Human Gene ELN (ENST00000252034.12) from GENCODE V43
Description: Homo sapiens elastin (ELN), transcript variant 1, mRNA. (from RefSeq NM_000501) RefSeq Summary (NM_000501): 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]. Gencode Transcript: ENST00000252034.12 Gencode Gene: ENSG00000049540.19 Transcript (Including UTRs) Position: hg38 chr7:74,028,173-74,069,907 Size: 41,735 Total Exon Count: 33 Strand: + Coding Region Position: hg38 chr7:74,028,188-74,068,700 Size: 40,513 Coding Exon Count: 33
ID:ELN_HUMAN DESCRIPTION: RecName: Full=Elastin; AltName: Full=Tropoelastin; Flags: Precursor; 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 (By similarity). 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. INTERACTION: O95967:EFEMP2; NbExp=5; IntAct=EBI-1222108, EBI-743414; Q9UBX5:FBLN5; NbExp=3; IntAct=EBI-1222108, EBI-947897; P28300:LOX; NbExp=2; IntAct=EBI-1222108, EBI-3893481; SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Note=Extracellular matrix of elastic fibers. TISSUE SPECIFICITY: Expressed within the outer myometrial smooth muscle and throughout the arteriolar tree of uterus (at protein level). Also expressed in the large arteries, lung and skin. PTM: 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. PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely 4-hydroxy as this fits the requirement for 4- hydroxylation in vertebrates (By similarity). DISEASE: Defects in ELN are the cause of cutis laxa, autosomal dominant, type 1 (ADCL1) [MIM:123700]. A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema. DISEASE: Defects in ELN are the cause of supravalvular aortic stenosis (SVAS) [MIM:185500]. SVAS is a congenital narrowing of the ascending aorta which can occur sporadically, as an autosomal dominant condition, or as one component of Williams-Beuren syndrome. DISEASE: Note=ELN is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of ELN may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. SIMILARITY: Belongs to the elastin family. SEQUENCE CAUTION: Sequence=CAD98065.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/ELN"; WEB RESOURCE: Name=Wikipedia; Note=Elastin entry; URL="http://en.wikipedia.org/wiki/Elastin";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P15502
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0005201 extracellular matrix structural constituent GO:0005515 protein binding