ELN_HUMAN
ID ELN_HUMAN Reviewed; 786 AA.
AC P15502; B3KTS6; O15336; O15337; Q14233; Q14234; Q14235; Q14238; Q6P0L4;
AC Q6ZWJ6; Q75MU5; Q7Z316; Q7Z3F5; Q9UMF5;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 4.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Elastin;
DE AltName: Full=Tropoelastin;
DE Flags: Precursor;
GN Name=ELN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3; 4 AND 6), AND VARIANT
RP SER-422.
RX PubMed=3039501; DOI=10.1073/pnas.84.16.5680;
RA Indik Z., Yeh H., Ornstein-Goldstein N., Sheppard P., Anderson N.,
RA Rosenbloom J.C., Peltonen L., Rosenbloom J.;
RT "Alternative splicing of human elastin mRNA indicated by sequence analysis
RT of cloned genomic and complementary DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5680-5684(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-422.
RC TISSUE=Skin fibroblast;
RX PubMed=3171221; DOI=10.1111/1523-1747.ep12476591;
RA Fazio M.J., Olsen D.R., Kauh E.A., Baldwin C.T., Indik Z.,
RA Ornstein-Goldstein N., Yeh H., Rosenbloom J., Uitto J.;
RT "Cloning of full-length elastin cDNAs from a human skin fibroblast
RT recombinant cDNA library: further elucidation of alternative splicing
RT utilizing exon-specific oligonucleotides.";
RL J. Invest. Dermatol. 91:458-464(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 11 AND 12), AND VARIANT
RP SER-422.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), AND VARIANTS SER-422
RP AND ARG-610.
RC TISSUE=Eye;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-27.
RX PubMed=2722804; DOI=10.1016/s0021-9258(18)81876-2;
RA Bashir M.M., Indik Z., Yeh H., Ornstein-Goldstein N., Rosenbloom J.C.,
RA Abrams W., Fazio M., Uitto J., Rosenbloom J.;
RT "Characterization of the complete human elastin gene. Delineation of
RT unusual features in the 5'-flanking region.";
RL J. Biol. Chem. 264:8887-8891(1989).
RN [10]
RP NUCLEOTIDE SEQUENCE OF 1-27.
RA Bressan G.M.;
RL Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP SEQUENCE REVISION.
RA Bressan G.M.;
RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-657 (ISOFORMS 9 AND 10), AND
RP VARIANTS SER-422 AND ARG-610.
RX PubMed=9215670; DOI=10.1093/hmg/6.7.1021;
RA Li D.Y., Toland A.E., Boak B.B., Atkinson D.L., Ensing G.J., Morris C.A.,
RA Keating M.T.;
RT "Elastin point mutations cause an obstructive vascular disease,
RT supravalvular aortic stenosis.";
RL Hum. Mol. Genet. 6:1021-1028(1997).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 164-724 (ISOFORM 2), AND VARIANT SER-422.
RC TISSUE=Placenta;
RX PubMed=2831431;
RA Fazio M.J., Olsen D.R., Kuivaniemi H., Chu M.L., Davidson J.M.,
RA Rosenbloom J., Uitto J.;
RT "Isolation and characterization of human elastin cDNAs, and age-associated
RT variation in elastin gene expression in cultured skin fibroblasts.";
RL Lab. Invest. 58:270-277(1988).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 496-786 (ISOFORM 1/10), AND TISSUE
RP SPECIFICITY.
RX PubMed=8812460; DOI=10.1006/geno.1996.0469;
RA Osborne L.R., Martindale D.W., Scherer S.W., Shi X.-M., Huizenga J.,
RA Heng H.H.Q., Costa T., Pober B., Lew L., Brinkman J., Rommens J.,
RA Koop B.F., Tsui L.-C.;
RT "Identification of genes from a 500-kb region at 7q11.23 that is commonly
RT deleted in Williams syndrome patients.";
RL Genomics 36:328-336(1996).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 659-786, AND VARIANT SER-422.
RC TISSUE=Hippocampus, and Placenta;
RX PubMed=8689688; DOI=10.1016/s0092-8674(00)80077-x;
RA Frangiskakis J.M., Ewart A.K., Morris C.A., Mervis C.B., Bertrand J.,
RA Robinson B.F., Klein B.P., Ensing G.J., Everett L.A., Green E.D.,
RA Proeschel C., Gutowski N.J., Noble M., Atkinson D.L., Odelberg S.J.,
RA Keating M.T.;
RT "LIM-kinase1 hemizygosity implicated in impaired visuospatial constructive
RT cognition.";
RL Cell 86:59-69(1996).
RN [16]
RP INVOLVEMENT IN ADCL1.
RX PubMed=9873040; DOI=10.1074/jbc.274.2.981;
RA Zhang M.-C., He L., Giro M., Yong S.L., Tiller G.E., Davidson J.M.;
RT "Cutis laxa arising from frameshift mutations in exon 30 of the elastin
RT gene (ELN).";
RL J. Biol. Chem. 274:981-986(1999).
RN [17]
RP INVOLVEMENT IN SVAS.
RX PubMed=10942104; DOI=10.1007/s004390000285;
RA Urban Z., Michels V.V., Thibodeau S.N., Davis E.C., Bonnefont J.-P.,
RA Munnich A., Eyskens B., Gewillig M., Devriendt K., Boyd C.D.;
RT "Isolated supravalvular aortic stenosis: functional haploinsufficiency of
RT the elastin gene as a result of nonsense-mediated decay.";
RL Hum. Genet. 106:577-588(2000).
RN [18]
RP INTERACTION WITH FBN1 AND FBLN5.
RX PubMed=15790312; DOI=10.1042/bj20050368;
RA Freeman L.J., Lomas A., Hodson N., Sherratt M.J., Mellody K.T., Weiss A.S.,
RA Shuttleworth A., Kielty C.M.;
RT "Fibulin-5 interacts with fibrillin-1 molecules and microfibrils.";
RL Biochem. J. 388:1-5(2005).
RN [19]
RP HYDROXYLATION AT PRO-65; PRO-67; PRO-88; PRO-116; PRO-156; PRO-177;
RP PRO-190; PRO-286; PRO-290; PRO-415; PRO-427; PRO-465; PRO-481; PRO-522;
RP PRO-580; PRO-607; PRO-646; PRO-677; PRO-769 AND PRO-772, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=16078697; DOI=10.1016/j.chroma.2005.06.034;
RA Schmelzer C.E.H., Getie M., Neubert R.H.H.;
RT "Mass spectrometric characterization of human skin elastin peptides
RT produced by proteolytic digestion with pepsin and thermitase.";
RL J. Chromatogr. A 1083:120-126(2005).
RN [20]
RP HYDROXYLATION AT PRO-34; PRO-167; PRO-170; PRO-190; PRO-283; PRO-286;
RP PRO-327; PRO-342; PRO-347; PRO-352; PRO-355; PRO-360; PRO-421; PRO-427;
RP PRO-550; PRO-580; PRO-589; PRO-598 AND PRO-677, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16161116; DOI=10.1002/prot.20643;
RA Getie M., Schmelzer C.E.H., Neubert R.H.H.;
RT "Characterization of peptides resulting from digestion of human skin
RT elastin with elastase.";
RL Proteins 61:649-657(2005).
RN [21]
RP INTERACTION WITH FBLN5, AND SUBCELLULAR LOCATION.
RX PubMed=17035250; DOI=10.1093/hmg/ddl414;
RA Hu Q., Loeys B.L., Coucke P.J., De Paepe A., Mecham R.P., Choi J.,
RA Davis E.C., Urban Z.;
RT "Fibulin-5 mutations: mechanisms of impaired elastic fiber formation in
RT recessive cutis laxa.";
RL Hum. Mol. Genet. 15:3379-3386(2006).
RN [22]
RP INTERACTION WITH EFEMP2.
RX PubMed=16478991; DOI=10.1128/mcb.26.5.1700-1709.2006;
RA McLaughlin P.J., Chen Q., Horiguchi M., Starcher B.C., Stanton J.B.,
RA Broekelmann T.J., Marmorstein A.D., McKay B., Mecham R., Nakamura T.,
RA Marmorstein L.Y.;
RT "Targeted disruption of fibulin-4 abolishes elastogenesis and causes
RT perinatal lethality in mice.";
RL Mol. Cell. Biol. 26:1700-1709(2006).
RN [23]
RP INTERACTION WITH EFEMP2.
