ID DLL1_HUMAN Reviewed; 723 AA. AC O00548; B2RAK7; B5M0B3; Q9NU41; Q9UJV2; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 02-SEP-2026, entry version 219. DE RecName: Full=Delta-like protein 1 {ECO:0000305}; DE AltName: Full=Drosophila Delta homolog 1; DE Short=Delta1; DE Short=H-Delta-1; DE Flags: Precursor; GN Name=DLL1 {ECO:0000312|HGNC:HGNC:2908}; ORFNames=UNQ146/PRO172; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10079256; DOI=10.1016/s0002-9440(10)65325-4; RA Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L., Banks A., RA Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.; RT "Human ligands of the Notch receptor."; RL Am. J. Pathol. 154:785-794(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10688816; DOI=10.1182/blood.v95.5.1616.005k31_1616_1625; RA Han W., Ye Q., Moore M.A.S.; RT "A soluble form of human Delta-like-1 inhibits differentiation of RT hematopoietic progenitor cells."; RL Blood 95:1616-1625(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=19906316; DOI=10.1186/1471-2164-10-518; RA Wang P., Yu P., Gao P., Shi T., Ma D.; RT "Discovery of novel human transcript variants by analysis of intronic RT single-block EST with polyadenylation site."; RL BMC Genomics 10:518-518(2009). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Oda T., Chandrasekharappa S.C.; RT "Human Delta 1 gene sequence."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION. RX PubMed=11006133; DOI=10.1006/bbrc.2000.3469; RA Shimizu K., Chiba S., Saito T., Kumano K., Hirai H.; RT "Physical interaction of Delta1, Jagged1, and Jagged2 with Notch1 and RT Notch3 receptors."; RL Biochem. Biophys. Res. Commun. 276:385-389(2000). RN [10] RP FUNCTION. RX PubMed=11581320; DOI=10.1084/jem.194.7.991; RA Jaleco A.C., Neves H., Hooijberg E., Gameiro P., Clode N., Haury M., RA Henrique D., Parreira L.; RT "Differential effects of Notch ligands Delta-1 and Jagged-1 in human RT lymphoid differentiation."; RL J. Exp. Med. 194:991-1001(2001). RN [11] RP INTERACTION WITH MAGI1; MAGI2; MAGI3 AND MPDZ. RX PubMed=15509766; DOI=10.1242/dev.01417; RA Wright G.J., Leslie J.D., Ariza-McNaughton L., Lewis J.; RT "Delta proteins and MAGI proteins: an interaction of Notch ligands with RT intracellular scaffolding molecules and its significance for zebrafish RT development."; RL Development 131:5659-5669(2004). RN [12] RP INTERACTION WITH SYNJ2BP. RX PubMed=24025447; DOI=10.1161/circresaha.113.301686; RA Adam M.G., Berger C., Feldner A., Yang W.J., Wuestehube-Lausch J., RA Herberich S.E., Pinder M., Gesierich S., Hammes H.P., Augustin H.G., RA Fischer A.; RT "Synaptojanin-2 binding protein stabilizes the Notch ligands DLL1 and DLL4 RT and inhibits sprouting angiogenesis."; RL Circ. Res. 113:1206-1218(2013). RN [13] RP INTERACTION WITH NOTCH2NLB. RX PubMed=29856955; DOI=10.1016/j.cell.2018.03.067; RA Suzuki I.K., Gacquer D., Van Heurck R., Kumar D., Wojno M., Bilheu A., RA Herpoel A., Lambert N., Cheron J., Polleux F., Detours V., RA Vanderhaeghen P.; RT "Human-specific NOTCH2NL genes expand cortical neurogenesis through RT Delta/Notch regulation."; RL Cell 173:1370-1384(2018). RN [14] RP VARIANTS NEDBAS ILE-GLY-GLY-GLN-18 INS; 19-VAL--VAL-723 DEL; RP 77-CYS--VAL-723 DEL; PHE-179; 498-GLU--VAL-723 DEL AND 509-ARG--VAL-723 RP DEL. RX PubMed=31353024; DOI=10.1016/j.ajhg.2019.07.002; RA Fischer-Zirnsak B., Segebrecht L., Schubach M., Charles P., Alderman E., RA Brown K., Cadieux-Dion M., Cartwright T., Chen Y., Costin C., Fehr S., RA Fitzgerald K.M., Fleming E., Foss K., Ha T., Hildebrand G., Horn D., RA Liu S., Marco E.J., McDonald M., McWalter K., Race S., Rush E.T., Si Y., RA Saunders C., Slavotinek A., Stockler-Ipsiroglu S., Telegrafi A., RA Thiffault I., Torti E., Tsai A.C., Wang X., Zafar M., Keren B., Kornak U., RA Boerkoel C.F., Mirzaa G., Ehmke N.; RT "Haploinsufficiency of the Notch Ligand DLL1 Causes Variable RT Neurodevelopmental Disorders."; RL Am. J. Hum. Genet. 