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Database: UniProt
Entry: Q9QXT5
LinkDB: Q9QXT5
Original site: Q9QXT5 
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   10-APR-2019, entry version 133.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, 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
RT   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.,
RA   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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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.,
RA   Frantz G., Palmieri S., Hillan K., Stainier D.Y.R., De Sauvage F.J.,
RA   Ye W.;
RT   "The endothelial-cell-derived secreted factor Egfl7 regulates vascular
RT   tube formation.";
RL   Nature 428:754-758(2004).
CC   -!- FUNCTION: Regulates vascular tubulogenesis in vivo. Inhibits
CC       platelet-derived growth factor (PDGF)-BB-induced smooth muscle
CC       cell migration and promotes endothelial cell adhesion to the
CC       extracellular matrix and angiogenesis.
CC       {ECO:0000269|PubMed:14592969, 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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed specifically by endothelial cells of
CC       the 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
CC       the yolk sac mesoderm and in the developing vascular system. At
CC       7.5 dpc, it is expressed in the primitive blood islands where the
CC       first endothelial cells differentiate. At 10.5 and 13.5 dpc
CC       expression is restricted to endothelial cells.
CC       {ECO:0000269|PubMed:14592969, 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};
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   RefSeq; NP_001158036.1; NM_001164564.1.
DR   RefSeq; NP_848538.3; NM_178444.4.
DR   RefSeq; NP_942017.2; NM_198724.2.
DR   RefSeq; NP_942018.2; NM_198725.2.
DR   UniGene; Mm.268933; -.
DR   ProteinModelPortal; Q9QXT5; -.
DR   SMR; Q9QXT5; -.
DR   BioGrid; 237257; 4.
DR   IntAct; Q9QXT5; 5.
DR   MINT; Q9QXT5; -.
DR   STRING; 10090.ENSMUSP00000128741; -.
DR   iPTMnet; Q9QXT5; -.
DR   PhosphoSitePlus; Q9QXT5; -.
DR   PaxDb; Q9QXT5; -.
DR   PRIDE; Q9QXT5; -.
DR   GeneID; 353156; -.
DR   KEGG; mmu:353156; -.
DR   UCSC; uc008ivq.2; mouse. [Q9QXT5-2]
DR   CTD; 51162; -.
DR   MGI; MGI:2449923; Egfl7.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   HOGENOM; HOG000231494; -.
DR   HOVERGEN; HBG051453; -.
DR   InParanoid; Q9QXT5; -.
DR   OrthoDB; 749722at2759; -.
DR   PRO; PR:Q9QXT5; -.
DR   Proteomes; UP000000589; Unplaced.
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:0030336; P:negative regulation of cell migration; IDA:MGI.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO: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:0001570; P:vasculogenesis; IEP:UniProtKB.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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;
KW   Coiled coil; Complete proteome; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    275       Epidermal growth factor-like protein 7.
FT                                /FTId=PRO_0000007529.
FT   DOMAIN       28    105       EMI. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00384}.
FT   DOMAIN      104    136       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      138    178       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   COILED      196    220       {ECO:0000255}.
FT   MOTIF       131    133       Cell attachment site. {ECO:0000250}.
FT   DISULFID     32     90       {ECO:0000250}.
FT   DISULFID     57     63       {ECO:0000250}.
FT   DISULFID     89    103       {ECO:0000250}.
FT   DISULFID    108    118       {ECO:0000250}.
FT   DISULFID    112    124       {ECO:0000250}.
FT   DISULFID    126    135       {ECO:0000250}.
FT   DISULFID    142    153       {ECO:0000250}.
FT   DISULFID    149    162       {ECO:0000250}.
FT   VAR_SEQ     257    269       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=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
//
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