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Database: UniProt
Entry: A0A2Y9MDP4_DELLE
LinkDB: A0A2Y9MDP4_DELLE
Original site: A0A2Y9MDP4_DELLE 
ID   A0A2Y9MDP4_DELLE        Unreviewed;       722 AA.
AC   A0A2Y9MDP4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN   Name=DLL1 {ECO:0000313|RefSeq:XP_022417182.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022417182.1};
RN   [1] {ECO:0000313|RefSeq:XP_022417182.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022417182.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC       signaling. {ECO:0000256|RuleBase:RU280815}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU280815}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU280815}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   RefSeq; XP_022417182.1; XM_022561474.2.
DR   AlphaFoldDB; A0A2Y9MDP4; -.
DR   Ensembl; ENSDLET00000015064; ENSDLEP00000013636; ENSDLEG00000010013.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005112; F:Notch binding; IEA:Ensembl.
DR   GO; GO:0048018; F:receptor ligand activity; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0030957; F:Tat protein binding; IEA:Ensembl.
DR   GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR   GO; GO:0021688; P:cerebellar molecular layer formation; IEA:Ensembl.
DR   GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; IEA:Ensembl.
DR   GO; GO:0007386; P:compartment pattern specification; IEA:Ensembl.
DR   GO; GO:0097102; P:endothelial tip cell fate specification; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR   GO; GO:0002085; P:inhibition of neuroepithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IEA:Ensembl.
DR   GO; GO:0046331; P:lateral inhibition; IEA:Ensembl.
DR   GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR   GO; GO:0072070; P:loop of Henle development; IEA:Ensembl.
DR   GO; GO:0002315; P:marginal zone B cell differentiation; IEA:Ensembl.
DR   GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
DR   GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0045611; P:negative regulation of hemocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045608; P:negative regulation of inner ear auditory receptor cell differentiation; IEA:Ensembl.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR   GO; GO:0060563; P:neuroepithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0048665; P:neuron fate specification; IEA:Ensembl.
DR   GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0060853; P:Notch signaling pathway involved in arterial endothelial cell fate commitment; IEA:Ensembl.
DR   GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IEA:Ensembl.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0072014; P:proximal tubule development; IEA:Ensembl.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
DR   GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0014807; P:regulation of somitogenesis; IEA:Ensembl.
DR   GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR   GO; GO:0048630; P:skeletal muscle tissue growth; IEA:Ensembl.
DR   GO; GO:0098773; P:skin epidermis development; IEA:Ensembl.
DR   GO; GO:0001757; P:somite specification; IEA:Ensembl.
DR   GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR   GO; GO:0003323; P:type B pancreatic cell development; IEA:Ensembl.
DR   CDD; cd00054; EGF_CA; 6.
DR   Gene3D; 2.10.25.140; -; 1.
DR   Gene3D; 2.60.40.3510; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 7.
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   InterPro; IPR011651; Notch_ligand_N.
DR   PANTHER; PTHR24044:SF380; DELTA-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR   Pfam; PF21700; DL-JAG_EGF-like; 1.
DR   Pfam; PF01414; DSL; 1.
DR   Pfam; PF00008; EGF; 4.
DR   Pfam; PF12661; hEGF; 2.
DR   Pfam; PF07657; MNNL; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 6.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 1.
PE   4: Predicted;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW   ECO:0000256|RuleBase:RU280815};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280815};
KW   Transmembrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..722
FT                   /note="Delta-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016181874"
FT   TRANSMEM        543..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..221
FT                   /note="DSL"
FT                   /evidence="ECO:0000259|PROSITE:PS51051"
FT   DOMAIN          288..326
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          328..364
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          366..403
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          405..441
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          443..479
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          481..517
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          578..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..696
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        179..188
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        192..204
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        212..221
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        316..325
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        354..363
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        393..402
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        431..440
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        469..478
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        507..516
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   722 AA;  77689 MW;  8A56927CBC419C66 CRC64;
     MGRRCALALA VLSALLCQVW SSGVFELKLQ EFVNKKGLLG NRNCCRGGAG PPPCACRTFF
     RVCLKHYQAS VSPEPPCTYG STVTPVLGVD SFSLPDGAGA DTAFSNPIRF PFGFTWPGTF
     SLIIEALHSD SPDDLATENP ERLISRLATQ RHLTVGEEWS QDLHSSGRTD LKYSYRFVCD
     EHYYGEGCSV FCRPRDDAFG HFTCGERGEK VCNPGWKGQY CTEPICLPGC DEQHGFCDKP
     GECKCRVGWQ GRYCDQCIRY PGCLHGTCQQ PWQCNCQEGW GGLFCNQDLN YCTHHKPCKN
     GATCTNTGQG SYTCSCRPGY TGANCETEVD ECSASPCRNG GSCTDLENSY SCTCPPGFYG
     RICELSAMVC ADGPCFNGGR CSDNPKGGYT CRCPGGFSGF NCEKKMDSCS SSPCSNGAQC
     VDLGDAYVCR CQAGFSGRHC DDSVDDCASS PCANGGTCRD GVNEYSCTCP PGYTGTNCSA
     PVSRCEHAPC HNGATCHERA LRYLCECARG YGGPNCQFLL PELPPGPVVV DLTEKYVEGQ
     AGAFPWVAVG AGAVLVLTLL LGCAAAVVCV RLRLQKRRPP ADPCPGEAET MNNLANRRRE
     KDISVSVIGA TQIKNTNKKV DLHTEPGTEK NSLKACDPAV GYNLLQDLKG AAASGEPHSK
     RDAKSQPQGS AGEEKSAPTL RGGEAAERKR PDSVYSTSKD TKYQSVYVIS EEKDECVIAT
     EV
//
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