105:631-639(2019). CC -!- FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 CC receptors that binds the extracellular domain (ECD) of Notch receptor CC in a cis and trans fashion manner (PubMed:11006133). Following CC transinteraction, ligand cells produce mechanical force that depends of CC a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 CC interaction, and actin polymerization; these events promote Notch CC receptor extracellular domain (NECD) transendocytosis and triggers CC Notch signaling through induction of cleavage, hyperphosphorylation, CC and nuclear accumulation of the intracellular domain of Notch receptors CC (NICD) (By similarity). Is required for embryonic development and CC maintenance of adult stem cells in many different tissues and immune CC systeme; the DLL1-induced Notch signaling is mediated through an CC intercellular communication that regulates cell lineage, cell CC specification, cell patterning and morphogenesis through effects on CC differentiation and proliferation (PubMed:11581320). Plays a role in CC brain development at different level, namely by regulating neuronal CC differentiation of neural precursor cells via cell-cell interaction, CC most likely through the lateral inhibitory system in an endogenous CC level dependent-manner. During neocortex development, Dll1-Notch CC signaling transmission is mediated by dynamic interactions between CC intermediate neurogenic progenitors and radial glia; the cell-cell CC interactions are mediated via dynamic and transient elongation CC processes, likely to reactivate/maintain Notch activity in neighboring CC progenitors, and coordinate progenitor cell division and CC differentiation across radial and zonal boundaries. During cerebellar CC development, regulates Bergmann glial monolayer formation and its CC morphological maturation through a Notch signaling pathway. At the CC retina and spinal cord level, regulates neurogenesis by preventing the CC premature differentiation of neural progenitors and also by maintaining CC progenitors in spinal cord through Notch signaling pathway. Also CC controls neurogenesis of the neural tube in a progenitor domain- CC specific fashion along the dorsoventral axis. Maintains quiescence of CC neural stem cells and plays a role as a fate determinant that CC segregates asymmetrically to one daughter cell during neural stem cells CC mitosis, resulting in neuronal differentiation in Dll1-inheriting cell. CC Plays a role in immune systeme development, namely the development of CC all T-cells and marginal zone (MZ) B-cells (By similarity). Blocks the CC differentiation of progenitor cells into the B-cell lineage while CC promoting the emergence of a population of cells with the CC characteristics of a T-cell/NK-cell precursor (PubMed:11581320). Also CC plays a role during muscle development. During early development, CC inhibits myoblasts differentiation from the medial dermomyotomal lip CC and later regulates progenitor cell differentiation. Directly modulates CC cell adhesion and basal lamina formation in satellite cells through CC Notch signaling. Maintains myogenic progenitors pool by suppressing CC