HP1_DROVI
ID HP1_DROVI Reviewed; 213 AA.
AC P29227; B4LUB7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Heterochromatin protein 1;
DE Short=HP1;
GN Name=HP1A; Synonyms=HP1, Su(var)205; ORFNames=GJ17281;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1461737; DOI=10.1093/nar/20.22.6067;
RA Clark R.F., Elgin S.C.R.;
RT "Heterochromatin protein 1, a known suppressor of position-effect
RT variegation, is highly conserved in Drosophila.";
RL Nucleic Acids Res. 20:6067-6074(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Structural component of heterochromatin, involved in gene
CC repression and the modification of position-effect-variegation.
CC Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to
CC epigenetic repression (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; M88753; AAB00733.1; -; Genomic_DNA.
DR EMBL; CH940649; EDW64103.1; -; Genomic_DNA.
DR PIR; S35522; S35522.
DR RefSeq; XP_002051948.1; XM_002051912.2.
DR AlphaFoldDB; P29227; -.
DR SMR; P29227; -.
DR STRING; 7244.FBpp0231698; -.
DR EnsemblMetazoa; FBtr0233206; FBpp0231698; FBgn0013097.
DR GeneID; 6627672; -.
DR KEGG; dvi:6627672; -.
DR eggNOG; KOG1911; Eukaryota.
DR HOGENOM; CLU_045874_1_1_1; -.
DR InParanoid; P29227; -.
DR OMA; RLTWHTN; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; P29227; -.
DR ChiTaRS; Su(var)205; fly.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblMetazoa.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:EnsemblMetazoa.
DR GO; GO:0000791; C:euchromatin; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblMetazoa.
DR GO; GO:0005701; C:polytene chromosome chromocenter; IEA:EnsemblMetazoa.
DR GO; GO:0005705; C:polytene chromosome interband; IEA:EnsemblMetazoa.
DR GO; GO:0005703; C:polytene chromosome puff; IEA:EnsemblMetazoa.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:EnsemblMetazoa.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblMetazoa.
DR GO; GO:0000182; F:rDNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0003723; F:RNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IEA:EnsemblMetazoa.
DR GO; GO:0003696; F:satellite DNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0031507; P:heterochromatin assembly; IEA:EnsemblMetazoa.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:EnsemblMetazoa.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:EnsemblMetazoa.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IEA:EnsemblMetazoa.
DR GO; GO:1905646; P:positive regulation of FACT complex assembly; IEA:EnsemblMetazoa.
DR GO; GO:1900111; P:positive regulation of histone H3-K9 dimethylation; IEA:EnsemblMetazoa.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IEA:EnsemblMetazoa.
DR GO; GO:1905632; P:protein localization to euchromatin; IEA:EnsemblMetazoa.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; IEA:EnsemblMetazoa.
DR GO; GO:0000723; P:telomere maintenance; IEA:EnsemblMetazoa.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF01393; Chromo_shadow; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
PE 3: Inferred from homology;
KW Chromatin regulator; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..213
FT /note="Heterochromatin protein 1"
FT /id="PRO_0000080198"
FT DOMAIN 24..82
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 154..212
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 213 AA; 23452 MW; 260888892FCFB875 CRC64;
MGKKTDNPET NNASSGAEEE EEEYAVEKIL DRRVRKGKVE YYLKWKGYAE TENTWEPEGN
LDCQDLIQQY ELSRKDEANA AASSSSSSSK KERPGSSTKV KETGRTSTTA SNSSGSKRKS
EEPAGPAGSK SKRVESEDTG DIVPAGGTGF DRGLEAEKIL GASDNNGRLT FLIQFKGVDQ
AEMVPSTVAN VKIPQMVIRF YEERLSWYSD NED