RX PubMed=19570982; DOI=10.1074/jbc.m109.019364;
RA Choudhury R., McGovern A., Ridley C., Cain S.A., Baldwin A., Wang M.C.,
RA Guo C., Mironov A. Jr., Drymoussi Z., Trump D., Shuttleworth A.,
RA Baldock C., Kielty C.M.;
RT "Differential regulation of elastic fiber formation by fibulin-4 and -5.";
RL J. Biol. Chem. 284:24553-24567(2009).
RN [24]
RP INTERACTION WITH FBN1; FBLN2 AND FBLN5.
RX PubMed=17255108; DOI=10.1074/jbc.m608204200;
RA El-Hallous E., Sasaki T., Hubmacher D., Getie M., Tiedemann K.,
RA Brinckmann J., Baetge B., Davis E.C., Reinhardt D.P.;
RT "Fibrillin-1 interactions with fibulins depend on the first hybrid domain
RT and provide an adaptor function to tropoelastin.";
RL J. Biol. Chem. 282:8935-8946(2007).
RN [25]
RP VARIANT SER-211.
RX PubMed=19194475; DOI=10.1038/jid.2008.450;
RA Megarbane H., Florence J., Sass J.O., Schwonbeck S., Foglio M., de Cid R.,
RA Cure S., Saker S., Megarbane A., Fischer J.;
RT "An autosomal-recessive form of cutis laxa is due to homozygous elastin
RT mutations, and the phenotype may be modified by a heterozygous fibulin 5
RT polymorphism.";
RL J. Invest. Dermatol. 129:1650-1655(2009).
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 (PubMed:15790312, PubMed:17035250). Interacts with FBN1
CC (PubMed:15790312). Forms a ternary complex with FBN1 and FBLN2 or FBLN5
CC (PubMed:17255108). Interacts with MFAP4 in a Ca (2+)-dependent manner;
CC this interaction promotes ELN self-assembly (By similarity)
CC (PubMed:15790312, PubMed:17035250, PubMed:17255108). Interacts with
CC EFEMP2 with moderate affinity (PubMed:16478991).
CC {ECO:0000250|UniProtKB:P04985, ECO:0000269|PubMed:15790312,
CC ECO:0000269|PubMed:16478991, ECO:0000269|PubMed:17035250,
CC ECO:0000269|PubMed:17255108}.
CC -!- INTERACTION:
CC P15502; O95967: EFEMP2; NbExp=5; IntAct=EBI-1222108, EBI-743414;
CC P15502; Q9UBX5: FBLN5; NbExp=3; IntAct=EBI-1222108, EBI-947897;
CC P15502; P28300: LOX; NbExp=2; IntAct=EBI-1222108, EBI-3893481;
CC P15502-2; Q9Y4K0: LOXL2; NbExp=2; IntAct=EBI-7882008, EBI-7172227;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:17035250}. Note=Extracellular matrix of
CC elastic fibers. {ECO:0000269|PubMed:17035250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Comment=Additional isoforms seem to exist.;
CC Name=3;
CC IsoId=P15502-3; Sequence=Displayed;
CC Name=1;
CC IsoId=P15502-1; Sequence=VSP_012484, VSP_012485, VSP_012487;
CC Name=2;
CC IsoId=P15502-2; Sequence=VSP_012484, VSP_012487;
CC Name=4;
CC IsoId=P15502-4; Sequence=VSP_012484;
CC Name=5;
CC IsoId=P15502-5; Sequence=VSP_012481, VSP_012484, VSP_012487,
CC VSP_012488;
CC Name=6;
CC IsoId=P15502-6; Sequence=VSP_012483, VSP_012487, VSP_012488;
CC Name=7;
CC IsoId=P15502-7; Sequence=VSP_012479, VSP_012483, VSP_012487,
CC VSP_012488;
CC Name=8;
CC IsoId=P15502-8; Sequence=VSP_012482, VSP_012483, VSP_012486,
CC VSP_012487, VSP_012488;
CC Name=9;
CC IsoId=P15502-9; Sequence=VSP_012485;
CC Name=10;
CC IsoId=P15502-10; Sequence=VSP_012485, VSP_012487;
CC Name=11;
CC IsoId=P15502-11; Sequence=VSP_012480, VSP_012482, VSP_012483,
CC VSP_012487, VSP_012488;
CC Name=12;
CC IsoId=P15502-12; Sequence=VSP_012481, VSP_012483, VSP_012487,
CC VSP_012488;
CC Name=13;
CC IsoId=P15502-13; Sequence=VSP_012483, VSP_012487;
CC -!- TISSUE SPECIFICITY: Expressed within the outer myometrial smooth muscle
CC and throughout the arteriolar tree of uterus (at protein level). Also
CC expressed in the large arteries, lung and skin.