differentiation through down-regulation of MYOD1 and is required for CC satellite cell homing and PAX7 expression. During craniofacial and CC trunk myogenesis suppresses differentiation of cranial mesoderm-derived CC and somite-derived muscle via MYOD1 regulation but in cranial mesoderm- CC derived progenitors, is neither required for satellite cell homing nor CC for PAX7 expression. Also plays a role during pancreatic cell CC development. During type B pancreatic cell development, may be involved CC in the initiation of proximodistal patterning in the early pancreatic CC epithelium. Stimulates multipotent pancreatic progenitor cells CC proliferation and pancreatic growth by maintaining HES1 expression and CC PTF1A protein levels. During fetal stages of development, is required CC to maintain arterial identity and the responsiveness of arterial CC endothelial cells for VEGFA through regulation of KDR activation and CC NRP1 expression. Controls sprouting angiogenesis and subsequent CC vertical branch formation through regulation on tip cell CC differentiation. Negatively regulates goblet cell differentiation in CC intestine and controls secretory fat commitment through lateral CC inhibition in small intestine. Plays a role during inner ear CC development; negatively regulates auditory hair cell differentiation. CC Plays a role during nephron development through Notch signaling CC pathway. Regulates growth, blood pressure and energy homeostasis (By CC similarity). {ECO:0000250|UniProtKB:P97677, CC ECO:0000250|UniProtKB:Q61483, ECO:0000269|PubMed:11006133, CC ECO:0000269|PubMed:11581320}. CC -!- SUBUNIT: Homodimer. Interacts with TJP1. Interacts with MAGI1 (via PDZ CC domain); forms a complex with CTNNB1 and CDH2 and promotes recruitment CC to the adherens junction and stabilization on the cell surface. CC Interacts with PSEN1; undergoes a presenilin-dependent gamma-secretase CC cleavage that releases a Dll1-intracellular form. Interacts with MFAP5. CC Interacts with MIB1. Interacts with NEURL1B; leads to ubiquitination. CC Interacts with NEURL1 (By similarity). Interacts with SYNJ2BP; enhances CC DLL1 protein stability, and promotes Notch signaling in endothelial CC cells (PubMed:24025447). Interacts with MAGI1, MAGI2, MAGI3 and MPDZ CC (PubMed:15509766). Interacts (via ubiquitin) with EPN1 (via IUM CC domain); binding with NOTCH1 attached to neighboring cell, promotes CC ligand ubiquitination and EPN1 interaction, leading to NECD CC transendocytosis and Notch signaling. Interacts with NOTCH1 (By CC similarity) (PubMed:15509766, PubMed:24025447). Interacts with CC NOTCH2NLB; leading to promote Notch signaling pathway in a cell- CC autonomous manner through inhibition of cis DLL1-NOTCH2 interactions CC (PubMed:29856955). {ECO:0000250|UniProtKB:P97677, CC ECO:0000250|UniProtKB:Q61483, ECO:0000269|PubMed:15509766, CC ECO:0000269|PubMed:24025447, ECO:0000269|PubMed:29856955}. CC -!- INTERACTION: CC O00548; Q02410: APBA1; NbExp=2; IntAct=EBI-11699911, EBI-368690; CC O00548; Q99767: APBA2; NbExp=2; IntAct=EBI-11699911, EBI-81711; CC O00548; Q12959: DLG1; NbExp=2; IntAct=EBI-11699911, EBI-357481; CC O00548; Q92796: DLG3; NbExp=3; IntAct=EBI-11699911, EBI-80440; CC O00548; P78352: DLG4; NbExp=3; IntAct=EBI-11699911, EBI-80389; CC O00548; Q68DX3: FRMPD2; NbExp=3; IntAct=EBI-11699911, EBI-53993476; CC O00548; Q9Y3R0: GRIP1; NbExp=5; IntAct=EBI-11699911, EBI-5349621; CC O00548; Q9C0E4: GRIP2; NbExp=5; IntAct=EBI-11699911, EBI-949557; CC O00548; Q14005: IL16; NbExp=2; IntAct=EBI-11699911, EBI-2831580; CC