Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Epidermal growth factor-like protein 7

Gene

Egfl7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Regulates vascular tubulogenesis in vivo. Inhibits platelet-derived growth factor (PDGF)-BB-induced smooth muscle cell migration and promotes endothelial cell adhesion to the extracellular matrix and angiogenesis.2 Publications

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • Notch binding Source: MGI

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • blood vessel development Source: UniProtKB
  • cell adhesion Source: UniProtKB-KW
  • negative regulation of cell migration Source: MGI
  • negative regulation of Notch signaling pathway Source: MGI
  • positive regulation of endothelial cell proliferation Source: MGI
  • regulation of cell migration Source: UniProtKB
  • vasculogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Cell adhesion, Differentiation

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor-like protein 7
Short name:
EGF-like protein 7
Alternative name(s):
Multiple epidermal growth factor-like domains protein 7
Short name:
Multiple EGF-like domains protein 7
NOTCH4-like protein
Vascular endothelial statin
Short name:
VE-statin
Zneu1
Gene namesi
Name:Egfl7
Synonyms:Megf7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2449923. Egfl7.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: MGI
  • extracellular region Source: UniProtKB
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 275254Epidermal growth factor-like protein 7PRO_0000007529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 90By similarity
Disulfide bondi57 ↔ 63By similarity
Disulfide bondi89 ↔ 103By similarity
Disulfide bondi108 ↔ 118By similarity
Disulfide bondi112 ↔ 124By similarity
Disulfide bondi126 ↔ 135By similarity
Disulfide bondi142 ↔ 153By similarity
Disulfide bondi149 ↔ 162By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9QXT5.
PRIDEiQ9QXT5.

PTM databases

PhosphoSiteiQ9QXT5.

Expressioni

Tissue specificityi

Expressed specifically by endothelial cells of the highly vascularized organs heart, lung and kidney.2 Publications

Developmental stagei

Expressed early during mouse embryogenesis in the yolk sac mesoderm and in the developing vascular system. At E7.5, it is expressed in the primitive blood islands where the first endothelial cells differentiate. At E10.5 and E13.5 expression is restricted to endothelial cells.2 Publications

Gene expression databases

BgeeiQ9QXT5.
CleanExiMM_EGFL7.
ExpressionAtlasiQ9QXT5. baseline and differential.
GenevisibleiQ9QXT5. MM.

Interactioni

Subunit structurei

Interacts with ITGAV/ITGB3 in an RGD-dependent manner, increasing endothelial cell's motility.By similarity

Protein-protein interaction databases

BioGridi237257. 4 interactions.
IntActiQ9QXT5. 5 interactions.
STRINGi10090.ENSMUSP00000099971.

Structurei

3D structure databases

ProteinModelPortaliQ9QXT5.
SMRiQ9QXT5. Positions 89-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 10578EMIPROSITE-ProRule annotationAdd
BLAST
Domaini104 – 13633EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini138 – 17841EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili196 – 22025Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi131 – 1333Cell attachment siteBy similarity

Sequence similaritiesi

Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 EMI domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG292943.
HOGENOMiHOG000231494.
HOVERGENiHBG051453.
InParanoidiQ9QXT5.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR011489. EMI_domain.
[Graphical view]
PfamiPF07645. EGF_CA. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QXT5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWGSGELLVA WFLVLAADGT TEHVYRPSRR VCTVGISGGS ISETFVQRVY
60 70 80 90 100
QPYLTTCDGH RACSTYRTIY RTAYRRSPGV TPARPRYACC PGWKRTSGLP
110 120 130 140 150
GACGAAICQP PCGNGGSCIR PGHCRCPVGW QGDTCQTDVD ECSTGEASCP
160 170 180 190 200
QRCVNTVGSY WCQGWEGQSP SADGTRCLSK EGPSPVAPNP TAGVDSMARE
210 220 230 240 250
EVYRLQARVD VLEQKLQLVL APLHSLASRS TEHGLQDPGS LLAHSFQQLD
260 270
RIDSLSEQVS FLEEHLGSCS CKKDL
Length:275
Mass (Da):29,765
Last modified:January 4, 2005 - v2
Checksum:i54A888CB51CFAA13
GO
Isoform 2 (identifier: Q9QXT5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     257-269: Missing.

