ELN

Protein identityUniProt · HPA

UniProt accession

P15502

Gene

ELN

Ensembl

ENSG00000049540

Chromosome

7

Canonical length

786 aa

Protein class

Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins

Subcellular location

Plasma membrane

Secretome location

Secreted to extracellular matrix

OverviewNCBI Gene

This gene encodes a protein that is one of the two components of elastic fibers. Elastic fibers comprise part of the extracellular matrix and confer elasticity to organs and tissues including the heart, skin, lungs, ligaments, and blood vessels. The encoded protein is rich in hydrophobic amino acids such as glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Degradation products of the encoded protein, known as elastin-derived peptides or elastokines, bind the elastin receptor complex and other receptors and stimulate migration and proliferation of monocytes and skin fibroblasts. Elastokines can also contribute to cancer progression. Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and autosomal dominant cutis laxa. [provided by RefSeq, Aug 2017]

Canonical amino-acid sequenceUniProt

786 residues, UniProt reviewed canonical sequence.

>P15502|ELN
     1  MAGLTAAAPR PGVLLLLLSI LHPSRPGGVP GAIPGGVPGG VFYPGAGLGA LGGGALGPGG
    61  KPLKPVPGGL AGAGLGAGLG AFPAVTFPGA LVPGGVADAA AAYKAAKAGA GLGGVPGVGG
   121  LGVSAGAVVP QPGAGVKPGK VPGVGLPGVY PGGVLPGARF PGVGVLPGVP TGAGVKPKAP
   181  GVGGAFAGIP GVGPFGGPQP GVPLGYPIKA PKLPGGYGLP YTTGKLPYGY GPGGVAGAAG
   241  KAGYPTGTGV GPQAAAAAAA KAAAKFGAGA AGVLPGVGGA GVPGVPGAIP GIGGIAGVGT
   301  PAAAAAAAAA AKAAKYGAAA GLVPGGPGFG PGVVGVPGAG VPGVGVPGAG IPVVPGAGIP
   361  GAAVPGVVSP EAAAKAAAKA AKYGARPGVG VGGIPTYGVG AGGFPGFGVG VGGIPGVAGV
   421  PGVGGVPGVG GVPGVGISPE AQAAAAAKAA KYGAAGAGVL GGLVPGAPGA VPGVPGTGGV
   481  PGVGTPAAAA AKAAAKAAQF GLVPGVGVAP GVGVAPGVGV APGVGLAPGV GVAPGVGVAP
   541  GVGVAPGIGP GGVAAAAKSA AKVAAKAQLR AAAGLGAGIP GLGVGVGVPG LGVGAGVPGL
   601  GVGAGVPGFG AGADEGVRRS LSPELREGDP SSSQHLPSTP SSPRVPGALA AAKAAKYGAA
   661  VPGVLGGLGA LGGVGIPGGV VGAGPAAAAA AAKAAAKAAQ FGLVGAAGLG GLGVGGLGVP
   721  GVGGLGGIPP AAAAKAAKYG AAGLGGVLGG AGQFPLGGVA ARPGFGLSPI FPGGACLGKA
   781  CGRKRK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ELN can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Secreted

Secreted

Yes

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.75

Highest tissue expression

1,228 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ELN.

Disease | AllUniProt

Conditions ELN is implicated in, by any mechanism.

• Cutis laxa, autosomal dominant, 1 (ADCL1) MIM:123700
• Supravalvular aortic stenosis (SVAS) MIM:185500

Disease | GeneticClinVar

201 pathogenic / likely-pathogenic of 1,317 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Supravalvar aortic stenosis
• Cutis laxa, autosomal dominant 1
• ELN-related disorder
• Inborn genetic diseases
• Williams syndrome

Disease | ImmuneIEDB

Conditions an epitope on ELN was assayed in.

• respiratory system disease T cell

Disease | AutoantibodyPubMed

Conditions in which antibodies against ELN are reported. Each links to that disease's full target list.

Showing 0 of 3 — disease pages carrying at least 10 antigens.

ReferencesPubMed · IEDB

Publications for ELN from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.87

gnomAD pLI

0

gnomAD missense Z

0.05

DepMap mean gene effect

0.03

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• animal organ morphogenesis
• aortic valve morphogenesis
• blood circulation
• extracellular matrix assembly
• outflow tract morphogenesis
• regulation of actin filament polymerization
• regulation of smooth muscle cell proliferation
• respiratory gaseous exchange by respiratory system
• skeletal muscle tissue development
• stress fiber assembly

Molecular functions

• extracellular matrix binding
• extracellular matrix constituent conferring elasticity
• extracellular matrix structural constituent

Cellular components

• elastic fiber
• extracellular matrix
• extracellular region

Protein domainsUniProt · Pfam · InterPro

• Tropoelastin

KeywordsUniProt

• Disulfide bond
• Extracellular matrix
• Hydroxylation
• Repeat
• Secreted
• Signal
• Williams-Beuren syndrome

InteractionsUniProt · HPA

Protein binding partners of ELN in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• FBLN5
• FBN1
• MFAP2
• MFAP4