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P54320

- ELN_MOUSE

UniProt

P54320 - ELN_MOUSE

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Protein
Elastin
Gene
Eln
Organism
Mus musculus (Mouse)
Status
Reviewed - 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
  3. protein binding Source: MGI

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
Note: Extracellular matrix of elastic fibers.

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 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 860833Elastin
PRO_0000021164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 3514-hydroxyproline By similarity
Modified residuei72 – 7214-hydroxyproline By similarity
Modified residuei84 – 841Hydroxyproline By similarity
Modified residuei105 – 10514-hydroxyproline By similarity
Modified residuei123 – 1231Allysine By similarity
Modified residuei127 – 1271Allysine By similarity
Modified residuei217 – 21714-hydroxyproline By similarity
Modified residuei230 – 23014-hydroxyproline By similarity
Modified residuei233 – 23314-hydroxyproline By similarity
Modified residuei253 – 25314-hydroxyproline By similarity
Modified residuei299 – 2991Allysine By similarity
Modified residuei318 – 3181Allysine By similarity
Modified residuei321 – 3211Allysine By similarity
Modified residuei346 – 34614-hydroxyproline By similarity
Modified residuei368 – 3681Allysine By similarity
Modified residuei371 – 3711Allysine By similarity
Modified residuei383 – 3831Hydroxyproline By similarity
Modified residuei399 – 39914-hydroxyproline By similarity
Modified residuei405 – 40514-hydroxyproline By similarity
Modified residuei410 – 4101Hydroxyproline By similarity
Modified residuei415 – 4151Hydroxyproline By similarity
Modified residuei431 – 4311Allysine By similarity
Modified residuei435 – 4351Allysine By similarity
Modified residuei438 – 4381Allysine By similarity
Modified residuei484 – 4841Allysine By similarity
Modified residuei498 – 49814-hydroxyproline By similarity
Modified residuei519 – 51914-hydroxyproline By similarity
Modified residuei534 – 5341Allysine By similarity
Modified residuei595 – 5951Allysine By similarity
Modified residuei599 – 5991Allysine By similarity
Modified residuei603 – 6031Allysine By similarity
Modified residuei617 – 61714-hydroxyproline By similarity
Modified residuei626 – 62614-hydroxyproline By similarity
Modified residuei644 – 64414-hydroxyproline By similarity
Modified residuei653 – 65314-hydroxyproline By similarity
Modified residuei661 – 66114-hydroxyproline By similarity
Modified residuei668 – 6681Allysine By similarity
Modified residuei671 – 6711Allysine By similarity
Modified residuei702 – 70214-hydroxyproline By similarity
Modified residuei719 – 7191Allysine By similarity
Modified residuei723 – 7231Allysine By similarity
Modified residuei783 – 7831Allysine By similarity
Modified residuei786 – 7861Allysine By similarity
Modified residuei832 – 83214-hydroxyproline By similarity
Disulfide bondi850 ↔ 855 By 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

PaxDbiP54320.
PRIDEiP54320.

PTM databases

PhosphoSiteiP54320.

Expressioni

Gene expression databases

ArrayExpressiP54320.
BgeeiP54320.
CleanExiMM_ELN.
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 manner By similarity.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP54320.

Family & Domainsi

Sequence similaritiesi

Belongs to the elastin family.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG331579.
GeneTreeiENSGT00730000111510.
InParanoidiQ8C9L8.
KOiK14211.
OMAiYYPGAGI.
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

MAGLTAVVPQ PGVLLILLLN LLHPAQPGGV PGAVPGGLPG GVPGGVYYPG    50
AGIGGLGGGG GALGPGGKPP KPGAGLLGTF GAGPGGLGGA GPGAGLGAFP 100
AGTFPGAGAL VPGGAAGAAA AYKAAAKAGA GLGGVGGVPG GVGVGGVPGG 150
VGVGGVPGGV GVGGVPGGVG GIGGIGGLGV STGAVVPQVG AGIGAGGKPG 200
KVPGVGLPGV YPGGVLPGTG ARFPGVGVLP GVPTGTGVKA KAPGGGGAFA 250
GIPGVGPFGG QQPGVPLGYP IKAPKLPGGY GLPYTNGKLP YGVAGAGGKA 300
GYPTGTGVGS QAAAAAAKAA KYGAGGAGVL PGVGGGGIPG GAGAIPGIGG 350
IAGAGTPAAA AAAKAAAKAA KYGAAGGLVP GGPGVRLPGA GIPGVGGIPG 400
VGGIPGVGGP GIGGPGIVGG PGAVSPAAAA KAAAKAAKYG ARGGVGIPTY 450
GVGAGGFPGY GVGAGAGLGG ASPAAAAAAA KAAKYGAGGA GALGGLVPGA 500
VPGALPGAVP AVPGAGGVPG AGTPAAAAAA AAAKAAAKAG LGPGVGGVPG 550
GVGVGGIPGG VGVGGVPGGV GPGGVTGIGA GPGGLGGAGS PAAAKSAAKA 600
AAKAQYRAAA GLGAGVPGFG AGAGVPGFGA GAGVPGFGAG AGVPGFGAGA 650
GVPGFGAGAV PGSLAASKAA KYGAAGGLGG PGGLGGPGGL GGPGGLGGAG 700
VPGRVAGAAP PAAAAAAAKA AAKAAQYGLG GAGGLGAGGL GAGGLGAGGL 750
GAGGLGAGGL GAGGLGAGGL GAGGGVSPAA AAKAAKYGAA GLGGVLGARP 800
FPGGGVAARP GFGLSPIYPG GGAGGLGVGG KPPKPYGGAL GALGYQGGGC 850
FGKSCGRKRK 860
Length:860
Mass (Da):71,938
Last modified:July 27, 2011 - v2
Checksum:i7C340F2FFFDC92E5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501A → S in AAA80155. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U08210 mRNA. Translation: AAA80155.1 .
AK041860 mRNA. Translation: BAC31084.1 .
CH466529 Genomic DNA. Translation: EDL19414.1 .
BC051649 mRNA. Translation: AAH51649.1 .
CCDSi CCDS19725.1.
PIRi A55721. EAMS.
RefSeqi NP_031951.2. NM_007925.3.
UniGenei Mm.275320.
Mm.404771.

3D structure databases

ProteinModelPortali P54320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199433. 2 interactions.
IntActi P54320. 1 interaction.
STRINGi 10090.ENSMUSP00000015138.

PTM databases

PhosphoSitei P54320.

Proteomic databases

PaxDbi P54320.
PRIDEi P54320.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015138 ; ENSMUSP00000015138 ; ENSMUSG00000029675 .
GeneIDi 13717.
KEGGi mmu:13717.
UCSCi uc008zwv.1. mouse.

Organism-specific databases

CTDi 2006.
MGIi MGI:95317. Eln.

Phylogenomic databases

eggNOGi NOG331579.
GeneTreei ENSGT00730000111510.
InParanoidi Q8C9L8.
KOi K14211.
OMAi YYPGAGI.
OrthoDBi EOG754HSW.

Enzyme and pathway databases

Reactomei REACT_198996. Elastic fibre formation.
REACT_198998. Molecules associated with elastic fibres.
REACT_199052. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSi ELN. mouse.
NextBioi 284500.
PROi P54320.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54320.
Bgeei P54320.
CleanExi MM_ELN.
Genevestigatori P54320.

Family and domain databases

InterProi IPR003979. Tropoelastin.
[Graphical view ]
PRINTSi PR01500. TROPOELASTIN.
ProtoNeti Search...

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: September 3, 2014
This is version 102 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

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