O00548; Q8TBB1: LNX1; NbExp=2; IntAct=EBI-11699911, EBI-739832; CC O00548; Q8N448: LNX2; NbExp=2; IntAct=EBI-11699911, EBI-2340947; CC O00548; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-11699911, EBI-924464; CC O00548; Q86UL8: MAGI2; NbExp=4; IntAct=EBI-11699911, EBI-311035; CC O00548; O75970: MPDZ; NbExp=2; IntAct=EBI-11699911, EBI-821405; CC O00548; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-11699911, EBI-8744528; CC O00548; Q8NI35: PATJ; NbExp=6; IntAct=EBI-11699911, EBI-724390; CC O00548; Q5T2W1: PDZK1; NbExp=2; IntAct=EBI-11699911, EBI-349819; CC O00548; Q14160: SCRIB; NbExp=2; IntAct=EBI-11699911, EBI-357345; CC O00548; P57105: SYNJ2BP; NbExp=2; IntAct=EBI-11699911, EBI-1049004; CC O00548; Q07157: TJP1; NbExp=2; IntAct=EBI-11699911, EBI-79553; CC O00548; Q9P202: WHRN; NbExp=3; IntAct=EBI-11699911, EBI-310886; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000250|UniProtKB:Q61483}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q61483}. Cell junction, adherens junction CC {ECO:0000250|UniProtKB:Q61483}. Membrane raft CC {ECO:0000250|UniProtKB:Q61483}. Note=Distributed around adherens CC junction in the apical endfeet through interactions with MAGI1. CC {ECO:0000250|UniProtKB:Q61483}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00548-1; Sequence=Displayed; CC Name=2; CC IsoId=O00548-2; Sequence=VSP_057186, VSP_057187; CC -!- TISSUE SPECIFICITY: Expressed in heart and pancreas, with lower CC expression in brain and muscle and almost no expression in placenta, CC lung, liver and kidney. CC -!- PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis CC and subsequent degradation (By similarity). Ubiquitinated; promotes CC recycling back to the plasma membrane and confers a strong affinity for CC NOTCH1. Multi-ubiquitination of Lys-613 by MIB1 promotes both cis and CC trans-interaction with NOTCH1, as well as activation of Notch CC signaling. Ubiquitinated by NEURL1B (By similarity). CC {ECO:0000250|UniProtKB:P10041, ECO:0000250|UniProtKB:Q61483}. CC -!- PTM: Phosphorylated in a membrane association-dependent manner. CC Phosphorylation at Ser-697 requires the presence of Ser-694, whereas CC phosphorylation at Ser-694 occurs independently of the other site. CC Phosphorylation is required for full ligand activity in vitro and CC affects surface presentation, ectodomain shedding, and endocytosis. CC {ECO:0000250|UniProtKB:Q61483}. CC -!- PTM: O-fucosylated. Can be elongated to a disaccharide by MFNG. CC {ECO:0000250|UniProtKB:P97677}. CC -!- DISEASE: Neurodevelopmental disorder with non-specific brain CC abnormalities and with or without seizures (NEDBAS) [MIM:618709]: An CC autosomal dominant disorder characterized by developmental delay, CC intellectual disability, seizures, autism spectrum disorder, behavioral CC abnormalities, and variable non-specific brain malformations. CC {ECO:0000269|PubMed:31353024}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF003522; AAB61286.1; -; mRNA. DR EMBL; AF196571; AAF05834.1; -; mRNA. DR EMBL; EU927387; ACH57449.1; -; mRNA. DR EMBL; AF222310; AAG09716.1; -; Genomic_DNA. DR EMBL; AY358892; AAQ89251.1; -; mRNA. DR EMBL; AK314234; BAG36904.1; -; mRNA. DR EMBL; AL078605; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47425.1; -; Genomic_DNA. DR CCDS; CCDS5313.1; -. [O00548-1] DR RefSeq; NP_005609.3; NM_005618.4. [O00548-1] DR PDB; 4XBM; X-ray; 3.20 A; A/B=21-545. DR AlphaFoldDB; O00548; -. DR SMR; O00548; -. DR BioGRID; 118391; 25. DR CORUM; O00548; -. DR FunCoup; O00548; 227. DR IntAct; O00548; 95. DR NDEx; IQUERY-CP-DLL1; 