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P54320

- ELN_MOUSE

UniProt

P54320 - ELN_MOUSE

Protein

Elastin

Gene

Eln

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle.1 Publication

    GO - Molecular functioni

    1. extracellular matrix binding Source: MGI
    2. extracellular matrix constituent conferring elasticity Source: Ensembl
    3. protein binding Source: MGI

    GO - Biological processi

    1. blood vessel remodeling Source: Ensembl
    2. extracellular matrix organization Source: MGI
    3. regulation of actin filament polymerization Source: MGI
    4. skeletal muscle tissue development Source: MGI
    5. stress fiber assembly Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_198996. Elastic fibre formation.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_199052. Degradation of the extracellular matrix.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elastin
    Alternative name(s):
    Tropoelastin
    Gene namesi
    Name:Eln
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:95317. Eln.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix
    Note: Extracellular matrix of elastic fibers.

    GO - Cellular componenti

    1. elastic fiber Source: MGI
    2. mitochondrion Source: MGI
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 860833ElastinPRO_0000021164Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 3514-hydroxyprolineBy similarity
    Modified residuei72 – 7214-hydroxyprolineBy similarity
    Modified residuei84 – 841HydroxyprolineBy similarity
    Modified residuei105 – 10514-hydroxyprolineBy similarity
    Modified residuei123 – 1231AllysineBy similarity
    Modified residuei127 – 1271AllysineBy similarity
    Modified residuei217 – 21714-hydroxyprolineBy similarity
    Modified residuei230 – 23014-hydroxyprolineBy similarity
    Modified residuei233 – 23314-hydroxyprolineBy similarity
    Modified residuei253 – 25314-hydroxyprolineBy similarity
    Modified residuei299 – 2991AllysineBy similarity
    Modified residuei318 – 3181AllysineBy similarity
    Modified residuei321 – 3211AllysineBy similarity
    Modified residuei346 – 34614-hydroxyprolineBy similarity
    Modified residuei368 – 3681AllysineBy similarity
    Modified residuei371 – 3711AllysineBy similarity
    Modified residuei383 – 3831HydroxyprolineBy similarity
    Modified residuei399 – 39914-hydroxyprolineBy similarity
    Modified residuei405 – 40514-hydroxyprolineBy similarity
    Modified residuei410 – 4101HydroxyprolineBy similarity
    Modified residuei415 – 4151HydroxyprolineBy similarity
    Modified residuei431 – 4311AllysineBy similarity
    Modified residuei435 – 4351AllysineBy similarity
    Modified residuei438 – 4381AllysineBy similarity
    Modified residuei484 – 4841AllysineBy similarity
    Modified residuei498 – 49814-hydroxyprolineBy similarity
    Modified residuei519 – 51914-hydroxyprolineBy similarity
    Modified residuei534 – 5341AllysineBy similarity
    Modified residuei595 – 5951AllysineBy similarity
    Modified residuei599 – 5991AllysineBy similarity
    Modified residuei603 – 6031AllysineBy similarity
    Modified residuei617 – 61714-hydroxyprolineBy similarity
    Modified residuei626 – 62614-hydroxyprolineBy similarity
    Modified residuei644 – 64414-hydroxyprolineBy similarity
    Modified residuei653 – 65314-hydroxyprolineBy similarity
    Modified residuei661 – 66114-hydroxyprolineBy similarity
    Modified residuei668 – 6681AllysineBy similarity
    Modified residuei671 – 6711AllysineBy similarity
    Modified residuei702 – 70214-hydroxyprolineBy similarity
    Modified residuei719 – 7191AllysineBy similarity
    Modified residuei723 – 7231AllysineBy similarity
    Modified residuei783 – 7831AllysineBy similarity
    Modified residuei786 – 7861AllysineBy similarity
    Modified residuei832 – 83214-hydroxyprolineBy similarity
    Disulfide bondi850 ↔ 855By similarity

    Post-translational modificationi

    Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tetrafunctional cross-links. The most abundant cross-links in mature elastin fibers are lysinonorleucine, allysine aldol, desmosine, and isodesmosine.
    Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity

    Keywords - PTMi

    Disulfide bond, Hydroxylation

    Proteomic databases

    PaxDbiP54320.
    PRIDEiP54320.

    PTM databases

    PhosphoSiteiP54320.

    Expressioni

    Gene expression databases

    ArrayExpressiP54320.
    BgeeiP54320.
    CleanExiMM_ELN.
    GenevestigatoriP54320.

    Interactioni

    Subunit structurei

    The polymeric elastin chains are cross-linked together into an extensible 3D network. Forms a ternary complex with BGN and MFAP2. Interacts with MFAP2 via divalent cations (calcium > magnesium > manganese) in a dose-dependent and saturating manner By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199433. 2 interactions.
    IntActiP54320. 1 interaction.
    STRINGi10090.ENSMUSP00000015138.

    Structurei

    3D structure databases

    ProteinModelPortaliP54320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the elastin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG331579.
    GeneTreeiENSGT00730000111510.
    InParanoidiQ8C9L8.
    KOiK14211.
    OMAiYYPGAGI.
    OrthoDBiEOG754HSW.

    Family and domain databases

    InterProiIPR003979. Tropoelastin.
    [Graphical view]
    PRINTSiPR01500. TROPOELASTIN.

    Sequencei

    Sequence statusi: Complete.

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

    P54320-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGLTAVVPQ PGVLLILLLN LLHPAQPGGV PGAVPGGLPG GVPGGVYYPG    50
    AGIGGLGGGG GALGPGGKPP KPGAGLLGTF GAGPGGLGGA GPGAGLGAFP 100
    AGTFPGAGAL VPGGAAGAAA AYKAAAKAGA GLGGVGGVPG GVGVGGVPGG 150
    VGVGGVPGGV GVGGVPGGVG GIGGIGGLGV STGAVVPQVG AGIGAGGKPG 200
    KVPGVGLPGV YPGGVLPGTG ARFPGVGVLP GVPTGTGVKA KAPGGGGAFA 250
    GIPGVGPFGG QQPGVPLGYP IKAPKLPGGY GLPYTNGKLP YGVAGAGGKA 300
    GYPTGTGVGS QAAAAAAKAA KYGAGGAGVL PGVGGGGIPG GAGAIPGIGG 350
    IAGAGTPAAA AAAKAAAKAA KYGAAGGLVP GGPGVRLPGA GIPGVGGIPG 400
    VGGIPGVGGP GIGGPGIVGG PGAVSPAAAA KAAAKAAKYG ARGGVGIPTY 450
    GVGAGGFPGY GVGAGAGLGG ASPAAAAAAA KAAKYGAGGA GALGGLVPGA 500
    VPGALPGAVP AVPGAGGVPG AGTPAAAAAA AAAKAAAKAG LGPGVGGVPG 550
    GVGVGGIPGG VGVGGVPGGV GPGGVTGIGA GPGGLGGAGS PAAAKSAAKA 600
    AAKAQYRAAA GLGAGVPGFG AGAGVPGFGA GAGVPGFGAG AGVPGFGAGA 650
    GVPGFGAGAV PGSLAASKAA KYGAAGGLGG PGGLGGPGGL GGPGGLGGAG 700
    VPGRVAGAAP PAAAAAAAKA AAKAAQYGLG GAGGLGAGGL GAGGLGAGGL 750
    GAGGLGAGGL GAGGLGAGGL GAGGGVSPAA AAKAAKYGAA GLGGVLGARP 800
    FPGGGVAARP GFGLSPIYPG GGAGGLGVGG KPPKPYGGAL GALGYQGGGC 850
    FGKSCGRKRK 860
    Length:860
    Mass (Da):71,938
    Last modified:July 27, 2011 - v2
    Checksum:i7C340F2FFFDC92E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti250 – 2501A → S in AAA80155. (PubMed:7829060)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08210 mRNA. Translation: AAA80155.1.
    AK041860 mRNA. Translation: BAC31084.1.
    CH466529 Genomic DNA. Translation: EDL19414.1.
    BC051649 mRNA. Translation: AAH51649.1.
    CCDSiCCDS19725.1.
    PIRiA55721. EAMS.
    RefSeqiNP_031951.2. NM_007925.3.
    UniGeneiMm.275320.
    Mm.404771.

    Genome annotation databases

    EnsembliENSMUST00000015138; ENSMUSP00000015138; ENSMUSG00000029675.
    GeneIDi13717.
    KEGGimmu:13717.
    UCSCiuc008zwv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08210 mRNA. Translation: AAA80155.1 .
    AK041860 mRNA. Translation: BAC31084.1 .
    CH466529 Genomic DNA. Translation: EDL19414.1 .
    BC051649 mRNA. Translation: AAH51649.1 .
    CCDSi CCDS19725.1.
    PIRi A55721. EAMS.
    RefSeqi NP_031951.2. NM_007925.3.
    UniGenei Mm.275320.
    Mm.404771.

    3D structure databases

    ProteinModelPortali P54320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199433. 2 interactions.
    IntActi P54320. 1 interaction.
    STRINGi 10090.ENSMUSP00000015138.

    PTM databases

    PhosphoSitei P54320.

    Proteomic databases

    PaxDbi P54320.
    PRIDEi P54320.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015138 ; ENSMUSP00000015138 ; ENSMUSG00000029675 .
    GeneIDi 13717.
    KEGGi mmu:13717.
    UCSCi uc008zwv.1. mouse.

    Organism-specific databases

    CTDi 2006.
    MGIi MGI:95317. Eln.

    Phylogenomic databases

    eggNOGi NOG331579.
    GeneTreei ENSGT00730000111510.
    InParanoidi Q8C9L8.
    KOi K14211.
    OMAi YYPGAGI.
    OrthoDBi EOG754HSW.

    Enzyme and pathway databases

    Reactomei REACT_198996. Elastic fibre formation.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_199052. Degradation of the extracellular matrix.

    Miscellaneous databases

    ChiTaRSi ELN. mouse.
    NextBioi 284500.
    PROi P54320.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54320.
    Bgeei P54320.
    CleanExi MM_ELN.
    Genevestigatori P54320.

    Family and domain databases

    InterProi IPR003979. Tropoelastin.
    [Graphical view ]
    PRINTSi PR01500. TROPOELASTIN.
    ProtoNeti Search...

    Publicationsi

    1. "Use of an intron polymorphism to localize the tropoelastin gene to mouse chromosome 5 in a region of linkage conservation with human chromosome 7."
      Wydner K.S., Sechler J.L., Boyd C.D., Passmore H.C.
      Genomics 23:125-131(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Lung.
    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: Thymus.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Elastin is an essential determinant of arterial morphogenesis."
      Li D.Y., Brooke B., Davis E.C., Mecham R.P., Sorensen L.K., Boak B.B., Eichwald E., Keating M.T.
      Nature 393:276-280(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiELN_MOUSE
    AccessioniPrimary (citable) accession number: P54320
    Secondary accession number(s): Q8C9L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 103 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