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Delta-like protein 1 (Drosophila Delta homolog 1) (Delta1) [Cleaved into: Dll1-soluble form (Dll1-EC) (Shed form); Dll1-derived cell-associated form (Dll1-TMIC) (Membrane-associated fragment); Dll1-intracellular form (Dll1-IC)]

 DLL1_MOUSE              Reviewed;         722 AA.
Q61483; Q6PFV7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 166.
RecName: Full=Delta-like protein 1 {ECO:0000305};
AltName: Full=Drosophila Delta homolog 1;
Short=Delta1 {ECO:0000303|PubMed:12794186};
Contains:
RecName: Full=Dll1-soluble form {ECO:0000303|PubMed:12794186};
Short=Dll1-EC {ECO:0000305|PubMed:12794186};
Short=Shed form {ECO:0000303|PubMed:12794186};
Contains:
RecName: Full=Dll1-derived cell-associated form {ECO:0000303|PubMed:12794186};
Short=Dll1-TMIC {ECO:0000305|PubMed:12794186};
Short=Membrane-associated fragment {ECO:0000303|PubMed:12794186};
Contains:
RecName: Full=Dll1-intracellular form {ECO:0000303|PubMed:12794186};
Short=Dll1-IC {ECO:0000305|PubMed:12794186};
Flags: Precursor;
Name=Dll1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
AND FUNCTION.
STRAIN=C57BL/6 X BALB/c; TISSUE=Embryo;
PubMed=7671806;
Bettenhausen B., de Angelis M.H., Simon D., Guenet J.-L., Gossler A.;
"Transient and restricted expression during mouse embryogenesis of
Dll1, a murine gene closely related to Drosophila Delta.";
Development 121:2407-2418(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 527-534 AND 536-543, PROTEOLYTIC CLEAVAGE BY
MMP14, INTERACTION WITH MMP14, IDENTIFICATION BY MASS SPECTROMETRY,
AND FUNCTION.
PubMed=21572390; DOI=10.1038/emboj.2011.136;
Jin G., Zhang F., Chan K.M., Xavier Wong H.L., Liu B., Cheah K.S.,
Liu X., Mauch C., Liu D., Zhou Z.;
"MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to
maintain normal B-cell development.";
EMBO J. 30:2281-2293(2011).
[6]
PROTEIN SEQUENCE OF 536-554, PROTEOLYTIC CLEAVAGE, HOMODIMERIZATION,
INTERACTION WITH PSEN1, AND SUBCELLULAR LOCATION.
PubMed=12794186; DOI=10.1073/pnas.1230693100;
Six E., Ndiaye D., Laabi Y., Brou C., Gupta-Rossi N., Israel A.,
Logeat F.;
"The Notch ligand Delta1 is sequentially cleaved by an ADAM protease
and gamma-secretase.";
Proc. Natl. Acad. Sci. U.S.A. 100:7638-7643(2003).
[7]
FUNCTION.
PubMed=10958687; DOI=10.1128/MCB.20.18.6913-6922.2000;
Shimizu K., Chiba S., Hosoya N., Kumano K., Saito T., Kurokawa M.,
Kanda Y., Hamada Y., Hirai H.;
"Binding of Delta1, Jagged1, and Jagged2 to Notch2 rapidly induces
cleavage, nuclear translocation, and hyperphosphorylation of Notch2.";
Mol. Cell. Biol. 20:6913-6922(2000).
[8]
FUNCTION.
PubMed=15146182; DOI=10.1038/ni1075;
Hozumi K., Negishi N., Suzuki D., Abe N., Sotomaru Y., Tamaoki N.,
Mailhos C., Ish-Horowicz D., Habu S., Owen M.J.;
"Delta-like 1 is necessary for the generation of marginal zone B cells
but not T cells in vivo.";
Nat. Immunol. 5:638-644(2004).
[9]
INTERACTION WITH MFAP5.
PubMed=15788413; DOI=10.1074/jbc.M500273200;
Nehring L.C., Miyamoto A., Hein P.W., Weinmaster G., Shipley J.M.;
"The extracellular matrix protein MAGP-2 interacts with Jagged1 and
induces its shedding from the cell surface.";
J. Biol. Chem. 280:20349-20355(2005).
[10]
INTERACTION WITH MAGI1, AND SUBCELLULAR LOCATION.
PubMed=15908431; DOI=10.1074/jbc.M500375200;
Mizuhara E., Nakatani T., Minaki Y., Sakamoto Y., Ono Y., Takai Y.;
"MAGI1 recruits Dll1 to cadherin-based adherens junctions and
stabilizes it on the cell surface.";
J. Biol. Chem. 280:26499-26507(2005).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16495313; DOI=10.1242/dev.02284;
Brooker R., Hozumi K., Lewis J.;
"Notch ligands with contrasting functions: Jagged1 and Delta1 in the
mouse inner ear.";
Development 133:1277-1286(2006).
[12]
INTERACTION WITH NEURL1B, AND UBIQUITINATION.
PubMed=17003037; DOI=10.1074/jbc.M606601200;
Song R., Koo B.-K., Yoon K.-J., Yoon M.-J., Yoo K.-W., Kim H.-T.,
Oh H.-J., Kim Y.-Y., Han J.-K., Kim C.-H., Kong Y.-Y.;
"Neuralized-2 regulates a Notch ligand in cooperation with Mind bomb-
1.";
J. Biol. Chem. 281:36391-36400(2006).
[13]
DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17194759; DOI=10.1073/pnas.0608281104;
Schuster-Gossler K., Cordes R., Gossler A.;
"Premature myogenic differentiation and depletion of progenitor cells
cause severe muscle hypotrophy in Delta1 mutants.";
Proc. Natl. Acad. Sci. U.S.A. 104:537-542(2007).
