HPF1_DROME
ID HPF1_DROME Reviewed; 449 AA.
AC Q9VNI3; Q8T050;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Histone PARylation factor 1-like {ECO:0000305};
GN ORFNames=CG1218;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=20088964; DOI=10.1111/j.1365-2443.2009.01369.x;
RA Isogai S., Kanno S., Ariyoshi M., Tochio H., Ito Y., Yasui A.,
RA Shirakawa M.;
RT "Solution structure of a zinc-finger domain that binds to poly-ADP-
RT ribose.";
RL Genes Cells 15:101-110(2010).
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/CG1218 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; AE014297; AAF51951.2; -; Genomic_DNA.
DR EMBL; AY069557; AAL39702.1; -; mRNA.
DR RefSeq; NP_649589.1; NM_141332.4.
DR AlphaFoldDB; Q9VNI3; -.
DR SMR; Q9VNI3; -.
DR BioGRID; 65923; 24.
DR IntAct; Q9VNI3; 9.
DR STRING; 7227.FBpp0078279; -.
DR iPTMnet; Q9VNI3; -.
DR PaxDb; Q9VNI3; -.
DR PRIDE; Q9VNI3; -.
DR DNASU; 40718; -.
DR EnsemblMetazoa; FBtr0078630; FBpp0078279; FBgn0037377.
DR GeneID; 40718; -.
DR KEGG; dme:Dmel_CG1218; -.
DR UCSC; CG1218-RA; d. melanogaster.
DR FlyBase; FBgn0037377; CG1218.
DR VEuPathDB; VectorBase:FBgn0037377; -.
DR eggNOG; KOG3952; Eukaryota.
DR GeneTree; ENSGT00390000014876; -.
DR HOGENOM; CLU_053037_0_1_1; -.
DR InParanoid; Q9VNI3; -.
DR OMA; RPQFIAI; -.
DR OrthoDB; 1077112at2759; -.
DR PhylomeDB; Q9VNI3; -.
DR BioGRID-ORCS; 40718; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40718; -.
DR PRO; PR:Q9VNI3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037377; Expressed in saliva-secreting gland and 44 other tissues.
DR Genevisible; Q9VNI3; DM.
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; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IDA:FlyBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR019406; APLF_PBZ.
DR InterPro; IPR019361; HPF1.
DR PANTHER; PTHR13386; PTHR13386; 1.
DR Pfam; PF10228; DUF2228; 1.
DR Pfam; PF10283; zf-CCHH; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..449
FT /note="Histone PARylation factor 1-like"
FT /id="PRO_0000342627"
FT ZN_FING 3..28
FT /note="CCHC-type"
FT /evidence="ECO:0000255"
FT REGION 18..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 384
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 449 AA; 51100 MW; 60C0B30E48548BD4 CRC64;
MPKEDCKYWD KCYQQNPAHL SKYNHPKKQQ EHEVDGAEGK KVAPKRSASS QSGEQKKEEQ
TEPVNKDKSN TSASSTEMVN KDTAKGSYEA ETEELHKEAM SNISGKNYME ILEKRIRLSV
QKEYDNLCES NEFIRHKFLV EMPPDFYEFW KFVGSLKIDP AKPKDAGLEH LDKVFQLQLV
GPFEFLAGKF HGAKLGEPGD YLRHWRFYYD PPEFQTIFVR RGTGIHYGYW RDVPQDKENL
LIARNDSAKG CQFQFVAGNA FDAFLYYLEH DFAATPFSCG QLAGTKKAVA KYLSDNSLEL
AQLDRLQRER NKRVVAKTFH RAGIVVPFDQ KTEVGYRPLA VSDSELKKML AMLERKDVDN
GAAKQAVLEK LQPVANAANI AVDESDFGSA LELGIDMFCS GHKELHMLAS SLLVPAYSML
SRPQFIAIAK AHMEQRSRED NLSIFDVLK
