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Delta-like protein D (DeltaD) (After eight protein)

 DLLD_DANRE              Reviewed;         717 AA.
Q8UWJ4; P87357;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 2.
10-MAY-2017, entry version 109.
RecName: Full=Delta-like protein D;
Short=DeltaD;
AltName: Full=After eight protein;
Flags: Precursor;
Name=dld; Synonyms=aei;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9203139; DOI=10.1016/S0925-4773(97)00037-3;
Dornseifer P., Takke C., Campos-Ortega J.A.;
"Overexpression of a zebrafish homologue of the Drosophila neurogenic
gene delta perturbs differentiation of primary neurons and somitic
development.";
Mech. Dev. 63:159-171(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=12361969;
Hans S., Campos-Ortega J.A.;
"On the organisation of the regulatory region of the zebrafish deltaD
gene.";
Development 129:4773-4784(2002).
[3]
TISSUE SPECIFICITY.
PubMed=9425132;
Haddon C., Smithers L., Schneider-Maunoury S., Coche T., Henrique D.,
Lewis J.;
"Multiple delta genes and lateral inhibition in zebrafish primary
neurogenesis.";
Development 125:359-370(1998).
[4]
FUNCTION.
PubMed=11100729; DOI=10.1038/35044091;
Jiang Y.-J., Aerne B.L., Smithers L., Haddon C., Ish-Horowicz D.,
Lewis J.;
"Notch signalling and the synchronization of the somite segmentation
clock.";
Nature 408:475-479(2000).
[5]
INTERACTION WITH MIB.
PubMed=15013799; DOI=10.1016/j.ydbio.2003.11.010;
Chen W., Corliss D.C.;
"Three modules of zebrafish Mind bomb work cooperatively to promote
Delta ubiquitination and endocytosis.";
Dev. Biol. 267:361-373(2004).
[6]
UBIQUITINATION.
PubMed=12530964; DOI=10.1016/S1534-5807(02)00409-4;
Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D.,
Yeo S.-Y., Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M.,
Lewis J., Chandrasekharappa S.C., Chitnis A.B.;
"Mind bomb is a ubiquitin ligase that is essential for efficient
activation of Notch signaling by Delta.";
Dev. Cell 4:67-82(2003).
[7]
TISSUE SPECIFICITY.
PubMed=15068793; DOI=10.1016/S1534-5807(04)00097-8;
Cheng Y.-C., Amoyel M., Qiu X., Jiang Y.-J., Xu Q., Wilkinson D.G.;
"Notch activation regulates the segregation and differentiation of
rhombomere boundary cells in the zebrafish hindbrain.";
Dev. Cell 6:539-550(2004).
-!- FUNCTION: Acts as a ligand for Notch receptors and is involved in
primary neurogenesis and somitogenesis. Can activate Notch
receptors, thereby playing a key role in lateral inhibition, a
process that prevents the immediate neighbors of each nascent
neural cell from simultaneously embarking on neural
differentiation. Required in somite segmentation to keep the
oscillations of neighboring presomitic mesoderm cells
synchronized. {ECO:0000269|PubMed:11100729}.
-!- SUBUNIT: Interacts with mib. {ECO:0000269|PubMed:15013799}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in both mesodermal and
neuroectodermal regions. In the developing nervous system, it is
expressed in overlapping regions with deltaB (dlb) and deltaA
(dla); in the neural plate, dld is expressed in patches of
contiguous cells with dla, while dlb is confined to scattered
cells within those patches that will differentiate as neurons. In
somites, it marks the anterior part of each formed somite, while
deltaC (dlc) marks the posterior part. In 24 hours embryos,
expressed in the hindbrain in stripes adjacent to rhombomere
boundaries, but not in the actual boundary cells.
{ECO:0000269|PubMed:12361969, ECO:0000269|PubMed:15068793,
ECO:0000269|PubMed:9203139, ECO:0000269|PubMed:9425132}.
-!- PTM: Ubiquitinated by mib, leading to its endocytosis and
subsequent degradation. {ECO:0000269|PubMed:12530964}.
-----------------------------------------------------------------------
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EMBL; Y11760; CAA72425.1; -; mRNA.
EMBL; AF426384; AAL31528.1; -; Genomic_DNA.
UniGene; Dr.75102; -.
ProteinModelPortal; Q8UWJ4; -.
SMR; Q8UWJ4; -.
STRING; 7955.ENSDARP00000089996; -.
PaxDb; Q8UWJ4; -.
ZFIN; ZDB-GENE-990415-47; dld.
eggNOG; ENOG410IR7B; Eukaryota.
eggNOG; ENOG410XUNS; LUCA.
HOGENOM; HOG000267024; -.
HOVERGEN; HBG007139; -.
InParanoid; Q8UWJ4; -.
PhylomeDB; Q8UWJ4; -.
PRO; PR:Q8UWJ4; -.
Proteomes; UP000000437; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:ZFIN.
GO; GO:0048471; C:perinuclear region of cytoplasm; IGI:ZFIN.
GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030165; F:PDZ domain binding; IDA:ZFIN.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:ZFIN.
GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IGI:ZFIN.
GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:ZFIN.
GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IMP:ZFIN.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:ZFIN.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:ZFIN.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:ZFIN.
GO; GO:0046331; P:lateral inhibition; IMP:ZFIN.
GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
GO; GO:0061056; P:sclerotome development; IGI:ZFIN.
GO; GO:0021523; P:somatic motor neuron differentiation; IMP:ZFIN.
GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IMP:ZFIN.
InterPro; IPR001774; DSL.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR011651; Notch_ligand_N.
Pfam; PF01414; DSL; 1.
Pfam; PF00008; EGF; 5.
Pfam; PF12661; hEGF; 1.
Pfam; PF07657; MNNL; 1.
SMART; SM00051; DSL; 1.
SMART; SM00181; EGF; 8.
SMART; SM00179; EGF_CA; 6.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS51051; DSL; 1.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 8.
PROSITE; PS01187; EGF_CA; 2.
1: Evidence at protein level;
Calcium; Complete proteome; Developmental protein; Differentiation;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Neurogenesis;
Notch signaling pathway; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 717 Delta-like protein D.
/FTId=PRO_0000007517.
TOPO_DOM 20 547 Extracellular. {ECO:0000255}.
TRANSMEM 548 568 Helical. {ECO:0000255}.
TOPO_DOM 569 717 Cytoplasmic. {ECO:0000255}.
DOMAIN 175 219 DSL. {ECO:0000255|PROSITE-
ProRule:PRU00377}.
DOMAIN 220 253 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 257 284 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 286 324 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 326 362 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 364 401 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 403 439 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 441 477 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 479 515 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 177 186 {ECO:0000250}.
DISULFID 190 202 {ECO:0000250}.
DISULFID 210 219 {ECO:0000250}.
DISULFID 224 235 {ECO:0000250}.
DISULFID 228 241 {ECO:0000250}.
DISULFID 243 252 {ECO:0000250}.
DISULFID 261 266 {ECO:0000250}.
DISULFID 274 283 {ECO:0000250}.
DISULFID 290 302 {ECO:0000250}.
DISULFID 296 312 {ECO:0000250}.
DISULFID 314 323 {ECO:0000250}.
DISULFID 330 341 {ECO:0000250}.
DISULFID 335 350 {ECO:0000250}.
DISULFID 352 361 {ECO:0000250}.
DISULFID 368 379 {ECO:0000250}.
DISULFID 373 389 {ECO:0000250}.
DISULFID 391 400 {ECO:0000250}.
DISULFID 407 418 {ECO:0000250}.
DISULFID 412 427 {ECO:0000250}.
DISULFID 429 438 {ECO:0000250}.
DISULFID 445 456 {ECO:0000250}.
DISULFID 450 465 {ECO:0000250}.
DISULFID 467 476 {ECO:0000250}.
DISULFID 483 494 {ECO:0000250}.
DISULFID 488 503 {ECO:0000250}.
DISULFID 505 514 {ECO:0000250}.
CONFLICT 95 95 E -> D (in Ref. 2; AAL31528).
{ECO:0000305}.
CONFLICT 717 717 V -> ISEC (in Ref. 2; AAL31528).
{ECO:0000305}.
SEQUENCE 717 AA; 79061 MW; 9C5A0162504593E4 CRC64;
MGRLMIAVLL CVMISQGFCS GVFELKLQEF LNKKGVTGNA NCCKGSAAEG HQCECKTFFR
ICLKHYQANV SPDPPCTYGG AVTPVLGSNS FQVPESFPDS SFTNPIPFAF GFTWPGTFSL
IIEALHTDST DDLSTENPDR LISRMTTQRH LTVGEEWSQD LQVGGRTELK YSYRFVCDEH
YYGEGCSVFC RPRDDTFGHF TCGERGEIIC NSGWKGQYCT EPICLPGCDE DHGFCDKPGE
CKCRVGFSGK YCDDCIRYPG CLHGTCQQPW QCNCQEGWGG LFCNQDLNYC THHKPCQNGA
TCTNTGQGSY TCSCRPGFTG DSCEIEVNEC SGSPCRNGGS CTDLENTYSC TCPPGFYGRN
CELSAMTCAD GPCFNGGHCA DNPEGGYFCQ CPMGYAGFNC EKKIDHCSSN PCSNDAQCLD
LVDSYLCQCP EGFTGTHCED NIDECATYPC QNGGTCQDGL SDYTCTCPPG YTGKNCTSAV
NKCLHNPCHN GATCHEMDNR YVCACIPGYG GRNCQFLLPE NPQGQAIVEG ADKRYSYEED
DGGFPWTAVC AGIILVLLVL IGGSVFVIYI RLKLQQRSQQ IDSHSEIETM NNLTNNRSRE
KDLSVSIIGA TQVKNINKKV DFQSDGDKNG FKSRYSLVDY NLVHELKQED LGKEDSERSE
ATKCEPLDSD SEEKHRNHLK SDSSERKRTE SLCKDTKYQS VFVLSEEKDE CIIATEV


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