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Q9WVH9

- FBLN5_MOUSE

UniProt

Q9WVH9 - FBLN5_MOUSE

Protein

Fibulin-5

Gene

Fbln5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Could be a vascular ligand for integrin receptors and may play a role in vascular development and remodeling.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. elastic fiber assembly Source: BHF-UCL
    3. extracellular matrix organization Source: MGI
    4. protein localization to cell surface Source: BHF-UCL
    5. regulation of cell growth Source: Ensembl
    6. regulation of removal of superoxide radicals Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_198996. Elastic fibre formation.
    REACT_198998. Molecules associated with elastic fibres.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibulin-5
    Short name:
    FIBL-5
    Alternative name(s):
    Developmental arteries and neural crest EGF-like protein
    Short name:
    Dance
    Gene namesi
    Name:Fbln5
    Synonyms:Dance
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1346091. Fbln5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular matrix Source: Ensembl
    3. extracellular region Source: Reactome
    4. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 448425Fibulin-5PRO_0000007578Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 59PROSITE-ProRule annotation
    Disulfide bondi53 ↔ 68PROSITE-ProRule annotation
    Disulfide bondi131 ↔ 144PROSITE-ProRule annotation
    Disulfide bondi138 ↔ 153PROSITE-ProRule annotation
    Disulfide bondi155 ↔ 166PROSITE-ProRule annotation
    Disulfide bondi172 ↔ 181PROSITE-ProRule annotation
    Disulfide bondi177 ↔ 190PROSITE-ProRule annotation
    Disulfide bondi192 ↔ 205PROSITE-ProRule annotation
    Disulfide bondi211 ↔ 221PROSITE-ProRule annotation
    Disulfide bondi217 ↔ 230PROSITE-ProRule annotation
    Disulfide bondi232 ↔ 245PROSITE-ProRule annotation
    Disulfide bondi251 ↔ 262PROSITE-ProRule annotation
    Disulfide bondi258 ↔ 271PROSITE-ProRule annotation
    Disulfide bondi273 ↔ 286PROSITE-ProRule annotation
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi292 ↔ 305PROSITE-ProRule annotation
    Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi299 ↔ 314PROSITE-ProRule annotation
    Disulfide bondi320 ↔ 332PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9WVH9.
    PRIDEiQ9WVH9.

    Expressioni

    Gene expression databases

    BgeeiQ9WVH9.
    CleanExiMM_FBLN5.
    GenevestigatoriQ9WVH9.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiQ9WVH9. 2 interactions.
    MINTiMINT-4094993.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WVH9.
    SMRiQ9WVH9. Positions 42-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 8241EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini127 – 16741EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini168 – 20639EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini207 – 24640EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini247 – 28741EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini288 – 33346EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi54 – 563Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Belongs to the fibulin family.Curated
    Contains 6 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG309650.
    GeneTreeiENSGT00740000115418.
    HOGENOMiHOG000234337.
    HOVERGENiHBG051560.
    InParanoidiQ9WVH9.
    KOiK17340.
    OMAiKGPRDIQ.
    OrthoDBiEOG7W9RTF.
    PhylomeDBiQ9WVH9.
    TreeFamiTF317514.

    Family and domain databases

    InterProiIPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    [Graphical view]
    PfamiPF12662. cEGF. 2 hits.
    PF07645. EGF_CA. 2 hits.
    [Graphical view]
    SMARTiSM00179. EGF_CA. 4 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
    PS01186. EGF_2. 4 hits.
    PS50026. EGF_3. 5 hits.
    PS01187. EGF_CA. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9WVH9-1 [UniParc]FASTAAdd to Basket

