HMGD_DROME
ID HMGD_DROME Reviewed; 112 AA.
AC Q05783; Q540Z0; Q9W2D3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=High mobility group protein D;
DE Short=HMG-D;
GN Name=HmgD; ORFNames=CG17950;
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], PROTEIN SEQUENCE OF 45-77, FUNCTION,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1373803; DOI=10.1128/mcb.12.5.1915-1923.1992;
RA Wagner C.R., Hamana K., Elgin S.C.R.;
RT "A high-mobility-group protein and its cDNAs from Drosophila
RT melanogaster.";
RL Mol. Cell. Biol. 12:1915-1923(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=8414994; DOI=10.1093/nar/21.18.4369;
RA Ner S.S., Churchill M.E.A., Searles M.A., Travers A.A.;
RT "dHMG-Z, a second HMG-1-related protein in Drosophila melanogaster.";
RL Nucleic Acids Res. 21:4369-4371(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL377,
RC ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8168480; DOI=10.1002/j.1460-2075.1994.tb06450.x;
RA Ner S.S., Travers A.A.;
RT "HMG-D, the Drosophila melanogaster homologue of HMG 1 protein, is
RT associated with early embryonic chromatin in the absence of histone H1.";
RL EMBO J. 13:1817-1822(1994).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7720717; DOI=10.1002/j.1460-2075.1995.tb07110.x;
RA Churchill M.E.A., Jones D.N.M., Glaser T., Hefner H., Searles M.A.,
RA Travers A.A.;
RT "HMG-D is an architecture-specific protein that preferentially binds to DNA
RT containing the dinucleotide TG.";
RL EMBO J. 14:1264-1275(1995).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-111, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; TYR-12; SER-103 AND
RP SER-111, AND 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).
RN [11]
RP STRUCTURE BY NMR OF 2-74.
RX PubMed=7922039; DOI=10.1016/s0969-2126(00)00063-0;
RA Jones D.N.M., Searles M.A., Shaw G.L., Churchill M.E.A., Ner S.S.,
RA Keeler J., Travers A.A., Neuhaus D.;
RT "The solution structure and dynamics of the DNA-binding domain of HMG-D
RT from Drosophila melanogaster.";
RL Structure 2:609-627(1994).
CC -!- FUNCTION: Binds preferentially single-stranded DNA and unwinds double-
CC stranded DNA. Prefers sites containing the sequence 5'-ttg-3'.
CC Facilitates DNA bending. Associated with early embryonic chromatin in
CC the absence of histone H1. {ECO:0000269|PubMed:1373803,
CC ECO:0000269|PubMed:7720717, ECO:0000269|PubMed:8168480}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Present in all stages of development.
CC {ECO:0000269|PubMed:1373803}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR EMBL; M77023; AAA28609.1; -; mRNA.
DR EMBL; X71138; CAA50468.1; -; mRNA.
DR EMBL; AM294353; CAL26283.1; -; Genomic_DNA.
DR EMBL; AM294354; CAL26284.1; -; Genomic_DNA.
DR EMBL; AM294355; CAL26285.1; -; Genomic_DNA.
DR EMBL; AM294356; CAL26286.1; -; Genomic_DNA.
DR EMBL; AM294357; CAL26287.1; -; Genomic_DNA.
DR EMBL; AM294358; CAL26288.1; -; Genomic_DNA.
DR EMBL; AM294359; CAL26289.1; -; Genomic_DNA.
DR EMBL; AM294360; CAL26290.1; -; Genomic_DNA.
DR EMBL; AM294361; CAL26291.1; -; Genomic_DNA.
DR EMBL; AM294362; CAL26292.1; -; Genomic_DNA.
DR EMBL; AM294363; CAL26293.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46759.1; -; Genomic_DNA.
DR EMBL; AY118333; AAM48362.1; -; mRNA.
DR PIR; A44382; A44382.
DR RefSeq; NP_001163244.1; NM_001169773.2.
DR RefSeq; NP_001286696.1; NM_001299767.1.
DR RefSeq; NP_726109.1; NM_166479.2.
DR RefSeq; NP_726110.1; NM_166480.2.
DR PDB; 1E7J; NMR; -; A=1-74.
DR PDB; 1HMA; NMR; -; A=2-74.
DR PDB; 1QRV; X-ray; 2.20 A; A/B=2-74.
DR PDB; 3NM9; X-ray; 2.85 A; A/D/G/J/M/P=2-74.
DR PDBsum; 1E7J; -.
DR PDBsum; 1HMA; -.
DR PDBsum; 1QRV; -.
DR PDBsum; 3NM9; -.
DR AlphaFoldDB; Q05783; -.
DR BMRB; Q05783; -.
DR SMR; Q05783; -.
DR BioGRID; 63106; 25.
DR DIP; DIP-22805N; -.
DR IntAct; Q05783; 3.
DR STRING; 7227.FBpp0071625; -.
DR iPTMnet; Q05783; -.
DR MetOSite; Q05783; -.
DR PaxDb; Q05783; -.
DR PRIDE; Q05783; -.
DR DNASU; 37481; -.
DR EnsemblMetazoa; FBtr0071708; FBpp0071625; FBgn0004362.
DR EnsemblMetazoa; FBtr0071709; FBpp0071626; FBgn0004362.
DR EnsemblMetazoa; FBtr0301410; FBpp0290624; FBgn0004362.
DR EnsemblMetazoa; FBtr0345487; FBpp0311598; FBgn0004362.
DR GeneID; 37481; -.
DR KEGG; dme:Dmel_CG17950; -.
DR CTD; 37481; -.
DR FlyBase; FBgn0004362; HmgD.
DR VEuPathDB; VectorBase:FBgn0004362; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000167382; -.
DR HOGENOM; CLU_082854_0_6_1; -.
DR InParanoid; Q05783; -.
DR OMA; PLSAYMH; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; Q05783; -.
DR Reactome; R-DME-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-DME-163282; Mitochondrial transcription initiation.
DR SignaLink; Q05783; -.
DR BioGRID-ORCS; 37481; 0 hits in 1 CRISPR screen.
DR ChiTaRS; HmgD; fly.
DR EvolutionaryTrace; Q05783; -.
DR GenomeRNAi; 37481; -.
DR PRO; PR:Q05783; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004362; Expressed in cleaving embryo and 39 other tissues.
DR ExpressionAtlas; Q05783; baseline and differential.
DR Genevisible; Q05783; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0008301; F:DNA binding, bending; IDA:FlyBase.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..112
FT /note="High mobility group protein D"
FT /id="PRO_0000048552"
FT DNA_BIND 5..71
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 72..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:1QRV"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3NM9"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1QRV"
FT HELIX 50..70
FT /evidence="ECO:0007829|PDB:1QRV"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1QRV"
SQ SEQUENCE 112 AA; 12416 MW; 3F537CCFD62FEC9F CRC64;
MSDKPKRPLS AYMLWLNSAR ESIKRENPGI KVTEVAKRGG ELWRAMKDKS EWEAKAAKAK
DDYDRAVKEF EANGGSSAAN GGGAKKRAKP AKKVAKKSKK EESDEDDDDE SE
