FINC_HUMAN
ID FINC_HUMAN Reviewed; 2477 AA.
AC P02751; B7ZLF0; E9PE77; E9PG29; O95609; O95610; Q14312; Q14325; Q14326;
AC Q17RV7; Q53S27; Q564H7; Q585T2; Q59EH1; Q60FE4; Q68DP8; Q68DP9; Q68DT4;
AC Q6LDP6; Q6MZS0; Q6MZU5; Q6N025; Q6N0A6; Q7Z391; Q86T27; Q8IVI8; Q96KP7;
AC Q96KP8; Q96KP9; Q9H1B8; Q9HAP3; Q9UMK2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 5.
DT 03-AUG-2022, entry version 271.
DE RecName: Full=Fibronectin {ECO:0000305};
DE Short=FN;
DE AltName: Full=Cold-insoluble globulin;
DE Short=CIG;
DE Contains:
DE RecName: Full=Anastellin;
DE Contains:
DE RecName: Full=Ugl-Y1;
DE Contains:
DE RecName: Full=Ugl-Y2;
DE Contains:
DE RecName: Full=Ugl-Y3;
DE Flags: Precursor;
GN Name=FN1 {ECO:0000312|HGNC:HGNC:3778}; Synonyms=FN;
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 [MRNA] (ISOFORMS 2 AND 16).
RX PubMed=11737888; DOI=10.1186/bcr325;
RA Schor S.L., Schor A.M.;
RT "Phenotypic and genetic alterations in mammary stroma: implications for
RT tumour progression.";
RL Breast Cancer Res. 3:373-379(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 16).
RX PubMed=16322219; DOI=10.1158/0008-5472.can-05-2038;
RA Kay R.A., Ellis I.R., Jones S.J., Perrier S., Florence M.M., Schor A.M.,
RA Schor S.L.;
RT "The expression of migration stimulating factor, a potent oncofetal
RT cytokine, is uniquely controlled by 3'-untranslated region-dependent
RT nuclear sequestration of its precursor messenger RNA.";
RL Cancer Res. 65:10742-10749(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), AND VARIANTS PRO-817 AND ILE-2261.
RC TISSUE=Retinal pigment epithelium;
RX PubMed=16106752; DOI=10.1093/dnares/12.1.53;
RA Kato S., Ohtoko K., Ohtake H., Kimura T.;
RT "Vector-capping: a simple method for preparing a high-quality full-length
RT cDNA library.";
RL DNA Res. 12:53-62(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 14), AND VARIANTS LEU-15;
RP PRO-817 AND ILE-2261.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 7; 8; 9; 10; 13; 14; 15
RP AND 16), AND VARIANTS LEU-15; PRO-817 AND ILE-2261.
RC TISSUE=Amygdala, Cervix, Colon endothelium, Endometrial tumor, and
RC Uterine endothelium;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LEU-15; PRO-817
RP AND ILE-2261.
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), AND VARIANTS LEU-15;
RP PRO-817 AND ILE-2261.
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 1-38.
RC TISSUE=Mammary cancer;
RX PubMed=3770189; DOI=10.1016/0014-5793(86)80029-1;
RA Gutman A., Yamada K.M., Kornblihtt A.R.;
RT "Human fibronectin is synthesized as a pre-propolypeptide.";
RL FEBS Lett. 207:145-148(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, AND VARIANT LEU-15.
RX PubMed=3031656; DOI=10.1073/pnas.84.7.1876;
RA Dean D.C., Bowlus C.L., Bourgeois S.;
RT "Cloning and analysis of the promotor region of the human fibronectin
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1876-1880(1987).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-2386 (ISOFORM 3), AND VARIANTS PRO-817 AND
RP ILE-2261.
RC TISSUE=Fibroblast;
RX PubMed=2992939; DOI=10.1002/j.1460-2075.1985.tb03847.x;
RA Kornblihtt A.R., Umezawa K., Vibe-Pedersen K., Baralle F.E.;
RT "Primary structure of human fibronectin: differential splicing may generate
RT at least 10 polypeptides from a single gene.";
RL EMBO J. 4:1755-1759(1985).
RN [12]
RP PROTEIN SEQUENCE OF 32-290, CLEAVAGE OF INITIATOR METHIONINE, AND
RP PYROGLUTAMATE FORMATION AT GLN-32.
RC TISSUE=Plasma;
RX PubMed=6630202; DOI=10.1016/s0021-9258(17)44228-1;
RA Garcia-Pardo A., Pearlstein E., Frangione B.;
RT "Primary structure of human plasma fibronectin. The 29,000-dalton NH2-
RT terminal domain.";
RL J. Biol. Chem. 258:12670-12674(1983).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-481 (ISOFORMS
RP 1/3/4/5/6/7/8/9/10/11/12/13/14/15), NUCLEOTIDE SEQUENCE [MRNA] OF 1116-1422
RP (ISOFORMS 1/3/4/5/6/8/9/10/14), NUCLEOTIDE SEQUENCE [MRNA] OF 1238-2160
RP (ISOFORMS 9 AND 12), NUCLEOTIDE SEQUENCE [MRNA] OF 1540-1916 (ISOFORMS
RP 8/9/10/13/14), NUCLEOTIDE SEQUENCE [MRNA] OF 2010-2252 (ISOFORMS 3/7/14),
RP AND NUCLEOTIDE SEQUENCE [MRNA] OF 2319-2477 (ISOFORMS
RP 1/3/6/7/8/9/10/11/12/13/14/15).
RC TISSUE=Peripheral blood T-cell, and Umbilical vein endothelial cell;
RA Godfrey H.P., Ebrahim A.A.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP PROTEIN SEQUENCE OF 291-302, AND BINDING TO M.BOVIS ANTIGEN 85B (FBPB)
RP (MICROBIAL INFECTION).
RX PubMed=8406884; DOI=10.1128/iai.61.11.4828-4834.1993;
RA Peake P., Gooley A., Britton W.J.;
RT "Mechanism of interaction of the 85B secreted protein of Mycobacterium
RT bovis with fibronectin.";
RL Infect. Immun. 61:4828-4834(1993).
RN [15]
RP PROTEIN SEQUENCE OF 309-608, FUNCTION, AND COLLAGEN-BINDING.
RX PubMed=3024962; DOI=10.1002/j.1460-2075.1986.tb04575.x;
RA Owens R.J., Baralle F.E.;
RT "Mapping the collagen-binding site of human fibronectin by expression in
RT Escherichia coli.";
RL EMBO J. 5:2825-2830(1986).
RN [16]
RP PROTEIN SEQUENCE OF 616-705, AND FUNCTION.
RX PubMed=3900070; DOI=10.1016/s0021-9258(17)38997-4;
RA Calaycay J., Pande H., Lee T., Borsi L., Siri A., Shively J.E., Zardi L.;
RT "Primary structure of a DNA- and heparin-binding domain (Domain III) in
RT human plasma fibronectin.";
RL J. Biol. Chem. 260:12136-12141(1985).
RN [17]
RP PROTEIN SEQUENCE OF 723-911, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP GLYCOSYLATION AT ASN-877, AND VARIANT PRO-817.
RC TISSUE=Urine;
RX PubMed=17614963; DOI=10.1111/j.1742-4658.2007.05926.x;
RA Iida R., Yasuda T., Kishi K.;
RT "Identification of novel fibronectin fragments detected specifically in
RT juvenile urine.";
RL FEBS J. 274:3939-3947(2007).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 973-2386 (ISOFORM 3), AND VARIANT ILE-2261.
RX PubMed=6462919; DOI=10.1093/nar/12.14.5853;
RA Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.;
RT "Human fibronectin: cell specific alternative mRNA splicing generates
RT polypeptide chains differing in the number of internal repeats.";
RL Nucleic Acids Res. 12:5853-5868(1984).
RN [19]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1232-1378, AND NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 1685-1873.
RX PubMed=3375063; DOI=10.1093/nar/16.8.3545;
RA Paolella G., Henchcliffe C., Sebastio G., Baralle F.E.;
RT "Sequence analysis and in vivo expression show that alternative splicing of
RT ED-B and ED-A regions of the human fibronectin gene are independent
RT events.";
RL Nucleic Acids Res. 16:3545-3557(1988).
RN [20]
RP PROTEIN SEQUENCE OF 1342-1349 AND 1352-1360 (ISOFORMS 7/11/13/15).
RX PubMed=2822387; DOI=10.1002/j.1460-2075.1987.tb02509.x;
RA Zardi L., Carnemolla B., Siri A., Petersen T.E., Paolella G., Sebastio G.,
RA Baralle F.E.;
RT "Transformed human cells produce a new fibronectin isoform by preferential
RT alternative splicing of a previously unobserved exon.";
RL EMBO J. 6:2337-2342(1987).
RN [21]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1257-1365.
RX PubMed=3478690; DOI=10.1073/pnas.84.20.7179;
RA Gutman A., Kornblihtt A.R.;
RT "Identification of a third region of cell-specific alternative splicing in
RT human fibronectin mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7179-7182(1987).
RN [22]
RP PROTEIN SEQUENCE OF 1532-1639.
RX PubMed=7050098; DOI=10.1016/s0021-9258(18)34113-9;
RA Pierschbacher M.D., Ruoslahti E., Sundelin J., Lind P., Peterson P.A.;
RT "The cell attachment domain of fibronectin. Determination of the primary
RT structure.";
RL J. Biol. Chem. 257:9593-9597(1982).
RN [23]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1539-1631.
RX PubMed=6688418; DOI=10.1016/s0021-9258(17)44437-1;
RA Oldberg A., Linney E., Ruoslahti E.;
RT "Molecular cloning and nucleotide sequence of a cDNA clone coding for the
RT cell attachment domain in human fibronectin.";
RL J. Biol. Chem. 258:10193-10196(1983).
RN [24]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1539-1631.
RX PubMed=3003095; DOI=10.1016/s0021-9258(17)35904-5;
RA Oldberg A., Ruoslahti E.;
RT "Evolution of the fibronectin gene. Exon structure of cell attachment
RT domain.";
RL J. Biol. Chem. 261:2113-2116(1986).
RN [25]
RP PROTEIN SEQUENCE OF 1680-2149 (ISOFORMS 8/14), AND FUNCTION.
RX PubMed=3593230; DOI=10.1042/bj2410923;
RA Garcia-Pardo A., Rostagno A., Frangione B.;
RT "Primary structure of human plasma fibronectin. Characterization of a 38
RT kDa domain containing the C-terminal heparin-binding site (Hep III site)
RT and a region of molecular heterogeneity.";
RL Biochem. J. 241:923-928(1987).
RN [26]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1685-2477 (ISOFORMS 1/11/15), AND VARIANT
RP ILE-2261.
RX PubMed=2992573; DOI=10.1021/bi00332a016;
RA Bernard M.P., Kolbe M., Weil D., Chu M.-L.;
RT "Human cellular fibronectin: comparison of the carboxyl-terminal portion
RT with rat identifies primary structural domains separated by hypervariable
RT regions.";
RL Biochemistry 24:2698-2704(1985).
RN [27]
RP PROTEIN SEQUENCE OF 1705-1719; 1821-1839; 1847-1850; 1894-1902; 1951-2014;
RP 2021-2036; 2042-2063 AND 2073-2080 (ISOFORMS
RP 1/3/4/5/6/7/8/9/10/11/12/13/14/15/17), PROTEIN SEQUENCE OF 2082-2094
RP (ISOFORMS 1/3/7/8/11/14/15), PROTEIN SEQUENCE OF 2111-2129 (ISOFORMS
RP 1/3/7/8/9/11/12/14/15/17), PROTEIN SEQUENCE OF 2151-2161 (ISOFORMS
RP 1/3/7/8/9/11/12/14/15), PROTEIN SEQUENCE OF 2162-2222 (ISOFORMS 1/8/11/15),
RP PROTEIN SEQUENCE OF 2241-2271 (ISOFORMS 1/3/5/7/8/9/10/11/12/13/14/15/17),
RP PROTEIN SEQUENCE OF 2276-2296 (ISOFORMS 1/3/7/8/9/10/11/12/13/14/15/17),
RP PROTEIN SEQUENCE OF 2322-2333 (ISOFORMS 1/3/6/7/8/9/10/11/12/13/14/15/17),
RP VARIANT ILE-2261, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=2012601; DOI=10.1042/bj2740731;
RA Tressel T., McCarthy J.B., Calaycay J., Lee T.D., Legesse K., Shively J.E.,
RA Pande H.;
RT "Human plasma fibronectin. Demonstration of structural differences between
RT the A- and B-chains in the III CS region.";
RL Biochem. J. 274:731-738(1991).
RN [28]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1632-1901 (ISOFORMS 1/3/6/7/11/15/17), AND
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1715-1818 (ISOFORMS 8/9/10/12/13/14).
RX PubMed=6200322; DOI=10.1002/j.1460-2075.1984.tb01787.x;
RA Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.;
RT "Human fibronectin: molecular cloning evidence for two mRNA species
RT differing by an internal segment coding for a structural domain.";
RL EMBO J. 3:221-226(1984).
RN [29]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1713-2218 (ISOFORMS 9/12).
RX PubMed=3021206; DOI=10.1021/bi00365a032;
RA Sekiguchi K., Klos A.M., Kurachi K., Yoshitake S., Hakomori S.;
RT "Human liver fibronectin complementary DNAs: identification of two
RT different messenger RNAs possibly encoding the alpha and beta subunits of
RT plasma fibronectin.";
RL Biochemistry 25:4936-4941(1986).
RN [30]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1879-2477 (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1879-2400 (ISOFORMS 5 AND 6), AND VARIANT ILE-2261.
RC TISSUE=Cartilage;
RX PubMed=12127832; DOI=10.1053/joca.2002.0792;
RA Parker A.E., Boutell J., Carr A., Maciewicz R.A.;
RT "Novel cartilage-specific splice variants of fibronectin.";
RL Osteoarthritis Cartilage 10:528-534(2002).
RN [31]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2039-2157 (ISOFORMS 1/3/7/8/11/14/15).
RX PubMed=2989004; DOI=10.1016/0014-5793(85)81333-8;
RA Umezawa K., Kornblihtt A.R., Baralle F.E.;
RT "Isolation and characterization of cDNA clones for human liver
RT fibronectin.";
RL FEBS Lett. 186:31-34(1985).
RN [32]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2083-2238.
RX PubMed=3770201; DOI=10.1016/0014-5793(86)81506-x;
RA Vibe-Pedersen K., Magnusson S., Baralle F.E.;
RT "Donor and acceptor splice signals within an exon of the human fibronectin
RT gene: a new type of differential splicing.";
RL FEBS Lett. 207:287-291(1986).
RN [33]
RP PROTEIN SEQUENCE OF 2162-2447 (ISOFORMS 3/7/9/12/14/17), AND VARIANT
RP ILE-2261.
RX PubMed=4019516; DOI=10.1016/s0021-9258(17)39250-5;
RA Garcia-Pardo A., Pearlstein E., Frangione B.;
RT "Primary structure of human plasma fibronectin. Characterization of a
RT 31,000-dalton fragment from the COOH-terminal region containing a free
RT sulfhydryl group and a fibrin-binding site.";
RL J. Biol. Chem. 260:10320-10325(1985).
RN [34]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2382-2477 (ISOFORMS
RP 1/3/5/6/7/8/9/10/11/12/13/14/15/17).
RC TISSUE=Mammary carcinoma;
RX PubMed=6304699; DOI=10.1073/pnas.80.11.3218;
RA Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.;
RT "Isolation and characterization of cDNA clones for human and bovine
RT fibronectins.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3218-3222(1983).
RN [35]
RP SULFATION.
RX PubMed=2414772; DOI=10.1073/pnas.82.21.7160;
RA Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.;
RT "Tyrosine sulfation of proteins from the human hepatoma cell line HepG2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985).
RN [36]
RP IDENTIFICATION OF UGL-Y1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RX PubMed=3584091; DOI=10.1093/oxfordjournals.jbchem.a121920;
RA Iida R., Yasuda T., Kishi K.;
RT "Purification of a young age-related glycoprotein (Ugl-Y) from normal human
RT urine.";
RL J. Biochem. 101:357-363(1987).
RN [37]
RP INTERACTION WITH FBLN1.
RX PubMed=1400330; DOI=10.1016/s0021-9258(19)88674-x;
RA Balbona K., Tran H., Godyna S., Ingham K.C., Strickland D.K.,
RA Argraves W.S.;
RT "Fibulin binds to itself and to the carboxyl-terminal heparin-binding
RT region of fibronectin.";
RL J. Biol. Chem. 267:20120-20125(1992).
RN [38]
RP FUNCTION, AND CHARACTERIZATION OF FIBRIN-BINDING SITE 1.
RX PubMed=7989369; DOI=10.1016/s0021-9258(18)31786-1;
RA Rostagno A., Williams M.J., Baron M., Campbell I.D., Gold L.I.;
RT "Further characterization of the NH2-terminal fibrin-binding site on
RT fibronectin.";
RL J. Biol. Chem. 269:31938-31945(1994).
RN [39]
RP SUBUNIT, AND FUNCTION (ANASTELLIN).
RX PubMed=8114919; DOI=10.1038/367193a0;
RA Morla A., Zhang Z., Ruoslahti E.;
RT "Superfibronectin is a functionally distinct form of fibronectin.";
RL Nature 367:193-196(1994).
RN [40]
RP INTERACTION WITH LGALS3BP.
RX PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
RA Sasaki T., Brakebusch C., Engel J., Timpl R.;
RT "Mac-2 binding protein is a cell-adhesive protein of the extracellular
RT matrix which self-assembles into ring-like structures and binds beta1
RT integrins, collagens and fibronectin.";
RL EMBO J. 17:1606-1613(1998).
RN [41]
RP INTERACTION WITH S.PNEUMONIAE FIBRONECTIN-BINDING PROTEIN (MICROBIAL
RP INFECTION).
RX PubMed=11580843; DOI=10.1046/j.1365-2958.2001.02610.x;
RA Holmes A.R., McNab R., Millsap K.W., Rohde M., Hammerschmidt S.,
RA Mawdsley J.L., Jenkinson H.F.;
RT "The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding
RT protein that is essential for virulence.";
RL Mol. Microbiol. 41:1395-1408(2001).
RN [42]
RP FUNCTION (ANASTELLIN).
RX PubMed=11209058; DOI=10.1073/pnas.98.2.620;
RA Yi M., Ruoslahti E.;
RT "A fibronectin fragment inhibits tumor growth, angiogenesis, and
RT metastasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:620-624(2001).
RN [43]
RP INTERACTION WITH COL13A1.
RX PubMed=11956183; DOI=10.1074/jbc.m107583200;
RA Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R.,
RA Pihlajaniemi T.;
RT "The type XIII collagen ectodomain is a 150-nm rod and capable of binding
RT to fibronectin, nidogen-2, perlecan, and heparin.";
RL J. Biol. Chem. 277:23092-23099(2002).
RN [44]
RP INTERACTION WITH COMP.
RX PubMed=12225811; DOI=10.1016/s0945-053x(02)00015-x;
RA Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P.,
RA Perris R., Fang C.;
RT "Matrix-matrix interaction of cartilage oligomeric matrix protein and
RT fibronectin.";
RL Matrix Biol. 21:461-470(2002).
RN [45]
RP INTERACTION WITH MYOC.
RX PubMed=11773026;
RA Filla M.S., Liu X., Nguyen T.D., Polansky J.R., Brandt C.R., Kaufman P.L.,
RA Peters D.M.;
RT "In vitro localization of TIGR/MYOC in trabecular meshwork extracellular
RT matrix and binding to fibronectin.";
RL Invest. Ophthalmol. Vis. Sci. 43:151-161(2002).
RN [46]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [47]
RP FUNCTION (ANASTELLIN).
RX PubMed=15665290;
RA Ambesi A., Klein R.M., Pumiglia K.M., McKeown-Longo P.J.;
RT "Anastellin, a fragment of the first type III repeat of fibronectin,
RT inhibits extracellular signal-regulated kinase and causes G(1) arrest in
RT human microvessel endothelial cells.";
RL Cancer Res. 65:148-156(2005).
RN [48]
RP GLYCOSYLATION AT THR-279; ASN-430; ASN-528; ASN-542; ASN-877; ASN-1007;
RP ASN-1244 AND ASN-2199.
RX PubMed=16037490; DOI=10.1093/glycob/cwj019;
RA Tajiri M., Yoshida S., Wada Y.;
RT "Differential analysis of site-specific glycans on plasma and cellular
RT fibronectins: application of a hydrophilic affinity method for glycopeptide
RT enrichment.";
RL Glycobiology 15:1332-1340(2005).
RN [49]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-430; ASN-528; ASN-542; ASN-1007
RP AND ASN-1244.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [50]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [51]
RP INTERACTION WITH FST3.
RX PubMed=16336961; DOI=10.1016/j.yexcr.2005.11.006;
RA Maguer-Satta V., Forissier S., Bartholin L., Martel S., Jeanpierre S.,
RA Bachelard E., Rimokh R.;
RT "A novel role for fibronectin type I domain in the regulation of human
RT hematopoietic cell adhesiveness through binding to follistatin domains of
RT FLRG and follistatin.";
RL Exp. Cell Res. 312:434-442(2006).
RN [52]
RP INTERACTION WITH TNFAIP6 AND THBS1.
RX PubMed=18042364; DOI=10.1016/j.matbio.2007.10.003;
RA Kuznetsova S.A., Mahoney D.J., Martin-Manso G., Ali T., Nentwich H.A.,
RA Sipes J.M., Zeng B., Vogel T., Day A.J., Roberts D.D.;
RT "TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin
RT and increases fibronectin matrix assembly.";
RL Matrix Biol. 27:201-210(2008).
RN [53]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [54]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-1007.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [55]
RP GLYCOSYLATION AT ASN-528; ASN-542 AND ASN-1007.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [56]
RP FUNCTION (ANASTELLIN), AND MUTAGENESIS OF LEU-663 AND TYR-666.
RX PubMed=19379667; DOI=10.1016/j.matbio.2009.01.003;
RA You R., Klein R.M., Zheng M., McKeown-Longo P.J.;
RT "Regulation of p38 MAP kinase by anastellin is independent of anastellin's
RT effect on matrix fibronectin.";
RL Matrix Biol. 28:101-109(2009).
RN [57]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [58]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2454 AND SER-2475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [59]
RP PHOSPHORYLATION AT SER-2475.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [60]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA Lako M.;
RT "Extracellular matrix component expression in human pluripotent stem cell-
RT derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT an important role for IMPG1 and CD44 in the development of photoreceptors
RT and interphotoreceptor matrix.";
RL Acta Biomater. 74:207-221(2018).
RN [61]
RP INTERACTION WITH S.SUIS FIBRONECTIN-BINDING PROTEIN (MICROBIAL INFECTION).
RX PubMed=27834729; DOI=10.1073/pnas.1608406113;
RA Musyoki A.M., Shi Z., Xuan C., Lu G., Qi J., Gao F., Zheng B., Zhang Q.,
RA Li Y., Haywood J., Liu C., Yan J., Shi Y., Gao G.F.;
RT "Structural and functional analysis of an anchorless fibronectin-binding
RT protein FBPS from Gram-positive bacterium Streptococcus suis.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:13869-13874(2016).
RN [62]
RP SUBCELLULAR LOCATION, INVOLVEMENT IN SMDCF, VARIANTS SMDCF PHE-87; ARG-123;
RP TRP-225; ASP-240; GLY-260 AND THR-809 DEL, AND CHARACTERIZATION OF VARIANTS
RP SMDCF PHE-87; ASP-240 AND GLY-260.
RX PubMed=29100092; DOI=10.1016/j.ajhg.2017.09.019;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA Lee C.S., Fu H., Baratang N., Rousseau J., Kumra H., Sutton V.R.,
RA Niceta M., Ciolfi A., Yamamoto G., Bertola D., Marcelis C.L.,
RA Lugtenberg D., Bartuli A., Kim C., Hoover-Fong J., Sobreira N., Pauli R.,
RA Bacino C., Krakow D., Parboosingh J., Yap P., Kariminejad A.,
RA McDonald M.T., Aracena M.I., Lausch E., Unger S., Superti-Furga A.,
RA Lu J.T., Cohn D.H., Tartaglia M., Lee B.H., Reinhardt D.P., Campeau P.M.;
RT "Mutations in fibronectin cause a subtype of spondylometaphyseal dysplasia
RT with 'corner fractures'.";
RL Am. J. Hum. Genet. 101:815-823(2017).
RN [63]
RP FUNCTION, AND LILRB4-BINDING REGION.
RX PubMed=34089617; DOI=10.1093/intimm/dxab028;
RA Su M.T., Inui M., Wong Y.L., Takahashi M., Sugahara-Tobinai A., Ono K.,
RA Miyamoto S., Murakami K., Itoh-Nakadai A., Kezuka D., Itoi S., Endo S.,
RA Hirayasu K., Arase H., Takai T.;
RT "Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin
RT ameliorates autoimmune disease in BXSB/Yaa mice.";
RL Int. Immunol. 33:447-458(2021).
RN [64]
RP STRUCTURE BY NMR OF 1538-1631.
RX PubMed=1311202; DOI=10.1021/bi00122a025;
RA Baron M., Main A.L., Driscoll P.C., Mardon H.J., Boyd J., Campbell I.D.;
RT "1H NMR assignment and secondary structure of the cell adhesion type III
RT module of fibronectin.";
RL Biochemistry 31:2068-2073(1992).
RN [65]
RP STRUCTURE BY NMR OF 1538-1631.
RX PubMed=1423622; DOI=10.1016/0092-8674(92)90600-h;
RA Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D.;
RT "The three-dimensional structure of the tenth type III module of
RT fibronectin: an insight into RGD-mediated interactions.";
RL Cell 71:671-678(1992).
RN [66]
RP STRUCTURE BY NMR OF 183-275, AND DISULFIDE BONDS.
RX PubMed=8308892; DOI=10.1006/jmbi.1994.1083;
RA Williams M.J., Phan I., Harvey T.S., Rostagno A., Gold L.I., Campbell I.D.;
RT "Solution structure of a pair of fibronectin type 1 modules with fibrin
RT binding activity.";
RL J. Mol. Biol. 235:1302-1311(1994).
RN [67]
RP STRUCTURE BY NMR OF 32-92.
RX PubMed=7583666; DOI=10.1038/nsb1195-946;
RA Potts J.R., Phan I., Williams M.J., Campbell I.D.;
RT "High-resolution structural studies of the factor XIIIa crosslinking site
RT and the first type 1 module of fibronectin.";
RL Nat. Struct. Biol. 2:946-950(1995).
RN [68]
RP STRUCTURE BY NMR OF 406-464.
RX PubMed=9514732; DOI=10.1006/jmbi.1997.1528;
RA Sticht H., Pickford A.R., Potts J.R., Campbell I.D.;
RT "Solution structure of the glycosylated second type 2 module of
RT fibronectin.";
RL J. Mol. Biol. 276:177-187(1998).
RN [69]
RP STRUCTURE BY NMR OF EXTRA DOMAIN B FROM ISOFORM 7.
RX PubMed=10196121; DOI=10.1016/s0969-2126(99)80051-3;
RA Fattorusso R., Pellecchia M., Viti F., Neri P., Neri D., Wuethrich K.;
RT "NMR structure of the human oncofoetal fibronectin ED-B domain, a specific
RT marker for angiogenesis.";
RL Structure 7:381-390(1999).
RN [70]
RP STRUCTURE BY NMR OF 305-405.
RX PubMed=10647176; DOI=10.1016/s0969-2126(00)88336-7;
RA Bocquier A.A., Potts J.R., Pickford A.R., Campbell I.D.;
RT "Solution structure of a pair of modules from the gelatin-binding domain of
RT fibronectin.";
RL Structure 7:1451-1460(1999).
RN [71]
RP STRUCTURE BY NMR OF 305-464, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-430.
RX PubMed=11285216; DOI=10.1093/emboj/20.7.1519;
RA Pickford A.R., Smith S.P., Staunton D., Boyd J., Campbell I.D.;
RT "The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human
RT fibronectin enhances gelatin binding.";
RL EMBO J. 20:1519-1529(2001).
RN [72]
RP STRUCTURE BY NMR OF 1722-1815.
RX PubMed=11775745; DOI=10.1023/a:1012947209393;
RA Niimi T., Osawa M., Yamaji N., Yasunaga K., Sakashita H., Mase T.,
RA Tanaka A., Fujita S.;
RT "NMR structure of human fibronectin EDA.";
RL J. Biomol. NMR 21:281-284(2001).
RN [73]
RP STRUCTURE BY NMR OF 631-705, AND MUTAGENESIS OF TYR-641; ILE-642; LEU-663;
RP TYR-666; LEU-681; ILE-682; SER-683; ILE-684; GLU-691; VAL-692; ARG-694;
RP PHE-695; ASP-696 AND PHE-697.
RX PubMed=12946358; DOI=10.1016/s0022-2836(03)00890-8;
RA Briknarova K., Aakerman M.E., Hoyt D.W., Ruoslahti E., Ely K.R.;
RT "Anastellin, an FN3 fragment with fibronectin polymerization activity,
RT resembles amyloid fibril precursors.";
RL J. Mol. Biol. 332:205-215(2003).
RN [74]
RP STRUCTURE BY NMR OF 48-140 IN COMPLEX WITH A STAPHYLOCOCCUS
RP FIBRONECTIN-BINDING PROTEIN, SUBUNIT (MICROBIAL INFECTION), AND DISULFIDE
RP BONDS.
RX PubMed=12736686; DOI=10.1038/nature01589;
RA Schwarz-Linek U., Werner J.M., Pickford A.R., Gurusiddappa S., Kim J.H.,
RA Pilka E.S., Briggs J.A., Gough T.S., Hoeoek M., Campbell I.D., Potts J.R.;
RT "Pathogenic bacteria attach to human fibronectin through a tandem beta-
RT zipper.";
RL Nature 423:177-181(2003).
RN [75]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1538-1626.
RX PubMed=8120888; DOI=10.1016/0022-2836(94)90013-2;
RA Dickinson C.D., Veerapandian B., Dai X.-P., Hamlin R.C., Xuong N.-H.,
RA Ruoslahti E., Ely K.R.;
RT "Crystal structure of the tenth type III cell adhesion module of human
RT fibronectin.";
RL J. Mol. Biol. 236:1079-1092(1994).
RN [76]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1173-1540.
RX PubMed=8548820; DOI=10.1016/s0092-8674(00)81002-8;
RA Leahy D.J., Aukhil I., Erickson H.P.;
RT "2.0 A crystal structure of a four-domain segment of human fibronectin
RT encompassing the RGD loop and synergy region.";
RL Cell 84:155-164(1996).
RN [77]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1812-2082.
RX PubMed=10075919; DOI=10.1093/emboj/18.6.1468;
RA Sharma A., Askari J.A., Humphries M.J., Jones E.Y., Stuart D.I.;
RT "Crystal structure of a heparin- and integrin-binding segment of human
RT fibronectin.";
RL EMBO J. 18:1468-1479(1999).
RN [78]
RP STRUCTURE BY NMR OF 608-701.
RX PubMed=14657397; DOI=10.1073/pnas.2334390100;
RA Gao M., Craig D., Lequin O., Campbell I.D., Vogel V., Schulten K.;
RT "Structure and functional significance of mechanically unfolded fibronectin
RT type III1 intermediates.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14784-14789(2003).
RN [79]
RP STRUCTURE BY NMR OF 609-809.
RX PubMed=17464288; DOI=10.1038/sj.emboj.7601694;
RA Vakonakis I., Staunton D., Rooney L.M., Campbell I.D.;
RT "Interdomain association in fibronectin: insight into cryptic sites and
RT fibrillogenesis.";
RL EMBO J. 26:2575-2583(2007).
RN [80]
RP STRUCTURE BY NMR OF 93-182, X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF
RP 93-182, AND DISULFIDE BONDS.
RX PubMed=17368672; DOI=10.1016/j.jmb.2007.02.061;
RA Rudino-Pinera E., Ravelli R.B., Sheldrick G.M., Nanao M.H.,
RA Korostelev V.V., Werner J.M., Schwarz-Linek U., Potts J.R., Garman E.F.;
RT "The solution and crystal structures of a module pair from the
RT Staphylococcus aureus-binding site of human fibronectin -- a tale with a
RT twist.";
RL J. Mol. Biol. 368:833-844(2007).
RN [81]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 93-275 IN COMPLEX WITH
RP STAPHYLOCOCCUS AUREUS FNBA.
RX PubMed=18713862; DOI=10.1073/pnas.0803556105;
RA Bingham R.J., Rudino-Pinera E., Meenan N.A.G., Schwarz-Linek U.,
RA Turkenburg J.P., Hoeoek M., Garman E.F., Potts J.R.;
RT "Crystal structures of fibronectin-binding sites from Staphylococcus aureus
RT FnBPA in complex with fibronectin domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12254-12258(2008).
RN [82]
RP STRUCTURE BY NMR OF 2330-2390.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 11th FN1 domain from human fibronectin 1.";
RL Submitted (MAR-2008) to the PDB data bank.
RN [83]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 516-608 IN COMPLEX WITH TYPE I
RP COLLAGEN.
RX PubMed=19251642; DOI=10.1073/pnas.0812516106;
RA Erat M.C., Slatter D.A., Lowe E.D., Millard C.J., Farndale R.W.,
RA Campbell I.D., Vakonakis I.;
RT "Identification and structural analysis of type I collagen sites in complex
RT with fibronectin fragments.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4195-4200(2009).
RN [84]
RP VARIANTS [LARGE SCALE ANALYSIS] ASN-940; PRO-1120 AND ASN-2471.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [85]
RP VARIANTS GFND2 CYS-973; ARG-1925 AND ARG-1974, VARIANTS LEU-15 AND
RP VAL-2051, AND CHARACTERIZATION OF VARIANTS GFND2 ARG-1925 AND ARG-1974.
RX PubMed=18268355; DOI=10.1073/pnas.0707730105;
RA Castelletti F., Donadelli R., Banterla F., Hildebrandt F., Zipfel P.F.,
RA Bresin E., Otto E., Skerka C., Renieri A., Todeschini M., Caprioli J.,
RA Caruso R.M., Artuso R., Remuzzi G., Noris M.;
RT "Mutations in FN1 cause glomerulopathy with fibronectin deposits.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2538-2543(2008).
RN [86]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-2261, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962,
CC PubMed:3900070, PubMed:3593230, PubMed:7989369). Fibronectins are
CC involved in cell adhesion, cell motility, opsonization, wound healing,
CC and maintenance of cell shape (PubMed:3024962, PubMed:3900070,
CC PubMed:3593230, PubMed:7989369). Involved in osteoblast compaction
CC through the fibronectin fibrillogenesis cell-mediated matrix assembly
CC process, essential for osteoblast mineralization (By similarity).
CC Participates in the regulation of type I collagen deposition by
CC osteoblasts (By similarity). Acts as a ligand for the LILRB4 receptor,
CC inhibiting FCGR1A/CD64-mediated monocyte activation (PubMed:34089617).
CC {ECO:0000250|UniProtKB:P11276, ECO:0000269|PubMed:3024962,
CC ECO:0000269|PubMed:34089617, ECO:0000269|PubMed:3593230,
CC ECO:0000269|PubMed:3900070, ECO:0000269|PubMed:7989369}.
CC -!- FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation.
CC This fibronectin polymer, named superfibronectin, exhibits enhanced
CC adhesive properties. Both anastellin and superfibronectin inhibit tumor
CC growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and
CC inhibits lysophospholipid signaling. {ECO:0000269|PubMed:11209058,
CC ECO:0000269|PubMed:15665290, ECO:0000269|PubMed:19379667,
CC ECO:0000269|PubMed:8114919}.