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    MPGLKRILTV TILALWLPHP GNAQQQCTNG FDLDRQSGQC LDIDECRTIP    50
    EACRGDMMCV NQNGGYLCIP RTNPVYRGPY SNPYSTSYSG PYPAAAPPVP 100
    ASNYPTISRP LVCRFGYQMD EGNQCVDVDE CATDSHQCNP TQICINTEGG 150
    YTCSCTDGYW LLEGQCLDID ECRYGYCQQL CANVPGSYSC TCNPGFTLND 200
    DGRSCQDVNE CETENPCVQT CVNTYGSFIC RCDPGYELEE DGIHCSDMDE 250
    CSFSEFLCQH ECVNQPGSYF CSCPPGYVLL DDNRSCQDIN ECEHRNHTCT 300
    SLQTCYNLQG GFKCIDPISC EEPYLLIGEN RCMCPAEHTS CRDQPFTILY 350
    RDMDVVSGRS VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI 400
    SATLVMTRPI KGPRDIQLDL EMITVNTVIN FRGSSVIRLR IYVSQYPF 448
    Length:448
    Mass (Da):50,193
    Last modified:November 1, 1999 - v1
    Checksum:iF15CC70CCFBFDC97
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF112151 mRNA. Translation: AAD41767.1.
    AK085170 mRNA. Translation: BAC39381.1.
    AK090129 mRNA. Translation: BAC41109.1.
    AK159471 mRNA. Translation: BAE35112.1.
    AK159960 mRNA. Translation: BAE35515.1.
    AK165018 mRNA. Translation: BAE38002.1.
    BC006636 mRNA. Translation: AAH06636.1.
    CCDSiCCDS36525.1.
    RefSeqiNP_035942.1. NM_011812.4.
    UniGeneiMm.288381.
    Mm.465863.

    Genome annotation databases

    EnsembliENSMUST00000021603; ENSMUSP00000021603; ENSMUSG00000021186.
    GeneIDi23876.
    KEGGimmu:23876.
    UCSCiuc007otp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF112151 mRNA. Translation: AAD41767.1 .
    AK085170 mRNA. Translation: BAC39381.1 .
    AK090129 mRNA. Translation: BAC41109.1 .
    AK159471 mRNA. Translation: BAE35112.1 .
    AK159960 mRNA. Translation: BAE35515.1 .
    AK165018 mRNA. Translation: BAE38002.1 .
    BC006636 mRNA. Translation: AAH06636.1 .
    CCDSi CCDS36525.1.
    RefSeqi NP_035942.1. NM_011812.4.
    UniGenei Mm.288381.
    Mm.465863.

    3D structure databases

    ProteinModelPortali Q9WVH9.
    SMRi Q9WVH9. Positions 42-327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WVH9. 2 interactions.
    MINTi MINT-4094993.

    Proteomic databases

    PaxDbi Q9WVH9.
    PRIDEi Q9WVH9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021603 ; ENSMUSP00000021603 ; ENSMUSG00000021186 .
    GeneIDi 23876.
    KEGGi mmu:23876.
    UCSCi uc007otp.1. mouse.

    Organism-specific databases

    CTDi 10516.
    MGIi MGI:1346091. Fbln5.

    Phylogenomic databases

    eggNOGi NOG309650.
    GeneTreei ENSGT00740000115418.
    HOGENOMi HOG000234337.
    HOVERGENi HBG051560.
    InParanoidi Q9WVH9.
    KOi K17340.
    OMAi KGPRDIQ.
    OrthoDBi EOG7W9RTF.
    PhylomeDBi Q9WVH9.
    TreeFami TF317514.

    Enzyme and pathway databases

    Reactomei REACT_198996. Elastic fibre formation.
    REACT_198998. Molecules associated with elastic fibres.

    Miscellaneous databases

    ChiTaRSi FBLN5. mouse.
    NextBioi 303595.
    PROi Q9WVH9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9WVH9.
    CleanExi MM_FBLN5.
    Genevestigatori Q9WVH9.

    Family and domain databases

    InterProi IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    [Graphical view ]
    Pfami PF12662. cEGF. 2 hits.
    PF07645. EGF_CA. 2 hits.
    [Graphical view ]
    SMARTi SM00179. EGF_CA. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
    PS01186. EGF_2. 4 hits.
    PS50026. EGF_3. 5 hits.
    PS01187. EGF_CA. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DANCE, a novel secreted RGD protein expressed in developing, atherosclerotic, and balloon-injured arteries."
      Nakamura T., Ruiz-Lozano P., Lindner V., Yabe D., Taniwaki M., Furukawa Y., Kobuke K., Tashiro K., Lu Z., Andon N.L., Schaub R., Matsumori A., Sasayama S., Chien K.R., Honjo T.
      J. Biol. Chem. 274:22476-22483(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Strain: C57BL/6J.
      Tissue: Eye and Lung.
    3. "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].
      Strain: C57BL/6J.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiFBLN5_MOUSE
    AccessioniPrimary (citable) accession number: Q9WVH9
    Secondary accession number(s): Q541Z7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 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