21 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000355718; -. DR GlyCosmos; O00548; 1 site, No reported glycans. DR GlyGen; O00548; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; O00548; -. DR PhosphoSitePlus; O00548; -. DR BioMuta; DLL1; -. DR MassIVE; O00548; -. DR PaxDb; 9606-ENSP00000355718; -. DR PeptideAtlas; O00548; -. DR ProteomicsDB; 47965; -. [O00548-1] DR ABCD; O00548; 5 sequenced antibodies. DR Antibodypedia; 20091; 561 antibodies from 43 providers. DR DNASU; 28514; -. DR Ensembl; ENST00000366756.4; ENSP00000355718.3; ENSG00000198719.10. [O00548-1] DR Ensembl; ENST00000616526.2; ENSP00000480905.1; ENSG00000275555.2. [O00548-1] DR Ensembl; ENST00000876123.1; ENSP00000546182.1; ENSG00000198719.10. [O00548-1] DR Ensembl; ENST00000876124.1; ENSP00000546183.1; ENSG00000198719.10. [O00548-1] DR Ensembl; ENST00000876125.1; ENSP00000546184.1; ENSG00000198719.10. [O00548-1] DR Ensembl; ENST00000915772.1; ENSP00000585831.1; ENSG00000198719.10. [O00548-1] DR Ensembl; ENST00000915773.1; ENSP00000585832.1; ENSG00000198719.10. [O00548-1] DR Ensembl; ENST00000915774.1; ENSP00000585833.1; ENSG00000198719.10. [O00548-1] DR Ensembl; ENST00000966433.1; ENSP00000636492.1; ENSG00000198719.10. [O00548-1] DR GeneID; 28514; -. DR KEGG; hsa:28514; -. DR MANE-Select; ENST00000366756.4; ENSP00000355718.3; NM_005618.4; NP_005609.3. DR UCSC; uc003qxm.4; human. [O00548-1] DR AGR; HGNC:2908; -. DR ClinPGx; PA27364; -. DR CTD; 28514; -. DR DisGeNET; 28514; -. DR GeneCards; DLL1; -. DR GeneReviews; DLL1; -. DR HGNC; HGNC:2908; DLL1. DR HPA; ENSG00000198719; Tissue enhanced (lymphoid). DR MalaCards; DLL1; -. DR MIM; 606582; gene. DR MIM; 618709; phenotype. DR OpenTargets; ENSG00000198719; -. DR Orphanet; 93925; Alobar holoprosencephaly. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR Orphanet; 93924; Lobar holoprosencephaly. DR Orphanet; 280200; Microform holoprosencephaly. DR Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly. DR Orphanet; 220386; Semilobar holoprosencephaly. DR Orphanet; 280195; Septopreoptic holoprosencephaly. DR VEuPathDB; HostDB:ENSG00000198719; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00940000159781; -. DR HOGENOM; CLU_012574_1_0_1; -. DR InParanoid; O00548; -. DR OMA; GPFPWAA; -. DR OrthoDB; 283575at2759; -. DR PAN-GO; O00548; 4 GO annotations based on evolutionary models. DR PhylomeDB; O00548; -. DR PathwayCommons; O00548; -. DR Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus. DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants. DR Reactome; R-HSA-2660826; Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant. DR Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants. DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants. DR Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus. DR Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus. DR Reactome; R-HSA-9022702; MECP2 regulates transcription of neuronal ligands. DR Reactome; R-HSA-9725554; Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin. DR Reactome; R-HSA-9793380; Formation of paraxial mesoderm. DR Reactome; R-HSA-9824272; Somitogenesis. DR Reactome; R-HSA-9831926; Nephron development. DR SignaLink; O00548; -. DR SIGNOR; O00548; -. DR Agora; ENSG00000198719; -. DR BioGRID-ORCS; 28514; 11 hits in 1147 CRISPR screens. DR ChiTaRS; DLL1; human. DR EvolutionaryTrace; O00548; -. DR GeneWiki; Delta-like_1; -. DR GenomeRNAi; 28514; -. DR Pharos; O00548; Tbio. DR PRO; PR:O00548; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O00548; protein. DR Bgee; ENSG00000198719; Expressed