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P54320 (ELN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elastin
Alternative name(s):
Tropoelastin
Gene names
Name:Eln
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length860 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.5

Subunit structure

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 By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix. Note: Extracellular matrix of elastic fibers.

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 By similarity.

Sequence similarities

Belongs to the elastin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 860833Elastin
PRO_0000021164

Amino acid modifications

Modified residue3514-hydroxyproline By similarity
Modified residue7214-hydroxyproline By similarity
Modified residue841Hydroxyproline By similarity
Modified residue10514-hydroxyproline By similarity
Modified residue1231Allysine By similarity
Modified residue1271Allysine By similarity
Modified residue21714-hydroxyproline By similarity
Modified residue23014-hydroxyproline By similarity
Modified residue23314-hydroxyproline By similarity
Modified residue25314-hydroxyproline By similarity
Modified residue2991Allysine By similarity
Modified residue3181Allysine By similarity
Modified residue3211Allysine By similarity
Modified residue34614-hydroxyproline By similarity
Modified residue3681Allysine By similarity
Modified residue3711Allysine By similarity
Modified residue3831Hydroxyproline By similarity
Modified residue39914-hydroxyproline By similarity
Modified residue40514-hydroxyproline By similarity
Modified residue4101Hydroxyproline By similarity
Modified residue4151Hydroxyproline By similarity
Modified residue4311Allysine By similarity
Modified residue4351Allysine By similarity
Modified residue4381Allysine By similarity
Modified residue4841Allysine By similarity
Modified residue49814-hydroxyproline By similarity
Modified residue51914-hydroxyproline By similarity
Modified residue5341Allysine By similarity
Modified residue5951Allysine By similarity
Modified residue5991Allysine By similarity
Modified residue6031Allysine By similarity
Modified residue61714-hydroxyproline By similarity
Modified residue62614-hydroxyproline By similarity
Modified residue64414-hydroxyproline By similarity
Modified residue65314-hydroxyproline By similarity
Modified residue66114-hydroxyproline By similarity
Modified residue6681Allysine By similarity
Modified residue6711Allysine By similarity
Modified residue70214-hydroxyproline By similarity
Modified residue7191Allysine By similarity
Modified residue7231Allysine By similarity
Modified residue7831Allysine By similarity
Modified residue7861Allysine By similarity
Modified residue83214-hydroxyproline By similarity
Disulfide bond850 ↔ 855 By similarity

Experimental info

Sequence conflict2501A → S in AAA80155. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54320 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7C340F2FFFDC92E5

FASTA86071,938
        10         20         30         40         50         60 
MAGLTAVVPQ PGVLLILLLN LLHPAQPGGV PGAVPGGLPG GVPGGVYYPG AGIGGLGGGG 

        70         80         90        100        110        120 
GALGPGGKPP KPGAGLLGTF GAGPGGLGGA GPGAGLGAFP AGTFPGAGAL VPGGAAGAAA 

       130        140        150        160        170        180 
AYKAAAKAGA GLGGVGGVPG GVGVGGVPGG VGVGGVPGGV GVGGVPGGVG GIGGIGGLGV 

       190        200        210        220        230        240 
STGAVVPQVG AGIGAGGKPG KVPGVGLPGV YPGGVLPGTG ARFPGVGVLP GVPTGTGVKA 

       250        260        270        280        290        300 
KAPGGGGAFA GIPGVGPFGG QQPGVPLGYP IKAPKLPGGY GLPYTNGKLP YGVAGAGGKA 

       310        320        330        340        350        360 
GYPTGTGVGS QAAAAAAKAA KYGAGGAGVL PGVGGGGIPG GAGAIPGIGG IAGAGTPAAA 

       370        380        390        400        410        420 
AAAKAAAKAA KYGAAGGLVP GGPGVRLPGA GIPGVGGIPG VGGIPGVGGP GIGGPGIVGG 

       430        440        450        460        470        480 
PGAVSPAAAA KAAAKAAKYG ARGGVGIPTY GVGAGGFPGY GVGAGAGLGG ASPAAAAAAA 

       490        500        510        520        530        540 
KAAKYGAGGA GALGGLVPGA VPGALPGAVP AVPGAGGVPG AGTPAAAAAA AAAKAAAKAG 

       550        560        570        580        590        600 
LGPGVGGVPG GVGVGGIPGG VGVGGVPGGV GPGGVTGIGA GPGGLGGAGS PAAAKSAAKA 

       610        620        630        640        650        660 
AAKAQYRAAA GLGAGVPGFG AGAGVPGFGA GAGVPGFGAG AGVPGFGAGA GVPGFGAGAV 

       670        680        690        700        710        720 
PGSLAASKAA KYGAAGGLGG PGGLGGPGGL GGPGGLGGAG VPGRVAGAAP PAAAAAAAKA 

       730        740        750        760        770        780 
AAKAAQYGLG GAGGLGAGGL GAGGLGAGGL GAGGLGAGGL GAGGLGAGGL GAGGGVSPAA 

       790        800        810        820        830        840 
AAKAAKYGAA GLGGVLGARP FPGGGVAARP GFGLSPIYPG GGAGGLGVGG KPPKPYGGAL 

       850        860 
GALGYQGGGC FGKSCGRKRK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U08210 mRNA. Translation: AAA80155.1.
AK041860 mRNA. Translation: BAC31084.1.
CH466529 Genomic DNA. Translation: EDL19414.1.
BC051649 mRNA. Translation: AAH51649.1.
IPIIPI00134505.
PIREAMS. A55721.
RefSeqNP_031951.2. NM_007925.3.
UniGeneMm.275320.
Mm.404771.

3D structure databases

ProteinModelPortalP54320.
SMRP54320. Positions 28-105.
ModBaseSearch...

Protein-protein interaction databases

IntActP54320. 1 interaction.
STRING10090.ENSMUSP00000015138.

PTM databases

PhosphoSiteP54320.

Proteomic databases

PaxDbP54320.
PRIDEP54320.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015138; ENSMUSP00000015138; ENSMUSG00000029675.
GeneID13717.
KEGGmmu:13717.

Organism-specific databases

CTD2006.
MGIMGI:95317. Eln.

Phylogenomic databases

eggNOGNOG331579.
GeneTreeENSGT00690000102270.
InParanoidQ8C9L8.
KOK14211.
OMAPPMTHIV.

Gene expression databases

ArrayExpressP54320.
BgeeP54320.
CleanExMM_ELN.
GenevestigatorP54320.
GermOnlineENSMUSG00000029675. Mus musculus.

Family and domain databases

InterProIPR003979. Tropoelastin.
[Graphical view]
PRINTSPR01500. TROPOELASTIN.
ProtoNetSearch...

Other

ChiTaRSELN. mouse.
NextBio284500.
SOURCESearch...

Entry information

Entry nameELN_MOUSE
AccessionPrimary (citable) accession number: P54320
Secondary accession number(s): Q8C9L8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents