GenomeNet

Database: UniProt
Entry: Q8UWJ4
LinkDB: Q8UWJ4
Original site: Q8UWJ4 
ID   DLLD_DANRE              Reviewed;         717 AA.
AC   Q8UWJ4; P87357;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   23-MAY-2018, entry version 112.
DE   RecName: Full=Delta-like protein D;
DE            Short=DeltaD;
DE   AltName: Full=After eight protein;
DE   Flags: Precursor;
GN   Name=dld; Synonyms=aei;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9203139; DOI=10.1016/S0925-4773(97)00037-3;
RA   Dornseifer P., Takke C., Campos-Ortega J.A.;
RT   "Overexpression of a zebrafish homologue of the Drosophila neurogenic
RT   gene delta perturbs differentiation of primary neurons and somitic
RT   development.";
RL   Mech. Dev. 63:159-171(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=12361969;
RA   Hans S., Campos-Ortega J.A.;
RT   "On the organisation of the regulatory region of the zebrafish deltaD
RT   gene.";
RL   Development 129:4773-4784(2002).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=9425132;
RA   Haddon C., Smithers L., Schneider-Maunoury S., Coche T., Henrique D.,
RA   Lewis J.;
RT   "Multiple delta genes and lateral inhibition in zebrafish primary
RT   neurogenesis.";
RL   Development 125:359-370(1998).
RN   [4]
RP   FUNCTION.
RX   PubMed=11100729; DOI=10.1038/35044091;
RA   Jiang Y.-J., Aerne B.L., Smithers L., Haddon C., Ish-Horowicz D.,
RA   Lewis J.;
RT   "Notch signalling and the synchronization of the somite segmentation
RT   clock.";
RL   Nature 408:475-479(2000).
RN   [5]
RP   INTERACTION WITH MIB.
RX   PubMed=15013799; DOI=10.1016/j.ydbio.2003.11.010;
RA   Chen W., Corliss D.C.;
RT   "Three modules of zebrafish Mind bomb work cooperatively to promote
RT   Delta ubiquitination and endocytosis.";
RL   Dev. Biol. 267:361-373(2004).
RN   [6]
RP   UBIQUITINATION.
RX   PubMed=12530964; DOI=10.1016/S1534-5807(02)00409-4;
RA   Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D.,
RA   Yeo S.-Y., Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M.,
RA   Lewis J., Chandrasekharappa S.C., Chitnis A.B.;
RT   "Mind bomb is a ubiquitin ligase that is essential for efficient
RT   activation of Notch signaling by Delta.";
RL   Dev. Cell 4:67-82(2003).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=15068793; DOI=10.1016/S1534-5807(04)00097-8;
RA   Cheng Y.-C., Amoyel M., Qiu X., Jiang Y.-J., Xu Q., Wilkinson D.G.;
RT   "Notch activation regulates the segregation and differentiation of
RT   rhombomere boundary cells in the zebrafish hindbrain.";
RL   Dev. Cell 6:539-550(2004).
CC   -!- FUNCTION: Acts as a ligand for Notch receptors and is involved in
CC       primary neurogenesis and somitogenesis. Can activate Notch
CC       receptors, thereby playing a key role in lateral inhibition, a
CC       process that prevents the immediate neighbors of each nascent
CC       neural cell from simultaneously embarking on neural
CC       differentiation. Required in somite segmentation to keep the
CC       oscillations of neighboring presomitic mesoderm cells
CC       synchronized. {ECO:0000269|PubMed:11100729}.
CC   -!- SUBUNIT: Interacts with mib. {ECO:0000269|PubMed:15013799}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in both mesodermal and
CC       neuroectodermal regions. In the developing nervous system, it is
CC       expressed in overlapping regions with deltaB (dlb) and deltaA
CC       (dla); in the neural plate, dld is expressed in patches of
CC       contiguous cells with dla, while dlb is confined to scattered
CC       cells within those patches that will differentiate as neurons. In
CC       somites, it marks the anterior part of each formed somite, while
CC       deltaC (dlc) marks the posterior part. In 24 hours embryos,
CC       expressed in the hindbrain in stripes adjacent to rhombomere
CC       boundaries, but not in the actual boundary cells.
CC       {ECO:0000269|PubMed:12361969, ECO:0000269|PubMed:15068793,
CC       ECO:0000269|PubMed:9203139, ECO:0000269|PubMed:9425132}.
