DLL4_HUMAN
ID DLL4_HUMAN Reviewed; 685 AA.
AC Q9NR61; Q3KP23; Q9NQT9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Delta-like protein 4;
DE AltName: Full=Drosophila Delta homolog 4;
DE Short=Delta4;
DE Flags: Precursor;
GN Name=DLL4; ORFNames=UNQ1895/PRO4341;
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].
RC TISSUE=Brain;
RX PubMed=10837024;
RA Shutter J.R., Scully S., Fan W., Richards W.G., Kitajewski J.,
RA Deblandre G.A., Kintner C.R., Stark K.L.;
RT "Dll4, a novel Notch ligand expressed in arterial endothelium.";
RL Genes Dev. 14:1313-1318(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sakano S.;
RT "Human Delta-2, Notch ligand gene.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11134954; DOI=10.1093/oxfordjournals.jbchem.a002832;
RA Yoneya T., Tahara T., Nagao K., Yamada Y., Yamamoto T., Miyatani S.,
RA Nishikawa M.;
RT "Molecular cloning of Delta-4, a new mouse and human Notch ligand.";
RL J. Biochem. 129:27-34(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [6]
RP PROTEIN SEQUENCE OF 27-41.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-685.
RC TISSUE=Placenta;
RA Mailhos C., Modlich U., Lewis J., Harris A., Bicknell R., Ish-Horowicz D.;
RT "A novel Delta gene expressed in embryonic and tumour vasculature.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION IN NEUROGENESIS.
RX PubMed=17728344; DOI=10.1242/dev.005868;
RA Del Barrio M.G., Taveira-Marques R., Muroyama Y., Yuk D.I., Li S.,
RA Wines-Samuelson M., Shen J., Smith H.K., Xiang M., Rowitch D.,
RA Richardson W.D.;
RT "A regulatory network involving Foxn4, Mash1 and delta-like 4/Notch1
RT generates V2a and V2b spinal interneurons from a common progenitor pool.";
RL Development 134:3427-3436(2007).
RN [9]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=20616313; DOI=10.1161/circresaha.110.217257;
RA Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E.,
RA Adam M.G., Telzerow A., Augustin H.G., Fischer A.;
RT "Integrin cytoplasmic domain-associated protein-1 attenuates sprouting
RT angiogenesis.";
RL Circ. Res. 107:592-601(2010).
RN [10]
RP INVOLVEMENT IN AOS6, AND VARIANTS AOS6 PRO-121; CYS-186; LEU-195; THR-267;
RP ARG-390; TYR-390 AND TRP-455.
RX PubMed=26299364; DOI=10.1016/j.ajhg.2015.07.015;
RA Meester J.A., Southgate L., Stittrich A.B., Venselaar H., Beekmans S.J.,
RA den Hollander N., Bijlsma E.K., Helderman-van den Enden A., Verheij J.B.,
RA Glusman G., Roach J.C., Lehman A., Patel M.S., de Vries B.B.,
RA Ruivenkamp C., Itin P., Prescott K., Clarke S., Trembath R., Zenker M.,
RA Sukalo M., Van Laer L., Loeys B., Wuyts W.;
RT "Heterozygous loss-of-function mutations in DLL4 cause Adams-Oliver
RT syndrome.";
RL Am. J. Hum. Genet. 97:475-482(2015).
CC -!- FUNCTION: Involved in the Notch signaling pathway as Notch ligand
CC (PubMed:11134954). Activates NOTCH1 and NOTCH4. Involved in
CC angiogenesis; negatively regulates endothelial cell proliferation and
CC migration and angiogenic sprouting (PubMed:20616313). Essential for
CC retinal progenitor proliferation. Required for suppressing rod fates in
CC late retinal progenitors as well as for proper generation of other
CC retinal cell types (By similarity). During spinal cord neurogenesis,
CC inhibits V2a interneuron fate (PubMed:17728344).
CC {ECO:0000250|UniProtKB:Q9JI71, ECO:0000269|PubMed:11134954,
CC ECO:0000269|PubMed:17728344, ECO:0000269|PubMed:20616313}.
CC -!- SUBUNIT: Interacts with NOTCH4. Interacts (via N-terminal DSL and MNNL
CC domains) with NOTCH1 (via EGF-like domains).
CC {ECO:0000250|UniProtKB:D3ZHH1}.
CC -!- INTERACTION:
CC Q9NR61; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-11700027, EBI-1049004;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular endothelium.
CC -!- DOMAIN: The Delta-Serrate-Lag2 (DSL) domain is required for binding to
CC the Notch receptor.
CC -!- DISEASE: Adams-Oliver syndrome 6 (AOS6) [MIM:616589]: A form of Adams-
CC Oliver syndrome, a disorder characterized by the congenital absence of
CC skin (aplasia cutis congenita) in combination with transverse limb
CC defects. Aplasia cutis congenita can be located anywhere on the body,
CC but in the vast majority of the cases, it is present on the posterior
CC parietal region where it is often associated with an underlying defect
CC of the parietal bones. Limb abnormalities are typically limb truncation
CC defects affecting the distal phalanges or entire digits (true
CC ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal
CC limb structures are also affected. Apart from transverse limb defects,
CC syndactyly, most commonly of second and third toes, can also be
CC observed. The clinical features are highly variable and can also
CC include cardiovascular malformations, brain abnormalities and vascular
CC defects such as cutis marmorata and dilated scalp veins.
