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 27-MAR-2024, entry version 151. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000015138; -. DR ProteomicsDB; 277820; -. DR Antibodypedia; 4380; 499 antibodies from 35 providers. DR DNASU; 13717; -. DR Ensembl; ENSMUST00000015138.13; ENSMUSP00000015138.10; ENSMUSG00000029675.13. DR GeneID; 13717; -. DR KEGG; mmu:13717; -. DR UCSC; uc008zwv.1; mouse. DR AGR; MGI:95317; -. 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; AKAAKYX; -. 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; 6 hits in 80 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 270 other cell types or tissues. DR ExpressionAtlas; P54320; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0071953; C:elastic fiber; IDA: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; IDA:BHF-UCL. DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL. DR GO; GO:0001974; P:blood vessel remodeling; ISO:MGI. DR GO; GO:0085029; P:extracellular matrix assembly; IMP:BHF-UCL. 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; ELASTIN; 1. DR PANTHER; PTHR24018:SF5; ELASTIN; 1. DR PRINTS; PR01500; TROPOELASTIN. DR Genevisible; P54320; MM. 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 //