HPF1_BOVIN
ID HPF1_BOVIN Reviewed; 346 AA.
AC A2VDY4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Histone PARylation factor 1 {ECO:0000305};
GN Name=HPF1 {ECO:0000250|UniProtKB:Q9NWY4};
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=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cofactor for serine ADP-ribosylation that confers serine
CC specificity on PARP1 and PARP2 and plays a key role in DNA damage
CC response. Initiates the repair of double-strand DNA breaks: recruited
CC to DNA damage sites by PARP1 and PARP2 and switches the amino acid
CC specificity of PARP1 and PARP2 from aspartate or glutamate to serine
CC residues, licensing serine ADP-ribosylation of target proteins. Serine
CC ADP-ribosylation of target proteins, such as histones, promotes
CC decompaction of chromatin and the recruitment of repair factors leading
CC to the reparation of DNA strand breaks. Serine ADP-ribosylation of
CC proteins constitutes the primary form of ADP-ribosylation of proteins
CC in response to DNA damage. HPF1 acts by completing the active site of
CC PARP1 and PARP2: forms a composite active site composed of residues
CC from HPF1 and PARP1 or PARP2. HPF1 also promotes tyrosine ADP-
CC ribosylation, probably by conferring tyrosine specificity on PARP1.
CC {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SUBUNIT: Interacts with PARP1 (via the PARP catalytic domain).
CC Interacts with PARP2 (via the PARP catalytic domain). Interacts with
CC core nucleosomes in a PARP1- and PARP2-dependent manner.
CC {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9NWY4}.
CC Nucleus {ECO:0000250|UniProtKB:Q9NWY4}. Note=Localizes to DNA damage
CC sites; chromatin localization is dependent on PARP1 and PARP2.
CC {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SIMILARITY: Belongs to the HPF1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC133472; AAI33473.1; -; mRNA.
DR RefSeq; NP_001075062.1; NM_001081593.1.
DR AlphaFoldDB; A2VDY4; -.
DR SMR; A2VDY4; -.
DR STRING; 9913.ENSBTAP00000026815; -.
DR PaxDb; A2VDY4; -.
DR PRIDE; A2VDY4; -.
DR Ensembl; ENSBTAT00000026815; ENSBTAP00000026815; ENSBTAG00000020132.
DR GeneID; 525698; -.
DR KEGG; bta:525698; -.
DR CTD; 54969; -.
DR VEuPathDB; HostDB:ENSBTAG00000020132; -.
DR VGNC; VGNC:56972; HPF1.
DR eggNOG; KOG3952; Eukaryota.
DR GeneTree; ENSGT00390000014876; -.
DR HOGENOM; CLU_053037_0_0_1; -.
DR InParanoid; A2VDY4; -.
DR OMA; RPQFIAI; -.
DR OrthoDB; 1077112at2759; -.
DR TreeFam; TF317026; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000020132; Expressed in oocyte and 107 other tissues.
DR ExpressionAtlas; A2VDY4; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0072572; F:poly-ADP-D-ribose binding; IBA:GO_Central.
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:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0031056; P:regulation of histone modification; ISS:UniProtKB.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISS:UniProtKB.
DR InterPro; IPR019361; HPF1.
DR PANTHER; PTHR13386; PTHR13386; 1.
DR Pfam; PF10228; DUF2228; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ADP-ribosylation; Chromosome; DNA damage; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Histone PARylation factor 1"
FT /id="PRO_0000294445"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..346
FT /note="Interaction with PARP1"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT COMPBIAS 11..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 284
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CFE2"
FT MOD_RES 97
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 238
FT /note="ADP-ribosyltyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
SQ SEQUENCE 346 AA; 39091 MW; 7D48F57A03BEC8D8 CRC64;
MVGGGAKRRL RGEGPQCEKP VDMKKSKSCE ADVPGDLRKE VESHYRLPLP EDFYHFWRFC
EGLDPEQPAD SLSASLGLRL VGPYDILAGK HKIKKKSASL NFNLHWRFYY DPPEFQTIII
GDSKTQFHMG YFRDSPDELP VFVGTNEAKK NCIIVQSGDN VFAAVKLFLM KKLKEVTDKK
KSSLLKTIDE KLTEAARELG FSLEQRTVRM KQRDKKVVTK TFHGAGLVVP VDKNDVGYRE
LPETDASLRR ICGTIVEAPS DADRLQAFAP VQEMMTYVQF ANDECDYGMG LELGLDLFCH
GSHYFHKVAG QLLPLAYNLL KRNLFAEIIE AHLANRSQDD VDQLAA
