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Q9QXT5

- EGFL7_MOUSE

UniProt

Q9QXT5 - EGFL7_MOUSE

Protein

Epidermal growth factor-like protein 7

Gene

Egfl7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    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

    1. calcium ion binding Source: UniProtKB
    2. Notch binding Source: MGI

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. blood vessel development Source: UniProtKB
    3. cell adhesion Source: UniProtKB-KW
    4. negative regulation of cell migration Source: MGI
    5. regulation of cell migration Source: UniProtKB
    6. vasculogenesis Source: UniProtKB

    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: Chromosome 2

    Organism-specific databases

    MGIiMGI:2449923. Egfl7.

    Subcellular locationi

    Secretedextracellular space 2 Publications

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: MGI

    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

    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.
    GenevestigatoriQ9QXT5.

    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.ENSMUSP00000099970.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QXT5.
    SMRiQ9QXT5. Positions 87-180.
    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.
    GeneTreeiENSGT00730000110993.
    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. Align

    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

    MWGSGELLVA WFLVLAADGT TEHVYRPSRR VCTVGISGGS ISETFVQRVY    50
    QPYLTTCDGH RACSTYRTIY RTAYRRSPGV TPARPRYACC PGWKRTSGLP 100
    GACGAAICQP PCGNGGSCIR PGHCRCPVGW QGDTCQTDVD ECSTGEASCP 150
    QRCVNTVGSY WCQGWEGQSP SADGTRCLSK EGPSPVAPNP TAGVDSMARE 200
    EVYRLQARVD VLEQKLQLVL APLHSLASRS TEHGLQDPGS LLAHSFQQLD 250
    RIDSLSEQVS FLEEHLGSCS CKKDL 275
    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.
    The sequence AAP74732.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB22222.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENSMUST00000100290; ENSMUSP00000097863; ENSMUSG00000026921.
    GeneIDi353156.
    KEGGimmu:353156.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_001158036.1. NM_001164564.1.
    NP_848538.3. NM_178444.4.
    NP_942017.2. NM_198724.2.
    NP_942018.2. NM_198725.2.
    UniGenei Mm.268933.

    3D structure databases

    ProteinModelPortali Q9QXT5.
    SMRi Q9QXT5. Positions 87-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 237257. 4 interactions.
    IntActi Q9QXT5. 5 interactions.
    STRINGi 10090.ENSMUSP00000099970.

    PTM databases

    PhosphoSitei Q9QXT5.

    Proteomic databases

    PRIDEi Q9QXT5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100290 ; ENSMUSP00000097863 ; ENSMUSG00000026921 .
    GeneIDi 353156.
    KEGGi mmu:353156.

    Organism-specific databases

    CTDi 51162.
    MGIi MGI:2449923. Egfl7.

    Phylogenomic databases

    eggNOGi NOG292943.
    GeneTreei ENSGT00730000110993.
    HOGENOMi HOG000231494.
    HOVERGENi HBG051453.
    InParanoidi Q9QXT5.

    Miscellaneous databases

    NextBioi 400295.
    PROi Q9QXT5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QXT5.
    CleanExi MM_EGFL7.
    Genevestigatori Q9QXT5.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR018097. EGF_Ca-bd_CS.
    IPR011489. EMI_domain.
    [Graphical view ]
    Pfami PF07645. EGF_CA. 1 hit.
    PF07546. EMI. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. 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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 109 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