HPF1_DANRE
ID HPF1_DANRE Reviewed; 348 AA.
AC Q7SXS8; A9JT12; Q5XJK8;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Histone PARylation factor 1 {ECO:0000250|UniProtKB:Q9NWY4};
GN Name=hpf1 {ECO:0000303|PubMed:29549427};
GN ORFNames=zgc:101819 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Olfactory epithelium, and Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29549427; DOI=10.1007/s00427-018-0608-9;
RA Zhang Z., Sun H., Chen Y., Cao T., Songyang Z., Huang J., Huang Y.;
RT "Analysis of hpf1 expression and function in early embryonic development of
RT zebrafish.";
RL Dev. Genes Evol. 228:141-147(2018).
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 -!- TISSUE SPECIFICITY: In adult, mainly expressed in gonads.
CC {ECO:0000269|PubMed:29549427}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally: detected as early as 0 hour
CC post-fertilization (hpf), before zygotic expression transcripts starts.
CC {ECO:0000269|PubMed:29549427}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC malformation anbd delayed hatching. {ECO:0000269|PubMed:29549427}.
CC -!- SIMILARITY: Belongs to the HPF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55260.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI55159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC055260; AAH55260.1; ALT_INIT; mRNA.
DR EMBL; BC083292; AAH83292.1; -; mRNA.
DR EMBL; BC155158; AAI55159.1; ALT_INIT; mRNA.
DR RefSeq; NP_001005769.1; NM_001005769.1.
DR AlphaFoldDB; Q7SXS8; -.
DR SMR; Q7SXS8; -.
DR STRING; 7955.ENSDARP00000074168; -.
DR PaxDb; Q7SXS8; -.
DR GeneID; 100002184; -.
DR KEGG; dre:100002184; -.
DR CTD; 54969; -.
DR ZFIN; ZDB-GENE-030131-740; hpf1.
DR eggNOG; KOG3952; Eukaryota.
DR InParanoid; Q7SXS8; -.
DR OrthoDB; 1077112at2759; -.
DR PhylomeDB; Q7SXS8; -.
DR PRO; PR:Q7SXS8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 Chromosome; Coiled coil; DNA damage; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..348
FT /note="Histone PARylation factor 1"
FT /id="PRO_0000342625"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..200
FT /evidence="ECO:0000255"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT CONFLICT 9
FT /note="P -> S (in Ref. 1; AAH83292)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="K -> E (in Ref. 1; AAH55260/AAH83292)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="K -> R (in Ref. 1; AAI55159)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="L -> P (in Ref. 1; AAH83292)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="N -> K (in Ref. 1; AAH83292/AAI55159)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="N -> S (in Ref. 1; AAI55159)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="Q -> H (in Ref. 1; AAI55159)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> T (in Ref. 1; AAH83292)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="L -> S (in Ref. 1; AAH83292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 39935 MW; 4440B7675DF7D3E9 CRC64;
MAGRGKRKPR SLPQTETPNG EVKKAKEGLK DDKTSVGEEM REEVERLYKL RMPDDFFQFW
DFCEGLNADC PQDALKNTLG LQLVGPFDIL SKKHKNSSSQ PNFHLHWRYF YDPPEFQTII
QGNADTQHHM GYFRDLPDAL PVFIGENEAK KGYTITQLGD NIFAAVLLFL QKKKKEKRQQ
KDDAALNRLE EDLKREAERL GLPLEQKTKS MKQRERKVVT KTFHGAGIVV PVDKNDVGYR
ELPESDASLK KICKAIAEAK DDEERMKAFA PIQEMITFVQ FANDECDYGM GYELGIDLFC
YGSHYFFKVV RQLLPMAYNL LKRGLFGEIL EAHLASRSQD NLDQLAAV
