ELN_MOUSE
ID ELN_MOUSE Reviewed; 860 AA.
AC P54320; Q8C9L8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Elastin;
DE AltName: Full=Tropoelastin;
DE Flags: Precursor;
GN Name=Eln;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=7829060; DOI=10.1006/geno.1994.1467;
RA Wydner K.S., Sechler J.L., Boyd C.D., Passmore H.C.;
RT "Use of an intron polymorphism to localize the tropoelastin gene to mouse
RT chromosome 5 in a region of linkage conservation with human chromosome 7.";
RL Genomics 23:125-131(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=9607766; DOI=10.1038/30522;
RA Li D.Y., Brooke B., Davis E.C., Mecham R.P., Sorensen L.K., Boak B.B.,
RA Eichwald E., Keating M.T.;
RT "Elastin is an essential determinant of arterial morphogenesis.";
RL Nature 393:276-280(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Major structural protein of tissues such as aorta and nuchal
CC ligament, which must expand rapidly and recover completely. Molecular
CC determinant of the late arterial morphogenesis, stabilizing arterial
CC structure by regulating proliferation and organization of vascular
CC smooth muscle. {ECO:0000269|PubMed:9607766}.
CC -!- SUBUNIT: The polymeric elastin chains are cross-linked together into an
CC extensible 3D network. Forms a ternary complex with BGN and MFAP2.
CC Interacts with MFAP2 via divalent cations (calcium > magnesium >
CC manganese) in a dose-dependent and saturating manner. Interacts with
CC FBLN5 and FBN1. Forms a ternary complex with FBN1 and FBLN2 or FBLN5.
CC Interacts with MFAP4 in a Ca (2+)-dependent manner; this interaction
CC promotes ELN self-assembly (By similarity). Interacts with EFEMP2 with
CC moderate affinity (By similarity). {ECO:0000250|UniProtKB:P04985,
CC ECO:0000250|UniProtKB:P15502}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P15502}. Note=Extracellular matrix of
CC elastic fibers. {ECO:0000250|UniProtKB:P15502}.
CC -!- PTM: Elastin is formed through the cross-linking of its soluble
CC precursor tropoelastin. Cross-linking is initiated through the action
CC of lysyl oxidase on exposed lysines to form allysine. Subsequent
CC spontaneous condensation reactions with other allysine or unmodified
CC lysine residues result in various bi-, tri-, and tetrafunctional cross-
CC links. The most abundant cross-links in mature elastin fibers are
CC lysinonorleucine, allysine aldol, desmosine, and isodesmosine.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the elastin family. {ECO:0000305}.
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DR EMBL; U08210; AAA80155.1; -; mRNA.
DR EMBL; AK041860; BAC31084.1; -; mRNA.
DR EMBL; CH466529; EDL19414.1; -; Genomic_DNA.
DR EMBL; BC051649; AAH51649.1; -; mRNA.
DR CCDS; CCDS19725.1; -.
DR PIR; A55721; EAMS.
DR RefSeq; NP_031951.2; NM_007925.4.
DR AlphaFoldDB; P54320; -.
DR BioGRID; 199433; 3.
DR IntAct; P54320; 1.
DR STRING; 10090.ENSMUSP00000015138; -.
DR PhosphoSitePlus; P54320; -.
DR MaxQB; P54320; -.
DR PaxDb; P54320; -.
DR PRIDE; P54320; -.
DR ProteomicsDB; 277820; -.
DR Antibodypedia; 4380; 434 antibodies from 35 providers.
DR DNASU; 13717; -.
DR Ensembl; ENSMUST00000015138; ENSMUSP00000015138; ENSMUSG00000029675.
DR GeneID; 13717; -.
DR KEGG; mmu:13717; -.
DR UCSC; uc008zwv.1; mouse.
DR CTD; 2006; -.
DR MGI; MGI:95317; Eln.
DR VEuPathDB; HostDB:ENSMUSG00000029675; -.
DR eggNOG; ENOG502RYNR; Eukaryota.
DR GeneTree; ENSGT00730000111510; -.
DR HOGENOM; CLU_021236_0_0_1; -.
DR InParanoid; P54320; -.
DR OMA; KTKTHHR; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 13717; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Eln; mouse.
DR PRO; PR:P54320; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P54320; protein.
DR Bgee; ENSMUSG00000029675; Expressed in ascending aorta and 269 other tissues.
DR ExpressionAtlas; P54320; baseline and differential.
DR Genevisible; P54320; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0071953; C:elastic fiber; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; ISO:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0043149; P:stress fiber assembly; IMP:MGI.
DR InterPro; IPR003979; Tropoelastin.
DR PANTHER; PTHR24018; PTHR24018; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Extracellular matrix; Hydroxylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:Q99372"
FT CHAIN 28..860
FT /note="Elastin"
FT /id="PRO_0000021164"
FT MOD_RES 35
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 123
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 127
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 217
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 230
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 233
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 253
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 299
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 318
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 321
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 346
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 368
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 371
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 383
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 399
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 405
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 410
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 415
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 431
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 435
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 438
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 481
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 484
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 498
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 519
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 534
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 595
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 599
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 603
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 617
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 626
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 644
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 653
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 661
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 668
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 671
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 702
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 719
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 723
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 783
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 786
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 832
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 850..855
FT /evidence="ECO:0000250"
FT CONFLICT 250
FT /note="A -> S (in Ref. 1; AAA80155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 860 AA; 71938 MW; 7C340F2FFFDC92E5 CRC64;
MAGLTAVVPQ PGVLLILLLN LLHPAQPGGV PGAVPGGLPG GVPGGVYYPG AGIGGLGGGG
GALGPGGKPP KPGAGLLGTF GAGPGGLGGA GPGAGLGAFP AGTFPGAGAL VPGGAAGAAA
AYKAAAKAGA GLGGVGGVPG GVGVGGVPGG VGVGGVPGGV GVGGVPGGVG GIGGIGGLGV
STGAVVPQVG AGIGAGGKPG KVPGVGLPGV YPGGVLPGTG ARFPGVGVLP GVPTGTGVKA
KAPGGGGAFA GIPGVGPFGG QQPGVPLGYP IKAPKLPGGY GLPYTNGKLP YGVAGAGGKA
GYPTGTGVGS QAAAAAAKAA KYGAGGAGVL PGVGGGGIPG GAGAIPGIGG IAGAGTPAAA
AAAKAAAKAA KYGAAGGLVP GGPGVRLPGA GIPGVGGIPG VGGIPGVGGP GIGGPGIVGG
PGAVSPAAAA KAAAKAAKYG ARGGVGIPTY GVGAGGFPGY GVGAGAGLGG ASPAAAAAAA
KAAKYGAGGA GALGGLVPGA VPGALPGAVP AVPGAGGVPG AGTPAAAAAA AAAKAAAKAG
LGPGVGGVPG GVGVGGIPGG VGVGGVPGGV GPGGVTGIGA GPGGLGGAGS PAAAKSAAKA
AAKAQYRAAA GLGAGVPGFG AGAGVPGFGA GAGVPGFGAG AGVPGFGAGA GVPGFGAGAV
PGSLAASKAA KYGAAGGLGG PGGLGGPGGL GGPGGLGGAG VPGRVAGAAP PAAAAAAAKA
AAKAAQYGLG GAGGLGAGGL GAGGLGAGGL GAGGLGAGGL GAGGLGAGGL GAGGGVSPAA
AAKAAKYGAA GLGGVLGARP FPGGGVAARP GFGLSPIYPG GGAGGLGVGG KPPKPYGGAL
GALGYQGGGC FGKSCGRKRK
