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Database: UniProt
Entry: Q49BM3_DROSI
LinkDB: Q49BM3_DROSI
Original site: Q49BM3_DROSI 
ID   Q49BM3_DROSI            Unreviewed;       206 AA.
AC   Q49BM3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   SubName: Full=GD22433 {ECO:0000313|EMBL:EDX04191.1};
DE   SubName: Full=Heterochromatin protein 1 {ECO:0000313|EMBL:AAY34032.1, ECO:0000313|EMBL:ACI96753.1};
GN   Name=HP1 {ECO:0000313|EMBL:ACI96753.1};
GN   Synonyms=Dsim\GD22433 {ECO:0000313|EMBL:EDX04191.1}, Dsim\HP1A
GN   {ECO:0000313|EMBL:KMY88977.1};
GN   ORFNames=Dsim_GD22433 {ECO:0000313|EMBL:EDX04191.1}, Dsimw501_GD22433
GN   {ECO:0000313|EMBL:KMY88977.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:AAY34032.1};
RN   [1] {ECO:0000313|EMBL:AAY34032.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2 {ECO:0000313|EMBL:AAY34032.1};
RX   PubMed=16103923; DOI=10.1371/journal.pgen.0010009;
RA   Vermaak D., Henikoff S., Malik H.S.;
RT   "Positive Selection Drives the Evolution of rhino, a Member of the
RT   Heterochromatin Protein 1 Family in Drosophila.";
RL   PLoS Genet. 1:E9-E9(2005).
RN   [2] {ECO:0000313|EMBL:EDX04191.1, ECO:0000313|Proteomes:UP000000304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDX04191.1}, and mosaic
RC   {ECO:0000313|Proteomes:UP000000304};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [3] {ECO:0000313|EMBL:EDX04191.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDX04191.1}, and W501
RC   {ECO:0000313|EMBL:KMY88977.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ACI96753.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C1674 {ECO:0000313|EMBL:ACI96759.1}, Md106
RC   {ECO:0000313|EMBL:ACI96756.1}, and Sim {ECO:0000313|EMBL:ACI96753.1};
RX   PubMed=18984573; DOI=10.1534/genetics.108.093807;
RA   Anderson J.A., Gilliland W.D., Langley C.H.;
RT   "Molecular population genetics and evolution of Drosophila meiosis genes.";
RL   Genetics 181:177-185(2009).
RN   [5] {ECO:0000313|EMBL:KMY88977.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W501 {ECO:0000313|EMBL:KMY88977.1};
RX   PubMed=22936249; DOI=10.1101/gr.141689.112;
RA   Hu T.T., Eisen M.B., Thornton K.R., Andolfatto P.;
RT   "A second-generation assembly of the Drosophila simulans genome provides
RT   new insights into patterns of lineage-specific divergence.";
RL   Genome Res. 23:89-98(2013).
RN   [6] {ECO:0000313|EMBL:KMY88977.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W501 {ECO:0000313|EMBL:KMY88977.1};
RA   Hu T., Eisen M.B., Thornton K.R., Andolfatto P.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY944311; AAY34032.1; -; Genomic_DNA.
DR   EMBL; FJ218605; ACI96753.1; -; Genomic_DNA.
DR   EMBL; FJ218608; ACI96756.1; -; Genomic_DNA.
DR   EMBL; FJ218611; ACI96759.1; -; Genomic_DNA.
DR   EMBL; CM000361; EDX04191.1; -; Genomic_DNA.
DR   EMBL; CM002910; KMY88977.1; -; Genomic_DNA.
DR   RefSeq; XP_016024109.1; XM_016178686.1.
DR   AlphaFoldDB; Q49BM3; -.
DR   EnsemblMetazoa; FBtr0222343; FBpp0220835; FBgn0264923.
DR   GeneID; 6731455; -.
DR   KEGG; dsi:Dsimw501_GD22433; -.
DR   HOGENOM; CLU_045874_1_1_1; -.
DR   OMA; KWQGFPL; -.
DR   OrthoDB; 75895at2759; -.
DR   Proteomes; UP000000304; Chromosome 2l.
DR   Proteomes; UP000035880; Chromosome 2L.
DR   Bgee; FBgn0264923; Expressed in embryo and 3 other cell types or tissues.
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:EnsemblMetazoa.
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: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 formation; IEA:EnsemblMetazoa.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:EnsemblMetazoa.
DR   GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IEA:EnsemblMetazoa.
DR   GO; GO:1905646; P:positive regulation of FACT complex assembly; IEA:EnsemblMetazoa.
DR   GO; GO:1905632; P:protein localization to euchromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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   CDD; cd18653; CD_HP1a_insect; 1.
DR   CDD; cd18658; CSD_HP1a_insect; 1.
DR   Gene3D; 2.40.50.40; -; 2.
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   PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR   PANTHER; PTHR22812:SF157; CHROMOBOX PROTEIN HOMOLOG 1; 1.
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; Chromo domain-like; 2.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000304}.
FT   DOMAIN          24..82
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          147..205
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  23154 MW;  84C5190B47D3547F CRC64;
     MGKKIDNPES SAKASDAEEE EEEYAVEKII DRRVRKGKVE YYLKWKGYPE TENTWEPENN
     LDCQDLIQQY EASRKDEEKS AASKKDRPSS SAKTKETPGR SSTSASTASK RKSEEPTAPA
     ANKSKRTTDA EQDTIPVSGS TGFDRGLEAE KILGASDNNG RLTFLIQFKG VDQAEMVPSS
     VANEKIPRMV IHFYEERLSW YSDNED
//
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