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Protein

Elastin

Gene

Eln

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 (By similarity).By similarity

GO - Molecular functioni

  • extracellular matrix constituent conferring elasticity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • aorta development Source: RGD
  • blood vessel remodeling Source: RGD
  • cellular response to copper ion Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to fibroblast growth factor stimulus Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to L-ascorbic acid Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cellular response to retinoic acid Source: RGD
  • cellular response to transforming growth factor beta stimulus Source: RGD
  • elastic fiber assembly Source: RGD
  • response to hyperoxia Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Elastin
Alternative name(s):
Tropoelastin
Gene namesi
Name:Eln
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi67394. Eln.

Subcellular locationi

  • Secretedextracellular spaceextracellular matrix By similarity

  • Note: Extracellular matrix of elastic fibers.By similarity

GO - Cellular componenti

  • extracellular matrix Source: RGD
  • extracellular region Source: RGD
  • extracellular space Source: RGD
  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 870843ElastinPRO_0000021165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 3914-hydroxyprolineBy similarity
Modified residuei75 – 7514-hydroxyprolineBy similarity
Modified residuei87 – 871HydroxyprolineBy similarity
Modified residuei105 – 10514-hydroxyprolineBy similarity
Modified residuei122 – 1221AllysineBy similarity
Modified residuei126 – 1261AllysineBy similarity
Modified residuei207 – 20714-hydroxyprolineBy similarity
Modified residuei220 – 22014-hydroxyprolineBy similarity
Modified residuei223 – 22314-hydroxyprolineBy similarity
Modified residuei244 – 24414-hydroxyprolineBy similarity
Modified residuei290 – 2901AllysineBy similarity
Modified residuei309 – 3091AllysineBy similarity
Modified residuei338 – 33814-hydroxyprolineBy similarity
Modified residuei360 – 3601AllysineBy similarity
Modified residuei363 – 3631AllysineBy similarity
Modified residuei375 – 3751HydroxyprolineBy similarity
Modified residuei402 – 40214-hydroxyprolineBy similarity
Modified residuei408 – 40814-hydroxyprolineBy similarity
Modified residuei413 – 4131HydroxyprolineBy similarity
Modified residuei418 – 4181HydroxyprolineBy similarity
Modified residuei434 – 4341AllysineBy similarity
Modified residuei438 – 4381AllysineBy similarity
Modified residuei441 – 4411AllysineBy similarity
Modified residuei488 – 4881AllysineBy similarity
Modified residuei518 – 51814-hydroxyprolineBy similarity
Modified residuei539 – 53914-hydroxyprolineBy similarity
Modified residuei554 – 5541AllysineBy similarity
Modified residuei558 – 5581AllysineBy similarity
Modified residuei615 – 6151AllysineBy similarity
Modified residuei619 – 6191AllysineBy similarity
Modified residuei623 – 6231AllysineBy similarity
Modified residuei637 – 63714-hydroxyprolineBy similarity
Modified residuei646 – 64614-hydroxyprolineBy similarity
Modified residuei662 – 66214-hydroxyprolineBy similarity
Modified residuei670 – 67014-hydroxyprolineBy similarity
Modified residuei677 – 6771AllysineBy similarity
Modified residuei680 – 6801AllysineBy similarity
Modified residuei715 – 71514-hydroxyprolineBy similarity
Modified residuei730 – 7301AllysineBy similarity
Modified residuei734 – 7341AllysineBy similarity
Modified residuei793 – 7931AllysineBy similarity
Modified residuei796 – 7961AllysineBy similarity
Modified residuei842 – 84214-hydroxyprolineBy similarity
Disulfide bondi860 ↔ 865By 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

PaxDbiQ99372.
PRIDEiQ99372.

PTM databases

PhosphoSiteiQ99372.

Expressioni

Inductioni

Down-regulated by DTR via activation of EGFR.1 Publication

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. Interacts with FBLN5 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000030301.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 866839Gly-richAdd
BLAST
Compositional biasi303 – 800498Ala-richAdd
BLAST

Sequence similaritiesi

Belongs to the elastin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IZT8. Eukaryota.
ENOG4111817. LUCA.
InParanoidiQ99372.
KOiK14211.
OrthoDBiEOG754HSW.
TreeFamiTF338594.

Family and domain databases

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

Sequences (8)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q99372-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGLTAAVPQ PGVLLILLLN LLHPAQPGGV PGAVPGGVPG GLPGGVPGGV
60 70 80 90 100
YYPGAGIGGG LGGGALGPGG KPPKPGAGLL GAFGAGPGGL GGAGPGAGLS
110 120 130 140 150
YASRPGGVLV PGGGAGAAAA YKAAAKAGAG LGGIGGVPGG VGVGGVPGAV
160 170 180 190 200
GVGGVPGAVG GIGGIGGLGV STGAVVPQLG AGVGAGGKPG KVPGVGLPGV
210 220 230 240 250
YPGGVLPGTG ARFPGVGVLP GVPTGTGVKA KVPGGGGGAF SGIPGVGPFG
260 270 280 290 300
GQQPGVPLGY PIKAPKLPGG YGLPYTNGKL PYGVAGAGGK AGYPTGTGVG
310 320 330 340 350
SQAAVAAAKA AKYAGAGGGG VLPGVGGGGI PGGAGAIPGI GGITGAGTPA
360 370 380 390 400
AAAAAKAAAK AAKYGAAGGL VPGGPGVRVP GAGIPGVGIP GVGGIPGVGG
410 420 430 440 450
IPGVGGIPGV GGPGIGGPGI VGGPGAVSPA AAAKAAAKAA KYGARGGVGI
460 470 480 490 500
PTYGVGAGGF PGYGVGAGAG LGGASQAAAA AAAAKAAKYG AGGAGTLGGL
510 520 530 540 550
VPGAVPGALP GAVPGALPGA VPGALPGAVP GVPGTGGVPG AGTPAAAAAA
560 570 580 590 600
AAAKAAAKAG QYGLGPGVGG VPGGVGVGGL PGGVGPGGVT GIGTGPGTGL
610 620 630 640 650
VPGDLGGAGT PAAAKSAAKA AAKAQYRAAA GLGAGVPGLG VGAGVPGFGA
660 670 680 690 700
GAGGFGAGAG VPGFGAGAVP GSLAASKAAK YGAAGGLGGP GGLGGPGGLG
710 720 730 740 750
GPGGFGGPGG LGGVPGGVAG GAPAAAAAAK AAAKAAQYGL GGAGGLGAGG
760 770 780 790 800
LGAGGLGAGG LGAGGLGAGG LGAGGVIPGA VGLGGVSPAA AAKAAKYGAA
810 820 830 840 850
GLGGVLGARP FPGGGVAARP GFGLSPIYPG GGAGGLGVGG KPPKPYGGAL
860 870
GALGYQGGGC FGKSCGRKRK
Length:870
Mass (Da):73,330
Last modified:December 6, 2005 - v2
Checksum:i75909F2432FC4054
GO
Isoform 2 (identifier: Q99372-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-313: Missing.

Show »
Length:825
Mass (Da):69,158
Checksum:iF3E089F8C8FCA22B
GO
Isoform 3 (identifier: Q99372-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     314-314: Missing.

Show »
Length:869
Mass (Da):73,259
Checksum:i12822008FC268B5A
GO
Isoform 4 (identifier: Q99372-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     815-829: Missing.

Show »
Length:855
Mass (Da):71,846
Checksum:i17749AE40323BAE4
GO
Isoform 5 (identifier: Q99372-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-313: Missing.
     314-314: Missing.

Show »
Length:824
Mass (Da):69,087
Checksum:i7294FCF2FCC4F4BD
GO
Isoform 6 (identifier: Q99372-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     314-314: Missing.
     815-829: Missing.

Show »
Length:854
Mass (Da):71,775
Checksum:iCB7DFD496CC4C546
GO
Isoform 7 (identifier: Q99372-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-313: Missing.
     815-829: Missing.

Show »
Length:810
Mass (Da):67,675
Checksum:iAD71B1A4B123BA30
GO
Isoform 8 (identifier: Q99372-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-313: Missing.
     314-314: Missing.
     815-829: Missing.

Show »
Length:809
Mass (Da):67,604
Checksum:i2E56BDFB6CC4118C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti705 – 7051F → L in AAH85910 (PubMed:15489334).Curated
Sequence conflicti713 – 7131G → GPGGLGG in AAH85910 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei269 – 31345Missing in isoform 2, isoform 5, isoform 7 and isoform 8. CuratedVSP_004244Add
BLAST
Alternative sequencei314 – 3141Missing in isoform 3, isoform 5, isoform 6 and isoform 8. 1 PublicationVSP_004245
Alternative sequencei815 – 82915Missing in isoform 4, isoform 6, isoform 7 and isoform 8. CuratedVSP_004246Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085910 mRNA. Translation: AAH85910.1.
M60647 mRNA. Translation: AAA42269.1.
M86372
, M86355, M86363, M86364, M86366, M86371 Genomic DNA. Translation: AAA42271.1.
M86376, M86373, M86375 Genomic DNA. Translation: AAA42272.1.
J04035 mRNA. Translation: AAA42268.1.
PIRiA36106. EART.
RefSeqiNP_036854.1. NM_012722.1.
UniGeneiRn.54384.

Genome annotation databases

GeneIDi25043.
KEGGirno:25043.
UCSCiRGD:67394. rat. [Q99372-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085910 mRNA. Translation: AAH85910.1.
M60647 mRNA. Translation: AAA42269.1.
M86372
, M86355, M86363, M86364, M86366, M86371 Genomic DNA. Translation: AAA42271.1.
M86376, M86373, M86375 Genomic DNA. Translation: AAA42272.1.
J04035 mRNA. Translation: AAA42268.1.
PIRiA36106. EART.
RefSeqiNP_036854.1. NM_012722.1.
UniGeneiRn.54384.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000030301.

PTM databases

PhosphoSiteiQ99372.

Proteomic databases

PaxDbiQ99372.
PRIDEiQ99372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25043.
KEGGirno:25043.
UCSCiRGD:67394. rat. [Q99372-1]

Organism-specific databases

CTDi2006.
RGDi67394. Eln.

Phylogenomic databases

eggNOGiENOG410IZT8. Eukaryota.
ENOG4111817. LUCA.
InParanoidiQ99372.
KOiK14211.
OrthoDBiEOG754HSW.
TreeFamiTF338594.

Miscellaneous databases

PROiQ99372.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 3).
    Tissue: Lung.
  2. "Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning."
    Pierce R.A., Deak S.B., Stolle C.A., Boyd C.D.
    Biochemistry 29:9677-9683(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-870 (ISOFORM 1), ALTERNATIVE SPLICING.
    Tissue: Aorta.
  3. Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
  4. "Role of tropoelastin fragmentation in elastogenesis in rat smooth muscle cells."
    Franzblau C., Pratt C.A., Faris B., Colannino N.M., Offner G.D., Mogayzel P.J. Jr., Troxler R.F.
    J. Biol. Chem. 264:15115-15119(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-37.
  5. "Elements of the rat tropoelastin gene associated with alternative splicing."
    Pierce R.A., Alatawi A., Deak S.B., Boyd C.D.
    Genomics 12:651-658(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-539 AND 564-870, ALTERNATIVE SPLICING.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  6. "Rat tropoelastin is synthesized from a 3.5-kilobase mRNA."
    Deak S.B., Pierce R.A., Belsky S.A., Riley D.J., Boyd C.D.
    J. Biol. Chem. 263:13504-13507(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 787-870.
  7. "Heparin-binding EGF-like growth factor regulates elastin and FGF-2 expression in pulmonary fibroblasts."
    Liu J., Rich C.B., Buczek-Thomas J.A., Nugent M.A., Panchenko M.P., Foster J.A.
    Am. J. Physiol. 285:L1106-L1115(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. Cited for: CLEAVAGE OF SIGNAL PEPTIDE AFTER PRO-27, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiELN_RAT
AccessioniPrimary (citable) accession number: Q99372
Secondary accession number(s): Q5RKH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 6, 2005
Last modified: June 8, 2016
This is version 111 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.