Note: No experimental confirmation available.
Show »
Length:262
Mass (Da):28,305
Checksum:i7AB272F68CB7D4A4
GO

Sequence cautioni

The sequence AAF01322.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAP74732.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB22222.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei257 – 26913Missing in isoform 2. 1 PublicationVSP_011765Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY239289 mRNA. Translation: AAP69825.1.
AY239290 mRNA. Translation: AAP69826.1.
AY309459 mRNA. Translation: AAP74732.1. Different initiation.
AF184973 mRNA. Translation: AAF01322.1. Different initiation.
AK002601 mRNA. Translation: BAB22222.1. Different initiation.
BC024610 mRNA. Translation: AAH24610.2.
RefSeqiNP_001158036.1. NM_001164564.1.
NP_848538.3. NM_178444.4.
NP_942017.2. NM_198724.2.
NP_942018.2. NM_198725.2.
UniGeneiMm.268933.

Genome annotation databases

GeneIDi353156.
KEGGimmu:353156.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY239289 mRNA. Translation: AAP69825.1.
AY239290 mRNA. Translation: AAP69826.1.
AY309459 mRNA. Translation: AAP74732.1. Different initiation.
AF184973 mRNA. Translation: AAF01322.1. Different initiation.
AK002601 mRNA. Translation: BAB22222.1. Different initiation.
BC024610 mRNA. Translation: AAH24610.2.
RefSeqiNP_001158036.1. NM_001164564.1.
NP_848538.3. NM_178444.4.
NP_942017.2. NM_198724.2.
NP_942018.2. NM_198725.2.
UniGeneiMm.268933.

3D structure databases

ProteinModelPortaliQ9QXT5.
SMRiQ9QXT5. Positions 89-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi237257. 4 interactions.
IntActiQ9QXT5. 5 interactions.
STRINGi10090.ENSMUSP00000099971.

PTM databases

PhosphoSiteiQ9QXT5.

Proteomic databases

MaxQBiQ9QXT5.
PRIDEiQ9QXT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi353156.
KEGGimmu:353156.

Organism-specific databases

CTDi51162.
MGIiMGI:2449923. Egfl7.

Phylogenomic databases

eggNOGiNOG292943.
HOGENOMiHOG000231494.
HOVERGENiHBG051453.
InParanoidiQ9QXT5.

Miscellaneous databases

NextBioi400295.
PROiQ9QXT5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXT5.
CleanExiMM_EGFL7.
ExpressionAtlasiQ9QXT5. baseline and differential.
GenevisibleiQ9QXT5. MM.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR011489. EMI_domain.
[Graphical view]
PfamiPF07645. EGF_CA. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "VE-statin, an endothelial repressor of smooth muscle cell migration."
    Soncin F., Mattot V., Lionneton F., Spruyt N., Lepretre F., Begue A., Stehelin D.
    EMBO J. 22:5700-5711(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: B6SJL.
  2. "Egfl7, a novel epidermal growth factor-domain gene expressed in endothelial cells."
    Fitch M.J., Campagnolo L., Kuhnert F., Stuhlmann H.
    Dev. Dyn. 230:316-324(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: CD-1.
  3. Sheppard P., Jelinek L., Whitmore T., Blumberg H., Lehner J., O'Hara P.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Kidney.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Liver.
  6. "The endothelial-cell-derived secreted factor Egfl7 regulates vascular tube formation."
    Parker L.H., Schmidt M., Jin S.-W., Gray A.M., Beis D., Pham T., Frantz G., Palmieri S., Hillan K., Stainier D.Y.R., De Sauvage F.J., Ye W.
    Nature 428:754-758(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiEGFL7_MOUSE
AccessioniPrimary (citable) accession number: Q9QXT5
Secondary accession number(s): Q6XD35, Q9DCP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: January 4, 2005
Last modified: June 24, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.