in spleen and 95 other cell types or tissues. DR ExpressionAtlas; O00548; baseline and differential. DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB. DR GO; GO:0048018; F:receptor ligand activity; IDA:BHF-UCL. DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl. DR GO; GO:0030957; F:Tat protein binding; IPI:UniProtKB. DR GO; GO:0014002; P:astrocyte development; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; TAS:UniProtKB. DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB. DR GO; GO:0021688; P:cerebellar molecular layer formation; ISS:UniProtKB. DR GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; ISS:UniProtKB. DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB. DR GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL. DR GO; GO:0097102; P:endothelial tip cell fate specification; ISS:UniProtKB. DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB. DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL. DR GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB. DR GO; GO:0046331; P:lateral inhibition; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IEA:Ensembl. DR GO; GO:0045596; P:negative regulation of cell differentiation; ISS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0045605; P:negative regulation of epidermal cell differentiation; ISS:UniProtKB. DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISS:UniProtKB. DR GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB. DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:UniProtKB. DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB. DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IBA:GO_Central. DR GO; GO:0072006; P:nephron development; ISS:UniProtKB. DR GO; GO:0048665; P:neuron fate specification; ISS:UniProtKB. DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEP:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; IDA:BHF-UCL. DR GO; GO:0060853; P:Notch signaling pathway involved in arterial endothelial cell fate commitment; ISS:UniProtKB. DR GO; GO:0035265; P:organ growth; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB. DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; ISS:UniProtKB. DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL. DR GO; GO:0072014; P:proximal tubule development; IEA:Ensembl. DR GO; GO:0009954; P:proximal/distal pattern formation; ISS:UniProtKB. DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB. DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB. DR GO; GO:0040008; P:regulation of growth; ISS:UniProtKB. DR GO; GO:0050767; P:regulation of neurogenesis; ISS:UniProtKB. DR GO; GO:0048631; P:regulation of skeletal muscle tissue growth; ISS:UniProtKB. DR GO; GO:0014807; P:regulation of somitogenesis; ISS:UniProtKB. DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB. DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISS:UniProtKB. DR GO; GO:0048630; P:skeletal muscle tissue growth; ISS:UniProtKB. DR GO; GO:0098773; P:skin epidermis development; ISS:UniProtKB. DR GO; GO:0001756; P:somitogenesis; ISS:UniProtKB. DR GO; GO:0021510; P:spinal cord development; ISS:UniProtKB. DR GO; GO:0003323; P:type B pancreatic cell development; ISS:UniProtKB. DR CDD; cd00054; EGF_CA; 6. DR DisProt; DP03838; -. DR FunFam; 2.10.25.10:FF:000018; Delta-like 1; 1. DR FunFam; 2.10.25.10:FF:000012; Delta-like protein; 4. DR FunFam; 2.10.25.10:FF:000064; Delta-like protein; 1. DR FunFam; 2.10.25.140:FF:000001; Delta-like protein; 1. DR FunFam; 2.60.40.3510:FF:000002; Delta-like protein; 1. DR FunFam; 2.10.25.10:FF:000004; Neurogenic locus notch 1; 1. 