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A0JNH9 (APLF_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aprataxin and PNK-like factor
EC=4.2.99.18
Alternative name(s):
Apurinic-apyrimidinic endonuclease APLF
Gene names
Name:APLF
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Nuclease involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage By similarity.

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.

Subunit structure

Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5 By similarity.

Subcellular location

Nucleus. Cytoplasm › cytosol. Note: Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers By similarity.

Domain

The PBZ-type zinc fingers (also named CYR) mediate non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and promotes its recruitment to DNA damage sites By similarity.

The FHA-like domain mediates interaction with XRCC1 and XRCC4 By similarity.

Post-translational modification

Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is also covalently poly-ADP-ribosylated by PARP1 By similarity.

Phosphorylated in an ATM-dependent manner upon double-strand DNA break By similarity.

Sequence similarities

Belongs to the APLF family.

Contains 1 FHA-like domain.

Contains 2 PBZ-type zinc fingers.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Aprataxin and PNK-like factor
PRO_0000287355

Regions

Domain1 – 8484FHA-like
Zinc finger351 – 37222PBZ-type 1
Zinc finger393 – 41422PBZ-type 2
Region380 – 39011Flexible linker By similarity

Sites

Binding site3501Poly-ADP-ribose By similarity
Binding site3551Poly-ADP-ribose By similarity
Binding site3601Poly-ADP-ribose By similarity
Binding site3611Poly-ADP-ribose By similarity
Binding site3971Poly-ADP-ribose By similarity
Binding site4021Poly-ADP-ribose By similarity
Binding site4031Poly-ADP-ribose By similarity

Amino acid modifications

Modified residue921Phosphoserine; by ATM By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JNH9 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: D88D75D4D7C9D456

FASTA48554,326
        10         20         30         40         50         60 
MSGGFELQPQ DGGPRVALAP GETVIGRGPL LGLHRNPCYY QSSEKSQLLP LKTNIWCWLN 

        70         80         90        100        110        120 
PGDHFSLLVD KYIFCVLSTH SEMEMECTLR NSQMLDEDDI LNEIPKSSSA DLPDKTPSAP 

       130        140        150        160        170        180 
RRERSTETAK PQAAANNMSF IGESRDLSKQ QPNPSERKRI LPAWMLTENS SDQNLSVISG 

       190        200        210        220        230        240 
GNNVTWESEK ERVCKDKTQV NITQPGKKRL ISSGSSESTS AKQDTGKKCK NDDQEESIIS 

       250        260        270        280        290        300 
SKEMPQSFSA AMLHNTEIDN TKTNPQRSKV PVEALGKVSE HKIITKGSSN EDSTARSCSE 

       310        320        330        340        350        360 
SYSSTQSKSF CDKPQKSHPE PSSNPPSPEC VQAKATDSVP NGSEENKVQR TSCMYGANCY 

       370        380        390        400        410        420 
RKNPVHFQHF SHPGDSDYGG VNITCQDEAD DRPECPYGAS CYRKNPQHKI EYRHSTFPVR 

       430        440        450        460        470        480 
SISDEDDNVG QPNEYNLNDS FIDDEEEEYE PTDEDSDWEP EKEDLEKEDM EGLLKEAKKF 


MKRKK

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC126691 mRNA. Translation: AAI26692.1.
IPIIPI00695070.
RefSeqNP_001071342.1. NM_001077874.1.
UniGeneBt.63859.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000042099.

Proteomic databases

PRIDEA0JNH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000044615; ENSBTAP00000042099; ENSBTAG00000018401.
GeneID507989.
KEGGbta:507989.

Organism-specific databases

CTD200558.

Phylogenomic databases

eggNOGNOG85452.
GeneTreeENSGT00390000010591.
HOGENOMHOG000033995.
HOVERGENHBG095728.
InParanoidA0JNH9.
KOK13295.
OrthoDBEOG4Q8501.

Gene expression databases

ArrayExpressA0JNH9.

Family and domain databases

InterProIPR008984. SMAD_FHA_domain.
IPR019406. Znf_C2H2_APLF-like.
[Graphical view]
PfamPF10283. zf-CCHH. 2 hits.
[Graphical view]
SUPFAMSSF49879. SMAD_FHA. 1 hit.
ProtoNetSearch...

Other

NextBio20868301.

Entry information

Entry nameAPLF_BOVIN
AccessionPrimary (citable) accession number: A0JNH9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: December 12, 2006
Last modified: April 3, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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