GenomeNet

Database: UniProt
Entry: O57409
LinkDB: O57409
Original site: O57409 
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   13-FEB-2019, entry version 128.
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   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
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   [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.,
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).
CC   -!- FUNCTION: Acts as a ligand for Notch receptors and is involved in
CC       primary neurogenesis. Can activate Notch receptors, thereby
CC       playing a key role in lateral inhibition, a process that prevents
CC       the immediate neighbors of each nascent neural cell from
CC       simultaneously embarking on neural differentiation.
CC       {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
CC       with deltaA (dla) and deltaD (dld), but differs in the neural
CC       plate: it is apparently confined to the scattered cells within
CC       those patches that differentiate as neurons, while dla and dld are
CC       expressed in patches of contiguous cells.
CC       {ECO:0000269|PubMed:9425132}.
CC   -!- PTM: Ubiquitinated by mib, leading to its endocytosis and
CC       subsequent degradation. {ECO:0000269|PubMed:12530964}.
DR   EMBL; AF006488; AAC41241.1; -; mRNA.
DR   EMBL; BC076414; AAH76414.1; -; mRNA.
DR   RefSeq; NP_571033.1; NM_130958.1.
DR   UniGene; Dr.574; -.
DR   ProteinModelPortal; O57409; -.
DR   SMR; O57409; -.
DR   STRING; 7955.ENSDARP00000021660; -.
DR   PaxDb; O57409; -.
DR   PRIDE; 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   eggNOG; ENOG410XP6K; LUCA.
DR   GeneTree; ENSGT00940000164418; -.
DR   HOGENOM; HOG000267024; -.
DR   HOVERGEN; HBG007139; -.
DR   InParanoid; O57409; -.
DR   KO; K06051; -.
DR   OrthoDB; 406049at2759; -.
DR   PhylomeDB; O57409; -.
DR   TreeFam; TF351835; -.
DR   PRO; PR:O57409; -.
DR   Proteomes; UP000000437; Chromosome 5.
DR   Bgee; ENSDARG00000004232; Expressed in 51 organ(s), highest expression level in cranial ganglion.
DR   ExpressionAtlas; O57409; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
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   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; 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     20       {ECO:0000255}.
FT   CHAIN        21    615       Delta-like protein B.
FT                                /FTId=PRO_0000007515.
FT   TOPO_DOM     21    522       Extracellular. {ECO:0000255}.
FT   TRANSMEM    523    543       Helical. {ECO:0000255}.
FT   TOPO_DOM    544    615       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      159    203       DSL. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00377}.
FT   DOMAIN      204    237       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      241    268       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      270    308       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      310    346       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      348    385       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      387    423       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      425    461       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      463    499       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    544    552       Poly-Arg.
FT   CARBOHYD    459    459       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    161    170       {ECO:0000250}.
FT   DISULFID    174    186       {ECO:0000250}.
FT   DISULFID    194    203       {ECO:0000250}.
FT   DISULFID    208    219       {ECO:0000250}.
FT   DISULFID    212    225       {ECO:0000250}.
FT   DISULFID    227    236       {ECO:0000250}.
FT   DISULFID    245    250       {ECO:0000250}.
FT   DISULFID    258    267       {ECO:0000250}.
FT   DISULFID    274    286       {ECO:0000250}.
FT   DISULFID    280    296       {ECO:0000250}.
FT   DISULFID    298    307       {ECO:0000250}.
FT   DISULFID    314    325       {ECO:0000250}.
FT   DISULFID    319    334       {ECO:0000250}.
FT   DISULFID    336    345       {ECO:0000250}.
FT   DISULFID    352    363       {ECO:0000250}.
FT   DISULFID    357    373       {ECO:0000250}.
FT   DISULFID    375    384       {ECO:0000250}.
FT   DISULFID    391    402       {ECO:0000250}.
FT   DISULFID    396    411       {ECO:0000250}.
FT   DISULFID    413    422       {ECO:0000250}.
FT   DISULFID    429    440       {ECO:0000250}.
FT   DISULFID    434    449       {ECO:0000250}.
FT   DISULFID    451    460       {ECO:0000250}.
FT   DISULFID    467    478       {ECO:0000250}.
FT   DISULFID    472    487       {ECO:0000250}.
FT   DISULFID    489    498       {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
//
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