CC   -!- PTM: Ubiquitinated by mib, leading to its endocytosis and
CC       subsequent degradation. {ECO:0000269|PubMed:12530964}.
DR   EMBL; Y11760; CAA72425.1; -; mRNA.
DR   EMBL; AF426384; AAL31528.1; -; Genomic_DNA.
DR   UniGene; Dr.75102; -.
DR   ProteinModelPortal; Q8UWJ4; -.
DR   SMR; Q8UWJ4; -.
DR   STRING; 7955.ENSDARP00000089996; -.
DR   PaxDb; Q8UWJ4; -.
DR   PRIDE; Q8UWJ4; -.
DR   ZFIN; ZDB-GENE-990415-47; dld.
DR   eggNOG; ENOG410IR7B; Eukaryota.
DR   eggNOG; ENOG410XUNS; LUCA.
DR   HOGENOM; HOG000267024; -.
DR   HOVERGEN; HBG007139; -.
DR   InParanoid; Q8UWJ4; -.
DR   PhylomeDB; Q8UWJ4; -.
DR   PRO; PR:Q8UWJ4; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:ZFIN.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IGI:ZFIN.
DR   GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030165; F:PDZ domain binding; IDA:ZFIN.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:ZFIN.
DR   GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR   GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IGI:ZFIN.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR   GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IMP:ZFIN.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:ZFIN.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:ZFIN.
DR   GO; GO:0046331; P:lateral inhibition; IMP:ZFIN.
DR   GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IMP:ZFIN.
DR   GO; GO:0061056; P:sclerotome development; IGI:ZFIN.
DR   GO; GO:0021523; P:somatic motor neuron differentiation; IMP:ZFIN.
DR   GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR   GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IMP:ZFIN.
DR   InterPro; IPR001774; DSL.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   Pfam; PF01414; DSL; 1.
DR   Pfam; PF00008; EGF; 5.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF07657; MNNL; 1.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 6.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 8.
DR   PROSITE; PS50026; EGF_3; 8.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Neurogenesis;
KW   Notch signaling pathway; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    717       Delta-like protein D.
FT                                /FTId=PRO_0000007517.
FT   TOPO_DOM     20    547       Extracellular. {ECO:0000255}.
FT   TRANSMEM    548    568       Helical. {ECO:0000255}.
FT   TOPO_DOM    569    717       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      175    219       DSL. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00377}.
FT   DOMAIN      220    253       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      257    284       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      286    324       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      326    362       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      364    401       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      403    439       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      441    477       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      479    515       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD    475    475       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    177    186       {ECO:0000250}.
FT   DISULFID    190    202       {ECO:0000250}.
FT   DISULFID    210    219       {ECO:0000250}.
FT   DISULFID    224    235       {ECO:0000250}.
FT   DISULFID    228    241       {ECO:0000250}.
FT   DISULFID    243    252       {ECO:0000250}.
FT   DISULFID    261    266       {ECO:0000250}.
FT   DISULFID    274    283       {ECO:0000250}.
FT   DISULFID    290    302       {ECO:0000250}.
FT   DISULFID    296    312       {ECO:0000250}.
FT   DISULFID    314    323       {ECO:0000250}.
FT   DISULFID    330    341       {ECO:0000250}.
FT   DISULFID    335    350       {ECO:0000250}.
FT   DISULFID    352    361       {ECO:0000250}.
FT   DISULFID    368    379       {ECO:0000250}.
FT   DISULFID    373    389       {ECO:0000250}.
FT   DISULFID    391    400       {ECO:0000250}.
FT   DISULFID    407    418       {ECO:0000250}.
FT   DISULFID    412    427       {ECO:0000250}.
FT   DISULFID    429    438       {ECO:0000250}.
FT   DISULFID    445    456       {ECO:0000250}.
FT   DISULFID    450    465       {ECO:0000250}.
FT   DISULFID    467    476       {ECO:0000250}.
FT   DISULFID    483    494       {ECO:0000250}.
FT   DISULFID    488    503       {ECO:0000250}.
FT   DISULFID    505    514       {ECO:0000250}.
FT   CONFLICT     95     95       E -> D (in Ref. 2; AAL31528).
FT                                {ECO:0000305}.
FT   CONFLICT    717    717       V -> ISEC (in Ref. 2; AAL31528).
FT                                {ECO:0000305}.
SQ   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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