CC -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC variants, connected by 2 disulfide bonds near the carboxyl ends; to a
CC lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and
CC COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP
CC (PubMed:12225811). Interacts (via type III repeats 9-14) with TNFAIP6
CC (via CUB domain); this interaction enhances fibronectin fibril
CC assembly. TNFAIP6 may act as a bridging molecule between FN1 and THBS1
CC (PubMed:18042364). Interacts with TNR; the interaction inhibits cell
CC adhesion and neurite outgrowth (By similarity). Interacts with FST3 and
CC MYOC. {ECO:0000250, ECO:0000269|PubMed:11773026,
CC ECO:0000269|PubMed:11956183, ECO:0000269|PubMed:12225811,
CC ECO:0000269|PubMed:1400330, ECO:0000269|PubMed:16336961,
CC ECO:0000269|PubMed:18042364, ECO:0000269|PubMed:18713862,
CC ECO:0000269|PubMed:19251642, ECO:0000269|PubMed:8114919,
CC ECO:0000269|PubMed:9501082}.
CC -!- SUBUNIT: (Microbial infection) Interacts with S.aureus FnbA.
CC {ECO:0000269|PubMed:12736686}.
CC -!- SUBUNIT: (Microbial infection) Interacts with M.bovis FbpB via the
CC collagen-binding region. {ECO:0000269|PubMed:8406884}.
CC -!- SUBUNIT: (Microbial infection) Interacts with recombinant S.pneumoniae
CC PavA (rqcH). {ECO:0000269|PubMed:11580843}.
CC -!- SUBUNIT: (Microbial infection) Interacts with recombinant S.suis FbpS
CC (rqcH) via fibronectin's N-terminal 30 kDa region.
CC {ECO:0000269|PubMed:27834729}.
CC -!- SUBUNIT: (Microbial infection) Interacts with fibronectin-binding
CC proteins from other Mycobacteria. {ECO:0000269|PubMed:12736686}.
CC -!- INTERACTION:
CC P02751; P29279: CCN2; NbExp=5; IntAct=EBI-1220319, EBI-2835375;
CC P02751; P02452: COL1A1; NbExp=3; IntAct=EBI-1220319, EBI-982999;
CC P02751; P07585: DCN; NbExp=9; IntAct=EBI-1220319, EBI-9663608;
CC P02751; P35555: FBN1; NbExp=2; IntAct=EBI-1220319, EBI-2505934;
CC P02751; P35556: FBN2; NbExp=2; IntAct=EBI-1220319, EBI-6164392;
CC P02751; O75636: FCN3; NbExp=3; IntAct=EBI-1220319, EBI-11786958;
CC P02751; P02751: FN1; NbExp=8; IntAct=EBI-1220319, EBI-1220319;
CC P02751; PRO_0000018520 [P28300]: LOX; NbExp=2; IntAct=EBI-1220319, EBI-20724846;
CC P02751; Q9Y4K0: LOXL2; NbExp=2; IntAct=EBI-1220319, EBI-7172227;
CC P02751; P08519: LPA; NbExp=2; IntAct=EBI-1220319, EBI-9232288;
CC P02751; P11684: SCGB1A1; NbExp=3; IntAct=EBI-1220319, EBI-7797649;
CC P02751; P05154: SERPINA5; NbExp=3; IntAct=EBI-1220319, EBI-722597;
CC P02751; P21980: TGM2; NbExp=4; IntAct=EBI-1220319, EBI-727668;
CC P02751; P07996: THBS1; NbExp=2; IntAct=EBI-1220319, EBI-2530274;
CC P02751; P98066: TNFAIP6; NbExp=8; IntAct=EBI-1220319, EBI-11700693;
CC P02751; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1220319, EBI-741480;
CC P02751; P40337: VHL; NbExp=2; IntAct=EBI-1220319, EBI-301246;
CC P02751; P14738: fnbA; Xeno; NbExp=23; IntAct=EBI-1220319, EBI-8398157;
CC P02751; Q53682: fnbB; Xeno; NbExp=19; IntAct=EBI-1220319, EBI-8398005;
CC P02751; Q53971: fnbB; Xeno; NbExp=4; IntAct=EBI-1220319, EBI-20719966;
CC P02751; Q93ED6: fne; Xeno; NbExp=8; IntAct=EBI-1220319, EBI-9826140;
CC P02751; P75358: gapA; Xeno; NbExp=3; IntAct=EBI-1220319, EBI-2259469;
CC P02751; Q4AAD6: MHJ_0194; Xeno; NbExp=3; IntAct=EBI-1220319, EBI-14034164;
CC P02751; Q601D1: mhp271; Xeno; NbExp=2; IntAct=EBI-1220319, EBI-13948049;
CC P02751; P75392: pdhC; Xeno; NbExp=2; IntAct=EBI-1220319, EBI-2259593;
CC P02751; Q9CKF6: PM1665; Xeno; NbExp=5; IntAct=EBI-1220319, EBI-11164515;
CC P02751; Q01924: Sfb; Xeno; NbExp=5; IntAct=EBI-1220319, EBI-20729956;
CC P02751; P23568: tuf; Xeno; NbExp=2; IntAct=EBI-1220319, EBI-2259072;
CC P02751; PRO_0000045603 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-1220319, EBI-6927928;
CC P02751-1; P20908: COL5A1; NbExp=2; IntAct=EBI-22099195, EBI-2464511;
CC P02751-7; P06241: FYN; NbExp=2; IntAct=EBI-7133890, EBI-515315;
CC PRO_0000390479; PRO_0000018520 [P28300]: LOX; NbExp=3; IntAct=EBI-15482592, EBI-20724846;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305|PubMed:29100092}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=17;
CC Comment=A number of isoforms are produced. The diversity of isoforms
CC depends on the V region and either of the two extra domains which can
CC be either included or excluded (partially or completely for the V
CC region). {ECO:0000305};
CC Name=15;
CC IsoId=P02751-15; Sequence=Displayed;
CC Name=1;
CC IsoId=P02751-1; Sequence=VSP_060347;
CC Name=2; Synonyms=MSF-FN70, Migration stimulation factor FN70;
CC IsoId=P02751-2; Sequence=VSP_060343, VSP_060344, VSP_060345;
CC Name=3; Synonyms=V89;
CC IsoId=P02751-3; Sequence=VSP_060347, VSP_060353;
CC Name=4; Synonyms=Fibronectin III-15X;
CC IsoId=P02751-4; Sequence=VSP_060347, VSP_060351, VSP_060354,
CC VSP_060355;
CC Name=5; Synonyms=Fibronectin (V+I-10)-;
CC IsoId=P02751-5; Sequence=VSP_060347, VSP_060351, VSP_060356;
CC Name=6; Synonyms=Fibronectin (V+III-15)-;
CC IsoId=P02751-6; Sequence=VSP_060347, VSP_060350;
CC Name=7; Synonyms=Fibronectin containing EDB domain;
CC IsoId=P02751-7; Sequence=VSP_060353;
CC Name=8; Synonyms=Fibronectin not containing EDA domain;
CC IsoId=P02751-8; Sequence=VSP_060347, VSP_060349;
CC Name=9; Synonyms=Fibronectin not containing EDA and EDB domains and
CC uses V64 variant of IIICS region;
CC IsoId=P02751-9; Sequence=VSP_060347, VSP_060349, VSP_060352,
CC VSP_060353;
CC Name=10;
CC IsoId=P02751-10; Sequence=VSP_060347, VSP_060349, VSP_060351;
CC Name=11; Synonyms=Fibronectin containing EDB domain, exon x+2;
CC IsoId=P02751-11; Sequence=VSP_060348;
CC Name=12;
CC IsoId=P02751-12; Sequence=VSP_060346, VSP_060349, VSP_060352,
CC VSP_060353;
CC Name=13;
CC IsoId=P02751-13; Sequence=VSP_060349, VSP_060351;
CC Name=14;
CC IsoId=P02751-14; Sequence=VSP_060347, VSP_060349, VSP_060353;
CC Name=16; Synonyms=Migration stimulation factor, MSF;
CC IsoId=P02751-16; Sequence=VSP_060344, VSP_060345;
CC Name=17;
CC IsoId=P02751-17; Sequence=VSP_060347, VSP_060352, VSP_060353;
CC -!- TISSUE SPECIFICITY: Expressed in the inner limiting membrane and around
CC blood vessels in the retina (at protein level) (PubMed:29777959).
CC Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular
CC FN (dimeric or cross-linked multimeric forms), made by fibroblasts,
CC epithelial and other cell types, is deposited as fibrils in the
CC extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine
CC (PubMed:17614963). {ECO:0000269|PubMed:17614963,
CC ECO:0000269|PubMed:29777959, ECO:0000269|PubMed:3584091}.
CC -!- DEVELOPMENTAL STAGE: Expressed between 12 and 19 weeks post-conception
CC (WPC) in Bruch's membrane, with expression in the choroid evident from
CC 14 WPC onwards (at protein level) (PubMed:29777959). Expressed in the
CC inner limiting membrane at 17 WPC (at protein level) (PubMed:29777959).
CC Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years
CC of age (PubMed:17614963, PubMed:3584091). {ECO:0000269|PubMed:17614963,
CC ECO:0000269|PubMed:29777959, ECO:0000269|PubMed:3584091}.
CC -!- PTM: Sulfated. {ECO:0000269|PubMed:2414772}.
CC -!- PTM: It is not known whether both or only one of Thr-2155 and Thr-2156
CC are/is glycosylated. {ECO:0000269|PubMed:11285216,
CC ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16037490,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17614963,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:2012601, ECO:0000269|PubMed:3584091}.
CC -!- PTM: Forms covalent cross-links mediated by a transglutaminase, such as
CC F13A or TGM2, between a glutamine and the epsilon-amino group of a
CC lysine residue, forming homopolymers and heteropolymers (e.g.
CC fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
CC {ECO:0000250|UniProtKB:P11276}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000269|PubMed:26091039}.
CC -!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
CC anastellin. {ECO:0000305|PubMed:8114919}.
CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting
CC fibronectin activation and matrix formation.
CC {ECO:0000250|UniProtKB:P11276}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia.
CC {ECO:0000250|UniProtKB:P07589}.
CC -!- DISEASE: Glomerulopathy with fibronectin deposits 2 (GFND2)
CC [MIM:601894]: Genetically heterogeneous autosomal dominant disorder
CC characterized clinically by proteinuria, microscopic hematuria, and
CC hypertension that leads to end-stage renal failure in the second to
CC fifth decade of life. {ECO:0000269|PubMed:18268355}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Spondylometaphyseal dysplasia, corner fracture type (SMDCF)
CC [MIM:184255]: An autosomal dominant form of spondylometaphyseal
CC dysplasia, a group of short stature disorders distinguished by
CC abnormalities in the vertebrae and the metaphyses of the tubular bones.
CC SMDCF is characterized by flake-like, triangular, or curvilinear
CC ossification centers at the edges of irregular metaphyses that simulate
CC fractures. These corner fractures involve the distal tibia, the ulnar
CC aspect of the distal radius, the proximal humerus, and the proximal
CC femur. They represent irregular ossification at the growth plates and
CC secondary ossification centers. {ECO:0000269|PubMed:29100092}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 16]: Expressed by fetal and tumor-associated
CC cells. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52463.1; Type=Erroneous translation; Evidence={ECO:0000305};
CC Sequence=AAX76513.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD93077.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD91166.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97964.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97965.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97984.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE45847.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18136.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Fibronectin entry;
CC URL="https://en.wikipedia.org/wiki/Fibronectin";
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DR EMBL; AJ276395; CAC20427.1; -; mRNA.
DR EMBL; AJ535086; CAD59389.1; -; mRNA.
DR EMBL; AJ849445; CAH60958.1; -; mRNA.
DR EMBL; AB191261; BAD52437.1; -; mRNA.
DR EMBL; AB209840; BAD93077.1; ALT_INIT; mRNA.
DR EMBL; AL832202; CAD91166.1; ALT_INIT; mRNA.
DR EMBL; BX537590; CAD97791.1; -; mRNA.
DR EMBL; BX538017; CAD97964.1; ALT_INIT; mRNA.
DR EMBL; BX538018; CAD97965.1; ALT_INIT; mRNA.
DR EMBL; BX538045; CAD97984.1; ALT_INIT; mRNA.
DR EMBL; BX640608; CAE45714.1; -; mRNA.
DR EMBL; BX640731; CAE45847.1; ALT_INIT; mRNA.
DR EMBL; BX640875; CAE45932.1; -; mRNA.
DR EMBL; BX640920; CAE45958.1; -; mRNA.
DR EMBL; CR749281; CAH18136.1; ALT_INIT; mRNA.
DR EMBL; CR749316; CAH18171.1; -; mRNA.
DR EMBL; CR749317; CAH18172.1; -; mRNA.
DR EMBL; AC012462; AAX76513.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC073284; AAY24063.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70536.1; -; Genomic_DNA.
DR EMBL; BC117176; AAI17177.1; -; mRNA.
DR EMBL; BC143763; AAI43764.1; -; mRNA.
DR EMBL; M15801; AAA53376.1; -; Genomic_DNA.
DR EMBL; AF312399; AAG30571.1; -; mRNA.
DR EMBL; X02761; CAA26536.1; -; mRNA.
DR EMBL; U41850; AAD00014.1; -; mRNA.
DR EMBL; U42404; AAD00015.1; -; mRNA.
DR EMBL; U42592; AAD00017.1; -; mRNA.
DR EMBL; U42593; AAD00018.1; -; mRNA.
DR EMBL; U42594; AAD00019.1; -; mRNA.
DR EMBL; U42455; AAD09448.1; -; mRNA.
DR EMBL; U42456; AAD09449.1; -; mRNA.
DR EMBL; U42458; AAD09450.1; -; mRNA.
DR EMBL; U42457; AAD04751.1; -; mRNA.
DR EMBL; X07718; CAB52436.1; -; Genomic_DNA.
DR EMBL; X07717; CAB52437.1; -; Genomic_DNA.
DR EMBL; M18179; AAA52461.1; -; Genomic_DNA.
DR EMBL; M18177; AAA52461.1; JOINED; Genomic_DNA.
DR EMBL; M18178; AAA52461.1; JOINED; Genomic_DNA.
DR EMBL; M12549; AAA58483.1; -; Genomic_DNA.
DR EMBL; M10905; AAA52462.1; -; mRNA.
DR EMBL; M14059; AAA52463.1; ALT_SEQ; mRNA.
DR EMBL; AJ320525; CAC86914.1; -; mRNA.
DR EMBL; AJ320526; CAC86915.1; -; mRNA.
DR EMBL; AJ320527; CAC86916.1; -; mRNA.
DR EMBL; M27589; AAA52465.1; -; mRNA.
DR EMBL; X04530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS2399.1; -. [P02751-3]
DR CCDS; CCDS2400.1; -. [P02751-10]
DR CCDS; CCDS42813.1; -. [P02751-8]
DR CCDS; CCDS42814.1; -. [P02751-15]
DR CCDS; CCDS46510.1; -. [P02751-17]
DR CCDS; CCDS46512.1; -. [P02751-16]
DR CCDS; CCDS77522.1; -. [P02751-9]
DR CCDS; CCDS77523.1; -. [P02751-14]
DR CCDS; CCDS77525.1; -. [P02751-13]
DR CCDS; CCDS77526.1; -. [P02751-7]
DR PIR; A26460; FNHU.
DR PIR; I52394; I52394.
DR PIR; S00848; S00848.
DR RefSeq; NP_001293058.1; NM_001306129.1. [P02751-7]
DR RefSeq; NP_001293059.1; NM_001306130.1. [P02751-13]
DR RefSeq; NP_001293060.1; NM_001306131.1. [P02751-14]
DR RefSeq; NP_001293061.1; NM_001306132.1. [P02751-9]
DR RefSeq; NP_002017.1; NM_002026.3. [P02751-3]
DR RefSeq; NP_473375.2; NM_054034.2. [P02751-16]
DR RefSeq; NP_997639.1; NM_212474.2. [P02751-10]
DR RefSeq; NP_997641.1; NM_212476.2. [P02751-8]
DR RefSeq; NP_997643.1; NM_212478.2. [P02751-17]
DR RefSeq; NP_997647.1; NM_212482.2. [P02751-15]
DR RefSeq; XP_005246463.1; XM_005246406.1.
DR PDB; 1E88; NMR; -; A=305-464.
DR PDB; 1E8B; NMR; -; A=305-464.
DR PDB; 1FBR; NMR; -; A=183-275.
DR PDB; 1FNA; X-ray; 1.80 A; A=1543-1633.
DR PDB; 1FNF; X-ray; 2.00 A; A=1173-1265, A=1357-1631.
DR PDB; 1FNH; X-ray; 2.80 A; A=1812-2082.
DR PDB; 1J8K; NMR; -; A=1722-1815.
DR PDB; 1O9A; NMR; -; A=48-140.
DR PDB; 1OWW; NMR; -; A=608-701.
DR PDB; 1Q38; NMR; -; A=631-705.
DR PDB; 1QGB; NMR; -; A=48-140.
DR PDB; 1QO6; NMR; -; A=305-405.
DR PDB; 1TTF; NMR; -; A=1538-1631.
DR PDB; 1TTG; NMR; -; A=1538-1631.
DR PDB; 2CG6; X-ray; 1.55 A; A=93-182.
DR PDB; 2CG7; X-ray; 1.20 A; A=93-182.
DR PDB; 2CK2; X-ray; 2.00 A; A/B=1538-1633.
DR PDB; 2CKU; NMR; -; A=93-182.
DR PDB; 2EC3; NMR; -; A=2330-2390.
DR PDB; 2FN2; NMR; -; A=406-464.
DR PDB; 2FNB; NMR; -; A=1266-1356.
DR PDB; 2GEE; X-ray; 2.01 A; A=1266-1447.
DR PDB; 2H41; NMR; -; A=721-809.
DR PDB; 2H45; NMR; -; A=721-809.
DR PDB; 2HA1; NMR; -; A=609-809.
DR PDB; 2MNU; NMR; -; A=907-995.
DR PDB; 2N1K; NMR; -; A=808-905.
DR PDB; 2OCF; X-ray; 2.95 A; D=1539-1631.
DR PDB; 2RKY; X-ray; 1.80 A; A/C=183-275.
DR PDB; 2RKZ; X-ray; 2.00 A; A/B/C/D/E/F=93-182.
DR PDB; 2RL0; X-ray; 2.00 A; A/B/D/F/I/K=184-272.
DR PDB; 3CAL; X-ray; 1.70 A; A/C=93-182.
DR PDB; 3EJH; X-ray; 2.10 A; A/B=516-608.
DR PDB; 3GXE; X-ray; 2.60 A; A/B=516-608.
DR PDB; 3M7P; X-ray; 2.50 A; A=297-604.
DR PDB; 3MQL; X-ray; 3.00 A; A=308-515.
DR PDB; 3R8Q; X-ray; 2.40 A; A=1812-2082.
DR PDB; 3T1W; X-ray; 2.40 A; A=1173-1539.
DR PDB; 3ZRZ; X-ray; 1.70 A; A/B=93-182.
DR PDB; 4GH7; X-ray; 2.60 A; B/D=1173-1447.
DR PDB; 4JE4; X-ray; 2.31 A; B=1539-1631.
DR PDB; 4JEG; X-ray; 2.30 A; B=1539-1631.
DR PDB; 4LXO; X-ray; 1.42 A; A/B=1448-1631.
DR PDB; 4MMX; X-ray; 3.32 A; C=1539-1631.
DR PDB; 4MMY; X-ray; 3.18 A; C=1539-1631.
DR PDB; 4MMZ; X-ray; 3.10 A; C=1539-1629.
DR PDB; 4PZ5; X-ray; 1.96 A; A=93-182.
DR PDB; 5DC0; X-ray; 2.23 A; A=1540-1631.
DR PDB; 5DC4; X-ray; 1.48 A; B=1539-1631.
DR PDB; 5DC9; X-ray; 1.56 A; B=1537-1631.
DR PDB; 5DFT; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1638-1726.
DR PDB; 5J6Z; NMR; -; A=806-834, B=631-705.
DR PDB; 5J7C; X-ray; 2.54 A; C/D=1540-1631.
DR PDB; 5M0A; NMR; -; A=2199-2284.
DR PDB; 5N47; X-ray; 3.00 A; B=1267-1448, D/F=1173-1448.
DR PDB; 5N48; X-ray; 1.60 A; B/D=907-995.
DR PDB; 6HNF; NMR; -; A=1995-2082.
DR PDB; 6MFA; X-ray; 1.75 A; A=903-1268.
DR PDB; 6MSV; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1085-1173.
DR PDB; 6NAJ; X-ray; 3.10 A; C=1539-1629.
DR PDB; 6XAX; X-ray; 2.40 A; A/B=1630-1903.
DR PDB; 6XAY; X-ray; 2.48 A; A/B/C/D=1538-1903.
DR PDB; 7NWL; EM; 3.10 A; C=1173-1631.
DR PDBsum; 1E88; -.
DR PDBsum; 1E8B; -.
DR PDBsum; 1FBR; -.
DR PDBsum; 1FNA; -.
DR PDBsum; 1FNF; -.
DR PDBsum; 1FNH; -.
DR PDBsum; 1J8K; -.
DR PDBsum; 1O9A; -.
DR PDBsum; 1OWW; -.
DR PDBsum; 1Q38; -.
DR PDBsum; 1QGB; -.
DR PDBsum; 1QO6; -.
DR PDBsum; 1TTF; -.
DR PDBsum; 1TTG; -.
DR PDBsum; 2CG6; -.
DR PDBsum; 2CG7; -.
DR PDBsum; 2CK2; -.
DR PDBsum; 2CKU; -.
DR PDBsum; 2EC3; -.
DR PDBsum; 2FN2; -.
DR PDBsum; 2FNB; -.
DR PDBsum; 2GEE; -.
DR PDBsum; 2H41; -.
DR PDBsum; 2H45; -.
DR PDBsum; 2HA1; -.
DR PDBsum; 2MNU; -.
DR PDBsum; 2N1K; -.
DR PDBsum; 2OCF; -.
DR PDBsum; 2RKY; -.
DR PDBsum; 2RKZ; -.
DR PDBsum; 2RL0; -.
DR PDBsum; 3CAL; -.
DR PDBsum; 3EJH; -.
DR PDBsum; 3GXE; -.
DR PDBsum; 3M7P; -.
DR PDBsum; 3MQL; -.
DR PDBsum; 3R8Q; -.
DR PDBsum; 3T1W; -.
DR PDBsum; 3ZRZ; -.
DR PDBsum; 4GH7; -.
DR PDBsum; 4JE4; -.
DR PDBsum; 4JEG; -.
DR PDBsum; 4LXO; -.
DR PDBsum; 4MMX; -.
DR PDBsum; 4MMY; -.
DR PDBsum; 4MMZ; -.
DR PDBsum; 4PZ5; -.
DR PDBsum; 5DC0; -.
DR PDBsum; 5DC4; -.
DR PDBsum; 5DC9; -.
DR PDBsum; 5DFT; -.
DR PDBsum; 5J6Z; -.
DR PDBsum; 5J7C; -.
DR PDBsum; 5M0A; -.
DR PDBsum; 5N47; -.
DR PDBsum; 5N48; -.
DR PDBsum; 6HNF; -.
DR PDBsum; 6MFA; -.
DR PDBsum; 6MSV; -.
DR PDBsum; 6NAJ; -.
DR PDBsum; 6XAX; -.
DR PDBsum; 6XAY; -.
DR PDBsum; 7NWL; -.
DR AlphaFoldDB; P02751; -.
DR SMR; P02751; -.
DR BioGRID; 108621; 797.
DR ComplexPortal; CPX-6232; Fibronectin complex.
DR CORUM; P02751; -.
DR DIP; DIP-29547N; -.
DR ELM; P02751; -.
DR IntAct; P02751; 541.
DR MINT; P02751; -.
DR STRING; 9606.ENSP00000346839; -.
DR ChEMBL; CHEMBL3810; -.
DR DrugBank; DB06245; Lanoteplase.
DR DrugBank; DB08888; Ocriplasmin.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR CarbonylDB; P02751; -.
DR GlyConnect; 161; 100 N-Linked glycans (6 sites).
DR GlyGen; P02751; 24 sites, 131 N-linked glycans (8 sites), 5 O-linked glycans (11 sites).
DR iPTMnet; P02751; -.
DR MetOSite; P02751; -.
DR PhosphoSitePlus; P02751; -.
DR SwissPalm; P02751; -.
DR BioMuta; FN1; -.
DR DMDM; 300669710; -.
DR DOSAC-COBS-2DPAGE; P02751; -.
DR CPTAC; non-CPTAC-1122; -.
DR CPTAC; non-CPTAC-2666; -.
DR EPD; P02751; -.
DR jPOST; P02751; -.
DR MassIVE; P02751; -.
DR MaxQB; P02751; -.
DR PeptideAtlas; P02751; -.
DR PRIDE; P02751; -.
DR ProteomicsDB; 19829; -.
DR ProteomicsDB; 20230; -.
DR ProteomicsDB; 51567; -. [P02751-1]
DR ProteomicsDB; 51568; -. [P02751-10]
DR ProteomicsDB; 51569; -. [P02751-11]
DR ProteomicsDB; 51570; -. [P02751-12]
DR ProteomicsDB; 51571; -. [P02751-13]
DR ProteomicsDB; 51572; -. [P02751-14]
DR ProteomicsDB; 51573; -. [P02751-15]
DR ProteomicsDB; 51574; -. [P02751-2]
DR ProteomicsDB; 51575; -. [P02751-3]
DR ProteomicsDB; 51576; -. [P02751-4]
DR ProteomicsDB; 51577; -. [P02751-5]
DR ProteomicsDB; 51578; -. [P02751-6]
DR ProteomicsDB; 51579; -. [P02751-7]
DR ProteomicsDB; 51580; -. [P02751-8]
DR ProteomicsDB; 51581; -. [P02751-9]
DR ABCD; P02751; 17 sequenced antibodies.
DR Antibodypedia; 3522; 2765 antibodies from 49 providers.
DR DNASU; 2335; -.
DR Ensembl; ENST00000323926.10; ENSP00000323534.6; ENSG00000115414.21. [P02751-7]
DR Ensembl; ENST00000336916.8; ENSP00000338200.4; ENSG00000115414.21. [P02751-3]
DR Ensembl; ENST00000354785.11; ENSP00000346839.4; ENSG00000115414.21. [P02751-15]
DR Ensembl; ENST00000356005.8; ENSP00000348285.4; ENSG00000115414.21. [P02751-8]
DR Ensembl; ENST00000357867.8; ENSP00000350534.4; ENSG00000115414.21. [P02751-10]
DR Ensembl; ENST00000359671.5; ENSP00000352696.1; ENSG00000115414.21. [P02751-1]
DR Ensembl; ENST00000421182.5; ENSP00000394423.1; ENSG00000115414.21. [P02751-9]
DR Ensembl; ENST00000426059.1; ENSP00000398907.1; ENSG00000115414.21. [P02751-16]
DR Ensembl; ENST00000432072.6; ENSP00000399538.2; ENSG00000115414.21. [P02751-13]
DR Ensembl; ENST00000443816.5; ENSP00000415018.1; ENSG00000115414.21. [P02751-14]
DR Ensembl; ENST00000446046.5; ENSP00000410422.1; ENSG00000115414.21. [P02751-17]
DR GeneID; 2335; -.
DR KEGG; hsa:2335; -.
DR MANE-Select; ENST00000354785.11; ENSP00000346839.4; NM_212482.4; NP_997647.2.
DR UCSC; uc002vfa.4; human. [P02751-15]
DR CTD; 2335; -.
DR DisGeNET; 2335; -.
DR GeneCards; FN1; -.
DR GeneReviews; FN1; -.
DR HGNC; HGNC:3778; FN1.
DR HPA; ENSG00000115414; Tissue enhanced (liver, placenta).
DR MalaCards; FN1; -.
DR MIM; 135600; gene.
DR MIM; 184255; phenotype.
DR MIM; 601894; phenotype.
DR neXtProt; NX_P02751; -.
DR OpenTargets; ENSG00000115414; -.
DR Orphanet; 84090; Fibronectin glomerulopathy.
DR Orphanet; 93315; Spondylometaphyseal dysplasia, 'corner fracture' type.
DR PharmGKB; PA28194; -.
DR VEuPathDB; HostDB:ENSG00000115414; -.
DR GeneTree; ENSGT00940000155126; -.
DR HOGENOM; CLU_000916_0_0_1; -.
DR InParanoid; P02751; -.
DR OMA; TTNPPMG; -.
DR OrthoDB; 6580at2759; -.
DR PhylomeDB; P02751; -.
DR TreeFam; TF329915; -.
DR PathwayCommons; P02751; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1474244; Extracellular matrix organization.
DR Reactome; R-HSA-1566977; Fibronectin matrix formation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR Reactome; R-HSA-9700645; ALK mutants bind TKIs.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR SignaLink; P02751; -.
DR SIGNOR; P02751; -.
DR BioGRID-ORCS; 2335; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; FN1; human.
DR EvolutionaryTrace; P02751; -.
DR GeneWiki; Fibronectin; -.
DR GenomeRNAi; 2335; -.
DR Pharos; P02751; Tchem.
DR PRO; PR:P02751; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P02751; protein.
DR Bgee; ENSG00000115414; Expressed in synovial joint and 200 other tissues.
DR ExpressionAtlas; P02751; baseline and differential.
DR Genevisible; P02751; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0005577; C:fibrinogen complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0051087; F:chaperone binding; IPI:CAFA.
DR GO; GO:0005518; F:collagen binding; NAS:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
DR GO; GO:0043394; F:proteoglycan binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IDA:CAFA.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007044; P:cell-substrate junction assembly; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0150102; P:negative regulation of monocyte activation; IDA:UniProtKB.
DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IDA:MGI.
DR GO; GO:0018149; P:peptide cross-linking; IDA:BHF-UCL.
DR GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; NAS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL.
DR CDD; cd00061; FN1; 12.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 17.
DR Gene3D; 2.10.10.10; -; 2.
DR Gene3D; 2.60.40.10; -; 17.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013806; Kringle-like.
DR Pfam; PF00039; fn1; 12.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 17.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 17.
DR SUPFAM; SSF49265; SSF49265; 11.
DR SUPFAM; SSF57440; SSF57440; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01253; FN1_1; 12.
DR PROSITE; PS51091; FN1_2; 12.
DR PROSITE; PS00023; FN2_1; 2.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 16.
PE 1: Evidence at protein level;
KW 3D-structure; Acute phase; Alternative splicing; Angiogenesis;
KW Cell adhesion; Cell shape; Direct protein sequencing; Disease variant;
KW Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Isopeptide bond; Oxidation; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:6630202"
FT CHAIN 32..2477
FT /note="Fibronectin"
FT /id="PRO_0000019235"
FT CHAIN 627..702
FT /note="Anastellin"
FT /id="PRO_0000390479"
FT CHAIN 723..911
FT /note="Ugl-Y1"
FT /evidence="ECO:0000269|PubMed:3584091,
FT ECO:0000303|PubMed:17614963"
FT /id="PRO_0000300249"
FT CHAIN 723..903
FT /note="Ugl-Y2"
FT /id="PRO_0000300250"
FT CHAIN 723..?
FT /note="Ugl-Y3"
FT /id="PRO_0000300251"
FT DOMAIN 50..90
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 95..138
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 139..182
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 184..228
FT /note="Fibronectin type-I 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 229..273
FT /note="Fibronectin type-I 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 306..345
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 355..403
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 415..463
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 468..511
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 516..558
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 559..602
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 610..702
FT /note="Fibronectin type-III 1"
FT DOMAIN 722..812
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 813..904
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 909..998
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 999..1088
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1089..1175
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1176..1270
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1271..1359
FT /note="Fibronectin type-III 8; extra domain B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1360..1452
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1453..1540
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1541..1634
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1635..1726
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1727..1814
FT /note="Fibronectin type-III 13; extra domain A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1815..1908
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1909..1995
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1996..2086
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2194..2288
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2295..2339
FT /note="Fibronectin type-I 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2340..2382
FT /note="Fibronectin type-I 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2384..2427
FT /note="Fibronectin type-I 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND 907..1172
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..272
FT /note="Fibrin- and heparin-binding 1"
FT /evidence="ECO:0000269|PubMed:7989369"
FT REGION 123..142
FT /note="Required for binding to LILRB4"
FT /evidence="ECO:0000269|PubMed:34089617"
FT REGION 308..608
FT /note="Collagen-binding"
FT REGION 464..477
FT /note="Critical for collagen binding"
FT REGION 1358..1631
FT /note="Cell-attachment"
FT REGION 1660..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..2082
FT /note="Heparin-binding 2"
FT REGION 1904..2082
FT /note="Binds to FBLN1"
FT REGION 2083..2202
FT /note="V region (type III connecting segment, IIICS)"
FT REGION 2149..2169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2297..2428
FT /note="Fibrin-binding 2"
FT MOTIF 1615..1617
FT /note="Cell attachment site"
FT SITE 663
FT /note="Important for superfibronectin formation"
FT SITE 666
FT /note="Important for superfibronectin formation"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:6630202"
FT MOD_RES 876
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 881
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2454
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2475
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 279
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:16037490"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11285216,
FT ECO:0000269|PubMed:16037490, ECO:0000269|PubMed:16335952"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16037490, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16037490,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16037490,
FT ECO:0000269|PubMed:17614963"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16037490,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 1244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16037490,
FT ECO:0000269|PubMed:16335952"
FT CARBOHYD 2199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16037490"
FT DISULFID 52..78
FT /evidence="ECO:0000269|PubMed:12736686"
FT DISULFID 76..87
FT /evidence="ECO:0000269|PubMed:12736686"
FT DISULFID 97..125
FT /evidence="ECO:0000269|PubMed:12736686,
FT ECO:0000269|PubMed:17368672"
FT DISULFID 123..135
FT /evidence="ECO:0000269|PubMed:17368672"
FT DISULFID 141..169
FT /evidence="ECO:0000269|PubMed:17368672"
FT DISULFID 167..179
FT /evidence="ECO:0000269|PubMed:17368672"
FT DISULFID 186..215
FT /evidence="ECO:0000269|PubMed:8308892"
FT DISULFID 213..225
FT /evidence="ECO:0000269|PubMed:8308892"
FT DISULFID 231..260
FT /evidence="ECO:0000269|PubMed:8308892"
FT DISULFID 258..270
FT /evidence="ECO:0000269|PubMed:8308892"
FT DISULFID 308..335
FT /evidence="ECO:0000269|PubMed:11285216"
FT DISULFID 333..342
FT /evidence="ECO:0000269|PubMed:11285216"
FT DISULFID 360..386
FT /evidence="ECO:0000269|PubMed:11285216"
FT DISULFID 374..401
FT /evidence="ECO:0000269|PubMed:11285216"
FT DISULFID 420..446
FT /evidence="ECO:0000269|PubMed:11285216"
FT DISULFID 434..461
FT /evidence="ECO:0000269|PubMed:11285216"
FT DISULFID 470..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 496..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 518..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 543..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 561..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 587..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2297..2326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2324..2336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2342..2369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2367..2379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2386..2410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2408..2424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2458
FT /note="Interchain (with C-2462)"
FT DISULFID 2462
FT /note="Interchain (with C-2458)"
FT CROSSLNK 34
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 35
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 47
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT VAR_SEQ 368..386
FT /note="GRTFYSCTTEGRQDGHLWC -> DRTD (in isoform 2)"
FT /id="VSP_060343"
FT VAR_SEQ 648..657
FT /note="KNSVGRWKEA -> VSIPPRNLGY (in isoform 2 and isoform
FT 16)"
FT /id="VSP_060344"
FT VAR_SEQ 658..2477
FT /note="Missing (in isoform 2 and isoform 16)"
FT /id="VSP_060345"
FT VAR_SEQ 1256..1578
FT /note="Missing (in isoform 12)"
FT /id="VSP_060346"
FT VAR_SEQ 1266..1356
FT /note="Missing (in isoform 1, isoform 3, isoform 4, isoform
FT 5, isoform 6, isoform 8, isoform 9, isoform 10, isoform 14
FT and isoform 17)"
FT /id="VSP_060347"
FT VAR_SEQ 1367..1457
FT /note="Missing (in isoform 11)"
FT /id="VSP_060348"
FT VAR_SEQ 1722..1813
FT /note="NIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDG
FT EEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAI -> TI (in isoform
FT 8, isoform 9, isoform 10, isoform 12, isoform 13 and
FT isoform 14)"
FT /id="VSP_060349"
FT VAR_SEQ 2081..2284
FT /note="KTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSG
FT QQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYP
FT HGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATL
FT TGLTRGATYNVIVEALKDQQRHKVREEVVTVGNS -> KT (in isoform 6)"
FT /id="VSP_060350"
FT VAR_SEQ 2081..2201
FT /note="KTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSG
FT QQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYP
FT HGPGLNPNAS -> K (in isoform 4, isoform 5, isoform 10 and
FT isoform 13)"
FT /id="VSP_060351"
FT VAR_SEQ 2081..2106
FT /note="KTDELPQLVTLPHPNLHGPEILDVPS -> K (in isoform 9,
FT isoform 12 and isoform 17)"
FT /id="VSP_060352"
FT VAR_SEQ 2173..2203
FT /note="Missing (in isoform 3, isoform 7, isoform 9, isoform
FT 12, isoform 14 and isoform 17)"
FT /id="VSP_060353"
FT VAR_SEQ 2239..2242
FT /note="FRVP -> STKA (in isoform 4)"
FT /id="VSP_060354"
FT VAR_SEQ 2243..2477
FT /note="Missing (in isoform 4)"
FT /id="VSP_060355"
FT VAR_SEQ 2285..2339
FT /note="Missing (in isoform 5)"
FT /id="VSP_060356"
FT VARIANT 15
FT /note="Q -> L (in dbSNP:rs1250259)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:18268355,
FT ECO:0000269|PubMed:3031656, ECO:0000269|Ref.4"
FT /id="VAR_043917"
FT VARIANT 87
FT /note="C -> F (in SMDCF; the mutant is not secreted;
FT dbSNP:rs1553669703)"
FT /evidence="ECO:0000269|PubMed:29100092"
FT /id="VAR_080523"
FT VARIANT 123
FT /note="C -> R (in SMDCF; dbSNP:rs1553667072)"
FT /evidence="ECO:0000269|PubMed:29100092"
FT /id="VAR_080524"
FT VARIANT 225
FT /note="C -> W (in SMDCF; dbSNP:rs1181638652)"
FT /evidence="ECO:0000269|PubMed:29100092"
FT /id="VAR_080525"
FT VARIANT 240
FT /note="Y -> D (in SMDCF; the mutant is not secreted;
FT dbSNP:rs1553659131)"
FT /evidence="ECO:0000269|PubMed:29100092"
FT /id="VAR_080526"
FT VARIANT 260
FT /note="C -> G (in SMDCF; the mutant is not secreted;
FT dbSNP:rs1553658926)"
FT /evidence="ECO:0000269|PubMed:29100092"
FT /id="VAR_080527"
FT VARIANT 809
FT /note="Missing (in SMDCF; unknown pathological
FT significance; dbSNP:rs1553636502)"
FT /evidence="ECO:0000269|PubMed:29100092"
FT /id="VAR_080528"
FT VARIANT 817
FT /note="T -> P (in dbSNP:rs2577301)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16106752, ECO:0000269|PubMed:17614963,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:2992939,
FT ECO:0000269|Ref.4"
FT /id="VAR_059529"
FT VARIANT 940
FT /note="D -> N (in a breast cancer sample; somatic mutation;
FT dbSNP:rs752106647)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036018"
FT VARIANT 973
FT /note="Y -> C (in GFND2; dbSNP:rs137854488)"
FT /evidence="ECO:0000269|PubMed:18268355"
FT /id="VAR_043918"
FT VARIANT 1120
FT /note="R -> P (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036019"
FT VARIANT 1558
FT /note="S -> R (in dbSNP:rs11687611)"
FT /id="VAR_056576"
FT VARIANT 1925
FT /note="W -> R (in GFND2; reduced binding to heparin,
FT endothelial cells and podocytes; impaired capability to
FT induce stress-fiber formation; dbSNP:rs137854486)"
FT /evidence="ECO:0000269|PubMed:18268355"
FT /id="VAR_043919"
FT VARIANT 1974
FT /note="L -> R (in GFND2; reduced binding to heparin,
FT endothelial cells and podocytes; impaired capability to
FT induce stress-fiber formation; dbSNP:rs137854487)"
FT /evidence="ECO:0000269|PubMed:18268355"
FT /id="VAR_043920"
FT VARIANT 2051
FT /note="I -> V (in dbSNP:rs1250209)"
FT /evidence="ECO:0000269|PubMed:18268355"
FT /id="VAR_043921"
FT VARIANT 2212
FT /note="I -> V (in dbSNP:rs17449032)"
FT /id="VAR_056577"
FT VARIANT 2261
FT /note="V -> I (in dbSNP:rs1250209)"
FT /evidence="ECO:0000269|PubMed:12127832,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16106752,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:2012601,
FT ECO:0000269|PubMed:2992573, ECO:0000269|PubMed:2992939,
FT ECO:0000269|PubMed:4019516, ECO:0000269|PubMed:6462919,
FT ECO:0000269|Ref.4, ECO:0007744|PubMed:21269460"
FT /id="VAR_061486"
FT VARIANT 2471
FT /note="D -> N (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1373375768)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036020"
FT MUTAGEN 641
FT /note="Y->A: Severely compromised ability to form
FT fibronectin aggregates; when associated with A-681 and A-
FT 683."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 642
FT /note="I->A: Little effect on ability to form fibronectin
FT aggregates; when associated with A-682; A-684 and A-692."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 663
FT /note="L->A: No effect on secondary structure nor on
FT fibronectin binding nor on activation of p38 K but
FT abolishes polymerization activity; when associated with A-
FT 666."
FT /evidence="ECO:0000269|PubMed:12946358,
FT ECO:0000269|PubMed:19379667"
FT MUTAGEN 666
FT /note="Y->A: No effect on secondary structure nor on
FT fibronectin binding nor on activation of p38 kinase but
FT abolishes polymerization activity; when associated with A-
FT 663."
FT /evidence="ECO:0000269|PubMed:12946358,
FT ECO:0000269|PubMed:19379667"
FT MUTAGEN 681
FT /note="L->A: Severely compromised ability to form
FT fibronectin aggregates; when associated with A-641 and A-
FT 683."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 682
FT /note="I->A: Little effect on ability to form fibronectin
FT aggregates; when associated with A-642; A-684 and A-692."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 683
FT /note="S->A: Severely compromised ability to form
FT fibronectin aggregates; when associated with A-641 and A-
FT 681."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 684
FT /note="I->A: Little effect on ability to form fibronectin
FT aggregates; when associated with A-642; A-682 and A-692."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 691
FT /note="E->A: Slightly enhanced ability to form fibronectin
FT aggregates; when associated with A-694 and A-696."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 692
FT /note="V->A: Little effect on ability to form fibronectin
FT aggregates; when associated with A-642; A-682 and A-684."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 694
FT /note="R->A: Slightly enhanced ability to form fibronectin
FT aggregates; when associated with A-691 and A-696."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 695
FT /note="F->A: Loss of ability to form fibronectin
FT aggregates; when associated with A-697."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 696
FT /note="D->A: Slightly enhanced ability to form fibronectin
FT aggregates; when associated with A-691 and A-694."
FT /evidence="ECO:0000269|PubMed:12946358"
FT MUTAGEN 697
FT /note="F->A: Loss of ability to form fibronectin
FT aggregates; when associated with A-695."
FT /evidence="ECO:0000269|PubMed:12946358"
FT CONFLICT 32
FT /note="Q -> R (in Ref. 5; CAH18171)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> C (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="C -> S (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="Y -> N (in Ref. 5; CAH18172)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> V (in Ref. 11; CAA26536)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="I -> V (in Ref. 5; CAH18136)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="E -> G (in Ref. 5; CAD91166)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="S -> R (in Ref. 1; CAD59389 and 2; CAH60958)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="C -> R (in Ref. 5; CAH18172)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="V -> A (in Ref. 5; CAE45847)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="S -> L (in Ref. 11; CAA26536 and 13; AAD00015)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="G -> E (in Ref. 5; CAD97984)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="T -> A (in Ref. 5; CAH18136)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="R -> Q (in Ref. 11; CAA26536 and 13; AAD00015)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="C -> R (in Ref. 5; CAD97791)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="R -> K (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="V -> A (in Ref. 5; CAH18172)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="E -> Q (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 704..705
FT /note="TP -> PT (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="V -> L (in Ref. 5; CAD97791)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="T -> A (in Ref. 5; CAH18136)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048
FT /note="V -> D (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="D -> G (in Ref. 5; CAH18136)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="S -> N (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1152
FT /note="T -> I (in Ref. 5; CAH18136)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="E -> G (in Ref. 5; CAD97791)"
FT /evidence="ECO:0000305"
FT CONFLICT 1226
FT /note="H -> Q (in Ref. 5; CAE45932)"
FT /evidence="ECO:0000305"
FT CONFLICT 1646
FT /note="D -> G (in Ref. 5; CAE45714)"
FT /evidence="ECO:0000305"
FT CONFLICT 1692
FT /note="G -> S (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1713
FT /note="Q -> E (in Ref. 27; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1806..1812
FT /note="IGTQSTA -> VQTAVTT (in Ref. 29; AAA52463)"
FT /evidence="ECO:0000305"
FT CONFLICT 1817
FT /note="T -> A (in Ref. 5; CAE45847)"
FT /evidence="ECO:0000305"
FT CONFLICT 1846
FT /note="R -> W (in Ref. 5; CAH18136)"
FT /evidence="ECO:0000305"
FT CONFLICT 1859
FT /note="I -> V (in Ref. 19; CAB52436)"
FT /evidence="ECO:0000305"
FT CONFLICT 1874
FT /note="M -> T (in Ref. 5; CAE45932)"
FT /evidence="ECO:0000305"
FT CONFLICT 2018
FT /note="R -> C (in Ref. 13; AAD00014)"
FT /evidence="ECO:0000305"
FT CONFLICT 2025
FT /note="I -> V (in Ref. 5; CAH18172)"
FT /evidence="ECO:0000305"
FT CONFLICT 2083
FT /note="D -> G (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 2114
FT /note="V -> A (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 2118
FT /note="G -> R (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 2342
FT /note="C -> R (in Ref. 5; CAH18172)"
FT /evidence="ECO:0000305"
FT CONFLICT 2403
FT /note="Y -> N (in Ref. 5; CAD97965/CAD97964)"
FT /evidence="ECO:0000305"
FT CONFLICT 2432
FT /note="S -> T (in Ref. 5; CAE45714/CAH18171/CAH18172/
FT CAE45958)"
FT /evidence="ECO:0000305"
FT CONFLICT 2458
FT /note="C -> Y (in Ref. 5; CAE45932)"
FT /evidence="ECO:0000305"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1QGB"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1QGB"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1O9A"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1O9A"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1QGB"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1O9A"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2CG7"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:2CG7"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:2CG7"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2CG7"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:2RKY"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2RKY"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:2RKY"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:2RKY"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:2RKY"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3M7P"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:1E88"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:3M7P"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:1E88"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:3M7P"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:3M7P"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:1E8B"