CC {ECO:0000269|PubMed:8812460}.
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 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- DISEASE: Cutis laxa, autosomal dominant, 1 (ADCL1) [MIM:123700]: A
CC connective tissue disorder characterized by loose, hyperextensible skin
CC with decreased resilience and elasticity leading to a premature aged
CC appearance. Face, hands, feet, joints, and torso may be differentially
CC affected. Additional variable clinical features are gastrointestinal
CC diverticula, hernia, and genital prolapse. Rare manifestations are
CC pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and
CC emphysema. {ECO:0000269|PubMed:9873040}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Supravalvular aortic stenosis (SVAS) [MIM:185500]: Congenital
CC narrowing of the ascending aorta which can occur sporadically, as an
CC autosomal dominant condition, or as one component of Williams-Beuren
CC syndrome. {ECO:0000269|PubMed:10942104}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Note=ELN is located in the Williams-Beuren syndrome (WBS)
CC critical region. WBS results from a hemizygous deletion of several
CC genes on chromosome 7q11.23, thought to arise as a consequence of
CC unequal crossing over between highly homologous low-copy repeat
CC sequences flanking the deleted region. Haploinsufficiency of ELN may be
CC the cause of certain cardiovascular and musculo-skeletal abnormalities
CC observed in the disease (PubMed:8812460). {ECO:0000269|PubMed:8812460}.
CC -!- SIMILARITY: Belongs to the elastin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD98065.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Elastin entry;
CC URL="https://en.wikipedia.org/wiki/Elastin";
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; M17282; AAC98393.1; -; Genomic_DNA.
DR EMBL; M16983; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17265; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17266; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17267; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17268; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17271; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17272; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17273; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17275; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17276; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17277; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17278; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17279; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17281; AAC98393.1; JOINED; Genomic_DNA.
DR EMBL; M17282; AAC98394.1; -; Genomic_DNA.
DR EMBL; M16983; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17265; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17266; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17267; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17268; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17270; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17271; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17272; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17273; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17275; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17276; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17277; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17278; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17279; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17280; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17281; AAC98394.1; JOINED; Genomic_DNA.
DR EMBL; M17282; AAC98395.1; -; Genomic_DNA.
DR EMBL; M16983; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17265; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17266; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17267; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17268; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17270; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17271; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17272; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17273; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17274; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17275; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17276; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17277; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17278; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17279; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17280; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M17281; AAC98395.1; JOINED; Genomic_DNA.
DR EMBL; M36860; AAA52382.1; -; mRNA.
DR EMBL; AK095990; BAG53188.1; -; mRNA.
DR EMBL; AK122731; BAC85506.1; -; mRNA.
DR EMBL; BX537939; CAD97910.1; -; mRNA.
DR EMBL; BX538199; CAD98065.1; ALT_INIT; mRNA.
DR EMBL; AK225659; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC005056; AAS07435.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69627.1; -; Genomic_DNA.
DR EMBL; BC065566; AAH65566.1; -; mRNA.
DR EMBL; X15603; CAA33627.1; -; Genomic_DNA.
DR EMBL; U93037; AAB65620.1; -; Genomic_DNA.
DR EMBL; U93034; AAB65620.1; JOINED; Genomic_DNA.
DR EMBL; U93035; AAB65620.1; JOINED; Genomic_DNA.
DR EMBL; U93036; AAB65620.1; JOINED; Genomic_DNA.
DR EMBL; U93037; AAB65621.1; -; Genomic_DNA.
DR EMBL; U93034; AAB65621.1; JOINED; Genomic_DNA.
DR EMBL; U93035; AAB65621.1; JOINED; Genomic_DNA.
DR EMBL; U93036; AAB65621.1; JOINED; Genomic_DNA.