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; IPR000742; EGF. DR InterPro; IPR001881; EGF-like_Ca-bd_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; PTHR24049; CRUMBS FAMILY MEMBER; 1. DR PANTHER; PTHR24049:SF38; DELTA-LIKE PROTEIN; 1. DR Pfam; PF01414; DSL; 1. DR Pfam; PF00008; EGF; 6. DR Pfam; PF21700; EGF_DL_JAG; 1. 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; SSF57184; Growth factor receptor domain; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 3. DR PROSITE; PS51051; DSL; 1. DR PROSITE; PS00022; EGF_1; 8. DR PROSITE; PS01186; EGF_2; 8. DR PROSITE; PS50026; EGF_3; 7. DR PROSITE; PS01187; EGF_CA; 1. DR PDBsum; 4XBM; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Autism spectrum disorder; KW Cell junction; Cell membrane; Developmental protein; Differentiation; KW Disulfide bond; EGF-like domain; Epilepsy; Glycoprotein; KW Intellectual disability; Isopeptide bond; Membrane; KW Notch signaling pathway; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..723 FT /note="Delta-like protein 1" FT /id="PRO_0000007506" FT TOPO_DOM 18..545 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 546..568 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 569..723 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 177..221 FT /note="DSL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377" FT DOMAIN 226..254 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 257..285 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 292..325 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 332..363 FT /note="EGF-like 4; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 370..402 FT /note="EGF-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 409..440 FT /note="EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 447..478 FT /note="EGF-like 7; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 485..516 FT /note="EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 653..702 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 720..723 FT /note="Interaction with MAGI1" FT /evidence="ECO:0000250|UniProtKB:Q61483" FT COMPBIAS 653..664 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 694 FT /note="Phosphoserine; by PKB" FT /evidence="ECO:0000250|UniProtKB:Q61483" FT MOD_RES 697 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61483" FT CARBOHYD 477 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 179..188 FT /evidence="ECO:0000250" FT DISULFID 192..204 FT /evidence="ECO:0000250" FT DISULFID 212..221 FT /evidence="ECO:0000250" FT DISULFID 226..237 FT /evidence="ECO:0000250" FT DISULFID 230..243 FT /evidence="ECO:0000250" FT DISULFID 245..254 FT /evidence="ECO:0000250" FT DISULFID 257..268 FT /evidence="ECO:0000250" FT DISULFID 263..274 FT /evidence="ECO:0000250" FT DISULFID 276..285 FT /evidence="ECO:0000250" FT DISULFID 292..304 FT /evidence="ECO:0000250" FT DISULFID 298..314 FT /evidence="ECO:0000250" FT DISULFID 316..325 FT /evidence="ECO:0000250" FT DISULFID 332..343 FT /evidence="ECO:0000250" FT DISULFID 337..352 FT /evidence="ECO:0000250" FT DISULFID 354..363 FT /evidence="ECO:0000250" FT DISULFID 370..381 FT /evidence="ECO:0000250" FT DISULFID 375..391 FT /evidence="ECO:0000250" FT DISULFID 393..402 FT /evidence="ECO:0000250" FT DISULFID 409..420 FT /evidence="ECO:0000250" FT DISULFID 414..429 FT /evidence="ECO:0000250" FT DISULFID 431..440 FT /evidence="ECO:0000250" FT DISULFID 447..458 FT /evidence="ECO:0000250" FT DISULFID 452..467 FT /evidence="ECO:0000250" FT DISULFID 469..478 FT /evidence="ECO:0000250" FT