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   27-MAR-2024, entry version 188.
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; 10090-ENSMUSP00000103951; -.
DR   ProteomicsDB; 279433; -. [O88516-1]
DR   ProteomicsDB; 279434; -. [O88516-2]
DR   ABCD; O88516; 8 sequenced antibodies.
DR   Antibodypedia; 30387; 619 antibodies from 32 providers.
DR   DNASU; 13389; -.
DR   Ensembl; ENSMUST00000108315.4; ENSMUSP00000103951.4; ENSMUSG00000003436.12. [O88516-2]
DR   GeneID; 13389; -.
DR   KEGG; mmu:13389; -.
DR   AGR; MGI:1096877; -.
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   OrthoDB; 5475408at2759; -.
DR   PhylomeDB; O88516; -.
DR   TreeFam; TF351835; -.
DR   BioGRID-ORCS; 13389; 3 hits in 79 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 95 other cell types or tissues.
DR   ExpressionAtlas; O88516; baseline and differential.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
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; IBA:GO_Central.
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   CDD; cd00054; EGF_CA; 5.
DR   Gene3D; 2.60.40.3510; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 6.
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   InterPro; IPR011651; Notch_ligand_N.
DR   PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 3.
DR   Pfam; PF12661; hEGF; 2.
DR   Pfam; PF07657; MNNL; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 6.
DR   Genevisible; O88516; MM.
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
//