DR EMBL; M24782; AAA53190.1; -; mRNA.
DR EMBL; U63721; AAC13884.1; -; Genomic_DNA.
DR EMBL; U62292; AAB17544.1; -; Genomic_DNA.
DR CCDS; CCDS43598.1; -. [P15502-5]
DR CCDS; CCDS43599.1; -. [P15502-7]
DR CCDS; CCDS47611.1; -. [P15502-12]
DR CCDS; CCDS47612.1; -. [P15502-13]
DR CCDS; CCDS5562.2; -. [P15502-2]
DR CCDS; CCDS64673.1; -. [P15502-1]
DR CCDS; CCDS64675.1; -. [P15502-8]
DR CCDS; CCDS75616.1; -. [P15502-3]
DR PIR; A32707; EAHU.
DR RefSeq; NP_000492.2; NM_000501.3. [P15502-2]
DR RefSeq; NP_001075221.1; NM_001081752.2. [P15502-7]
DR RefSeq; NP_001075222.1; NM_001081753.2. [P15502-12]
DR RefSeq; NP_001075223.1; NM_001081754.2. [P15502-5]
DR RefSeq; NP_001075224.1; NM_001081755.2. [P15502-13]
DR RefSeq; NP_001265844.1; NM_001278915.1. [P15502-1]
DR RefSeq; NP_001265845.1; NM_001278916.1. [P15502-8]
DR RefSeq; NP_001265868.1; NM_001278939.1. [P15502-3]
DR AlphaFoldDB; P15502; -.
DR SASBDB; P15502; -.
DR BioGRID; 108321; 16.
DR CORUM; P15502; -.
DR IntAct; P15502; 13.
DR MINT; P15502; -.
DR STRING; 9606.ENSP00000351807; -.
DR ChEMBL; CHEMBL3713712; -.
DR DrugBank; DB00533; Rofecoxib.
DR Allergome; 11040; Hom s Elastin.
DR GlyGen; P15502; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P15502; -.
DR PhosphoSitePlus; P15502; -.
DR BioMuta; ELN; -.
DR DMDM; 306526276; -.
DR jPOST; P15502; -.
DR MassIVE; P15502; -.
DR PaxDb; P15502; -.
DR PeptideAtlas; P15502; -.
DR PRIDE; P15502; -.
DR ProteomicsDB; 53144; -. [P15502-3]
DR ProteomicsDB; 53145; -. [P15502-1]
DR ProteomicsDB; 53146; -. [P15502-10]
DR ProteomicsDB; 53147; -. [P15502-11]
DR ProteomicsDB; 53148; -. [P15502-12]
DR ProteomicsDB; 53149; -. [P15502-13]
DR ProteomicsDB; 53150; -. [P15502-2]
DR ProteomicsDB; 53151; -. [P15502-4]
DR ProteomicsDB; 53152; -. [P15502-5]
DR ProteomicsDB; 53153; -. [P15502-6]
DR ProteomicsDB; 53154; -. [P15502-7]
DR ProteomicsDB; 53155; -. [P15502-8]
DR ProteomicsDB; 53156; -. [P15502-9]
DR Antibodypedia; 4380; 434 antibodies from 35 providers.
DR DNASU; 2006; -.
DR Ensembl; ENST00000252034.12; ENSP00000252034.7; ENSG00000049540.19. [P15502-2]
DR Ensembl; ENST00000320399.10; ENSP00000313565.6; ENSG00000049540.19. [P15502-4]
DR Ensembl; ENST00000357036.9; ENSP00000349540.5; ENSG00000049540.19. [P15502-5]
DR Ensembl; ENST00000380553.8; ENSP00000369926.4; ENSG00000049540.19. [P15502-11]
DR Ensembl; ENST00000380562.8; ENSP00000369936.4; ENSG00000049540.19. [P15502-1]
DR Ensembl; ENST00000380575.8; ENSP00000369949.4; ENSG00000049540.19. [P15502-7]
DR Ensembl; ENST00000380576.9; ENSP00000369950.5; ENSG00000049540.19. [P15502-13]
DR Ensembl; ENST00000380584.8; ENSP00000369958.4; ENSG00000049540.19. [P15502-8]
DR Ensembl; ENST00000429192.5; ENSP00000391129.1; ENSG00000049540.19. [P15502-12]
DR Ensembl; ENST00000692049.1; ENSP00000510104.1; ENSG00000049540.19. [P15502-3]
DR GeneID; 2006; -.
DR KEGG; hsa:2006; -.
DR MANE-Select; ENST00000252034.12; ENSP00000252034.7; NM_000501.4; NP_000492.2. [P15502-2]
DR UCSC; uc003tzn.5; human. [P15502-3]
DR CTD; 2006; -.
DR DisGeNET; 2006; -.
DR GeneCards; ELN; -.
DR GeneReviews; ELN; -.
DR HGNC; HGNC:3327; ELN.
DR HPA; ENSG00000049540; Low tissue specificity.
DR MalaCards; ELN; -.
DR MIM; 123700; phenotype.
DR MIM; 130160; gene.
DR MIM; 185500; phenotype.
DR neXtProt; NX_P15502; -.
DR OpenTargets; ENSG00000049540; -.
DR Orphanet; 90348; Autosomal dominant cutis laxa.
DR Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
DR Orphanet; 3193; Supravalvular aortic stenosis.
DR Orphanet; 904; Williams syndrome.
DR PharmGKB; PA27757; -.
DR VEuPathDB; HostDB:ENSG00000049540; -.
DR eggNOG; ENOG502RYNR; Eukaryota.
DR GeneTree; ENSGT00730000111510; -.
DR HOGENOM; CLU_021236_0_0_1; -.
DR InParanoid; P15502; -.
DR OMA; KTKTHHR; -.
DR TreeFam; TF338594; -.
DR PathwayCommons; P15502; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1566948; Elastic fibre formation.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; P15502; -.
DR SIGNOR; P15502; -.
DR BioGRID-ORCS; 2006; 17 hits in 1067 CRISPR screens.
DR ChiTaRS; ELN; human.
DR GeneWiki; Elastin; -.
DR GenomeRNAi; 2006; -.
DR Pharos; P15502; Tbio.
DR PRO; PR:P15502; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P15502; protein.
DR Bgee; ENSG00000049540; Expressed in descending thoracic aorta and 145 other tissues.
DR ExpressionAtlas; P15502; baseline and differential.
DR Genevisible; P15502; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0071953; C:elastic fiber; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0003180; P:aortic valve morphogenesis; IC:BHF-UCL.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; TAS:GO_Central.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:ProtInc.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
DR InterPro; IPR003979; Tropoelastin.
DR PANTHER; PTHR24018; PTHR24018; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal; Williams-Beuren syndrome.
FT SIGNAL 1..26
FT /evidence="ECO:0000250|UniProtKB:Q99372"
FT CHAIN 27..786
FT /note="Elastin"
FT /id="PRO_0000021163"
FT REGION 615..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 65
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 67
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 88
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 104
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 107
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 116
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 156
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 167
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 170
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 177
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 190
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697,
FT ECO:0000269|PubMed:16161116"
FT MOD_RES 241
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 261
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 265
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 283
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 286
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697,
FT ECO:0000269|PubMed:16161116"
FT MOD_RES 290
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 312
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 315
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 327
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 342
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 347
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 352
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 355
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 360
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 375
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 379
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 382
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 415
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 421
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 427
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697,
FT ECO:0000269|PubMed:16161116"
FT MOD_RES 448
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 451
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 465
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 481
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 492
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 496
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 522
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 550
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16161116"
