DAR1_DROME
ID DAR1_DROME Reviewed; 751 AA.
AC Q9VZN4; Q4V6V6;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Dendritic arbor reduction protein 1 {ECO:0000312|EMBL:AAF47785.2};
GN Name=dar1 {ECO:0000312|FlyBase:FBgn0263239};
GN ORFNames=CG12029 {ECO:0000312|FlyBase:FBgn0263239};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:AAY51594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAY51594.1};
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21368042; DOI=10.1523/jneurosci.6307-10.2011;
RA Ye B., Kim J.H., Yang L., McLachlan I., Younger S., Jan L.Y., Jan Y.N.;
RT "Differential regulation of dendritic and axonal development by the novel
RT Krueppel-like factor Dar1.";
RL J. Neurosci. 31:3309-3319(2011).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26490864; DOI=10.1523/jneurosci.1610-15.2015;
RA Wang X., Zhang M.W., Kim J.H., Macara A.M., Sterne G., Yang T., Ye B.;
RT "The Krueppel-Like factor Dar1 determines multipolar neuron morphology.";
RL J. Neurosci. 35:14251-14259(2015).
CC -!- FUNCTION: Transcriptional regulator which promotes dendrite growth by
CC suppressing, either directly or indirectly, the expression of the
CC microtubule-severing protein spas (PubMed:21368042). Determines
CC multipolar neuron morphology in postmitotic neurons by positively
CC regulating the expression of genes involved in nuclear positioning
CC including several dynein genes and the nuclear migration protein nudC
CC (PubMed:26490864). {ECO:0000269|PubMed:21368042,
CC ECO:0000269|PubMed:26490864}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21368042}.
CC -!- TISSUE SPECIFICITY: Highly enriched in the peripheral nervous system
CC but is absent from the central nervous system (PubMed:21368042).
CC Expressed in neurons with more than one dendrite including da neurons,
CC bd neurons and the dmd1 neuron but undetectable in neurons with single
CC dendrites such as external sensory organ neurons and chodonotal neurons
CC (PubMed:26490864). {ECO:0000269|PubMed:21368042,
CC ECO:0000269|PubMed:26490864}.
CC -!- DISRUPTION PHENOTYPE: Severely reduced growth of microtubule-based
CC dendritic branches and elevated levels of microtubule-severing protein
CC spas (PubMed:21368042). Gradual conversion of multipolar neurons into
CC the bipolar or unipolar morphology (PubMed:26490864).
CC {ECO:0000269|PubMed:21368042, ECO:0000269|PubMed:26490864}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AE014296; AAF47785.2; -; Genomic_DNA.
DR EMBL; BT022200; AAY51594.1; -; mRNA.
DR RefSeq; NP_001097493.1; NM_001104023.2.
DR AlphaFoldDB; Q9VZN4; -.
DR SMR; Q9VZN4; -.
DR IntAct; Q9VZN4; 9.
DR STRING; 7227.FBpp0112047; -.
DR PaxDb; Q9VZN4; -.
DR DNASU; 38436; -.
DR EnsemblMetazoa; FBtr0113134; FBpp0112047; FBgn0263239.
DR GeneID; 38436; -.
DR KEGG; dme:Dmel_CG12029; -.
DR UCSC; CG12029-RB; d. melanogaster.
DR CTD; 38436; -.
DR FlyBase; FBgn0263239; dar1.
DR VEuPathDB; VectorBase:FBgn0263239; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164016; -.
DR HOGENOM; CLU_014863_1_0_1; -.
DR InParanoid; Q9VZN4; -.
DR OMA; HLYQHHP; -.
DR OrthoDB; 982312at2759; -.
DR PhylomeDB; Q9VZN4; -.
DR SignaLink; Q9VZN4; -.
DR BioGRID-ORCS; 38436; 0 hits in 3 CRISPR screens.
DR ChiTaRS; dar1; fly.
DR GenomeRNAi; 38436; -.
DR PRO; PR:Q9VZN4; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0263239; Expressed in dorsal ridge (Drosophila) and 14 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:FlyBase.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:FlyBase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..751
FT /note="Dendritic arbor reduction protein 1"
FT /id="PRO_0000436601"
FT ZN_FING 664..688
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 694..718
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 724..746
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 57..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..123
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 82348 MW; 51B3A48DA4A4263E CRC64;
MHTDIIIGDQ FAANNNYWVM QSPELDYRHE LMGRLHKIEP ADVELEVLAA AAAAANNNNN
TSSNNNHSSN SSSNNSNGSQ TPNGNNNSSL ATGGHQHHQF HHHLHHHHSH QHHHQHHHLH
QHHSHSLQSG ESGASEAWPH LPAPSYASDV PHAQQQQLQP AGSPNSNSNG AYGCAPLYDG
APYEVALGYG GAVVASTGGA TSSDKEYLYE TKNKEALYAD PLDDPYQRPV LWDDITTSIQ
NIDPENALML SSSGSSNNNG SSNSSSNTGE SATSQLPQVK MEAIDESLLE TFSTPLLSPL
EIKTEKQQRQ QQHQHQQQQQ QQQQQQQQHQ QQHQQQYQQQ HYQQHYQQQH LYQHHPSLAL
PGLPPAVDVV ELQLQQQHQQ QQHLQHNNSS SSSPKLATPG DNSGNTSSYQ QQYASQLVSG
SGGGYLNGSS SNSYGYSWHS SQSFHTKYQI HPPSAAASAT ASATATPTAQ LGAQQQQQQQ
QQQQLQQLCP PAAPSTPSTS SSSISSSSAS SASRHMFVPP LTPPSSDPGS PGSSMVAAAA
AAAAQRRTTP PPPYQQGHVM GLINPPPTLQ LLGGAATGSN NSCTTTLTTL TPASAIQQQQ
QQPQQQQVPQ QQPPPTPRSS GGGRRGRHSH HQPGTAAHIA SLMSVRTVRY NRRNNPELEK
RRIHHCDFVG CSKVYTKSSH LKAHQRIHTG EKPYTCQWPE CEWRFARSDE LTRHYRKHTG
AKPFKCIVCE RSFARSDHLA LHMKRHLPKN K