DISULFID 485..496 FT /evidence="ECO:0000250" FT DISULFID 490..505 FT /evidence="ECO:0000250" FT DISULFID 507..516 FT /evidence="ECO:0000250" FT CROSSLNK 613 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q61483" FT VAR_SEQ 224..247 FT /note="PICLPGCDEQHGFCDKPGECKCRV -> RESLGRHRWLTRPRTRTTRRDGAS FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:19906316" FT /id="VSP_057186" FT VAR_SEQ 248..723 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:19906316" FT /id="VSP_057187" FT VARIANT 18 FT /note="Q -> QIGGQ (in NEDBAS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31353024" FT /id="VAR_083465" FT VARIANT 19..723 FT /note="Missing (in NEDBAS)" FT /evidence="ECO:0000269|PubMed:31353024" FT /id="VAR_083466" FT VARIANT 77..723 FT /note="Missing (in NEDBAS)" FT /evidence="ECO:0000269|PubMed:31353024" FT /id="VAR_083467" FT VARIANT 179 FT /note="C -> F (in NEDBAS)" FT /evidence="ECO:0000269|PubMed:31353024" FT /id="VAR_083468" FT VARIANT 444 FT /note="V -> M (in dbSNP:rs16901311)" FT /id="VAR_048976" FT VARIANT 498..723 FT /note="Missing (in NEDBAS)" FT /evidence="ECO:0000269|PubMed:31353024" FT /id="VAR_083469" FT VARIANT 509..723 FT /note="Missing (in NEDBAS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31353024" FT /id="VAR_083470" FT CONFLICT 498 FT /note="E -> Q (in Ref. 2; AAF05834)" FT /evidence="ECO:0000305" FT CONFLICT 502 FT /note="R -> G (in Ref. 1; AAB61286, 2; AAF05834 and 3; FT AAG09716)" FT /evidence="ECO:0000305" FT CONFLICT 510 FT /note="G -> S (in Ref. 2; AAF05834)" FT /evidence="ECO:0000305" FT STRAND 23..30 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 57..66 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 78..83 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 118..128 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 143..152 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 156..166 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 169..179 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 200..204 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:4XBM" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:4XBM" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 303..306 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 312..315 FT /evidence="ECO:0007829|PDB:4XBM" FT TURN 322..325 FT /evidence="ECO:0007829|PDB:4XBM" FT TURN 331..334 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 342..346 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 399..402 FT /evidence="ECO:0007829|PDB:4XBM" FT HELIX 408..411 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 419..422 FT /evidence="ECO:0007829|PDB:4XBM" FT STRAND 427..430 FT /evidence="ECO:0007829|PDB:4XBM" SQ SEQUENCE 723 AA; 78056 MW; 094B8F235DFD899D CRC64; MGSRCALALA VLSALLCQVW SSGVFELKLQ EFVNKKGLLG NRNCCRGGAG PPPCACRTFF RVCLKHYQAS VSPEPPCTYG SAVTPVLGVD SFSLPDGGGA DSAFSNPIRF PFGFTWPGTF SLIIEALHTD SPDDLATENP ERLISRLATQ RHLTVGEEWS QDLHSSGRTD LKYSYRFVCD EHYYGEGCSV FCRPRDDAFG HFTCGERGEK VCNPGWKGPY CTEPICLPGC DEQHGFCDKP GECKCRVGWQ GRYCDECIRY PGCLHGTCQQ PWQCNCQEGW GGLFCNQDLN YCTHHKPCKN GATCTNTGQG SYTCSCRPGY TGATCELGID ECDPSPCKNG GSCTDLENSY SCTCPPGFYG KICELSAMTC ADGPCFNGGR CSDSPDGGYS CRCPVGYSGF NCEKKIDYCS SSPCSNGAKC VDLGDAYLCR CQAGFSGRHC DDNVDDCASS PCANGGTCRD GVNDFSCTCP PGYTGRNCSA PVSRCEHAPC HNGATCHERG HRYVCECARG YGGPNCQFLL PELPPGPAVV DLTEKLEGQG GPFPWVAVCA GVILVLMLLL GCAAVVVCVR LRLQKHRPPA DPCRGETETM NNLANCQREK DISVSIIGAT QIKNTNKKAD FHGDHSADKN GFKARYPAVD YNLVQDLKGD DTAVRDAHSK RDTKCQPQGS SGEEKGTPTT LRGGEASERK RPDSGCSTSK DTKYQSVYVI SEEKDECVIA TEV //