomeRNAii 41872.
NextBioi 826032.
PROi A8JR14.

Family and domain databases

InterProi IPR019406. Znf_C2H2_APLF-like.
[Graphical view ]
Pfami PF10283. zf-CCHH. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiAPLF_DROME
AccessioniPrimary (citable) accession number: A8JR14
Secondary accession number(s): Q9VF76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: December 4, 2007
Last modified: July 9, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi