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 27-MAR-2024, entry version 227. 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 GlyCosmos; P15502; 2 sites, 1 glycan. 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; 9606-ENSP00000351807; -. DR PeptideAtlas; 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; 499 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 AGR; HGNC:3327; -. 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; AKAAKYX; -. 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; 23 hits in 1143 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 147 other cell types or tissues. DR ExpressionAtlas; P15502; baseline and differential. 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:0030023; F:extracellular matrix constituent conferring elasticity; IEA:Ensembl. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc. DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL. DR GO; GO:0008015; P:blood circulation; TAS:ProtInc. DR GO; GO:0085029; P:extracellular matrix assembly; ISS:BHF-UCL. 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; ELASTIN; 1. DR PANTHER; PTHR24018:SF5; ELASTIN; 1. DR PRINTS; PR01500; TROPOELASTIN. DR Genevisible; P15502; HS. 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 in a patient with autosomal recessive FT cutis laxa also carrying a mutation in FBLN5; uncertain FT significance; 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 //