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 24-JAN-2024, entry version 161.
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; DOI=10.1016/s0021-9258(18)83195-7;
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.
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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 AlphaFoldDB; P22058; -.
DR BioGRID; 66262; 26.
DR DIP; DIP-17744N; -.
DR IntAct; P22058; 13.
DR STRING; 7227.FBpp0081467; -.
DR iPTMnet; P22058; -.
DR PaxDb; 7227-FBpp0081467; -.
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 AGR; FB:FBgn0000412; -.
DR CTD; 41095; -.
DR FlyBase; FBgn0000412; D1.
DR VEuPathDB; VectorBase:FBgn0000412; -.
DR eggNOG; ENOG502TC9F; Eukaryota.
DR HOGENOM; CLU_055706_0_0_1; -.
DR InParanoid; P22058; -.
DR OMA; ECISDEP; -.
DR OrthoDB; 3597171at2759; -.
DR PhylomeDB; P22058; -.
DR SignaLink; 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 imaginal disc and 13 other cell types or 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
//