CC {ECO:0000269|PubMed:26299364}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF253468; AAF76427.1; -; mRNA.
DR EMBL; AB036931; BAB16085.1; -; mRNA.
DR EMBL; AB043894; BAB18581.1; -; mRNA.
DR EMBL; AY358894; AAQ89253.1; -; mRNA.
DR EMBL; BC106950; AAI06951.1; -; mRNA.
DR EMBL; AF279305; AAF81912.1; -; mRNA.
DR CCDS; CCDS45232.1; -.
DR PIR; JC7570; JC7570.
DR RefSeq; NP_061947.1; NM_019074.3.
DR PDB; 5MVX; X-ray; 2.17 A; A=27-325.
DR PDBsum; 5MVX; -.
DR AlphaFoldDB; Q9NR61; -.
DR SMR; Q9NR61; -.
DR BioGRID; 120045; 1.
DR IntAct; Q9NR61; 1.
DR STRING; 9606.ENSP00000249749; -.
DR ChEMBL; CHEMBL3712916; -.
DR GlyGen; Q9NR61; 4 sites.
DR iPTMnet; Q9NR61; -.
DR PhosphoSitePlus; Q9NR61; -.
DR BioMuta; DLL4; -.
DR DMDM; 13431490; -.
DR jPOST; Q9NR61; -.
DR MassIVE; Q9NR61; -.
DR PaxDb; Q9NR61; -.
DR PeptideAtlas; Q9NR61; -.
DR PRIDE; Q9NR61; -.
DR ProteomicsDB; 82285; -.
DR ABCD; Q9NR61; 67 sequenced antibodies.
DR Antibodypedia; 5995; 882 antibodies from 45 providers.
DR DNASU; 54567; -.
DR Ensembl; ENST00000249749.7; ENSP00000249749.5; ENSG00000128917.8.
DR GeneID; 54567; -.
DR KEGG; hsa:54567; -.
DR MANE-Select; ENST00000249749.7; ENSP00000249749.5; NM_019074.4; NP_061947.1.
DR UCSC; uc001zng.3; human.
DR CTD; 54567; -.
DR DisGeNET; 54567; -.
DR GeneCards; DLL4; -.
DR GeneReviews; DLL4; -.
DR HGNC; HGNC:2910; DLL4.
DR HPA; ENSG00000128917; Low tissue specificity.
DR MalaCards; DLL4; -.
DR MIM; 605185; gene.
DR MIM; 616589; phenotype.
DR neXtProt; NX_Q9NR61; -.
DR OpenTargets; ENSG00000128917; -.
DR Orphanet; 974; Adams-Oliver syndrome.
DR Orphanet; 1114; Aplasia cutis congenita.
DR PharmGKB; PA27366; -.
DR VEuPathDB; HostDB:ENSG00000128917; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000157441; -.
DR HOGENOM; CLU_012574_1_0_1; -.
DR InParanoid; Q9NR61; -.
DR OMA; CTEQNGY; -.
DR OrthoDB; 406049at2759; -.
DR PhylomeDB; Q9NR61; -.
DR TreeFam; TF351835; -.
DR PathwayCommons; Q9NR61; -.
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-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus.
DR SignaLink; Q9NR61; -.
DR SIGNOR; Q9NR61; -.
DR BioGRID-ORCS; 54567; 11 hits in 1069 CRISPR screens.
DR GeneWiki; DLL4; -.
DR GenomeRNAi; 54567; -.
DR Pharos; Q9NR61; Tbio.
DR PRO; PR:Q9NR61; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NR61; protein.
DR Bgee; ENSG00000128917; Expressed in vena cava and 136 other tissues.
DR Genevisible; Q9NR61; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISS:BHF-UCL.