[14]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=18997111; DOI=10.1242/dev.024570;
Kawaguchi D., Yoshimatsu T., Hozumi K., Gotoh Y.;
"Selection of differentiating cells by different levels of delta-like
1 among neural precursor cells in the developing mouse
telencephalon.";
Development 135:3849-3858(2008).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17960184; DOI=10.1038/sj.jid.5701113;
Estrach S., Cordes R., Hozumi K., Gossler A., Watt F.M.;
"Role of the Notch ligand Delta1 in embryonic and adult mouse
epidermis.";
J. Invest. Dermatol. 128:825-832(2008).
[16]
UBIQUITINATION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18676613; DOI=10.1073/pnas.0800695105;
Heuss S.F., Ndiaye-Lobry D., Six E.M., Israel A., Logeat F.;
"The intracellular region of Notch ligands Dll1 and Dll3 regulates
their trafficking and signaling activity.";
Proc. Natl. Acad. Sci. U.S.A. 105:11212-11217(2008).
[17]
INTERACTION WITH NEURL1 AND NEURL1B.
PubMed=19723503; DOI=10.1016/j.bbrc.2009.08.147;
Rullinkov G., Tamme R., Sarapuu A., Lauren J., Sepp M., Palm K.,
Timmusk T.;
"Neuralized-2: Expression in human and rodents and interaction with
Delta-like ligands.";
Biochem. Biophys. Res. Commun. 389:420-425(2009).
[18]
DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19144989; DOI=10.1182/blood-2008-08-174508;
Soerensen I., Adams R.H., Gossler A.;
"DLL1-mediated Notch activation regulates endothelial identity in
mouse fetal arteries.";
Blood 113:5680-5688(2009).
[19]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=19389377; DOI=10.1016/j.ydbio.2009.01.011;
Rocha S.F., Lopes S.S., Gossler A., Henrique D.;
"Dll1 and Dll4 function sequentially in the retina and pV2 domain of
the spinal cord to regulate neurogenesis and create cell diversity.";
Dev. Biol. 328:54-65(2009).
[20]
FUNCTION.
PubMed=19217325; DOI=10.1016/j.immuni.2008.12.016;
Tan J.B., Xu K., Cretegny K., Visan I., Yuan J.S., Egan S.E.,
Guidos C.J.;
"Lunatic and manic fringe cooperatively enhance marginal zone B cell
precursor competition for delta-like 1 in splenic endothelial
niches.";
Immunity 30:254-263(2009).
[21]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19562077; DOI=10.1371/journal.pone.0006054;
Rubio-Aliaga I., Przemeck G.K., Fuchs H., Gailus-Durner V., Adler T.,
Hans W., Horsch M., Rathkolb B., Rozman J., Schrewe A., Wagner S.,
Hoelter S.M., Becker L., Klopstock T., Wurst W., Wolf E.,
Klingenspor M., Ivandic B.T., Busch D.H., Beckers J.,
Hrabe de Angelis M.;
"Dll1 haploinsufficiency in adult mice leads to a complex phenotype
affecting metabolic and immunological processes.";
PLoS ONE 4:E6054-E6054(2009).
[22]
FUNCTION.
PubMed=20081190; DOI=10.1242/dev.036806;
Marklund U., Hansson E.M., Sundstroem E., de Angelis M.H.,
Przemeck G.K., Lendahl U., Muhr J., Ericson J.;
"Domain-specific control of neurogenesis achieved through patterned
regulation of Notch ligand expression.";
Development 137:437-445(2010).
[23]
MUTAGENESIS OF 613-LYS--LYS-618; LYS-613; LYS-689; LYS-699 AND
LYS-713, INTERACTION WITH MIB1, SUBCELLULAR LOCATION, FUNCTION, AND
UBIQUITINATION AT LYS-613.
PubMed=21985982; DOI=10.1016/j.bbamcr.2011.08.019;
Zhang L., Widau R.C., Herring B.P., Gallagher P.J.;
"Delta-like 1-Lysine613 regulates notch signaling.";
Biochim. Biophys. Acta 1813:2036-2043(2011).
[24]
FUNCTION.
PubMed=21238454; DOI=10.1053/j.gastro.2011.01.005;
Pellegrinet L., Rodilla V., Liu Z., Chen S., Koch U., Espinosa L.,
Kaestner K.H., Kopan R., Lewis J., Radtke F.;
"Dll1- and dll4-mediated notch signaling are required for homeostasis
of intestinal stem cells.";
Gastroenterology 140:1230-1240(2011).
[25]
FUNCTION.
PubMed=21915337; DOI=10.1371/journal.pone.0024484;
Stamataki D., Holder M., Hodgetts C., Jeffery R., Nye E.,
Spencer-Dene B., Winton D.J., Lewis J.;
"Delta1 expression, cell cycle exit, and commitment to a specific
secretory fate coincide within a few hours in the mouse intestinal
stem cell system.";
PLoS ONE 6:E24484-E24484(2011).
[26]
FUNCTION.
PubMed=22282195; DOI=10.1161/CIRCRESAHA.111.263319;
Napp L.C., Augustynik M., Paesler F., Krishnasamy K., Woiterski J.,
Limbourg A., Bauersachs J., Drexler H., Le Noble F., Limbourg F.P.;
"Extrinsic Notch ligand Delta-like 1 regulates tip cell selection and
vascular branching morphogenesis.";
Circ. Res. 110:530-535(2012).
[27]
FUNCTION, AND INDUCTION.
PubMed=22096075; DOI=10.1242/dev.071761;
Ahnfelt-Roenne J., Joergensen M.C., Klinck R., Jensen J.N.,
Fuechtbauer E.M., Deering T., MacDonald R.J., Wright C.V.,
Madsen O.D., Serup P.;
"Ptf1a-mediated control of Dll1 reveals an alternative to the lateral
inhibition mechanism.";
Development 139:33-45(2012).
[28]
INDUCTION.
PubMed=22015720; DOI=10.1016/j.ydbio.2011.09.034;
Grainger S., Lam J., Savory J.G., Mears A.J., Rijli F.M., Lohnes D.;
"Cdx regulates Dll1 in multiple lineages.";
Dev. Biol. 361:1-11(2012).
[29]
FUNCTION.
PubMed=22940113; DOI=10.1016/j.devcel.2012.07.014;
Broehl D., Vasyutina E., Czajkowski M.T., Griger J., Rassek C.,
Rahn H.P., Purfuerst B., Wende H., Birchmeier C.;
"Colonization of the satellite cell niche by skeletal muscle
progenitor cells depends on Notch signals.";
Dev. Cell 23:469-481(2012).
[30]
FUNCTION.
PubMed=22529374; DOI=10.1073/pnas.1203605109;
Horn S., Kobberup S., Joergensen M.C., Kalisz M., Klein T.,
Kageyama R., Gegg M., Lickert H., Lindner J., Magnuson M.A.,
Kong Y.Y., Serup P., Ahnfelt-Roenne J., Jensen J.N.;
"Mind bomb 1 is required for pancreatic beta-cell formation.";
Proc. Natl. Acad. Sci. U.S.A. 109:7356-7361(2012).
[31]
FUNCTION.
PubMed=23806616; DOI=10.1016/j.devcel.2013.05.022;
Liu Z., Chen S., Boyle S., Zhu Y., Zhang A., Piwnica-Worms D.R.,
Ilagan M.X., Kopan R.;
"The extracellular domain of Notch2 increases its cell-surface
abundance and ligand responsiveness during kidney development.";
Dev. Cell 25:585-598(2013).
[32]
FUNCTION.
PubMed=23699523; DOI=10.1523/JNEUROSCI.0791-13.2013;
Nelson B.R., Hodge R.D., Bedogni F., Hevner R.F.;
"Dynamic interactions between intermediate neurogenic progenitors and
radial glia in embryonic mouse neocortex: potential role in Dll1-Notch
signaling.";
J. Neurosci. 33:9122-9139(2013).
[33]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=23688253; DOI=10.1186/1756-6606-6-25;
Hiraoka Y., Komine O., Nagaoka M., Bai N., Hozumi K., Tanaka K.;
"Delta-like 1 regulates Bergmann glial monolayer formation during
cerebellar development.";
Mol. Brain 6:25-25(2013).
[34]
FUNCTION.
PubMed=23695674; DOI=10.1038/ncomms2895;
Kawaguchi D., Furutachi S., Kawai H., Hozumi K., Gotoh Y.;
"Dll1 maintains quiescence of adult neural stem cells and segregates
asymmetrically during mitosis.";
Nat. Commun. 4:1880-1880(2013).
[35]
INTERACTION WITH TJP1, AND SUBCELLULAR LOCATION.
PubMed=24715457; DOI=10.1242/dev.102988;
Hatakeyama J., Wakamatsu Y., Nagafuchi A., Kageyama R., Shigemoto R.,
Shimamura K.;
"Cadherin-based adhesions in the apical endfoot are required for
active Notch signaling to control neurogenesis in vertebrates.";
Development 141:1671-1682(2014).
[36]
FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=25220152; DOI=10.1016/j.ydbio.2014.09.005;
Czajkowski M.T., Rassek C., Lenhard D.C., Broehl D., Birchmeier C.;
"Divergent and conserved roles of Dll1 signaling in development of
craniofacial and trunk muscle.";
Dev. Biol. 395:307-316(2014).
[37]
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-638;
SER-693 AND SER-696, AND MUTAGENESIS OF THR-638; SER-693 AND SER-696.
PubMed=24449764; DOI=10.1128/MCB.00965-13;
Braune E.B., Schuster-Gossler K., Lyszkiewicz M., Serth K.,
Preusse K., Madlung J., Macek B., Krueger A., Gossler A.;
"S/T phosphorylation of DLL1 is required for full ligand activity in
vitro but dispensable for DLL1 function in vivo during embryonic
patterning and marginal zone B cell development.";
Mol. Cell. Biol. 34:1221-1233(2014).
[38]
FUNCTION.
PubMed=26114479; DOI=10.1371/journal.pgen.1005328;
Preusse K., Tveriakhina L., Schuster-Gossler K., Gaspar C., Rosa A.I.,
Henrique D., Gossler A., Stauber M.;
"Context-dependent functional divergence of the Notch ligands DLL1 and
DLL4 in vivo.";
PLoS Genet. 11:E1005328-E1005328(2015).
