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   16-JAN-2019, entry version 140.
DE   RecName: Full=Chromosomal protein D1;
GN   Name=D1; ORFNames=CG9745;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT MET-1, AND PROTEIN SEQUENCE
RP   OF 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
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   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.
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.,
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   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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
RP   IDENTIFICATION BY MASS 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   IDENTIFICATION BY 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. Chromosome.
CC   -!- MISCELLANEOUS: D1 may be the most abundant member of a small
CC       family of 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   UniGene; Dm.5095; -.
DR   BioGrid; 66262; 21.
DR   DIP; DIP-17744N; -.
DR   IntAct; P22058; 10.
DR   STRING; 7227.FBpp0081467; -.
DR   iPTMnet; P22058; -.
DR   PaxDb; P22058; -.
DR   PRIDE; P22058; -.
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; ENOG410KB6G; Eukaryota.
DR   eggNOG; ENOG4110NKF; LUCA.
DR   InParanoid; P22058; -.
DR   OMA; YNDSESV; -.
DR   OrthoDB; 1351942at2759; -.
DR   PhylomeDB; P22058; -.
DR   GenomeRNAi; 41095; -.
DR   PRO; PR:P22058; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0000412; Expressed in 36 organ(s), highest expression level in eye disc (Drosophila).
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:AT 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; Complete proteome; Direct protein sequencing;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; 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.
FT                                {ECO:0000305|PubMed:2542275}.
FT   MOD_RES      30     30       Phosphoserine.
FT                                {ECO:0000269|PubMed:17372656}.
FT   MOD_RES      80     80       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      88     88       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      89     89       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     107    107       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     109    109       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     112    112       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     115    115       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     118    118       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     133    133       Phosphoserine; by CK2. {ECO:0000255}.
FT   MOD_RES     135    135       Phosphoserine; by CK2. {ECO:0000255}.
FT   MOD_RES     149    149       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     150    150       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     161    161       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     164    164       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     170    170       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     186    186       Phosphoserine; by CK2. {ECO:0000255}.
FT   MOD_RES     208    208       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     246    246       Phosphoserine.
FT                                {ECO:0000269|PubMed:17372656,
FT                                ECO:0000269|PubMed:18327897}.
FT   MOD_RES     252    252       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     253    253       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     299    299       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     307    307       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     311    311       Phosphoserine; by CK2. {ECO:0000255}.
FT   MOD_RES     321    321       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     332    332       Phosphoserine; by CK2. {ECO:0000255}.
FT   CONFLICT    291    291       D -> E (in Ref. 2; AAB01211).
FT                                {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
//