DALY_DROME
ID DALY_DROME Reviewed; 626 AA.
AC Q24114; Q9VSQ8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Division abnormally delayed protein;
DE Short=Dally protein;
DE Flags: Precursor;
GN Name=dally; ORFNames=CG4974;
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].
RX PubMed=8582281; DOI=10.1242/dev.121.11.3687;
RA Nakato H., Futch T.A., Selleck S.B.;
RT "The division abnormally delayed (dally) gene: a putative integral membrane
RT proteoglycan required for cell division patterning during postembryonic
RT development of the nervous system in Drosophila.";
RL Development 121:3687-3702(1995).
RN [2]
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 [3]
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97 AND ASN-101, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC Required for cell division patterning during post-embryonic development
CC of the nervous system.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}; Extracellular side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
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DR EMBL; U31985; AAA97401.1; -; mRNA.
DR EMBL; AE014296; AAF50358.1; -; Genomic_DNA.
DR RefSeq; NP_001246685.1; NM_001259756.2.
DR RefSeq; NP_523983.1; NM_079259.4.
DR AlphaFoldDB; Q24114; -.
DR SMR; Q24114; -.
DR BioGRID; 64418; 27.
DR DIP; DIP-23816N; -.
DR IntAct; Q24114; 194.
DR STRING; 7227.FBpp0297069; -.
DR GlyGen; Q24114; 8 sites.
DR iPTMnet; Q24114; -.
DR PaxDb; Q24114; -.
DR PRIDE; Q24114; -.
DR DNASU; 39013; -.
DR EnsemblMetazoa; FBtr0076583; FBpp0076310; FBgn0263930.
DR EnsemblMetazoa; FBtr0305901; FBpp0297069; FBgn0263930.
DR GeneID; 39013; -.
DR KEGG; dme:Dmel_CG4974; -.
DR CTD; 39013; -.
DR FlyBase; FBgn0263930; dally.
DR VEuPathDB; VectorBase:FBgn0263930; -.
DR eggNOG; KOG3821; Eukaryota.
DR HOGENOM; CLU_024658_3_0_1; -.
DR InParanoid; Q24114; -.
DR OMA; FKAQANN; -.
DR OrthoDB; 1097767at2759; -.
DR PhylomeDB; Q24114; -.
DR Reactome; R-DME-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-DME-2022928; HS-GAG biosynthesis.
DR Reactome; R-DME-2024096; HS-GAG degradation.
DR Reactome; R-DME-209471; Formation and transport of the N-HH ligand.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-5362798; Release of Hh-Np from the secreting cell.
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q24114; -.
DR BioGRID-ORCS; 39013; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39013; -.
DR PRO; PR:Q24114; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0263930; Expressed in wing disc and 33 other tissues.
DR ExpressionAtlas; Q24114; baseline and differential.
DR Genevisible; Q24114; DM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IMP:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0098595; C:perivitelline space; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IGI:FlyBase.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0071694; P:maintenance of protein location in extracellular region; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:2001261; P:negative regulation of semaphorin-plexin signaling pathway; IGI:FlyBase.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:FlyBase.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
DR GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:1905475; P:regulation of protein localization to membrane; IBA:GO_Central.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0008052; P:sensory organ boundary specification; IMP:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR GO; GO:0035222; P:wing disc pattern formation; IMP:FlyBase.
DR InterPro; IPR031187; Dally.
DR InterPro; IPR001863; Glypican.
DR PANTHER; PTHR10822; PTHR10822; 1.
DR PANTHER; PTHR10822:SF29; PTHR10822:SF29; 1.
DR Pfam; PF01153; Glypican; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Heparan sulfate; Lipoprotein;
KW Membrane; Proteoglycan; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..602
FT /note="Division abnormally delayed protein"
FT /id="PRO_0000012327"
FT PROPEP 603..626
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012328"
FT REGION 41..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 602
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 626 AA; 69031 MW; 1182AD8A0D0E4DD3 CRC64;
MAARSVRLAQ LLLFTLLCGF VGLSAAKHLD LDGIHHHQHH LHSATTHHRR RLQRDSRAKD
AVGGSTHQCD AVKSYFESID IKSSGTYSEK GAICGGNCCN NATELELRDK AAGMFEQLLH
HHTSSLRGVL ETNAKQFQSH VLELAQISEN MTHSLFSKVY TRMVPSSRMM IHQLYTEIMN
HLIYTSNYTN SNGQLGRRGI GSVQSNLEEA VRHFFVQLFP VAYHQMVHLS KNNLGDLHED
YVNCLQHNFD EMHPFGDIPQ QVQSNLGKSV HMSNVFMNAL LQAAEVLSEA DALYGEQLTD
TCKLHLLKMH YCPNCNGHHS SSRSETKLCY GYCKNVMRGC SAEYAGLLDS PWSGVVDSLN
NLVTTHILSD TGIINVIKHL QTYFSEAIMA AMHNGPELEK KVKKTCGTPS LTPYSSGEPD
ARPPPHKNNV KWATDPDPGM VLFLSTIDKS KEFYTTIVDN FCDEQQHSRD DHSCWSGDRF
GDYTQLLINP GTDSQRYNPE VPFNAKAQTG KLNELVDKLF KIRKSIGAAA PSNSIQATHD
IQNDMGEGSG GGEGQIGDDE EEYGGAHGSG DGSGDGPHTP IEESEGTTTN EVESRDSGKT
SGSNPLEGTA TWMLLTLVTM LFSSCS