DR GO; GO:0003180; P:aortic valve morphogenesis; IC:BHF-UCL.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0072554; P:blood vessel lumenization; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003209; P:cardiac atrium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003208; P:cardiac ventricle morphogenesis; ISS:BHF-UCL.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IDA:UniProtKB.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0061314; P:Notch signaling involved in heart development; ISS:BHF-UCL.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0003344; P:pericardium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0061074; P:regulation of neural retina development; ISS:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR GO; GO:0060579; P:ventral spinal cord interneuron fate commitment; IMP:UniProtKB.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR DisProt; DP01490; -.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011651; Notch_ligand_N.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF07657; MNNL; 1.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Cell membrane; Developmental protein;
KW Differentiation; Direct protein sequencing; Disease variant;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Neurogenesis;
KW Notch signaling pathway; Reference proteome; Repeat; Sensory transduction;
KW Signal; Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 27..685
FT /note="Delta-like protein 4"
FT /id="PRO_0000007512"
FT TOPO_DOM 27..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 173..217
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 218..251
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 252..282
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 284..322
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 324..360
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 362..400
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 402..438
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 440..476
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 480..518
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 185..187
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT REGION 191..195
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT SITE 110
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT SITE 216
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..54
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 61..74
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 175..184
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 188..200
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 208..217
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 222..233
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 226..239
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 241..250
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 253..264
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 259..270
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 272..281
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 288..300
FT /evidence="ECO:0000250"
FT DISULFID 294..310
FT /evidence="ECO:0000250"
FT DISULFID 312..321
FT /evidence="ECO:0000250"
FT DISULFID 328..339
FT /evidence="ECO:0000250"
FT DISULFID 333..348
FT /evidence="ECO:0000250"
FT DISULFID 350..359
FT /evidence="ECO:0000250"
FT DISULFID 366..377
FT /evidence="ECO:0000250"
FT DISULFID 371..388
FT /evidence="ECO:0000250"
FT DISULFID 390..399
FT /evidence="ECO:0000250"
FT DISULFID 406..417
FT /evidence="ECO:0000250"
FT DISULFID 411..426
FT /evidence="ECO:0000250"
FT DISULFID 428..437
FT /evidence="ECO:0000250"
FT DISULFID 444..455
FT /evidence="ECO:0000250"
FT DISULFID 449..464
FT /evidence="ECO:0000250"
FT DISULFID 466..475
FT /evidence="ECO:0000250"
FT DISULFID 484..495
FT /evidence="ECO:0000250"
FT DISULFID 489..506
FT /evidence="ECO:0000250"
FT DISULFID 508..517
FT /evidence="ECO:0000250"
FT VARIANT 121
FT /note="A -> P (in AOS6; dbSNP:rs796065350)"
FT /evidence="ECO:0000269|PubMed:26299364"
FT /id="VAR_075858"
FT VARIANT 186
FT /note="R -> C (in AOS6; dbSNP:rs796065348)"
FT /evidence="ECO:0000269|PubMed:26299364"
FT /id="VAR_075859"
FT VARIANT 195
FT /note="F -> L (in AOS6; dbSNP:rs796065351)"
FT /evidence="ECO:0000269|PubMed:26299364"
FT /id="VAR_075860"
FT VARIANT 267
FT /note="P -> T (in AOS6; dbSNP:rs796065349)"
FT /evidence="ECO:0000269|PubMed:26299364"
FT /id="VAR_075861"
FT VARIANT 390
FT /note="C -> R (in AOS6; dbSNP:rs796065347)"
FT /evidence="ECO:0000269|PubMed:26299364"
FT /id="VAR_075862"
FT VARIANT 390
FT /note="C -> Y (in AOS6; dbSNP:rs796065346)"
FT /evidence="ECO:0000269|PubMed:26299364"
FT /id="VAR_075863"
FT VARIANT 455
FT /note="C -> W (in AOS6; dbSNP:rs796065345)"
FT /evidence="ECO:0000269|PubMed:26299364"
FT /id="VAR_075864"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5MVX"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5MVX"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5MVX"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5MVX"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:5MVX"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:5MVX"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:5MVX"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:5MVX"
SQ SEQUENCE 685 AA; 74605 MW; 6CF89D3C220ACC89 CRC64;
MAAASRSASG WALLLLVALW QQRAAGSGVF QLQLQEFINE RGVLASGRPC EPGCRTFFRV
CLKHFQAVVS PGPCTFGTVS TPVLGTNSFA VRDDSSGGGR NPLQLPFNFT WPGTFSLIIE
AWHAPGDDLR PEALPPDALI SKIAIQGSLA VGQNWLLDEQ TSTLTRLRYS YRVICSDNYY
GDNCSRLCKK RNDHFGHYVC QPDGNLSCLP GWTGEYCQQP ICLSGCHEQN GYCSKPAECL
CRPGWQGRLC NECIPHNGCR HGTCSTPWQC TCDEGWGGLF CDQDLNYCTH HSPCKNGATC
SNSGQRSYTC TCRPGYTGVD CELELSECDS NPCRNGGSCK DQEDGYHCLC PPGYYGLHCE
HSTLSCADSP CFNGGSCRER NQGANYACEC PPNFTGSNCE KKVDRCTSNP CANGGQCLNR
GPSRMCRCRP GFTGTYCELH VSDCARNPCA HGGTCHDLEN GLMCTCPAGF SGRRCEVRTS
IDACASSPCF NRATCYTDLS TDTFVCNCPY GFVGSRCEFP VGLPPSFPWV AVSLGVGLAV
LLVLLGMVAV AVRQLRLRRP DDGSREAMNN LSDFQKDNLI PAAQLKNTNQ KKELEVDCGL
DKSNCGKQQN HTLDYNLAPG PLGRGTMPGK FPHSDKSLGE KAPLRLHSEK PECRISAICS
PRDSMYQSVC LISEERNECV IATEV
