EGFL7_MOUSE
ID EGFL7_MOUSE Reviewed; 275 AA.
AC Q9QXT5; Q6XD35; Q9DCP5;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Epidermal growth factor-like protein 7;
DE Short=EGF-like protein 7;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 7;
DE Short=Multiple EGF-like domains protein 7;
DE AltName: Full=NOTCH4-like protein;
DE AltName: Full=Vascular endothelial statin;
DE Short=VE-statin;
DE AltName: Full=Zneu1;
DE Flags: Precursor;
GN Name=Egfl7; Synonyms=Megf7;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=B6SJL;
RX PubMed=14592969; DOI=10.1093/emboj/cdg549;
RA Soncin F., Mattot V., Lionneton F., Spruyt N., Lepretre F., Begue A.,
RA Stehelin D.;
RT "VE-statin, an endothelial repressor of smooth muscle cell migration.";
RL EMBO J. 22:5700-5711(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1;
RX PubMed=15162510; DOI=10.1002/dvdy.20063;
RA Fitch M.J., Campagnolo L., Kuhnert F., Stuhlmann H.;
RT "Egfl7, a novel epidermal growth factor-domain gene expressed in
RT endothelial cells.";
RL Dev. Dyn. 230:316-324(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Sheppard P., Jelinek L., Whitmore T., Blumberg H., Lehner J., O'Hara P.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 FUNCTION.
RX PubMed=15085134; DOI=10.1038/nature02416;
RA Parker L.H., Schmidt M., Jin S.-W., Gray A.M., Beis D., Pham T., Frantz G.,
RA Palmieri S., Hillan K., Stainier D.Y.R., De Sauvage F.J., Ye W.;
RT "The endothelial-cell-derived secreted factor Egfl7 regulates vascular tube
RT formation.";
RL Nature 428:754-758(2004).
CC -!- FUNCTION: Regulates vascular tubulogenesis in vivo. Inhibits platelet-
CC derived growth factor (PDGF)-BB-induced smooth muscle cell migration
CC and promotes endothelial cell adhesion to the extracellular matrix and
CC angiogenesis. {ECO:0000269|PubMed:14592969,
CC ECO:0000269|PubMed:15085134}.
CC -!- SUBUNIT: Interacts with ITGAV/ITGB3 in an RGD-dependent manner,
CC increasing endothelial cell's motility. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:14592969, ECO:0000269|PubMed:15162510}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QXT5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QXT5-2; Sequence=VSP_011765;
CC -!- TISSUE SPECIFICITY: Expressed specifically by endothelial cells of the
CC highly vascularized organs heart, lung and kidney.
CC {ECO:0000269|PubMed:14592969, ECO:0000269|PubMed:15162510}.
CC -!- DEVELOPMENTAL STAGE: Expressed early during mouse embryogenesis in the
CC yolk sac mesoderm and in the developing vascular system. At 7.5 dpc, it
CC is expressed in the primitive blood islands where the first endothelial
CC cells differentiate. At 10.5 and 13.5 dpc expression is restricted to
CC endothelial cells. {ECO:0000269|PubMed:14592969,
CC ECO:0000269|PubMed:15162510}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01322.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP74732.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB22222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY239289; AAP69825.1; -; mRNA.
DR EMBL; AY239290; AAP69826.1; -; mRNA.
DR EMBL; AY309459; AAP74732.1; ALT_INIT; mRNA.
DR EMBL; AF184973; AAF01322.1; ALT_INIT; mRNA.
DR EMBL; AK002601; BAB22222.1; ALT_INIT; mRNA.
DR EMBL; BC024610; AAH24610.2; -; mRNA.
DR CCDS; CCDS15807.3; -. [Q9QXT5-1]
DR CCDS; CCDS15808.3; -. [Q9QXT5-2]
DR RefSeq; NP_001158036.1; NM_001164564.1. [Q9QXT5-1]
DR RefSeq; NP_848538.3; NM_178444.4. [Q9QXT5-1]
DR RefSeq; NP_942017.2; NM_198724.2. [Q9QXT5-1]
DR RefSeq; NP_942018.2; NM_198725.2. [Q9QXT5-2]
DR AlphaFoldDB; Q9QXT5; -.
DR BioGRID; 237257; 4.
