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 15-JUN-2010, entry version 89. DE RecName: Full=Chromosomal protein D1; GN Name=D1; ORFNames=CG9745; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-33. RX MEDLINE=89255282; 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 RT chromosomal protein D1. A repeating motif in proteins which recognize RT 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 MEDLINE=20196006; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic 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 MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., 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 MASS RP SPECTROMETRY. RX PubMed=17372656; DOI=10.1039/b617545g; RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., RA Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; RT "An integrated chemical, mass spectrometric and computational strategy RT for (quantitative) phosphoproteomics: application to Drosophila RT melanogaster Kc167 cells."; RL Mol. Biosyst. 3:275-286(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-88; SER-89; RP SER-107; SER-109; SER-112; THR-115; SER-118; SER-133; SER-135; RP SER-149; SER-150; SER-161; SER-164; SER-170; SER-208; SER-246; RP SER-252; SER-253; SER-299; SER-307; SER-311; THR-321 AND SER-332, AND 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). CC -!- FUNCTION: This satellite DNA-associated protein is a double- CC stranded DNA binding protein specific for tracts of pure at DNA. CC It may play a role in organizing the higher order structure of CC euchromatin as well as heterochromatin. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: D1 may be the most abundant member of a small CC family of D1-like proteins. CC -!- SIMILARITY: Contains 11 A.T hook DNA-binding domains. 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; -. DR RefSeq; NP_731319.1; -. DR RefSeq; NP_731320.1; -. DR UniGene; Dm.5095; -. DR DIP; DIP-17744N; -. DR IntAct; P22058; 24. DR STRING; P22058; -. DR PRIDE; P22058; -. DR EnsemblMetazoa; FBtr0081987; FBpp0081467; FBgn0000412. DR EnsemblMetazoa; FBtr0081988; FBpp0081468; FBgn0000412. DR EnsemblMetazoa; FBtr0081989; FBpp0081469; FBgn0000412. DR GeneID; 41095; -. DR KEGG; dme:Dmel_CG9745; -. DR CTD; 41095; -. DR FlyBase; FBgn0000412; D1. DR InParanoid; P22058; -. DR OMA; NYNDSES; -. DR OrthoDB; EOG9S7JXB; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-010672-MONOMER; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-010673-MONOMER; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-010674-MONOMER; -. DR NextBio; 822145; -. DR GermOnline; CG9745; Drosophila melanogaster. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0003696; F:satellite DNA binding; IDA:FlyBase. DR InterPro; IPR020478; A.T_hook_like. DR InterPro; IPR017956; AT_hook_DNA-bd_motif. DR PRINTS; PR00929; ATHOOK. DR SMART; SM00384; AT_hook; 10. PE 1: Evidence at protein level; KW Acetylation; Chromosomal protein; Complete proteome; KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; KW Repeat. FT CHAIN 1 355 Chromosomal protein D1. FT /FTId=PRO_0000206715. FT DNA_BIND 7 14 A.T hook 1. FT DNA_BIND 34 41 A.T hook 2. FT DNA_BIND 60 67 A.T hook 3. FT DNA_BIND 94 101 A.T hook 4. FT DNA_BIND 122 129 A.T hook 5. FT DNA_BIND 155 162 A.T hook 6. FT DNA_BIND 174 181 A.T hook 7. FT DNA_BIND 196 203 A.T hook 8. FT DNA_BIND 219 226 A.T hook 9. FT DNA_BIND 262 269 A.T hook 10. FT DNA_BIND 281 288 A.T hook 11. FT MOD_RES 1 1 N-acetylmethionine (Probable). FT MOD_RES 30 30 Phosphoserine. FT MOD_RES 80 80 Phosphoserine. FT MOD_RES 88 88 Phosphoserine. FT MOD_RES 89 89 Phosphoserine. FT MOD_RES 107 107 Phosphoserine. FT MOD_RES 109 109 Phosphoserine. FT MOD_RES 112 112 Phosphoserine. FT MOD_RES 115 115 Phosphothreonine. FT MOD_RES 118 118 Phosphoserine. FT MOD_RES 133 133 Phosphoserine; by CK2 (Potential). FT MOD_RES 135 135 Phosphoserine; by CK2 (Potential). FT MOD_RES 149 149 Phosphoserine. FT MOD_RES 150 150 Phosphoserine. FT MOD_RES 161 161 Phosphoserine. FT MOD_RES 164 164 Phosphoserine. FT MOD_RES 170 170 Phosphoserine. FT MOD_RES 186 186 Phosphoserine; by CK2 (Potential). FT MOD_RES 208 208 Phosphoserine. FT MOD_RES 246 246 Phosphoserine. FT MOD_RES 252 252 Phosphoserine. FT MOD_RES 253 253 Phosphoserine. FT MOD_RES 299 299 Phosphoserine. FT MOD_RES 307 307 Phosphoserine. FT MOD_RES 311 311 Phosphoserine; by CK2 (Potential). FT MOD_RES 321 321 Phosphothreonine. FT MOD_RES 332 332 Phosphoserine; by CK2 (Potential). FT CONFLICT 291 291 D -> E (in Ref. 2; AAB01211). 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 //