-!- FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and
NOTCH3 receptors that binds the extracellular domain (ECD) of
Notch receptor in a cis and trans fashion manner (PubMed:21985982,
PubMed:10958687). Following transinteraction, ligand cells produce
mechanical force that depends of a clathrin-mediated endocytosis,
requiring ligand ubiquitination, EPN1 interaction, and actin
polymerisation; these events promote Notch receptor extracellular
domain (NECD) transendocytosis and triggers Notch signaling
through induction of cleavage, hyperphosphorylation, and nuclear
accumulation of the intracellular domain of Notch receptors (NICD)
(PubMed:10958687, PubMed:18676613). Is required for embryonic
development and maintenance of adult stem cells in many different
tissues and immune systeme; the DLL1-induced Notch signaling is
mediated through an intercellular communication that regulates
cell lineage, cell specification, cell patterning and
morphogenesis through effects on differentiation and proliferation
(PubMed:17194759, PubMed:19562077, PubMed:18997111,
PubMed:23695674, PubMed:16495313, PubMed:21238454,
PubMed:22282195, PubMed:7671806, PubMed:17960184, PubMed:22529374,
PubMed:19389377, PubMed:23699523, PubMed:19144989,
PubMed:23688253, PubMed:23806616, PubMed:26114479,
PubMed:22940113, PubMed:25220152, PubMed:20081190,
PubMed:21572390, PubMed:22096075). Plays a role in brain
development at different level, namely by regulating neuronal
differentiation of neural precursor cells via cell-cell
interaction, most likely through the lateral inhibitory system in
an endogenous level dependent-manner (PubMed:7671806,
PubMed:18997111). During neocortex development, Dll1-Notch
signaling transmission is mediated by dynamic interactions between
intermediate neurogenic progenitors and radial glia; the cell-cell
interactions are mediated via dynamic and transient elongation
processes, likely to reactivate/maintain Notch activity in
neighboring progenitors, and coordinate progenitor cell division
and differentiation across radial and zonal boundaries
(PubMed:23699523). During cerebellar development, regulates
Bergmann glial monolayer formation and its morphological
maturation through a Notch signaling pathway (PubMed:23688253). At
the retina and spinal cord level, regulates neurogenesis by
preventing the premature differentiation of neural progenitors and
also by maintaining progenitors in spinal cord through Notch
signaling pathway (PubMed:19389377, PubMed:26114479). Also
controls neurogenesis of the neural tube in a progenitor domain-
specific fashion along the dorsoventral axis (PubMed:20081190).
Maintains quiescence of neural stem cells and plays a role as a
fate determinant that segregates asymmetrically to one daughter
cell during neural stem cells mitosis, resulting in neuronal
differentiation in Dll1-inheriting cell (PubMed:23695674). Plays a
role in immune systeme development, namely the development of all
T-cells and marginal zone (MZ) B cells (PubMed:15146182,
PubMed:19217325). Blocks the differentiation of progenitor cells
into the B-cell lineage while promoting the emergence of a
population of cells with the characteristics of a T-cell/NK-cell
precursor (By similarity). Upon MMP14 cleavage, negatively
regulates Notch signaling in haematopoietic progenitor cells to
specifically maintain normal B-cell development in bone marrow
(PubMed:21572390). Also plays a role during muscle development.
During early development, inhibits myoblasts differentiation from
the medial dermomyotomal lip and later regulates progenitor cell
differentiation (PubMed:17194759). Directly modulates cell
adhesion and basal lamina formation in satellite cells through
Notch signaling. Maintains myogenic progenitors pool by
suppressing differentiation through down-regulation of MYOD1 and
is required for satellite cell homing and PAX7 expression
(PubMed:22940113). During craniofacial and trunk myogenesis
suppresses differentiation of cranial mesoderm-derived and somite-
derived muscle via MYOD1 regulation but in cranial mesoderm-
derived progenitors, is neither required for satellite cell homing
nor for PAX7 expression (PubMed:25220152). Also plays a role
during pancreatic cell development. During type B pancreatic cell
development, may be involved in the initiation of proximodistal
patterning in the early pancreatic epithelium (PubMed:22529374).
Stimulates multipotent pancreatic progenitor cells proliferation
and pancreatic growth by maintaining HES1 expression and PTF1A
protein levels (PubMed:22096075). During fetal stages of
development, is required to maintain arterial identity and the
responsiveness of arterial endothelial cells for VEGFA through
regulation of KDR activation and NRP1 expression
(PubMed:19144989). Controls sprouting angiogenesis and subsequent
vertical branch formation througth regulation on tip cell
differentiation (PubMed:22282195). Negatively regulates goblet
cell differentiation in intestine and controls secretory fat
commitment through lateral inhibition in small intestine
(PubMed:21238454, PubMed:21915337). Plays a role during inner ear
development; negatively regulates auditory hair cell
differentiation (PubMed:16495313). Plays a role during nephron
development through Notch signaling pathway (PubMed:23806616).
