DLLB_DANRE
ID DLLB_DANRE Reviewed; 615 AA.
AC O57409;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Delta-like protein B;
DE Short=DeltaB;
DE Flags: Precursor;
GN Name=dlb;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9425132; DOI=10.1242/dev.125.3.359;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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., Yeo S.-Y.,
RA Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M., Lewis J.,
RA Chandrasekharappa S.C., Chitnis A.B.;
RT "Mind bomb is a ubiquitin ligase that is essential for efficient activation
RT of Notch signaling by Delta.";
RL Dev. Cell 4:67-82(2003).
CC -!- FUNCTION: Acts as a ligand for Notch receptors and is involved in
CC primary neurogenesis. Can activate Notch receptors, thereby playing a
CC key role in lateral inhibition, a process that prevents the immediate
CC neighbors of each nascent neural cell from simultaneously embarking on
CC neural differentiation. {ECO:0000269|PubMed:9425132}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the epiblast (the future
CC neurectoderm) and in neuroblasts. Expressed in overlapping regions with
CC deltaA (dla) and deltaD (dld), but differs in the neural plate: it is
CC apparently confined to the scattered cells within those patches that
CC differentiate as neurons, while dla and dld are expressed in patches of
CC contiguous cells. {ECO:0000269|PubMed:9425132}.
CC -!- PTM: Ubiquitinated by mib, leading to its endocytosis and subsequent
CC degradation. {ECO:0000269|PubMed:12530964}.
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DR EMBL; AF006488; AAC41241.1; -; mRNA.
DR EMBL; BC076414; AAH76414.1; -; mRNA.
DR RefSeq; NP_571033.1; NM_130958.1.
DR AlphaFoldDB; O57409; -.
DR SMR; O57409; -.
DR STRING; 7955.ENSDARP00000021660; -.
DR PaxDb; O57409; -.
DR Ensembl; ENSDART00000019259; ENSDARP00000021660; ENSDARG00000004232.
DR GeneID; 30141; -.
DR KEGG; dre:30141; -.
DR CTD; 30141; -.
DR ZFIN; ZDB-GENE-980526-114; dlb.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000164418; -.
DR InParanoid; O57409; -.
DR OrthoDB; 406049at2759; -.
DR PhylomeDB; O57409; -.
DR TreeFam; TF351835; -.
DR PRO; PR:O57409; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000004232; Expressed in neuron and 48 other tissues.
DR ExpressionAtlas; O57409; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0021536; P:diencephalon development; IMP:ZFIN.
DR GO; GO:0030901; P:midbrain development; IGI:ZFIN.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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 Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 6.
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; 2.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS01187; EGF_CA; 2.
PE 1: Evidence at protein level;
KW Calcium; Developmental protein; Differentiation; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Neurogenesis;
KW Notch signaling pathway; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..615
FT /note="Delta-like protein B"
FT /id="PRO_0000007515"
FT TOPO_DOM 21..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 159..203
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 204..237
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 241..268
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 270..308
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 310..346
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 348..385
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 387..423
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 425..461
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 463..499
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..170
FT /evidence="ECO:0000250"
FT DISULFID 174..186
FT /evidence="ECO:0000250"
FT DISULFID 194..203
FT /evidence="ECO:0000250"
FT DISULFID 208..219
FT /evidence="ECO:0000250"
FT DISULFID 212..225
FT /evidence="ECO:0000250"
FT DISULFID 227..236
FT /evidence="ECO:0000250"
FT DISULFID 245..250
FT /evidence="ECO:0000250"
FT DISULFID 258..267
FT /evidence="ECO:0000250"
FT DISULFID 274..286
FT /evidence="ECO:0000250"
FT DISULFID 280..296
FT /evidence="ECO:0000250"
FT DISULFID 298..307
FT /evidence="ECO:0000250"
FT DISULFID 314..325
FT /evidence="ECO:0000250"
FT DISULFID 319..334
FT /evidence="ECO:0000250"
FT DISULFID 336..345
FT /evidence="ECO:0000250"
FT DISULFID 352..363
FT /evidence="ECO:0000250"
FT DISULFID 357..373
FT /evidence="ECO:0000250"
FT DISULFID 375..384
FT /evidence="ECO:0000250"
FT DISULFID 391..402
FT /evidence="ECO:0000250"
FT DISULFID 396..411
FT /evidence="ECO:0000250"
FT DISULFID 413..422
FT /evidence="ECO:0000250"
FT DISULFID 429..440
FT /evidence="ECO:0000250"
FT DISULFID 434..449
FT /evidence="ECO:0000250"
FT DISULFID 451..460
FT /evidence="ECO:0000250"
FT DISULFID 467..478
FT /evidence="ECO:0000250"
FT DISULFID 472..487
FT /evidence="ECO:0000250"
FT DISULFID 489..498
FT /evidence="ECO:0000250"
SQ SEQUENCE 615 AA; 67593 MW; CA18004428F5603C CRC64;
MAHLSLYCLL SVSLLQLVAS SGVFELKVHS FSTTRRFCRR TRDCNIFFRI CLKHSEDVIS
AEPPCTFGTG QTSVLRADQS SIASSAAIRV PFHFKWPGTF SLIIEAWNAE SPKEHHDYTE
NQNNLISRLA TRRRLAVGED WSQDVHFGDQ SELRYSYHVF CDEFYFGEAC SDYCRPRDDT
LGHYTCDENG NKECLVGWQG DYCSDPICSS DCSERHGYCE SPGECKCRLG WQGPSCSECV
HYPGCLHGTC SQPWQCVCKE GWGGLFCNQD LNYCTNHKPC ANGATCTNTG QGSYTCTCRP
GFGGTNCELE INECDCNPCK NGGSCNDLEN DYSCTCPQGF YGKNCEIIAM TCADDPCFNG
GTCEEKFTGG YVCRCPPTFT GSNCEKRLDR CSHKPCANGG ECVDLGASAL CRCRPGFSGS
RCETNIDDCA RYPCQNAGTC QDGINDYTCT CTLGFTGKNC SLRADACLTN PCLHGGTCFT
HFSGPVCQCV PGFMGSTCEF PVQASLEKMA PRVGQTSPSA VAVSCVLGVL AVFLGVCVGL
VVLRRRRHRL RRQQLCDSVF NDLETVNNLD RQHYPYDRDF SQVKPCNTEG RISLAASHTL
PAGQEFLWSA GGGLR
