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Protein

Elastin

Gene

Eln

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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

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
Complete GO annotation...

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 By similarity
Note: Extracellular matrix of elastic fibers.By similarity

GO - Cellular componenti

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

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

MaxQBiP54320.
PaxDbiP54320.
PRIDEiP54320.

PTM databases

PhosphoSiteiP54320.

Expressioni

Gene expression databases

BgeeiP54320.
CleanExiMM_ELN.
ExpressionAtlasiP54320. baseline and differential.
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 mannerInteracts with FBLN5 (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.
InParanoidiP54320.
KOiK14211.
OMAiNGKLPYG.
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

        10         20         30         40         50
MAGLTAVVPQ PGVLLILLLN LLHPAQPGGV PGAVPGGLPG GVPGGVYYPG
60 70 80 90 100
AGIGGLGGGG GALGPGGKPP KPGAGLLGTF GAGPGGLGGA GPGAGLGAFP
110 120 130 140 150
AGTFPGAGAL VPGGAAGAAA AYKAAAKAGA GLGGVGGVPG GVGVGGVPGG
160 170 180 190 200
VGVGGVPGGV GVGGVPGGVG GIGGIGGLGV STGAVVPQVG AGIGAGGKPG
210 220 230 240 250
KVPGVGLPGV YPGGVLPGTG ARFPGVGVLP GVPTGTGVKA KAPGGGGAFA
260 270 280 290 300
GIPGVGPFGG QQPGVPLGYP IKAPKLPGGY GLPYTNGKLP YGVAGAGGKA
310 320 330 340 350
GYPTGTGVGS QAAAAAAKAA KYGAGGAGVL PGVGGGGIPG GAGAIPGIGG
360 370 380 390 400
IAGAGTPAAA AAAKAAAKAA KYGAAGGLVP GGPGVRLPGA GIPGVGGIPG
410 420 430 440 450
VGGIPGVGGP GIGGPGIVGG PGAVSPAAAA KAAAKAAKYG ARGGVGIPTY
460 470 480 490 500
GVGAGGFPGY GVGAGAGLGG ASPAAAAAAA KAAKYGAGGA GALGGLVPGA
510 520 530 540 550
VPGALPGAVP AVPGAGGVPG AGTPAAAAAA AAAKAAAKAG LGPGVGGVPG
560 570 580 590 600
GVGVGGIPGG VGVGGVPGGV GPGGVTGIGA GPGGLGGAGS PAAAKSAAKA
610 620 630 640 650
AAKAQYRAAA GLGAGVPGFG AGAGVPGFGA GAGVPGFGAG AGVPGFGAGA
660 670 680 690 700
GVPGFGAGAV PGSLAASKAA KYGAAGGLGG PGGLGGPGGL GGPGGLGGAG
710 720 730 740 750
VPGRVAGAAP PAAAAAAAKA AAKAAQYGLG GAGGLGAGGL GAGGLGAGGL
760 770 780 790 800
GAGGLGAGGL GAGGLGAGGL GAGGGVSPAA AAKAAKYGAA GLGGVLGARP
810 820 830 840 850
FPGGGVAARP GFGLSPIYPG GGAGGLGVGG KPPKPYGGAL GALGYQGGGC
860
FGKSCGRKRK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP54320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP54320.

Proteomic databases

MaxQBiP54320.
PaxDbiP54320.
PRIDEiP54320.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2006.
MGIiMGI:95317. Eln.

Phylogenomic databases

eggNOGiNOG331579.
GeneTreeiENSGT00730000111510.
InParanoidiP54320.
KOiK14211.
OMAiNGKLPYG.
OrthoDBiEOG754HSW.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiEln. mouse.
NextBioi284500.
PROiP54320.
SOURCEiSearch...

Gene expression databases

BgeeiP54320.
CleanExiMM_ELN.
ExpressionAtlasiP54320. baseline and differential.
GenevestigatoriP54320.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 107 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.