P54320 · ELN_MOUSE
- ProteinElastin
- GeneEln
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids860 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | elastic fiber | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | mitochondrion | |
Molecular Function | extracellular matrix binding | |
Molecular Function | extracellular matrix constituent conferring elasticity | |
Biological Process | aortic valve morphogenesis | |
Biological Process | blood vessel remodeling | |
Biological Process | extracellular matrix assembly | |
Biological Process | extracellular matrix organization | |
Biological Process | outflow tract morphogenesis | |
Biological Process | regulation of actin filament polymerization | |
Biological Process | skeletal muscle tissue development | |
Biological Process | stress fiber assembly |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElastin
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP54320
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Extracellular matrix of elastic fibers.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MAGLTAVVPQPGVLLILLLNLLHPAQP | ||||||
Chain | PRO_0000021164 | 28-860 | Elastin | |||
Sequence: GGVPGAVPGGLPGGVPGGVYYPGAGIGGLGGGGGALGPGGKPPKPGAGLLGTFGAGPGGLGGAGPGAGLGAFPAGTFPGAGALVPGGAAGAAAAYKAAAKAGAGLGGVGGVPGGVGVGGVPGGVGVGGVPGGVGVGGVPGGVGGIGGIGGLGVSTGAVVPQVGAGIGAGGKPGKVPGVGLPGVYPGGVLPGTGARFPGVGVLPGVPTGTGVKAKAPGGGGAFAGIPGVGPFGGQQPGVPLGYPIKAPKLPGGYGLPYTNGKLPYGVAGAGGKAGYPTGTGVGSQAAAAAAKAAKYGAGGAGVLPGVGGGGIPGGAGAIPGIGGIAGAGTPAAAAAAKAAAKAAKYGAAGGLVPGGPGVRLPGAGIPGVGGIPGVGGIPGVGGPGIGGPGIVGGPGAVSPAAAAKAAAKAAKYGARGGVGIPTYGVGAGGFPGYGVGAGAGLGGASPAAAAAAAKAAKYGAGGAGALGGLVPGAVPGALPGAVPAVPGAGGVPGAGTPAAAAAAAAAKAAAKAGLGPGVGGVPGGVGVGGIPGGVGVGGVPGGVGPGGVTGIGAGPGGLGGAGSPAAAKSAAKAAAKAQYRAAAGLGAGVPGFGAGAGVPGFGAGAGVPGFGAGAGVPGFGAGAGVPGFGAGAVPGSLAASKAAKYGAAGGLGGPGGLGGPGGLGGPGGLGGAGVPGRVAGAAPPAAAAAAAKAAAKAAQYGLGGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGGVSPAAAAKAAKYGAAGLGGVLGARPFPGGGVAARPGFGLSPIYPGGGAGGLGVGGKPPKPYGGALGALGYQGGGCFGKSCGRKRK | ||||||
Modified residue | 35 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 72 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 84 | Hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 105 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 123 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 127 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 217 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 230 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 233 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 253 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 299 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 318 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 321 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 346 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 368 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 371 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 383 | Hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 399 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 405 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 410 | Hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 415 | Hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 431 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 435 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 438 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 481 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 484 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 498 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 519 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 534 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 595 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 599 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 603 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 617 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 626 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 644 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 653 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 661 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 668 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 671 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 702 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 719 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 723 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 783 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 786 | Allysine | ||||
Sequence: K | ||||||
Modified residue | 832 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Disulfide bond | 850↔855 | |||||
Sequence: CFGKSC |
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
- PTM
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).
Interacts with EFEMP2 with moderate affinity (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Sequence similarities
Belongs to the elastin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length860
- Mass (Da)71,938
- Last updated2011-07-27 v2
- Checksum7C340F2FFFDC92E5
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YV95 | A0A0J9YV95_MOUSE | Eln | 287 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 250 | in Ref. 1; AAA80155 | ||||
Sequence: A → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |