EDIL3_HUMAN
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 03-AUG-2022, entry version 173.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Quertermous E.E.,
RA Aoka Y., Fukagawa M., Matsui Y., Platika D., Auerbach R., Hogan B.L.M.,
RA 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., 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 [3]
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 (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 project:
RT 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 interaction
CC with the alpha-v/beta-3 integrin receptor. Inhibits formation of
CC vascular-like structures. May be involved in regulation of vascular
CC morphogenesis of remodeling in embryonic 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 ion
CC binding site, while the long linker between EGF1 and EGF2 lends
CC considerable flexibility to EGF1.
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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 PDB; 4D90; X-ray; 2.60 A; A/B=24-157.
DR PDBsum; 4D90; -.
DR AlphaFoldDB; O43854; -.
DR SMR; O43854; -.
DR BioGRID; 115394; 25.
DR ELM; O43854; -.
DR IntAct; O43854; 11.
DR STRING; 9606.ENSP00000296591; -.
DR GlyGen; O43854; 3 sites.
DR iPTMnet; O43854; -.
DR PhosphoSitePlus; O43854; -.
DR BioMuta; EDIL3; -.
DR EPD; O43854; -.
DR jPOST; O43854; -.
DR MassIVE; O43854; -.
DR MaxQB; O43854; -.
DR PaxDb; O43854; -.
DR PeptideAtlas; O43854; -.
DR PRIDE; O43854; -.
DR ProteomicsDB; 49207; -. [O43854-1]
DR ProteomicsDB; 49208; -. [O43854-2]
DR Antibodypedia; 24753; 293 antibodies from 30 providers.
DR DNASU; 10085; -.
DR Ensembl; ENST00000296591.10; ENSP00000296591.4; ENSG00000164176.13. [O43854-1]
DR Ensembl; ENST00000380138.3; ENSP00000369483.3; ENSG00000164176.13. [O43854-2]
DR GeneID; 10085; -.
DR KEGG; hsa:10085; -.
DR MANE-Select; ENST00000296591.10; ENSP00000296591.4; NM_005711.5; NP_005702.3.
DR UCSC; uc003kio.3; human. [O43854-1]
DR CTD; 10085; -.
DR DisGeNET; 10085; -.
DR GeneCards; EDIL3; -.
DR HGNC; HGNC:3173; EDIL3.
DR HPA; ENSG00000164176; Tissue enriched (brain).
DR MIM; 606018; gene.
DR neXtProt; NX_O43854; -.
DR OpenTargets; ENSG00000164176; -.
DR PharmGKB; PA27613; -.
DR VEuPathDB; HostDB:ENSG00000164176; -.
DR eggNOG; ENOG502QU9M; Eukaryota.
DR GeneTree; ENSGT00940000158144; -.
DR HOGENOM; CLU_030066_0_1_1; -.
DR InParanoid; O43854; -.
DR OMA; CEADPCK; -.
DR OrthoDB; 441415at2759; -.
DR PhylomeDB; O43854; -.
DR TreeFam; TF330156; -.
DR PathwayCommons; O43854; -.
DR SignaLink; O43854; -.
DR BioGRID-ORCS; 10085; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; EDIL3; human.
DR GenomeRNAi; 10085; -.
DR Pharos; O43854; Tbio.
DR PRO; PR:O43854; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O43854; protein.
DR Bgee; ENSG00000164176; Expressed in lateral globus pallidus and 191 other tissues.
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:0005178; F:integrin binding; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR CDD; cd00057; FA58C; 2.
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 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 Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..480
FT /note="EGF-like repeat and discoidin I-like domain-
FT containing protein 3"
FT /id="PRO_0000007522"
FT DOMAIN 24..60
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 74..117
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 119..155
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 158..314
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 319..476
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT MOTIF 96..98
FT /note="Cell attachment site"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT CARBOHYD 73
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:22601780"
FT CARBOHYD 88
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:22601780"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 26..37
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 31..48
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 50..59
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 78..89
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 83..105
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 107..116
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 123..134
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 128..143
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 145..154
FT /evidence="ECO:0000269|PubMed:22601780"
FT DISULFID 158..314
FT /evidence="ECO:0000250"
FT DISULFID 301..305
FT /evidence="ECO:0000250"
FT DISULFID 319..476
FT /evidence="ECO:0000250"
FT VAR_SEQ 66
FT /note="A -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9420328"
FT /id="VSP_050006"
FT VAR_SEQ 67..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9420328"
FT /id="VSP_050007"
FT CONFLICT 16
FT /note="G -> S (in Ref. 4; AAH30828)"
FT /evidence="ECO:0000305"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:4D90"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4D90"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4D90"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4D90"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:4D90"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4D90"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4D90"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4D90"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:4D90"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4D90"
FT STRAND 140..144
FT /evidence="ECO:0007829|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