Regulates growth, blood pressure and energy homeostasis
(PubMed:19562077). {ECO:0000250|UniProtKB:O00548,
ECO:0000250|UniProtKB:P97677, ECO:0000269|PubMed:10958687,
ECO:0000269|PubMed:15146182, ECO:0000269|PubMed:16495313,
ECO:0000269|PubMed:17194759, ECO:0000269|PubMed:17960184,
ECO:0000269|PubMed:18676613, ECO:0000269|PubMed:18997111,
ECO:0000269|PubMed:19144989, ECO:0000269|PubMed:19217325,
ECO:0000269|PubMed:19389377, ECO:0000269|PubMed:19562077,
ECO:0000269|PubMed:20081190, ECO:0000269|PubMed:21238454,
ECO:0000269|PubMed:21572390, ECO:0000269|PubMed:21915337,
ECO:0000269|PubMed:21985982, ECO:0000269|PubMed:22096075,
ECO:0000269|PubMed:22282195, ECO:0000269|PubMed:22529374,
ECO:0000269|PubMed:22940113, ECO:0000269|PubMed:23688253,
ECO:0000269|PubMed:23695674, ECO:0000269|PubMed:23699523,
ECO:0000269|PubMed:23806616, ECO:0000269|PubMed:25220152,
ECO:0000269|PubMed:26114479, ECO:0000269|PubMed:7671806}.
-!- SUBUNIT: Homodimer (PubMed:12794186). Interacts with TJP1
(PubMed:24715457). Interacts with MMP14; inhibits DLL1-induced
Notch signaling (PubMed:21572390). Interacts with MAGI1 (via PDZ
domain); forms a complex with CTNNB1 and CDH2 and promotes
recruitment to the adherens junction and stabilization on the cell
surface (PubMed:15908431). Interacts with PSEN1; undergoes a
presenilin-dependent gamma-secretase cleavage that releases a
Dll1-intracellular form (PubMed:12794186). Interacts with MFAP5
(PubMed:15788413). Interacts with MIB1 (PubMed:21985982).
Interacts with NEURL1B; leads to ubiquitination (PubMed:17003037,
PubMed:19723503). Interacts with NEURL1 (PubMed:19723503).
Interacts with SYNJ2BP; enhances DLL1 protein stability, and
promotes Notch signaling in endothelial cells (By similarity).
Interacts with MAGI1, MAGI2, MAGI3 and MPDZ (By similarity).
Interacts (via ubiquitin) with EPN1 (via IUM domain); binding with
NOTCH1 attached to neighboring cell, promotes ligand
ubiquitination and EPN1 interaction, leading to NECD
transendocytosis and Notch signaling (By similarity).
{ECO:0000250|UniProtKB:O00548, ECO:0000250|UniProtKB:P97677,
ECO:0000269|PubMed:12794186, ECO:0000269|PubMed:15788413,
ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:17003037,
ECO:0000269|PubMed:19723503, ECO:0000269|PubMed:21572390,
ECO:0000269|PubMed:21985982, ECO:0000269|PubMed:24715457}.
-!- INTERACTION:
Q9WVQ1:Magi2; NbExp=2; IntAct=EBI-297125, EBI-297151;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:24715457}; Single-pass type I membrane protein
{ECO:0000269|PubMed:24715457}. Cell junction, adherens junction
{ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:24715457}.
Membrane raft {ECO:0000269|PubMed:18676613,
ECO:0000269|PubMed:21985982}. Note=Distributed around adherens
junction in the apical endfeet through interactions with MAGI1.
{ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:24715457}.
-!- SUBCELLULAR LOCATION: Dll1-derived cell-associated form: Cell
membrane {ECO:0000269|PubMed:12794186}.
-!- SUBCELLULAR LOCATION: Dll1-intracellular form: Nucleus
{ECO:0000269|PubMed:12794186}.
-!- TISSUE SPECIFICITY: In the embryo, expressed in the paraxial
mesoderm and nervous system. Expressed at high levels in adult
heart and at lower levels, in adult lung. Highly expressed in
satellite cells from masseter and tongue than in satellite cells
from leg and extraocular muscle.? (PubMed:25220152).
{ECO:0000269|PubMed:25220152, ECO:0000269|PubMed:7671806}.
-!- DEVELOPMENTAL STAGE: Expressed until E15. Expression then
decreases and increases again in the adult. In differentiating
somites, is expressed at low levels in cells emerging from the
dorsomedial lip and subsequently throughout myotomes. In the limb
buds, is found in myoblasts and myocytes but not in the progenitor
cells (PubMed:17194759). Highly expressed in the endothelium and
in the smooth muscle layer starting at E13.5 in arterial vessels,
but not in veins. At E12.5, there is no detectable expression in
arteries or veins. This pattern persists until E18.5
(PubMed:19144989). Strongly expressed in developing muscle of
tongue, cheek, and in extraocular muscle at E11.5. Found at E18
and P21 in head muscle (PubMed:25220152). Detected in a subset of
cells in the ventricular zone (VZ), the intermediate zone (IZ) and
the cortical plate (CP) of neocortex and in the ganglionic
eminences at E13.5. At later stages, such as at E16.5, found in
the VZ and IZ, but at very low levels in the CP of the neocortex
(PubMed:18997111). Highly expressed in embryonic cells located in
the ventricular zone (VZ) of the retinal neuroepithelium that form
clusters; is first detected in cells located in the central
retina. As the retina grows, expression spreads peripherally along
the expanding neurogenic region, being always absent from the
ciliary margin zone (CMZ) (PubMed:19389377).
{ECO:0000269|PubMed:17194759, ECO:0000269|PubMed:18997111,
ECO:0000269|PubMed:19144989, ECO:0000269|PubMed:19389377,
ECO:0000269|PubMed:25220152, ECO:0000269|PubMed:7671806}.
