APLF_BOVIN
ID APLF_BOVIN Reviewed; 485 AA.
AC A0JNH9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Aprataxin and PNK-like factor;
DE EC=3.1.1.- {ECO:0000250|UniProtKB:Q8IW19};
DE AltName: Full=Apurinic-apyrimidinic endonuclease APLF;
GN Name=APLF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Nuclease involved in single-strand and double-strand DNA
CC break repair. Recruited to sites of DNA damage through interaction with
CC poly(ADP-ribose), a polymeric post-translational modification
CC synthesized transiently at sites of chromosomal damage to accelerate
CC DNA strand break repair reactions. Displays apurinic-apyrimidinic (AP)
CC endonuclease and 3'-5' exonuclease activities in vitro. Also able to
CC introduce nicks at hydroxyuracil and other types of pyrimidine base
CC damage. Together with PARP3, promotes the retention of the LIG4-XRCC4
CC complex on chromatin and accelerate DNA ligation during non-homologous
CC end-joining (NHEJ). {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- SUBUNIT: Interacts with LIG4. Interacts with PARP1. Interacts with
CC XRCC4. Interacts (via KBM motif) with XRCC5 and XRCC6; promoting
CC recruitment to DNA damage sites. Interacts with XRCC1.
CC {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IW19}.
CC Chromosome {ECO:0000250|UniProtKB:Q8IW19}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8IW19}. Note=Localizes to DNA damage sites.
CC Accumulates at single-strand breaks and double-strand breaks via the
CC PBZ-type zinc fingers. {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- DOMAIN: The PBZ-type zinc fingers (also named CYR) mediate non-covalent
CC poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the
CC presence of zinc and promotes its recruitment to DNA damage sites.
CC {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- DOMAIN: The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80
CC and XRCC6/Ku70 and recruitment to DNA damage sites.
CC {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- DOMAIN: The FHA-like domain mediates interaction with XRCC1 and XRCC4.
CC {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- PTM: Poly-ADP-ribosylated. In addition to binding non covalently
CC poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is also
CC covalently poly-ADP-ribosylated by PARP1.
CC {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- PTM: Phosphorylated in an ATM-dependent manner upon double-strand DNA
CC break. {ECO:0000250|UniProtKB:Q8IW19}.
CC -!- SIMILARITY: Belongs to the APLF family. {ECO:0000305}.
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DR EMBL; BC126691; AAI26692.1; -; mRNA.
DR RefSeq; NP_001071342.1; NM_001077874.1.
DR AlphaFoldDB; A0JNH9; -.
DR SMR; A0JNH9; -.
DR STRING; 9913.ENSBTAP00000055056; -.
DR Ensembl; ENSBTAT00000044615; ENSBTAP00000042099; ENSBTAG00000018401.
DR GeneID; 507989; -.
DR KEGG; bta:507989; -.
DR CTD; 200558; -.
DR VEuPathDB; HostDB:ENSBTAG00000018401; -.
DR VGNC; VGNC:59203; APLF.
DR eggNOG; ENOG502R7QZ; Eukaryota.
DR GeneTree; ENSGT00390000010591; -.
DR InParanoid; A0JNH9; -.
DR OrthoDB; 1606181at2759; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000018401; Expressed in oocyte and 105 other tissues.
DR ExpressionAtlas; A0JNH9; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; ISS:UniProtKB.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR InterPro; IPR039253; APLF.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR21315; PTHR21315; 1.
DR Pfam; PF10283; zf-CCHH; 2.
DR SUPFAM; SSF49879; SSF49879; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Chromosome; Coiled coil; Cytoplasm; DNA damage;
KW DNA repair; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="Aprataxin and PNK-like factor"
FT /id="PRO_0000287355"
FT DOMAIN 1..84
FT /note="FHA-like"
FT ZN_FING 351..372
FT /note="PBZ-type 1"
FT ZN_FING 393..414
FT /note="PBZ-type 2"
FT REGION 103..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..390
FT /note="Flexible linker"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT REGION 420..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..166
FT /note="KBM"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT COMPBIAS 129..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..466
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT BINDING 355
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT BINDING 360
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT BINDING 361
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT BINDING 397
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT BINDING 402
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT BINDING 403
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT MOD_RES 92
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D842"
SQ SEQUENCE 485 AA; 54326 MW; D88D75D4D7C9D456 CRC64;
MSGGFELQPQ DGGPRVALAP GETVIGRGPL LGLHRNPCYY QSSEKSQLLP LKTNIWCWLN
PGDHFSLLVD KYIFCVLSTH SEMEMECTLR NSQMLDEDDI LNEIPKSSSA DLPDKTPSAP
RRERSTETAK PQAAANNMSF IGESRDLSKQ QPNPSERKRI LPAWMLTENS SDQNLSVISG
GNNVTWESEK ERVCKDKTQV NITQPGKKRL ISSGSSESTS AKQDTGKKCK NDDQEESIIS
SKEMPQSFSA AMLHNTEIDN TKTNPQRSKV PVEALGKVSE HKIITKGSSN EDSTARSCSE
SYSSTQSKSF CDKPQKSHPE PSSNPPSPEC VQAKATDSVP NGSEENKVQR TSCMYGANCY
RKNPVHFQHF SHPGDSDYGG VNITCQDEAD DRPECPYGAS CYRKNPQHKI EYRHSTFPVR
SISDEDDNVG QPNEYNLNDS FIDDEEEEYE PTDEDSDWEP EKEDLEKEDM EGLLKEAKKF
MKRKK
