ID CPD1_DROME Reviewed; 355 AA. AC P22058; Q24215; Q8SX69; Q9VHH3; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 02-JUN-2021, entry version 152. DE RecName: Full=Chromosomal protein D1; GN Name=D1; ORFNames=CG9745; 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 [MRNA], ACETYLATION AT MET-1, AND PROTEIN SEQUENCE OF RP 1-33. RX PubMed=2542275; RA Ashley C.T., Pendleton C.G., Jennings W.W., Saxena A., Glover C.V.C.; RT "Isolation and sequencing of cDNA clones encoding Drosophila chromosomal RT protein D1. A repeating motif in proteins which recognize at DNA."; RL J. Biol. Chem. 264:8394-8401(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kleven D.T., Murdock D.G., Crawford M.J., Glover C.V.C.; RT "Structure of the gene encoding Drosophila chromosomal protein D1."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo, and Testis; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-246, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17372656; DOI=10.1039/b617545g; RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., RA Eng J.K., Aebersold R., Tao W.A.; RT "An integrated chemical, mass spectrometric and computational strategy for RT (quantitative) phosphoproteomics: application to Drosophila melanogaster RT Kc167 cells."; RL Mol. Biosyst. 3:275-286(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-88; SER-89; SER-107; RP SER-109; SER-112; THR-115; SER-118; SER-133; SER-135; SER-149; SER-150; RP SER-161; SER-164; SER-170; SER-208; SER-246; SER-252; SER-253; SER-299; RP SER-307; SER-311; THR-321 AND SER-332, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: This satellite DNA-associated protein is a double-stranded CC DNA binding protein specific for tracts of pure at DNA. It may play a CC role in organizing the higher-order structure of euchromatin as well as CC heterochromatin. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- MISCELLANEOUS: D1 may be the most abundant member of a small family of CC D1-like proteins. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04725; AAA28440.1; -; mRNA. DR EMBL; U56393; AAB01211.1; -; Genomic_DNA. DR EMBL; AE014297; AAF54341.1; -; Genomic_DNA. DR EMBL; AY094819; AAM11172.1; -; mRNA. DR EMBL; BT001362; AAN71117.1; -; mRNA. DR EMBL; BT001636; AAN71391.1; -; mRNA. DR PIR; A33821; A33821. DR RefSeq; NP_524286.1; NM_079562.3. DR RefSeq; NP_731319.1; NM_169261.3. DR RefSeq; NP_731320.1; NM_169262.2. DR BioGRID; 66262; 26. DR DIP; DIP-17744N; -. DR IntAct; P22058; 13. DR STRING; 7227.FBpp0081467; -. DR iPTMnet; P22058; -. DR PaxDb; P22058; -. DR PRIDE; P22058; -. DR DNASU; 41095; -. DR EnsemblMetazoa; FBtr0081987; FBpp0081467; FBgn0000412. DR EnsemblMetazoa; FBtr0081988; FBpp0081468; FBgn0000412. DR EnsemblMetazoa; FBtr0301524; FBpp0290739; FBgn0000412. DR GeneID; 41095; -. DR KEGG; dme:Dmel_CG9745; -. DR CTD; 41095; -. DR FlyBase; FBgn0000412; D1. DR eggNOG; ENOG502TC9F; Eukaryota. DR HOGENOM; CLU_055706_0_0_1; -. DR InParanoid; P22058; -. DR OMA; GEPQVPK; -. DR OrthoDB; 1351942at2759; -. DR PhylomeDB; P22058; -. DR BioGRID-ORCS; 41095; 0 hits in 1 CRISPR screen. DR ChiTaRS; D1; fly. DR GenomeRNAi; 41095; -. DR PRO; PR:P22058; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0000412; Expressed in eye disc (Drosophila) and 43 other tissues. DR ExpressionAtlas; P22058; baseline and differential. DR Genevisible; P22058; DM. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase. DR GO; GO:0000786; C:nucleosome; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase. DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:FlyBase. DR GO; GO:0003696; F:satellite DNA binding; IDA:FlyBase. DR InterPro; IPR017956; AT_hook_DNA-bd_motif. DR Pfam; PF02178; AT_hook; 10. DR PRINTS; PR00929; ATHOOK. DR SMART; SM00384; AT_hook; 10. PE 1: Evidence at protein level; KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..355 FT /note="Chromosomal protein D1" FT /id="PRO_0000206715" FT DNA_BIND 7..14 FT /note="A.T hook 1" FT DNA_BIND 34..41 FT /note="A.T hook 2" FT DNA_BIND 60..67 FT /note="A.T hook 3" FT DNA_BIND 94..101 FT /note="A.T hook 4" FT DNA_BIND 122..129 FT /note="A.T hook 5" FT DNA_BIND 155..162 FT /note="A.T hook 6" FT DNA_BIND 174..181 FT /note="A.T hook 7" FT DNA_BIND 196..203 FT /note="A.T hook 8" FT DNA_BIND 219..226 FT /note="A.T hook 9" FT DNA_BIND 262..269 FT /note="A.T hook 10" FT DNA_BIND 281..288 FT /note="A.T hook 11" FT REGION 1..355 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 65..79 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..96 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 178..198 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..322 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..355 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000305|PubMed:2542275" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17372656" FT MOD_RES 80 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 88 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 107 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 109 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 112 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 115 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 133 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000255" FT MOD_RES 135 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000255" FT MOD_RES 149 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 150 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 186 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000255" FT MOD_RES 208 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17372656, FT ECO:0000269|PubMed:18327897" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 307 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 311 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000255" FT MOD_RES 321 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 332 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000255" FT CONFLICT 291 FT /note="D -> E (in Ref. 2; AAB01211)" FT /evidence="ECO:0000305" SQ SEQUENCE 355 AA; 37000 MW; 516744AF0D048969 CRC64; MEEVAVKKRG RPSKASVGGK SSTAAVAAIS PGIKKRGRPA KNKGSSGGGG QRGRPPKASK IQNDEDPEDE GEEDGDGDGS GAELANNSSP SPTKGRGRPK SSGGAGSGSG DSVKTPGSAK KRKAGRPKKH QPSDSENEDD QDEDDDGNSS IEERRPVGRP SAGSVNLNIS RTGRGLGRPK KRAVESNGDG EPQVPKKRGR PPQNKSGSGG STGYVPTGRP RGRPKANAAP VEKHEDNDDD QDDENSGEEE HSSPEKTVVA PKKRGRPSLA AGKVSKEETT KPRSRPAKNI DDDADDADSA DQGQHNSKKE SNDEDRAVDG TPTKGDGLKW NSDGENDAND GYVSDNYNDS ESVAA //