-!- INDUCTION: Induced by PTF1A in multipotent pancreatic progenitor
cells (PubMed:22096075). Induced by CDX1 and CDX2 during
somitogenesis and goblet cell differentiation (PubMed:22015720).
{ECO:0000269|PubMed:22015720, ECO:0000269|PubMed:22096075}.
-!- PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its
endocytosis and subsequent degradation. Ubiquitinated; promotes
recycling back to the plasma membrane and confers a strong
affinity for NOTCH1 (PubMed:18676613). Multi-ubiquitination of
LYS-613 by MIB1 promotes both cis and trans-interaction with
NOTCH1, as well as activation of Notch signaling
(PubMed:21985982). Ubiquitinated by NEURL1B (PubMed:17003037).
{ECO:0000250|UniProtKB:P10041, ECO:0000269|PubMed:17003037,
ECO:0000269|PubMed:18676613, ECO:0000269|PubMed:21985982}.
-!- PTM: Phosphorylated in a membrane association-dependent manner.
Phosphorylation at Ser-696 requires the presence of Ser-693,
whereas phosphorylation at Thr-638 and Ser-693 occurs
independently of the other sites. Phosphorylation is required for
full ligand activity in vitro and affects surface presentation,
ectodomain shedding, and endocytosis.
{ECO:0000269|PubMed:24449764}.
-!- PTM: Cleaved by MMP14; negatively regulates DLL1-induced Notch
signaling in HPCs, modulating B-lymphocyte differentiation in bone
marrow (PubMed:21572390). Undergoes two consecutive processing
events: a shedding event, partially by ADAM10, that generates a
soluble extracellular form and an intracellular membrane-anchored
form, followed by a gamma-secretase cleavage releasing an
intracellular fragment (PubMed:12794186).
{ECO:0000269|PubMed:12794186, ECO:0000269|PubMed:21572390}.
-!- PTM: O-fucosylated. Can be elongated to a disaccharide by MFNG.
{ECO:0000250|UniProtKB:P97677}.
-!- DISRUPTION PHENOTYPE: Heterozygous Dll1 mice mutants are lighter
and smaller, with altered fat to lean ratio and have increased
blood pressure and a slight bradycardia. The animals have reduced
cholesterol and triglyceride levels in blood (PubMed:19562077).
Heterozygous Dll1 mice mutants and hypomorphic Dll1 mice mutants
survive until birth, despite significantly reduced Notch activity
(PubMed:17194759). Conditional knockout in inner ear leads to an
early and excessive production of hair cells and have vestibular
defects (PubMed:16495313). Conditional knockout in a small
proportion of neural precursor cells reduces neurogenesis, whereas
conditional knockout in a large proportion promotes premature
neurogenesis (PubMed:18997111). Hypomorph Dll1 pups mutant survive
until birth but are smaller. Conditional knockout Dll1 mice mutant
in epidermis, survive and have no gross abnormalities
(PubMed:17960184). Hypomorph Dll1 mice mutant survive until birth
and have severe skeletal muscle defects (PubMed:19144989).
Heterozygous Dll1 mutant embryos show disrupted muscle growth
(PubMed:25220152). Conditional knockout Dll1 mice mutant show
disorganization of Bergmann fibers, ectopic localization of
Bergmann glia in the molecular layer and a reduction in the number
of Bergmann glia (PubMed:23688253). {ECO:0000269|PubMed:16495313,
ECO:0000269|PubMed:17194759, ECO:0000269|PubMed:17960184,
ECO:0000269|PubMed:18997111, ECO:0000269|PubMed:19144989,
ECO:0000269|PubMed:19562077, ECO:0000269|PubMed:23688253,
ECO:0000269|PubMed:25220152}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X80903; CAA56865.1; -; mRNA.
EMBL; AY497019; AAR30869.1; -; Genomic_DNA.
EMBL; CH466630; EDL20466.1; -; Genomic_DNA.
EMBL; BC057400; AAH57400.1; -; mRNA.
EMBL; BC065063; AAH65063.1; -; mRNA.
CCDS; CCDS37452.1; -.
PIR; I48324; I48324.
RefSeq; NP_031891.2; NM_007865.3.
UniGene; Mm.4875; -.
ProteinModelPortal; Q61483; -.
SMR; Q61483; -.
BioGrid; 199232; 6.
DIP; DIP-32600N; -.
IntAct; Q61483; 4.
MINT; MINT-8187263; -.
STRING; 10090.ENSMUSP00000014917; -.
iPTMnet; Q61483; -.
PhosphoSitePlus; Q61483; -.
PaxDb; Q61483; -.
PRIDE; Q61483; -.
Ensembl; ENSMUST00000014917; ENSMUSP00000014917; ENSMUSG00000014773.
GeneID; 13388; -.
KEGG; mmu:13388; -.
UCSC; uc008aoi.2; mouse.
CTD; 28514; -.
MGI; MGI:104659; Dll1.
eggNOG; ENOG410IR7B; Eukaryota.
eggNOG; ENOG410XUNS; LUCA.
GeneTree; ENSGT00810000125346; -.
HOGENOM; HOG000267024; -.
HOVERGEN; HBG007139; -.
InParanoid; Q61483; -.
KO; K06051; -.
OMA; DKPCHQG; -.
OrthoDB; EOG091G07YQ; -.
TreeFam; TF351835; -.
Reactome; R-MMU-1980148; Signaling by NOTCH3.
Reactome; R-MMU-1980150; Signaling by NOTCH4.
Reactome; R-MMU-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
PMAP-CutDB; Q6PFV7; -.