DR IntAct; Q9QXT5; 5.
DR MINT; Q9QXT5; -.
DR STRING; 10090.ENSMUSP00000128741; -.
DR iPTMnet; Q9QXT5; -.
DR PhosphoSitePlus; Q9QXT5; -.
DR MaxQB; Q9QXT5; -.
DR PaxDb; Q9QXT5; -.
DR PRIDE; Q9QXT5; -.
DR ProteomicsDB; 277559; -. [Q9QXT5-1]
DR ProteomicsDB; 277560; -. [Q9QXT5-2]
DR Antibodypedia; 32209; 353 antibodies from 37 providers.
DR DNASU; 353156; -.
DR Ensembl; ENSMUST00000100290; ENSMUSP00000097863; ENSMUSG00000026921. [Q9QXT5-2]
DR Ensembl; ENSMUST00000102907; ENSMUSP00000099971; ENSMUSG00000026921. [Q9QXT5-1]
DR Ensembl; ENSMUST00000150404; ENSMUSP00000115482; ENSMUSG00000026921. [Q9QXT5-1]
DR Ensembl; ENSMUST00000166920; ENSMUSP00000128741; ENSMUSG00000026921. [Q9QXT5-1]
DR Ensembl; ENSMUST00000239075; ENSMUSP00000159032; ENSMUSG00000026921. [Q9QXT5-1]
DR GeneID; 353156; -.
DR KEGG; mmu:353156; -.
DR UCSC; uc008ivq.2; mouse. [Q9QXT5-2]
DR CTD; 51162; -.
DR MGI; MGI:2449923; Egfl7.
DR VEuPathDB; HostDB:ENSMUSG00000026921; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160015; -.
DR InParanoid; Q9QXT5; -.
DR OrthoDB; 749722at2759; -.
DR BioGRID-ORCS; 353156; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Egfl7; mouse.
DR PRO; PR:Q9QXT5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QXT5; protein.
DR Bgee; ENSMUSG00000026921; Expressed in lung and 84 other tissues.
DR ExpressionAtlas; Q9QXT5; baseline and differential.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0005112; F:Notch binding; IPI:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001568; P:blood vessel development; IEP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; TAS:UniProtKB.
DR GO; GO:0014909; P:smooth muscle cell migration; IDA:MGI.
DR GO; GO:0001570; P:vasculogenesis; IEP:UniProtKB.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR011489; EMI_domain.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07546; EMI; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51041; EMI; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Angiogenesis; Calcium; Cell adhesion; Coiled coil;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..275
FT /note="Epidermal growth factor-like protein 7"
FT /id="PRO_0000007529"
FT DOMAIN 28..105
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 104..136
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 138..178
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 173..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..220
FT /evidence="ECO:0000255"
FT MOTIF 131..133
FT /note="Cell attachment site"
FT /evidence="ECO:0000250"
FT DISULFID 32..90
FT /evidence="ECO:0000250"
FT DISULFID 57..63
FT /evidence="ECO:0000250"
FT DISULFID 89..103
FT /evidence="ECO:0000250"
FT DISULFID 108..118
FT /evidence="ECO:0000250"
FT DISULFID 112..124
FT /evidence="ECO:0000250"
FT DISULFID 126..135
FT /evidence="ECO:0000250"
FT DISULFID 142..153
FT /evidence="ECO:0000250"
FT DISULFID 149..162
FT /evidence="ECO:0000250"
FT VAR_SEQ 257..269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011765"
SQ SEQUENCE 275 AA; 29765 MW; 54A888CB51CFAA13 CRC64;
MWGSGELLVA WFLVLAADGT TEHVYRPSRR VCTVGISGGS ISETFVQRVY QPYLTTCDGH
RACSTYRTIY RTAYRRSPGV TPARPRYACC PGWKRTSGLP GACGAAICQP PCGNGGSCIR
PGHCRCPVGW QGDTCQTDVD ECSTGEASCP QRCVNTVGSY WCQGWEGQSP SADGTRCLSK
EGPSPVAPNP TAGVDSMARE EVYRLQARVD VLEQKLQLVL APLHSLASRS TEHGLQDPGS
LLAHSFQQLD RIDSLSEQVS FLEEHLGSCS CKKDL
