P54320 · ELN_MOUSE

Function

function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentelastic fiber
Cellular Componentextracellular region
Cellular Componentextracellular space
Cellular Componentmitochondrion
Molecular Functionextracellular matrix binding
Molecular Functionextracellular matrix constituent conferring elasticity
Biological Processaortic valve morphogenesis
Biological Processblood vessel remodeling
Biological Processextracellular matrix assembly
Biological Processextracellular matrix organization
Biological Processoutflow tract morphogenesis
Biological Processregulation of actin filament polymerization
Biological Processskeletal muscle tissue development
Biological Processstress fiber assembly

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Elastin
  • Alternative names
    • Tropoelastin

Gene names

    • Name
      Eln

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P54320
  • Secondary accessions
    • Q8C9L8

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, modified residue, disulfide bond.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_000002116428-860Elastin
Modified residue354-hydroxyproline
Modified residue724-hydroxyproline
Modified residue84Hydroxyproline
Modified residue1054-hydroxyproline
Modified residue123Allysine
Modified residue127Allysine
Modified residue2174-hydroxyproline
Modified residue2304-hydroxyproline
Modified residue2334-hydroxyproline
Modified residue2534-hydroxyproline
Modified residue299Allysine
Modified residue318Allysine
Modified residue321Allysine
Modified residue3464-hydroxyproline
Modified residue368Allysine
Modified residue371Allysine
Modified residue383Hydroxyproline
Modified residue3994-hydroxyproline
Modified residue4054-hydroxyproline
Modified residue410Hydroxyproline
Modified residue415Hydroxyproline
Modified residue431Allysine
Modified residue435Allysine
Modified residue438Allysine
Modified residue481Allysine
Modified residue484Allysine
Modified residue4984-hydroxyproline
Modified residue5194-hydroxyproline
Modified residue534Allysine
Modified residue595Allysine
Modified residue599Allysine
Modified residue603Allysine
Modified residue6174-hydroxyproline
Modified residue6264-hydroxyproline
Modified residue6444-hydroxyproline
Modified residue6534-hydroxyproline
Modified residue6614-hydroxyproline
Modified residue668Allysine
Modified residue671Allysine
Modified residue7024-hydroxyproline
Modified residue719Allysine
Modified residue723Allysine
Modified residue783Allysine
Modified residue786Allysine
Modified residue8324-hydroxyproline
Disulfide bond850↔855

Post-translational modification

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.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

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. Interacts with FBLN5 and FBN1. Forms a ternary complex with FBN1 and FBLN2 or FBLN5. Interacts with MFAP4 in a Ca 2+-dependent manner; this interaction promotes ELN self-assembly (By similarity).
Interacts with EFEMP2 with moderate affinity (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the elastin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    860
  • Mass (Da)
    71,938
  • Last updated
    2011-07-27 v2
  • Checksum
    7C340F2FFFDC92E5
MAGLTAVVPQPGVLLILLLNLLHPAQPGGVPGAVPGGLPGGVPGGVYYPGAGIGGLGGGGGALGPGGKPPKPGAGLLGTFGAGPGGLGGAGPGAGLGAFPAGTFPGAGALVPGGAAGAAAAYKAAAKAGAGLGGVGGVPGGVGVGGVPGGVGVGGVPGGVGVGGVPGGVGGIGGIGGLGVSTGAVVPQVGAGIGAGGKPGKVPGVGLPGVYPGGVLPGTGARFPGVGVLPGVPTGTGVKAKAPGGGGAFAGIPGVGPFGGQQPGVPLGYPIKAPKLPGGYGLPYTNGKLPYGVAGAGGKAGYPTGTGVGSQAAAAAAKAAKYGAGGAGVLPGVGGGGIPGGAGAIPGIGGIAGAGTPAAAAAAKAAAKAAKYGAAGGLVPGGPGVRLPGAGIPGVGGIPGVGGIPGVGGPGIGGPGIVGGPGAVSPAAAAKAAAKAAKYGARGGVGIPTYGVGAGGFPGYGVGAGAGLGGASPAAAAAAAKAAKYGAGGAGALGGLVPGAVPGALPGAVPAVPGAGGVPGAGTPAAAAAAAAAKAAAKAGLGPGVGGVPGGVGVGGIPGGVGVGGVPGGVGPGGVTGIGAGPGGLGGAGSPAAAKSAAKAAAKAQYRAAAGLGAGVPGFGAGAGVPGFGAGAGVPGFGAGAGVPGFGAGAGVPGFGAGAVPGSLAASKAAKYGAAGGLGGPGGLGGPGGLGGPGGLGGAGVPGRVAGAAPPAAAAAAAKAAAKAAQYGLGGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGGVSPAAAAKAAKYGAAGLGGVLGARPFPGGGVAARPGFGLSPIYPGGGAGGLGVGGKPPKPYGGALGALGYQGGGCFGKSCGRKRK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0J9YV95A0A0J9YV95_MOUSEEln287

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict250in Ref. 1; AAA80155

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U08210
EMBL· GenBank· DDBJ
AAA80155.1
EMBL· GenBank· DDBJ
mRNA
AK041860
EMBL· GenBank· DDBJ
BAC31084.1
EMBL· GenBank· DDBJ
mRNA
CH466529
EMBL· GenBank· DDBJ
EDL19414.1
EMBL· GenBank· DDBJ
Genomic DNA
BC051649
EMBL· GenBank· DDBJ
AAH51649.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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