EDIL3_MOUSE
ID EDIL3_MOUSE Reviewed; 480 AA.
AC O35474; O35475; Q8CBF7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHARACTERIZATION.
RC TISSUE=Embryo;
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 STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
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=O35474-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=O35474-2; Sequence=VSP_050400, VSP_050401;
CC -!- TISSUE SPECIFICITY: Expressed in angioblasts and early endothelial
CC cells. By embryonic day 13.5, also expressed in a restricted group of
CC non-endothelial cells including chondrocytes and retinal neurons.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo from day 7. After day
CC 15.5, expression decreases and disappears completely by the time of
CC birth.
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. {ECO:0000250}.
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DR EMBL; AF031524; AAB86585.1; -; mRNA.
DR EMBL; AF031525; AAB86586.1; -; mRNA.
DR EMBL; AK036117; BAC29310.1; -; mRNA.
DR EMBL; AK139093; BAE23887.1; -; mRNA.
DR EMBL; AC121916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466567; EDL00986.1; -; Genomic_DNA.
DR EMBL; BC056386; AAH56386.1; -; mRNA.
DR CCDS; CCDS26669.1; -. [O35474-1]
DR RefSeq; NP_001033076.1; NM_001037987.3. [O35474-1]
DR RefSeq; NP_034233.1; NM_010103.4.
DR AlphaFoldDB; O35474; -.
DR SMR; O35474; -.
DR STRING; 10090.ENSMUSP00000080462; -.
DR GlyGen; O35474; 3 sites.
DR PhosphoSitePlus; O35474; -.
DR MaxQB; O35474; -.
DR PaxDb; O35474; -.
DR PeptideAtlas; O35474; -.
DR PRIDE; O35474; -.
DR ProteomicsDB; 277680; -. [O35474-1]
DR ProteomicsDB; 277681; -. [O35474-2]
DR Antibodypedia; 24753; 293 antibodies from 30 providers.
DR DNASU; 13612; -.
DR Ensembl; ENSMUST00000081769; ENSMUSP00000080462; ENSMUSG00000034488. [O35474-1]
DR GeneID; 13612; -.
DR KEGG; mmu:13612; -.
DR UCSC; uc007rjb.2; mouse. [O35474-2]
DR UCSC; uc007rjd.2; mouse. [O35474-1]
DR CTD; 10085; -.
DR MGI; MGI:1329025; Edil3.
DR VEuPathDB; HostDB:ENSMUSG00000034488; -.
DR eggNOG; ENOG502QU9M; Eukaryota.
DR GeneTree; ENSGT00940000158144; -.
DR InParanoid; O35474; -.
DR OMA; CEADPCK; -.
DR PhylomeDB; O35474; -.
DR TreeFam; TF330156; -.
DR BioGRID-ORCS; 13612; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Edil3; mouse.
DR PRO; PR:O35474; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O35474; protein.
DR Bgee; ENSMUSG00000034488; Expressed in lateral geniculate body and 180 other tissues.
DR ExpressionAtlas; O35474; baseline and differential.
DR Genevisible; O35474; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
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; 3.
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 Alternative splicing; Calcium; Cell adhesion; Developmental protein;
KW Disulfide bond; EGF-like domain; Glycoprotein; Metal-binding;
KW 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_0000007523"
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 /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 88
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..37
FT /evidence="ECO:0000250"
FT DISULFID 31..48
FT /evidence="ECO:0000250"
FT DISULFID 50..59
FT /evidence="ECO:0000250"
FT DISULFID 78..89
FT /evidence="ECO:0000250"
FT DISULFID 83..105
FT /evidence="ECO:0000250"
FT DISULFID 107..116
FT /evidence="ECO:0000250"
FT DISULFID 123..134
FT /evidence="ECO:0000250"
FT DISULFID 128..143
FT /evidence="ECO:0000250"
FT DISULFID 145..154
FT /evidence="ECO:0000250"
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 218..221
FT /note="INLQ -> VTVG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9420328"
FT /id="VSP_050400"
FT VAR_SEQ 222..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9420328"
FT /id="VSP_050401"
FT CONFLICT 187
FT /note="Q -> R (in Ref. 1; AAB86585/AAB86586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 53712 MW; 10DBA65C19F1C70F CRC64;
MKHLVAAWLL VGLSLGVPQF GKGDICNPNP CENGGICLSG LADDSFSCEC PEGFAGPNCS
SVVEVASDEE KPTSAGPCIP NPCHNGGTCE ISEAYRGDTF IGYVCKCPRG FNGIHCQHNI
NECEAEPCRN GGICTDLVAN YSCECPGEFM GRNCQYKCSG PLGIEGGIIS NQQITASSTH
RALFGLQKWY PYYARLNKKG LINAWTAAEN DRWPWIQINL QRKMRVTGVI TQGAKRIGSP
EYIKSYKIAY SNDGKTWAMY KVKGTNEEMV FRGNVDNNTP YANSFTPPIK AQYVRLYPQI
CRRHCTLRME LLGCELSGCS EPLGMKSGHI QDYQITASSV FRTLNMDMFT WEPRKARLDK
QGKVNAWTSG HNDQSQWLQV DLLVPTKVTG IITQGAKDFG HVQFVGSYKL AYSNDGEHWM
VHQDEKQRKD KVFQGNFDND THRKNVIDPP IYARFIRILP WSWYGRITLR SELLGCAEEE