FT MOD_RES 558
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 562
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 566
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 580
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697,
FT ECO:0000269|PubMed:16161116"
FT MOD_RES 589
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:16161116"
FT MOD_RES 598
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:16161116"
FT MOD_RES 607
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 646
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 653
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 656
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 677
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697,
FT ECO:0000269|PubMed:16161116"
FT MOD_RES 693
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 697
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 735
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 738
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P04985"
FT MOD_RES 769
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT MOD_RES 772
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:16078697"
FT DISULFID 776..781
FT /evidence="ECO:0000250"
FT VAR_SEQ 45..54
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012479"
FT VAR_SEQ 78..180
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012480"
FT VAR_SEQ 125
FT /note="A -> AAPSVP (in isoform 5 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_012481"
FT VAR_SEQ 215..228
FT /note="Missing (in isoform 8 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012482"
FT VAR_SEQ 453..500
FT /note="Missing (in isoform 6, isoform 7, isoform 8, isoform
FT 11, isoform 12 and isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.5"
FT /id="VSP_012483"
FT VAR_SEQ 453..481
FT /note="Missing (in isoform 1, isoform 2, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:2831431, ECO:0000303|PubMed:3171221"
FT /id="VSP_012484"
FT VAR_SEQ 500
FT /note="F -> FALLNLA (in isoform 1, isoform 9 and isoform
FT 10)"
FT /evidence="ECO:0000303|PubMed:3171221"
FT /id="VSP_012485"
FT VAR_SEQ 555..570
FT /note="AAAKSAAKVAAKAQLR -> G (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012486"
FT VAR_SEQ 612..644
FT /note="Missing (in isoform 1, isoform 2, isoform 5, isoform
FT 6, isoform 7, isoform 8, isoform 10, isoform 11, isoform 12
FT and isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:2831431, ECO:0000303|PubMed:3171221,
FT ECO:0000303|Ref.5"
FT /id="VSP_012487"
FT VAR_SEQ 740..757
FT /note="Missing (in isoform 5, isoform 6, isoform 7, isoform
FT 8, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_012488"
FT VARIANT 211
FT /note="P -> S (found as homozygous mutation in a patient
FT with autosomal recessive cutis laxa also carrying a
FT mutation in FBLN5; unknown pathological significance;
FT dbSNP:rs1064793880)"
FT /evidence="ECO:0000269|PubMed:19194475"
FT /id="VAR_072395"
FT VARIANT 422
FT /note="G -> S (in dbSNP:rs2071307)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2831431,
FT ECO:0000269|PubMed:3039501, ECO:0000269|PubMed:3171221,
FT ECO:0000269|PubMed:8689688, ECO:0000269|PubMed:9215670"
FT /id="VAR_020882"
FT VARIANT 610
FT /note="G -> R (in dbSNP:rs17855988)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9215670"
FT /id="VAR_056869"
FT CONFLICT 317
FT /note="G -> E (in Ref. 4; CAD97910)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="V -> I (in Ref. 3; BAC85506)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="A -> T (in Ref. 4; CAD98065)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="G -> D (in Ref. 4; CAD97910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 68398 MW; 4A128EC9EA2CC29F CRC64;
MAGLTAAAPR PGVLLLLLSI LHPSRPGGVP GAIPGGVPGG VFYPGAGLGA LGGGALGPGG
KPLKPVPGGL AGAGLGAGLG AFPAVTFPGA LVPGGVADAA AAYKAAKAGA GLGGVPGVGG
LGVSAGAVVP QPGAGVKPGK VPGVGLPGVY PGGVLPGARF PGVGVLPGVP TGAGVKPKAP
GVGGAFAGIP GVGPFGGPQP GVPLGYPIKA PKLPGGYGLP YTTGKLPYGY GPGGVAGAAG
KAGYPTGTGV GPQAAAAAAA KAAAKFGAGA AGVLPGVGGA GVPGVPGAIP GIGGIAGVGT
PAAAAAAAAA AKAAKYGAAA GLVPGGPGFG PGVVGVPGAG VPGVGVPGAG IPVVPGAGIP
GAAVPGVVSP EAAAKAAAKA AKYGARPGVG VGGIPTYGVG AGGFPGFGVG VGGIPGVAGV
PGVGGVPGVG GVPGVGISPE AQAAAAAKAA KYGAAGAGVL GGLVPGAPGA VPGVPGTGGV
PGVGTPAAAA AKAAAKAAQF GLVPGVGVAP GVGVAPGVGV APGVGLAPGV GVAPGVGVAP
GVGVAPGIGP GGVAAAAKSA AKVAAKAQLR AAAGLGAGIP GLGVGVGVPG LGVGAGVPGL
GVGAGVPGFG AGADEGVRRS LSPELREGDP SSSQHLPSTP SSPRVPGALA AAKAAKYGAA
VPGVLGGLGA LGGVGIPGGV VGAGPAAAAA AAKAAAKAAQ FGLVGAAGLG GLGVGGLGVP
GVGGLGGIPP AAAAKAAKYG AAGLGGVLGG AGQFPLGGVA ARPGFGLSPI FPGGACLGKA
CGRKRK
