DLL3_MOUSE
ID DLL3_MOUSE Reviewed; 592 AA.
AC O88516; O35675; Q80W06; Q9QWL9; Q9QWZ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Delta-like protein 3;
DE AltName: Full=Drosophila Delta homolog 3;
DE Short=Delta3;
DE Short=M-Delta-3;
DE Flags: Precursor;
GN Name=Dll3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6 X DBA; TISSUE=Embryo;
RX PubMed=9272948; DOI=10.1242/dev.124.16.3065;
RA Dunwoodie S.L., Henrique D.M.P., Harrison S.M., Beddington R.S.P.;
RT "Mouse Dll3: a novel divergent Delta gene which may complement the function
RT of other Delta homologues during early pattern formation in the mouse
RT embryo.";
RL Development 124:3065-3076(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND INVOLVEMENT IN
RP PU.
RC STRAIN=129/SvJ;
RX PubMed=9662403; DOI=10.1038/961;
RA Kusumi K., Sun E.S., Kerrebrock A.W., Bronson R.T., Chi D.-C.,
RA Bulotsky M.S., Spencer J.B., Birren B.W., Frankel W.N., Lander E.S.;
RT "The mouse pudgy mutation disrupts Delta homologue Dll3 and initiation of
RT early somite boundaries.";
RL Nat. Genet. 19:274-278(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Neural tube;
RA Nakayama K., Nakayama N., Tomooka Y., Hayashi Y., Takahashi M.;
RT "Specific expression of a divergent type of Delta in a set of earliest
RT generated neurons including the prospective subplate neurons.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Inhibits primary neurogenesis. May be required to divert
CC neurons along a specific differentiation pathway. Plays a role in the
CC formation of somite boundaries during segmentation of the paraxial
CC mesoderm.
CC -!- SUBUNIT: Can bind and activate Notch-1 or another Notch receptor.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=O88516-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O88516-2; Sequence=VSP_001376;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the neuroectoderm and
CC paraxial mesoderm during embryogenesis.
CC -!- DOMAIN: The DSL domain is required for binding to the Notch receptor.
CC -!- PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis
CC and subsequent degradation. {ECO:0000250}.
CC -!- DISEASE: Note=A truncating mutation in Dll3 is the cause of the pudgy
CC (pu) phenotype. Pudgy mice exhibit patterning defects at the earliest
CC stages of somitogenesis. Adult pudgy mice present severe vertebral and
CC rib deformities. {ECO:0000269|PubMed:9662403}.
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DR EMBL; AF068865; AAC40170.1; -; Genomic_DNA.
DR EMBL; AF068865; AAC40169.1; -; Genomic_DNA.
DR EMBL; Y11895; CAA72637.1; -; mRNA.
DR EMBL; AB013440; BAA33716.1; -; mRNA.
DR EMBL; BC052002; AAH52002.1; -; mRNA.
DR CCDS; CCDS39856.1; -. [O88516-2]
DR RefSeq; NP_031892.2; NM_007866.2. [O88516-2]
DR AlphaFoldDB; O88516; -.
DR SMR; O88516; -.
DR BioGRID; 199233; 1.
DR STRING; 10090.ENSMUSP00000103951; -.
DR PhosphoSitePlus; O88516; -.
DR MaxQB; O88516; -.
DR PaxDb; O88516; -.
DR PRIDE; O88516; -.
DR ProteomicsDB; 279433; -. [O88516-1]
DR ProteomicsDB; 279434; -. [O88516-2]
DR ABCD; O88516; 8 sequenced antibodies.
DR Antibodypedia; 30387; 281 antibodies from 32 providers.
DR DNASU; 13389; -.
DR Ensembl; ENSMUST00000108315; ENSMUSP00000103951; ENSMUSG00000003436. [O88516-2]
DR GeneID; 13389; -.
DR KEGG; mmu:13389; -.
DR CTD; 10683; -.
DR MGI; MGI:1096877; Dll3.
DR VEuPathDB; HostDB:ENSMUSG00000003436; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000162127; -.
DR HOGENOM; CLU_033244_0_0_1; -.
DR InParanoid; O88516; -.
DR OMA; WSHPEDG; -.
DR PhylomeDB; O88516; -.
DR TreeFam; TF351835; -.
DR BioGRID-ORCS; 13389; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Dll3; mouse.
DR PRO; PR:O88516; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O88516; protein.
DR Bgee; ENSMUSG00000003436; Expressed in presomitic mesoderm and 92 other tissues.
DR ExpressionAtlas; O88516; baseline and differential.
DR Genevisible; O88516; MM.
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:0005112; F:Notch binding; ISO:MGI.
DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR GO; GO:0007386; P:compartment pattern specification; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; NAS:UniProtKB.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IDA:MGI.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; NAS:UniProtKB.
DR GO; GO:0048339; P:paraxial mesoderm development; IMP:MGI.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IDA:MGI.
DR GO; GO:0009888; P:tissue development; IDA:MGI.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF12661; hEGF; 2.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Membrane; Notch signaling pathway;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..592
FT /note="Delta-like protein 3"
FT /id="PRO_0000007510"
FT TOPO_DOM 33..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 174..213
FT /note="DSL"
FT DOMAIN 214..247
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 272..308
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 310..349
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 351..387
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 389..425
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 427..463
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 548..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 218..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 222..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 237..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 276..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 281..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 298..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 314..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 319..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 339..348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 355..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 360..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 377..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 393..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 398..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 415..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 431..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 436..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 453..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 585..592
FT /note="DWLIQVLF -> A (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9272948, ECO:0000303|Ref.3"
FT /id="VSP_001376"
FT CONFLICT 94
FT /note="E -> K (in Ref. 3; BAA33716)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="G -> A (in Ref. 1; CAA72637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 62069 MW; 1A84F8022E7E7DCC CRC64;
MVSLQVSPLS QTLILAFLLP QALPAGVFEL QIHSFGPGPG LGTPRSPCNA RGPCRLFFRV
CLKPGVSQEA TESLCALGAA LSTSVPVYTE HPGESAAALP LPDGLVRVPF RDAWPGTFSL
VIETWREQLG EHAGGPAWNL LARVVGRRRL AAGGPWARDV QRTGTWELHF SYRARCEPPA
VGAACARLCR SRSAPSRCGP GLRPCTPFPD ECEAPSVCRP GCSPEHGYCE EPDECRCLEG
WTGPLCTVPV STSSCLNSRV PGPASTGCLL PGPGPCDGNP CANGGSCSET SGSFECACPR
GFYGLRCEVS GVTCADGPCF NGGLCVGGED PDSAYVCHCP PGFQGSNCEK RVDRCSLQPC
QNGGLCLDLG HALRCRCRAG FAGPRCEHDL DDCAGRACAN GGTCVEGGGS RRCSCALGFG
GRDCRERADP CASRPCAHGG RCYAHFSGLV CACAPGYMGV RCEFAVRPDG ADAVPAAPRG
LRQADPQRFL LPPALGLLVA AGLAGAALLV IHVRRRGPGQ DTGTRLLSGT REPSVHTLPD
ALNNLRLQDG AGDGPSSSAD WNHPEDGDSR SIYVIPAPSI YAREDWLIQV LF
