ELN_RAT
ID ELN_RAT Reviewed; 870 AA.
AC Q99372; Q5RKH4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Elastin;
DE AltName: Full=Tropoelastin;
DE Flags: Precursor;
GN Name=Eln;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-870 (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC TISSUE=Aorta;
RX PubMed=1702999; DOI=10.1021/bi00493a024;
RA Pierce R.A., Deak S.B., Stolle C.A., Boyd C.D.;
RT "Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning.";
RL Biochemistry 29:9677-9683(1990).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2913947; DOI=10.1016/0003-9861(89)90322-6;
RA Rich C.B., Foster J.A.;
RT "Characterization of rat heart tropoelastin.";
RL Arch. Biochem. Biophys. 268:551-558(1989).
RN [4]
RP PROTEIN SEQUENCE OF 28-37.
RX PubMed=2768256; DOI=10.1016/s0021-9258(18)63819-0;
RA Franzblau C., Pratt C.A., Faris B., Colannino N.M., Offner G.D.,
RA Mogayzel P.J. Jr., Troxler R.F.;
RT "Role of tropoelastin fragmentation in elastogenesis in rat smooth muscle
RT cells.";
RL J. Biol. Chem. 264:15115-15119(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-539 AND 564-870, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1572637; DOI=10.1016/0888-7543(92)90289-5;
RA Pierce R.A., Alatawi A., Deak S.B., Boyd C.D.;
RT "Elements of the rat tropoelastin gene associated with alternative
RT splicing.";
RL Genomics 12:651-658(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 787-870.
RX PubMed=2971041; DOI=10.1016/s0021-9258(18)68269-9;
RA Deak S.B., Pierce R.A., Belsky S.A., Riley D.J., Boyd C.D.;
RT "Rat tropoelastin is synthesized from a 3.5-kilobase mRNA.";
RL J. Biol. Chem. 263:13504-13507(1988).
RN [7]
RP INDUCTION.
RX PubMed=12882762; DOI=10.1152/ajplung.00180.2003;
RA Liu J., Rich C.B., Buczek-Thomas J.A., Nugent M.A., Panchenko M.P.,
RA Foster J.A.;
RT "Heparin-binding EGF-like growth factor regulates elastin and FGF-2
RT expression in pulmonary fibroblasts.";
RL Am. J. Physiol. 285:L1106-L1115(2003).
RN [8]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER PRO-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
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 (By similarity). {ECO:0000250|UniProtKB:P54320}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q99372-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99372-2; Sequence=VSP_004244;
CC Name=3;
CC IsoId=Q99372-3; Sequence=VSP_004245;
CC Name=4;
CC IsoId=Q99372-4; Sequence=VSP_004246;
CC Name=5;
CC IsoId=Q99372-5; Sequence=VSP_004244, VSP_004245;
CC Name=6;
CC IsoId=Q99372-6; Sequence=VSP_004245, VSP_004246;
CC Name=7;
CC IsoId=Q99372-7; Sequence=VSP_004244, VSP_004246;
CC Name=8;
CC IsoId=Q99372-8; Sequence=VSP_004244, VSP_004245, VSP_004246;
CC -!- INDUCTION: Down-regulated by DTR via activation of EGFR.
CC {ECO:0000269|PubMed:12882762}.
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; BC085910; AAH85910.1; -; mRNA.
DR EMBL; M60647; AAA42269.1; -; mRNA.
DR EMBL; M86372; AAA42271.1; -; Genomic_DNA.
DR EMBL; M86355; AAA42271.1; JOINED; Genomic_DNA.
DR EMBL; M86363; AAA42271.1; JOINED; Genomic_DNA.
DR EMBL; M86364; AAA42271.1; JOINED; Genomic_DNA.
DR EMBL; M86366; AAA42271.1; JOINED; Genomic_DNA.
DR EMBL; M86371; AAA42271.1; JOINED; Genomic_DNA.
DR EMBL; M86376; AAA42272.1; -; Genomic_DNA.
DR EMBL; M86373; AAA42272.1; JOINED; Genomic_DNA.
DR EMBL; M86375; AAA42272.1; JOINED; Genomic_DNA.
DR EMBL; J04035; AAA42268.1; -; mRNA.
DR PIR; A36106; EART.
DR RefSeq; NP_036854.1; NM_012722.1.
DR AlphaFoldDB; Q99372; -.
DR STRING; 10116.ENSRNOP00000030301; -.
DR CarbonylDB; Q99372; -.
DR PhosphoSitePlus; Q99372; -.
DR jPOST; Q99372; -.
DR PaxDb; Q99372; -.
DR DNASU; 25043; -.
DR GeneID; 25043; -.
DR KEGG; rno:25043; -.
DR UCSC; RGD:67394; rat. [Q99372-1]
DR CTD; 2006; -.
DR RGD; 67394; Eln.
DR eggNOG; ENOG502RYNR; Eukaryota.
DR InParanoid; Q99372; -.
DR TreeFam; TF338594; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1566948; Elastic fibre formation.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR PRO; PR:Q99372; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0071953; C:elastic fiber; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; IMP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0035904; P:aorta development; IEP:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; IDA:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071298; P:cellular response to L-ascorbic acid; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0048251; P:elastic fiber assembly; TAS:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0043149; P:stress fiber assembly; ISO:RGD.
DR InterPro; IPR003979; Tropoelastin.
DR PANTHER; PTHR24018; PTHR24018; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:26479776"
FT CHAIN 28..870
FT /note="Elastin"
FT /id="PRO_0000021165"
FT MOD_RES 39
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 87
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 122
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 126
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 207
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 220
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 223
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 244
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 290
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 309
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 338
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 360
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 363
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 375
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 402
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 408
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 413
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 418
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 434
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 441
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 485
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 488
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 518
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 539
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 554
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 558
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 615
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 619
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 623
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 637
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 646
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 662
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 670
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 677
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 680
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 715
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 730
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 734
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 793
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 796
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 842
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 860..865
FT /evidence="ECO:0000250"
FT VAR_SEQ 269..313
FT /note="Missing (in isoform 2, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_004244"
FT VAR_SEQ 314
FT /note="Missing (in isoform 3, isoform 5, isoform 6 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004245"
FT VAR_SEQ 815..829
FT /note="Missing (in isoform 4, isoform 6, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_004246"
FT CONFLICT 705
FT /note="F -> L (in Ref. 1; AAH85910)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="G -> GPGGLGG (in Ref. 1; AAH85910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 73330 MW; 75909F2432FC4054 CRC64;
MAGLTAAVPQ PGVLLILLLN LLHPAQPGGV PGAVPGGVPG GLPGGVPGGV YYPGAGIGGG
LGGGALGPGG KPPKPGAGLL GAFGAGPGGL GGAGPGAGLS YASRPGGVLV PGGGAGAAAA
YKAAAKAGAG LGGIGGVPGG VGVGGVPGAV GVGGVPGAVG GIGGIGGLGV STGAVVPQLG
AGVGAGGKPG KVPGVGLPGV YPGGVLPGTG ARFPGVGVLP GVPTGTGVKA KVPGGGGGAF
SGIPGVGPFG GQQPGVPLGY PIKAPKLPGG YGLPYTNGKL PYGVAGAGGK AGYPTGTGVG
SQAAVAAAKA AKYAGAGGGG VLPGVGGGGI PGGAGAIPGI GGITGAGTPA AAAAAKAAAK
AAKYGAAGGL VPGGPGVRVP GAGIPGVGIP GVGGIPGVGG IPGVGGIPGV GGPGIGGPGI
VGGPGAVSPA AAAKAAAKAA KYGARGGVGI PTYGVGAGGF PGYGVGAGAG LGGASQAAAA
AAAAKAAKYG AGGAGTLGGL VPGAVPGALP GAVPGALPGA VPGALPGAVP GVPGTGGVPG
AGTPAAAAAA AAAKAAAKAG QYGLGPGVGG VPGGVGVGGL PGGVGPGGVT GIGTGPGTGL
VPGDLGGAGT PAAAKSAAKA AAKAQYRAAA GLGAGVPGLG VGAGVPGFGA GAGGFGAGAG
VPGFGAGAVP GSLAASKAAK YGAAGGLGGP GGLGGPGGLG GPGGFGGPGG LGGVPGGVAG
GAPAAAAAAK AAAKAAQYGL GGAGGLGAGG LGAGGLGAGG LGAGGLGAGG LGAGGVIPGA
VGLGGVSPAA AAKAAKYGAA GLGGVLGARP FPGGGVAARP GFGLSPIYPG GGAGGLGVGG
KPPKPYGGAL GALGYQGGGC FGKSCGRKRK