FT TURN 413..417
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:2FN2"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:3M7P"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:3M7P"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:3MQL"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:3M7P"
FT TURN 501..504
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 505..513
FT /evidence="ECO:0007829|PDB:3M7P"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 540..547
FT /evidence="ECO:0007829|PDB:3EJH"
FT TURN 548..551
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:3EJH"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 585..591
FT /evidence="ECO:0007829|PDB:3EJH"
FT TURN 592..595
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 596..601
FT /evidence="ECO:0007829|PDB:3EJH"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:1OWW"
FT STRAND 626..631
FT /evidence="ECO:0007829|PDB:1OWW"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:1OWW"
FT STRAND 638..647
FT /evidence="ECO:0007829|PDB:1OWW"
FT TURN 648..651
FT /evidence="ECO:0007829|PDB:1Q38"
FT STRAND 655..659
FT /evidence="ECO:0007829|PDB:1OWW"
FT STRAND 661..664
FT /evidence="ECO:0007829|PDB:1Q38"
FT STRAND 665..668
FT /evidence="ECO:0007829|PDB:1OWW"
FT STRAND 673..688
FT /evidence="ECO:0007829|PDB:1OWW"
FT STRAND 690..699
FT /evidence="ECO:0007829|PDB:1OWW"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:2H41"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:2H41"
FT STRAND 747..756
FT /evidence="ECO:0007829|PDB:2H41"
FT TURN 757..759
FT /evidence="ECO:0007829|PDB:2H41"
FT STRAND 764..769
FT /evidence="ECO:0007829|PDB:2H41"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:2H41"
FT STRAND 785..794
FT /evidence="ECO:0007829|PDB:2H41"
FT STRAND 799..808
FT /evidence="ECO:0007829|PDB:2H41"
FT STRAND 818..822
FT /evidence="ECO:0007829|PDB:2N1K"
FT STRAND 824..830
FT /evidence="ECO:0007829|PDB:2N1K"
FT STRAND 839..847
FT /evidence="ECO:0007829|PDB:2N1K"
FT STRAND 854..859
FT /evidence="ECO:0007829|PDB:2N1K"
FT STRAND 864..869
FT /evidence="ECO:0007829|PDB:2N1K"
FT STRAND 875..883
FT /evidence="ECO:0007829|PDB:2N1K"
FT STRAND 892..897
FT /evidence="ECO:0007829|PDB:2N1K"
FT STRAND 911..918
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 923..928
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 936..945
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 947..949
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 951..958
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 960..964
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 972..981
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 989..994
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1001..1007
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1013..1018
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1025..1033
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1040..1044
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1049..1053
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1061..1070
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1078..1083
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1094..1098
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1103..1107
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1113..1121
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1129..1140
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1148..1157
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1166..1171
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1178..1184
FT /evidence="ECO:0007829|PDB:6MFA"
FT TURN 1186..1188
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1191..1196
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1199..1202
FT /evidence="ECO:0007829|PDB:7NWL"
FT STRAND 1205..1212
FT /evidence="ECO:0007829|PDB:6MFA"
FT TURN 1213..1215
FT /evidence="ECO:0007829|PDB:1FNF"
FT STRAND 1221..1225
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1230..1234
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1239..1241
FT /evidence="ECO:0007829|PDB:5N47"
FT STRAND 1243..1251
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1259..1263
FT /evidence="ECO:0007829|PDB:6MFA"
FT STRAND 1274..1277
FT /evidence="ECO:0007829|PDB:5N48"
FT STRAND 1280..1286
FT /evidence="ECO:0007829|PDB:5N48"
FT STRAND 1291..1294
FT /evidence="ECO:0007829|PDB:2GEE"
FT STRAND 1295..1304
FT /evidence="ECO:0007829|PDB:5N48"
FT TURN 1305..1308
FT /evidence="ECO:0007829|PDB:4GH7"
FT STRAND 1311..1317
FT /evidence="ECO:0007829|PDB:5N48"
FT STRAND 1322..1327
FT /evidence="ECO:0007829|PDB:5N48"
FT STRAND 1333..1342
FT /evidence="ECO:0007829|PDB:5N48"
FT STRAND 1350..1355
FT /evidence="ECO:0007829|PDB:5N48"
FT STRAND 1362..1368
FT /evidence="ECO:0007829|PDB:1FNF"
FT STRAND 1374..1379
FT /evidence="ECO:0007829|PDB:1FNF"
FT STRAND 1387..1395
FT /evidence="ECO:0007829|PDB:1FNF"
FT HELIX 1396..1398
FT /evidence="ECO:0007829|PDB:3T1W"
FT HELIX 1399..1401
FT /evidence="ECO:0007829|PDB:2GEE"
FT STRAND 1403..1407
FT /evidence="ECO:0007829|PDB:1FNF"
FT STRAND 1413..1416
FT /evidence="ECO:0007829|PDB:1FNF"
FT STRAND 1424..1433
FT /evidence="ECO:0007829|PDB:1FNF"
FT STRAND 1441..1446
FT /evidence="ECO:0007829|PDB:1FNF"
FT STRAND 1453..1459
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1465..1470
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1477..1485
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1493..1497
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1503..1506
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1514..1523
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1531..1536
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1543..1551
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1554..1560
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1567..1575
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1578..1580
FT /evidence="ECO:0007829|PDB:5DC9"
FT STRAND 1583..1588
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1593..1596
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1604..1613
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1616..1618
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1625..1630
FT /evidence="ECO:0007829|PDB:4LXO"
FT STRAND 1637..1644
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1649..1654
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1661..1674
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1677..1681
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1687..1690
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1698..1706
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1715..1720
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1727..1733
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1739..1744
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1751..1759
FT /evidence="ECO:0007829|PDB:6XAX"
FT TURN 1760..1762
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1763..1766
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1772..1774
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1777..1780
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1788..1797
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1805..1810
FT /evidence="ECO:0007829|PDB:6XAX"
FT STRAND 1817..1824
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1829..1834
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1842..1854
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1857..1861
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1867..1870
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1878..1887
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1895..1900
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1909..1916
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1921..1926
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1934..1944
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1948..1952
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1957..1961
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1969..1978
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1986..1991
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 1998..2006
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 2009..2015
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 2023..2029
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 2033..2037
FT /evidence="ECO:0007829|PDB:6HNF"
FT STRAND 2048..2051
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 2059..2068
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 2076..2081
FT /evidence="ECO:0007829|PDB:3R8Q"
FT STRAND 2206..2213
FT /evidence="ECO:0007829|PDB:5M0A"
FT STRAND 2221..2232
FT /evidence="ECO:0007829|PDB:5M0A"
FT STRAND 2237..2242
FT /evidence="ECO:0007829|PDB:5M0A"
FT STRAND 2247..2254
FT /evidence="ECO:0007829|PDB:5M0A"
FT STRAND 2257..2267
FT /evidence="ECO:0007829|PDB:5M0A"
FT STRAND 2270..2280
FT /evidence="ECO:0007829|PDB:5M0A"
FT STRAND 2344..2346
FT /evidence="ECO:0007829|PDB:2EC3"
FT STRAND 2354..2358
FT /evidence="ECO:0007829|PDB:2EC3"
FT STRAND 2360..2371
FT /evidence="ECO:0007829|PDB:2EC3"
FT TURN 2372..2375
FT /evidence="ECO:0007829|PDB:2EC3"
FT STRAND 2376..2381
FT /evidence="ECO:0007829|PDB:2EC3"
SQ SEQUENCE 2477 AA; 272320 MW; 6C436A7A5FEE6DEB CRC64;
MLRGPGPGLL LLAVQCLGTA VPSTGASKSK RQAQQMVQPQ SPVAVSQSKP GCYDNGKHYQ
INQQWERTYL GNALVCTCYG GSRGFNCESK PEAEETCFDK YTGNTYRVGD TYERPKDSMI
WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL GNGKGEWTCK
PIAEKCFDHA AGTSYVVGET WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY
RIGDTWSKKD NRGNLLQCIC TGNGRGEWKC ERHTSVQTTS SGSGPFTDVR AAVYQPQPHP
QPPPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHTVLVQT RGGNSNGALC
HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI
GDQWDKQHDM GHMMRCTCVG NGRGEWTCIA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
LNCTCFGQGR GRWKCDPVDQ CQDSETGTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
PLQTYPSSSG PVEVFITETP SQPNSHPIQW NAPQPSHISK YILRWRPKNS VGRWKEATIP
GHLNSYTIKG LKPGVVYEGQ LISIQQYGHQ EVTRFDFTTT STSTPVTSNT VTGETTPFSP
LVATSESVTE ITASSFVVSW VSASDTVSGF RVEYELSEEG DEPQYLDLPS TATSVNIPDL
LPGRKYIVNV YQISEDGEQS LILSTSQTTA PDAPPDTTVD QVDDTSIVVR WSRPQAPITG
YRIVYSPSVE GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVVIQQETTG
TPRSDTVPSP RDLQFVEVTD VKVTIMWTPP ESAVTGYRVD VIPVNLPGEH GQRLPISRNT
FAEVTGLSPG VTYYFKVFAV SHGRESKPLT AQQTTKLDAP TNLQFVNETD STVLVRWTPP
RAQITGYRLT VGLTRRGQPR QYNVGPSVSK YPLRNLQPAS EYTVSLVAIK GNQESPKATG
VFTTLQPGSS IPPYNTEVTE TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV
SGLTPGVEYV YTIQVLRDGQ ERDAPIVNKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
PDITGYRITT TPTNGQQGNS LEEVVHADQS SCTFDNLSPG LEYNVSVYTV KDDKESVPIS
DTIIPEVPQL TDLSFVDITD SSIGLRWTPL NSSTIIGYRI TVVAAGEGIP IFEDFVDSSV
GYYTVTGLEP GIDYDISVIT LINGGESAPT TLTQQTAVPP PTDLRFTNIG PDTMRVTWAP
PPSIDLTNFL VRYSPVKNEE DVAELSISPS DNAVVLTNLL PGTEYVVSVS SVYEQHESTP
LRGRQKTGLD SPTGIDFSDI TANSFTVHWI APRATITGYR IRHHPEHFSG RPREDRVPHS
RNSITLTNLT PGTEYVVSIV ALNGREESPL LIGQQSTVSD VPRDLEVVAA TPTSLLISWD
APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK PGVDYTITVY AVTGRGDSPA
SSKPISINYR TEIDKPSQMQ VTDVQDNSIS VKWLPSSSPV TGYRVTTTPK NGPGPTKTKT
AGPDQTEMTI EGLQPTVEYV VSVYAQNPSG ESQPLVQTAV TNIDRPKGLA FTDVDVDSIK
IAWESPQGQV SRYRVTYSSP EDGIHELFPA PDGEEDTAEL QGLRPGSEYT VSVVALHDDM
ESQPLIGTQS TAIPAPTDLK FTQVTPTSLS AQWTPPNVQL TGYRVRVTPK EKTGPMKEIN
LAPDSSSVVV SGLMVATKYE VSVYALKDTL TSRPAQGVVT TLENVSPPRR ARVTDATETT
ITISWRTKTE TITGFQVDAV PANGQTPIQR TIKPDVRSYT ITGLQPGTDY KIYLYTLNDN
ARSSPVVIDA STAIDAPSNL RFLATTPNSL LVSWQPPRAR ITGYIIKYEK PGSPPREVVP
RPRPGVTEAT ITGLEPGTEY TIYVIALKNN QKSEPLIGRK KTDELPQLVT LPHPNLHGPE
ILDVPSTVQK TPFVTHPGYD TGNGIQLPGT SGQQPSVGQQ MIFEEHGFRR TTPPTTATPI
RHRPRPYPPN VGEEIQIGHI PREDVDYHLY PHGPGLNPNA STGQEALSQT TISWAPFQDT
SEYIISCHPV GTDEEPLQFR VPGTSTSATL TGLTRGATYN VIVEALKDQQ RHKVREEVVT
VGNSVNEGLN QPTDDSCFDP YTVSHYAVGD EWERMSESGF KLLCQCLGFG SGHFRCDSSR
WCHDNGVNYK IGEKWDRQGE NGQMMSCTCL GNGKGEFKCD PHEATCYDDG KTYHVGEQWQ
KEYLGAICSC TCFGGQRGWR CDNCRRPGGE PSPEGTTGQS YNQYSQRYHQ RTNTNVNCPI
ECFMPLDVQA DREDSRE
