ID EDIL3_HUMAN Reviewed; 480 AA. AC O43854; B2R763; O43855; Q5D094; Q8N610; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 13-FEB-2019, entry version 156. DE RecName: Full=EGF-like repeat and discoidin I-like domain-containing protein 3; DE AltName: Full=Developmentally-regulated endothelial cell locus 1 protein; DE AltName: Full=Integrin-binding protein DEL1; DE Flags: Precursor; GN Name=EDIL3; Synonyms=DEL1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHARACTERIZATION. RC TISSUE=Embryonic lung; RX PubMed=9420328; DOI=10.1101/gad.12.1.21; RA Hidai C., Zupancic T.J., Penta K., Mikhail A., Kawana M., RA Quertermous E.E., Aoka Y., Fukagawa M., Matsui Y., Platika D., RA Auerbach R., Hogan B.L.M., Snodgrass R., Quertermous T.; RT "Cloning and characterization of developmental endothelial locus-1: an RT embryonic endothelial cell protein that binds the alphavbeta3 integrin RT receptor."; RL Genes Dev. 12:21-33(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Trachea; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-157, RGD MOTIF, DISULFIDE RP BONDS, CALCIUM-BINDING SITES, AND GLYCOSYLATION AT THR-73; THR-88 AND RP ASN-140. RX PubMed=22601780; DOI=10.1096/fj.11-202036; RA Schurpf T., Chen Q., Liu J.H., Wang R., Springer T.A., Wang J.H.; RT "The RGD finger of Del-1 is a unique structural feature critical for RT integrin binding."; RL FASEB J. 26:3412-3420(2012). CC -!- FUNCTION: Promotes adhesion of endothelial cells through CC interaction with the alpha-v/beta-3 integrin receptor. Inhibits CC formation of vascular-like structures. May be involved in CC regulation of vascular morphogenesis of remodeling in embryonic CC development. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long; CC IsoId=O43854-1; Sequence=Displayed; CC Name=2; Synonyms=Short, Z20; CC IsoId=O43854-2; Sequence=VSP_050006, VSP_050007; CC -!- DOMAIN: EGF2 and EGF3 form a rigid rod via an interdomain calcium CC ion binding site, while the long linker between EGF1 and EGF2 CC lends considerable flexibility to EGF1. 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; U70312; AAC02648.1; -; mRNA. DR EMBL; U70313; AAC02649.1; -; mRNA. DR EMBL; AK312858; BAG35710.1; -; mRNA. DR EMBL; CH471084; EAW95917.1; -; Genomic_DNA. DR EMBL; CH471084; EAW95918.1; -; Genomic_DNA. DR EMBL; BC030828; AAH30828.1; -; mRNA. DR EMBL; BC053656; AAH53656.1; -; mRNA. DR CCDS; CCDS4062.1; -. [O43854-1] DR CCDS; CCDS64195.1; -. [O43854-2] DR RefSeq; NP_001265571.1; NM_001278642.1. [O43854-2] DR RefSeq; NP_005702.3; NM_005711.4. [O43854-1] DR UniGene; Hs.482730; -. DR PDB; 4D90; X-ray; 2.60 A; A/B=24-157. DR PDBsum; 4D90; -. DR ProteinModelPortal; O43854; -. DR SMR; O43854; -. DR BioGrid; 115394; 11. DR ELM; O43854; -. DR IntAct; O43854; 2. DR STRING; 9606.ENSP00000296591; -. DR iPTMnet; O43854; -. DR PhosphoSitePlus; O43854; -. DR BioMuta; EDIL3; -. DR EPD; O43854; -. DR jPOST; O43854; -. DR MaxQB; O43854; -. DR PaxDb; O43854; -. DR PeptideAtlas; O43854; -. DR PRIDE; O43854; -. DR ProteomicsDB; 49207; -. DR ProteomicsDB; 49208; -. [O43854-2] DR DNASU; 10085; -. DR Ensembl; ENST00000296591; ENSP00000296591; ENSG00000164176. [O43854-1] DR Ensembl; ENST00000380138; ENSP00000369483; ENSG00000164176. [O43854-2] DR GeneID; 10085; -. DR KEGG; hsa:10085; -. DR UCSC; uc003kio.3; human. [O43854-1] DR CTD; 10085; -. DR DisGeNET; 10085; -. DR EuPathDB; HostDB:ENSG00000164176.12; -. DR GeneCards; EDIL3; -. DR HGNC; HGNC:3173; EDIL3. DR HPA; HPA020415; -. DR MIM; 606018; gene. DR neXtProt; NX_O43854; -. DR OpenTargets; ENSG00000164176; -. DR PharmGKB; PA27613; -. DR eggNOG; ENOG410IFBC; Eukaryota. DR eggNOG; ENOG41114BV; LUCA. DR GeneTree; ENSGT00940000158144; -. DR HOGENOM; HOG000236278; -. DR HOVERGEN; HBG002385; -. DR InParanoid; O43854; -. DR OMA; CKGDICD; -. DR OrthoDB; 441415at2759; -. DR PhylomeDB; O43854; -. DR TreeFam; TF330156; -. DR ChiTaRS; EDIL3; human. DR GenomeRNAi; 10085; -. DR PRO; PR:O43854; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000164176; Expressed in 216 organ(s), highest expression level in Brodmann (1909) area 46. DR Genevisible; O43854; HS. