HPF1_NEMVE
ID HPF1_NEMVE Reviewed; 327 AA.
AC A7RS11;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Histone PARylation factor 1 {ECO:0000305};
GN Name=HPF1 {ECO:0000303|PubMed:17615350};
GN ORFNames=v1g201271 {ECO:0000303|PubMed:17615350};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6;
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
RN [2] {ECO:0007744|PDB:6TVH, ECO:0007744|PDB:6TX1}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=32028527; DOI=10.1038/s41586-020-2013-6;
RA Suskiewicz M.J., Zobel F., Ogden T.E.H., Fontana P., Ariza A., Yang J.C.,
RA Zhu K., Bracken L., Hawthorne W.J., Ahel D., Neuhaus D., Ahel I.;
RT "HPF1 completes the PARP active site for DNA damage-induced ADP-
RT ribosylation.";
RL Nature 579:598-602(2020).
CC -!- FUNCTION: Cofactor for serine ADP-ribosylation that confers serine
CC specificity on PARP. Switches the amino acid specificity of PARP from
CC aspartate or glutamate to serine residues. Acts by completing the
CC active site of PARP: forms a composite active site composed of residues
CC from HPF1 and PARP. {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9NWY4}.
CC Nucleus {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SIMILARITY: Belongs to the HPF1 family. {ECO:0000305}.
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DR EMBL; DS469533; EDO45721.1; -; Genomic_DNA.
DR RefSeq; XP_001637784.1; XM_001637734.1.
DR PDB; 6TVH; X-ray; 2.65 A; A/B=1-327.
DR PDB; 6TX1; X-ray; 2.09 A; A/B=1-327.
DR PDBsum; 6TVH; -.
DR PDBsum; 6TX1; -.
DR AlphaFoldDB; A7RS11; -.
DR SMR; A7RS11; -.
DR STRING; 45351.EDO45721; -.
DR EnsemblMetazoa; EDO45721; EDO45721; NEMVEDRAFT_v1g201271.
DR eggNOG; KOG3952; Eukaryota.
DR HOGENOM; CLU_053037_0_0_1; -.
DR InParanoid; A7RS11; -.
DR OMA; RPQFIAI; -.
DR OrthoDB; 1077112at2759; -.
DR PhylomeDB; A7RS11; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IBA:GO_Central.
DR InterPro; IPR019361; HPF1.
DR PANTHER; PTHR13386; PTHR13386; 1.
DR Pfam; PF10228; DUF2228; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Nucleus; Reference proteome.
FT CHAIN 1..327
FT /note="Histone PARylation factor 1"
FT /id="PRO_0000452423"
FT ACT_SITE 266
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:6TX1"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:6TX1"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:6TX1"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:6TX1"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6TX1"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6TVH"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6TX1"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6TX1"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6TVH"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 164..181
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:6TX1"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 244..265
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:6TX1"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:6TX1"
SQ SEQUENCE 327 AA; 37071 MW; BC6D0C508151BFC3 CRC64;
MAEVSSKRRK RTKTDIGCQS SAIKKIKEMF DAVMPEDFYD FWAFCEELNP KNPEDALMDT
MGLQLVGPYD VLTGKLDGLS ESSYHLHWRY YYDPPEFMTV IRGNEDQGFH IGYYRDEPQA
LPVFVASNKA KVSCEMSVIG ENLFSALNTC ITENLKKIKD KSQQSSLKKM QTSLITKAKE
LQYSLATTTP AIKARNKKVN SKTLHKAGIV VPVNAMDVGY RPLTVTDAEL KKMLKTITES
ENKSAKDKAS DELQELLTFV QFANDEGDYG MGLELGLDLF CFGSKQFHNT ILQLLPLAYQ
LLGREKYAKI IQEHLENRDR EKLSEAS