PRO; PR:Q61483; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000014773; -.
CleanEx; MM_DLL1; -.
Genevisible; Q61483; MM.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
GO; GO:0030957; F:Tat protein binding; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
GO; GO:0014002; P:astrocyte development; IMP:UniProtKB.
GO; GO:0042491; P:auditory receptor cell differentiation; NAS:UniProtKB.
GO; GO:0009912; P:auditory receptor cell fate commitment; NAS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
GO; GO:0021688; P:cerebellar molecular layer formation; IMP:UniProtKB.
GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; IMP:UniProtKB.
GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
GO; GO:0007386; P:compartment pattern specification; IMP:MGI.
GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
GO; GO:0097102; P:endothelial tip cell fate specification; IMP:UniProtKB.
GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; NAS:UniProtKB.
GO; GO:0048839; P:inner ear development; IMP:MGI.
GO; GO:0042472; P:inner ear morphogenesis; NAS:UniProtKB.
GO; GO:0046331; P:lateral inhibition; IDA:UniProtKB.
GO; GO:0070986; P:left/right axis specification; IMP:BHF-UCL.
GO; GO:0072070; P:loop of Henle development; IEP:UniProtKB.
GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
GO; GO:0045608; P:negative regulation of auditory receptor cell differentiation; IMP:MGI.
GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0045605; P:negative regulation of epidermal cell differentiation; IMP:UniProtKB.
GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IMP:UniProtKB.
GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:MGI.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:0072006; P:nephron development; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
GO; GO:0048665; P:neuron fate specification; IDA:UniProtKB.
GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:UniProtKB.
GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
GO; GO:0061314; P:Notch signaling involved in heart development; IC:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IMP:UniProtKB.
GO; GO:0060853; P:Notch signaling pathway involved in arterial endothelial cell fate commitment; IMP:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; NAS:UniProtKB.
GO; GO:0035265; P:organ growth; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IMP:UniProtKB.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0072014; P:proximal tubule development; IEP:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; IMP:UniProtKB.
GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
GO; GO:0050767; P:regulation of neurogenesis; IMP:UniProtKB.
GO; GO:0048631; P:regulation of skeletal muscle tissue growth; IMP:UniProtKB.
GO; GO:0014807; P:regulation of somitogenesis; IMP:UniProtKB.
GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IMP:UniProtKB.
GO; GO:0060041; P:retina development in camera-type eye; IMP:UniProtKB.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:UniProtKB.
GO; GO:0048630; P:skeletal muscle tissue growth; IMP:UniProtKB.
GO; GO:0098773; P:skin epidermis development; IMP:UniProtKB.
GO; GO:0001757; P:somite specification; IMP:MGI.
GO; GO:0001756; P:somitogenesis; IMP:UniProtKB.
GO; GO:0021510; P:spinal cord development; IMP:UniProtKB.
GO; GO:0003323; P:type B pancreatic cell development; IMP:UniProtKB.
InterPro; IPR001774; DSL.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR011651; Notch_ligand_N.
Pfam; PF01414; DSL; 1.
Pfam; PF00008; EGF; 5.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF07657; MNNL; 1.
SMART; SM00051; DSL; 1.
SMART; SM00181; EGF; 8.
SMART; SM00179; EGF_CA; 6.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS51051; DSL; 1.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 7.
PROSITE; PS01187; EGF_CA; 2.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; EGF-like domain; Glycoprotein; Isopeptide bond;
Membrane; Notch signaling pathway; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 722 Delta-like protein 1.
/FTId=PRO_0000007507.
CHAIN 18 535 Dll1-soluble form.
{ECO:0000269|PubMed:12794186}.
/FTId=PRO_0000434830.
CHAIN 536 722 Dll1-derived cell-associated form.
{ECO:0000269|PubMed:12794186}.
/FTId=PRO_0000434831.
CHAIN ? 722 Dll1-intracellular form.
{ECO:0000269|PubMed:12794186}.
/FTId=PRO_0000434832.
TOPO_DOM 18 545 Extracellular. {ECO:0000255}.
TRANSMEM 546 568 Helical. {ECO:0000255}.
TOPO_DOM 569 722 Cytoplasmic. {ECO:0000255}.
DOMAIN 176 220 DSL. {ECO:0000255|PROSITE-
ProRule:PRU00377}.
DOMAIN 225 253 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 256 284 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 291 324 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 331 362 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 369 401 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 408 439 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 446 477 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 484 515 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 719 722 Interaction with MAGI1.
{ECO:0000269|PubMed:15908431}.
SITE 527 528 Cleavage; by MMP14.
{ECO:0000269|PubMed:21572390}.
SITE 535 536 Cleavage; by ADAM protease.
{ECO:0000269|PubMed:12794186}.
MOD_RES 638 638 Phosphothreonine.
{ECO:0000269|PubMed:24449764}.
MOD_RES 693 693 Phosphoserine; by PKB.
{ECO:0000269|PubMed:24449764}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000269|PubMed:24449764}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 178 187 {ECO:0000250}.
DISULFID 191 203 {ECO:0000250}.
DISULFID 211 220 {ECO:0000250}.
DISULFID 225 236 {ECO:0000250}.
DISULFID 229 242 {ECO:0000250}.
DISULFID 244 253 {ECO:0000250}.
DISULFID 256 267 {ECO:0000250}.
DISULFID 262 273 {ECO:0000250}.