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL. DR GO; GO:0005178; F:integrin binding; TAS:ProtInc. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl. DR CDD; cd00057; FA58C; 2. DR Gene3D; 2.60.120.260; -; 2. DR InterPro; IPR029828; EDIL-3. 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; IPR000421; FA58C. DR InterPro; IPR008979; Galactose-bd-like_sf. DR PANTHER; PTHR44122:SF3; PTHR44122:SF3; 1. DR Pfam; PF00008; EGF; 2. DR Pfam; PF00754; F5_F8_type_C; 2. DR Pfam; PF12661; hEGF; 1. DR SMART; SM00181; EGF; 3. DR SMART; SM00179; EGF_CA; 3. DR SMART; SM00231; FA58C; 2. DR SUPFAM; SSF49785; SSF49785; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS01285; FA58C_1; 2. DR PROSITE; PS01286; FA58C_2; 2. DR PROSITE; PS50022; FA58C_3; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; KW Complete proteome; Developmental protein; Disulfide bond; KW EGF-like domain; Glycoprotein; Metal-binding; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 480 EGF-like repeat and discoidin I-like FT domain-containing protein 3. FT /FTId=PRO_0000007522. FT DOMAIN 24 60 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 74 117 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 119 155 EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 158 314 F5/8 type C 1. {ECO:0000255|PROSITE- FT ProRule:PRU00081}. FT DOMAIN 319 476 F5/8 type C 2. {ECO:0000255|PROSITE- FT ProRule:PRU00081}. FT MOTIF 96 98 Cell attachment site. FT METAL 119 119 Calcium. FT METAL 120 120 Calcium; via carbonyl oxygen. FT METAL 122 122 Calcium. FT METAL 136 136 Calcium. FT METAL 137 137 Calcium; via carbonyl oxygen. FT CARBOHYD 73 73 O-linked (GalNAc...) threonine. FT {ECO:0000305|PubMed:22601780}. FT CARBOHYD 88 88 O-linked (Fuc...) threonine. FT {ECO:0000269|PubMed:22601780}. FT CARBOHYD 140 140 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22601780}. FT DISULFID 26 37 {ECO:0000269|PubMed:22601780}. FT DISULFID 31 48 {ECO:0000269|PubMed:22601780}. FT DISULFID 50 59 {ECO:0000269|PubMed:22601780}. FT DISULFID 78 89 {ECO:0000269|PubMed:22601780}. FT DISULFID 83 105 {ECO:0000269|PubMed:22601780}. FT DISULFID 107 116 {ECO:0000269|PubMed:22601780}. FT DISULFID 123 134 {ECO:0000269|PubMed:22601780}. FT DISULFID 128 143 {ECO:0000269|PubMed:22601780}. FT DISULFID 145 154 {ECO:0000269|PubMed:22601780}. FT DISULFID 158 314 {ECO:0000250}. FT DISULFID 301 305 {ECO:0000250}. FT DISULFID 319 476 {ECO:0000250}. FT VAR_SEQ 66 66 A -> G (in isoform 2). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9420328}. FT /FTId=VSP_050006. FT VAR_SEQ 67 76 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9420328}. FT /FTId=VSP_050007. FT CONFLICT 16 16 G -> S (in Ref. 4; AAH30828). FT {ECO:0000305}. FT HELIX 32 34 {ECO:0000244|PDB:4D90}. FT STRAND 36 38 {ECO:0000244|PDB:4D90}. FT STRAND 47 49 {ECO:0000244|PDB:4D90}. FT TURN 56 59 {ECO:0000244|PDB:4D90}. FT TURN 66 70 {ECO:0000244|PDB:4D90}. FT STRAND 88 91 {ECO:0000244|PDB:4D90}. FT STRAND 103 106 {ECO:0000244|PDB:4D90}. FT STRAND 111 113 {ECO:0000244|PDB:4D90}. FT TURN 122 125 {ECO:0000244|PDB:4D90}. FT STRAND 133 137 {ECO:0000244|PDB:4D90}. FT STRAND 140 144 {ECO:0000244|PDB:4D90}. SQ SEQUENCE 480 AA; 53765 MW; F7171E23A309FD48 CRC64; MKRSVAVWLL VGLSLGVPQF GKGDICDPNP CENGGICLPG LADGSFSCEC PDGFTDPNCS SVVEVASDEE EPTSAGPCTP NPCHNGGTCE ISEAYRGDTF IGYVCKCPRG FNGIHCQHNI NECEVEPCKN GGICTDLVAN YSCECPGEFM GRNCQYKCSG PLGIEGGIIS NQQITASSTH RALFGLQKWY PYYARLNKKG LINAWTAAEN DRWPWIQINL QRKMRVTGVI TQGAKRIGSP EYIKSYKIAY SNDGKTWAMY KVKGTNEDMV FRGNIDNNTP YANSFTPPIK AQYVRLYPQV CRRHCTLRME LLGCELSGCS EPLGMKSGHI QDYQITASSI FRTLNMDMFT WEPRKARLDK QGKVNAWTSG HNDQSQWLQV DLLVPTKVTG IITQGAKDFG HVQFVGSYKL AYSNDGEHWT VYQDEKQRKD KVFQGNFDND THRKNVIDPP IYARHIRILP WSWYGRITLR SELLGCTEEE //