DAN_DROME
ID DAN_DROME Reviewed; 678 AA.
AC Q9VBW6; Q960P9;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein distal antenna {ECO:0000303|PubMed:12571108};
GN Name=dan {ECO:0000312|EMBL:AAF56411.2, ECO:0000312|FlyBase:FBgn0039286};
GN ORFNames=CG11849;
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] {ECO:0000312|EMBL:AAF56411.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF56411.2}
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 [3] {ECO:0000312|EMBL:AAK93348.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93348.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=12571108; DOI=10.1242/dev.00323;
RA Emerald B.S., Curtiss J., Mlodzik M., Cohen S.M.;
RT "Distal antenna and distal antenna related encode nuclear proteins
RT containing pipsqueak motifs involved in antenna development in
RT Drosophila.";
RL Development 130:1171-1180(2003).
RN [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH DANR; EY AND DAC, AND TISSUE
RP SPECIFICITY.
RX PubMed=17493605; DOI=10.1016/j.ydbio.2007.04.006;
RA Curtiss J., Burnett M., Mlodzik M.;
RT "distal antenna and distal antenna-related function in the retinal
RT determination network during eye development in Drosophila.";
RL Dev. Biol. 306:685-702(2007).
RN [6] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
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 [7]
RP STRUCTURE BY NMR OF 1-80.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CENP-B N-terminal DNA-binding domain of fruit
RT fly distal antenna CG11849-PA.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Probable transcription factor with a role in the retinal
CC determination (RD) network. Regulates ato expression and is required
CC for normal R8 induction and differentiation. Danr appears to repress
CC Dan expression, but Dan is required for Danr expression anterior to the
CC morphogenetic furrow (MF). Dan and Danr lie downstream of so and
CC require dac function for highest levels of expression. Contributes to
CC differentiation of antenna-specific characteristics; effector gene that
CC acts downstream of homothorax (hth), Distal-less (Dll), cut (ct) and
CC spineless (ss) genes to control differentiation of distal antennal
CC structures. {ECO:0000269|PubMed:12571108, ECO:0000269|PubMed:17493605}.
CC -!- SUBUNIT: Homomers. Interacts with itself, danr, ey and dac to form a
CC complex (or complexes) containing the RD factors.
CC {ECO:0000269|PubMed:17493605}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320,
CC ECO:0000269|PubMed:12571108}.
CC -!- TISSUE SPECIFICITY: Coexpressed with danr in the presumptive distal
CC antenna, but not in the leg imaginal disk. Both proteins are also
CC expressed in the brain and the eye region of the eye-antenna disk.
CC First detected in early L3 eye disks in cells surrounding the newly
CC initiated MF. Levels are uniform and high anterior to the furrow, lower
CC levels within and posterior to the furrow. Limited expression is seen
CC in small groups of cells in leg and wing. These appear in the location
CC of prominent sense organ progenitors at relatively late stages of disk
CC development. {ECO:0000269|PubMed:12571108,
CC ECO:0000269|PubMed:17493605}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit partial transformation of antenna
CC toward leg identity and small rough eyes. Ectopic expression causes
CC partial transformation of distal leg structures toward antennal
CC identity and antennal precursors into eye tissue.
CC {ECO:0000269|PubMed:12571108}.
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DR EMBL; AE014297; AAF56411.2; -; Genomic_DNA.
DR EMBL; AY051924; AAK93348.1; -; mRNA.
DR RefSeq; NP_001262949.1; NM_001276020.1.
DR RefSeq; NP_651346.1; NM_143089.4.
DR PDB; 2ELH; NMR; -; A=1-80.
DR PDBsum; 2ELH; -.
DR AlphaFoldDB; Q9VBW6; -.
DR SMR; Q9VBW6; -.
DR BioGRID; 67943; 14.
DR IntAct; Q9VBW6; 10.
DR STRING; 7227.FBpp0303321; -.
DR iPTMnet; Q9VBW6; -.
DR PaxDb; Q9VBW6; -.
DR DNASU; 43023; -.
DR EnsemblMetazoa; FBtr0084803; FBpp0084178; FBgn0039286.
DR EnsemblMetazoa; FBtr0330289; FBpp0303321; FBgn0039286.
DR GeneID; 43023; -.
DR KEGG; dme:Dmel_CG11849; -.
DR UCSC; CG11849-RA; d. melanogaster.
DR CTD; 43023; -.
DR FlyBase; FBgn0039286; dan.
DR VEuPathDB; VectorBase:FBgn0039286; -.
DR eggNOG; ENOG502S5K1; Eukaryota.
DR GeneTree; ENSGT00530000068878; -.
DR HOGENOM; CLU_405596_0_0_1; -.
DR InParanoid; Q9VBW6; -.
DR OMA; HMNIRMG; -.
DR OrthoDB; 1534815at2759; -.
DR PhylomeDB; Q9VBW6; -.
DR SignaLink; Q9VBW6; -.
DR BioGRID-ORCS; 43023; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; Q9VBW6; -.
DR GenomeRNAi; 43023; -.
DR PRO; PR:Q9VBW6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039286; Expressed in ectoderm anlage and 50 other tissues.
DR ExpressionAtlas; Q9VBW6; baseline and differential.
DR Genevisible; Q9VBW6; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0007469; P:antennal development; IMP:UniProtKB.
DR GO; GO:0021556; P:central nervous system formation; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007379; P:segment specification; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007889; HTH_Psq.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF04218; CENP-B_N; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50960; HTH_PSQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..678
FT /note="Protein distal antenna"
FT /id="PRO_0000351200"
FT DOMAIN 7..58
FT /note="HTH psq-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DNA_BIND 34..54
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT REGION 232..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:2ELH"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:2ELH"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:2ELH"
SQ SEQUENCE 678 AA; 71914 MW; 821E4FC920048BE2 CRC64;
MNIRMGTKGK RPLRSLTPRD KIHAIQRIHD GESKASVARD IGVPESTLRG WCKNEDKLRF
MSRQSATDNL CADALGDKMD GGGGGGGGAG GGGLLGPPEK RQRLDGALPL NFSNKLKFDE
LAFKRSPLNG LDYSTNKNLA DLGYNGLPVD YAAFNGGVKA KVFGADINRP AADPSLNAIS
PLSSLTHLSG LTGISQSPLA ISFNELTTNL NLLAQLNPGL AAMSGLNSFP AGAGNLRTPK
PSGQTPLQVQ SPRSDSGDRS AQGLSVKNWA KQKPGEGQGS LNLSIKNEGK GGDIKSPSPS
IAPSQMGGPM TLSNLAEDPL LYWLKSQQTM LGLNPLYPPT IPMGVTSPPI RSSTPQHMSQ
LAQTPPIPSA PLTPSSTPSG SLDEKNAAWY NWCKAFGASL HTLNPNAATL AALQANQLQQ
QVATTAAEGG SMGDPSNILY SHLTKETETP SVRSLSSNEQ NPEADEATET DLDGEVEPEA
SGKPEDLSAA GKVMTPSQSP IAHSSGSRSP EPKAKTKTPE TTNSTSECKK ILDNMLFKMG
GMEATGPLMP EQGSSESEGS FQDTSNPHTN NNDVSASNNN NNNNSNKTDE EEKAKYLDCT
ADEDIEAIRH GEKFLQWLEN CSNPRVTAVQ LMQLRFLIAA IKSGNETPMI EKSALPEDSE
EHAAEEEGSG RGKSRRRK