DISULFID 275 284 {ECO:0000250}.
DISULFID 291 303 {ECO:0000250}.
DISULFID 297 313 {ECO:0000250}.
DISULFID 315 324 {ECO:0000250}.
DISULFID 331 342 {ECO:0000250}.
DISULFID 336 351 {ECO:0000250}.
DISULFID 353 362 {ECO:0000250}.
DISULFID 369 380 {ECO:0000250}.
DISULFID 374 390 {ECO:0000250}.
DISULFID 392 401 {ECO:0000250}.
DISULFID 408 419 {ECO:0000250}.
DISULFID 413 428 {ECO:0000250}.
DISULFID 430 439 {ECO:0000250}.
DISULFID 446 457 {ECO:0000250}.
DISULFID 451 466 {ECO:0000250}.
DISULFID 468 477 {ECO:0000250}.
DISULFID 484 495 {ECO:0000250}.
DISULFID 489 504 {ECO:0000250}.
DISULFID 506 515 {ECO:0000250}.
CROSSLNK 613 613 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21985982}.
MUTAGEN 613 618 KNTNKK->RNTNRR: Highly decreases Notch
signaling pathway. Multi-ubiquitination
pattern is reduced, although it does
appear to be mono-ubiquitinated.
Interacts with MIB1. Loss of cis
interaction with NOTCH1.
{ECO:0000269|PubMed:21985982}.
MUTAGEN 613 613 K->R: Highly decreases Notch signaling
pathway. Multi-ubiquitination pattern is
reduced, although it does appear to be
mono-ubiquitinated. Interacts with MIB1.
Loss of cis and trans interaction with
NOTCH1. Increases its association with
lipid raft microdomains.
{ECO:0000269|PubMed:21985982}.
MUTAGEN 638 638 T->V: Not phosphorylated; when associated
with A-693 and A-696. Not phosphorylated
and doesn't prevent phosphorylation at S-
693 and S-696. Reduces NOTCH1
transactivation; when associated with A-
693 and A-696. Reduces cell surface
levels of proteins; when associated with
A-693 and A-696. Increases ectodomain
shedding; when associated with A-693 and
A-696. {ECO:0000269|PubMed:24449764}.
MUTAGEN 689 689 K->R: Decreases Notch signaling pathway.
{ECO:0000269|PubMed:21985982}.
MUTAGEN 693 693 S->A: Not phosphorylated; when associated
with V-638 and A-696. Not phosphorylated
and prevents phosphorylation at S-696.
Reduces NOTCH1 transactivation; when
associated with V-638 and A-696. Reduces
cell surface levels of proteins; when
associated with V-638 and A-696.
Increases ectodomain shedding; when
associated with V-638 and A-696.
{ECO:0000269|PubMed:24449764}.
MUTAGEN 696 696 S->A: Not phosphorylated; when associated
with V-638 and A-693. Not phosphorylated
and doesn't prevent phosphorylation at T-
638 and S-693, Reduces NOTCH1
transactivation; when associated with V-
638 and A-693. Reduces cell surface
levels of proteins; when associated with
V-638 and A-693. Increases ectodomain
shedding; when associated with V-638 and
A-693. {ECO:0000269|PubMed:24449764}.
MUTAGEN 699 699 K->R: Decreases Notch signaling pathway.
{ECO:0000269|PubMed:21985982}.
MUTAGEN 713 713 K->R: Decreases Notch signaling pathway.
{ECO:0000269|PubMed:21985982}.
CONFLICT 628 628 E -> K (in Ref. 1; CAA56865).
{ECO:0000305}.
SEQUENCE 722 AA; 78449 MW; 9D570B9DC7EEC75E CRC64;
MGRRSALALA VVSALLCQVW SSGVFELKLQ EFVNKKGLLG NRNCCRGGSG PPCACRTFFR
VCLKHYQASV SPEPPCTYGS AVTPVLGVDS FSLPDGAGID PAFSNPIRFP FGFTWPGTFS
LIIEALHTDS PDDLATENPE RLISRLTTQR HLTVGEEWSQ DLHSSGRTDL RYSYRFVCDE
HYYGEGCSVF CRPRDDAFGH FTCGDRGEKM CDPGWKGQYC TDPICLPGCD DQHGYCDKPG
ECKCRVGWQG RYCDECIRYP GCLHGTCQQP WQCNCQEGWG GLFCNQDLNY CTHHKPCRNG
ATCTNTGQGS YTCSCRPGYT GANCELEVDE CAPSPCKNGA SCTDLEDSFS CTCPPGFYGK
VCELSAMTCA DGPCFNGGRC SDNPDGGYTC HCPLGFSGFN CEKKMDLCGS SPCSNGAKCV
DLGNSYLCRC QAGFSGRYCE DNVDDCASSP CANGGTCRDS VNDFSCTCPP GYTGKNCSAP
VSRCEHAPCH NGATCHQRGQ RYMCECAQGY GGPNCQFLLP EPPPGPMVVD LSERHMESQG
GPFPWVAVCA GVVLVLLLLL GCAAVVVCVR LKLQKHQPPP EPCGGETETM NNLANCQREK
DVSVSIIGAT QIKNTNKKAD FHGDHGAEKS SFKVRYPTVD YNLVRDLKGD EATVRDTHSK
RDTKCQSQSS AGEEKIAPTL RGGEIPDRKR PESVYSTSKD TKYQSVYVLS AEKDECVIAT
EV


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