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 27-MAR-2024, entry version 280. 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; DOI=10.1158/0008-5472.148.65.1; 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 -!- FUNCTION: Secreted by contracting muscle, induces liver autophagy, a CC degradative pathway for nutrient mobilization and damage removal, and CC systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin CC receptor signaling. {ECO:0000250|UniProtKB:P11276}. 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. Interacts with SVEP1 (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P11276, 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; Q9NY15: STAB1; NbExp=2; IntAct=EBI-1220319, EBI-2797815; 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}. Secreted CC {ECO:0000250|UniProtKB:P11276}. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 CCDS; CCDS92940.1; -. [P02751-1] 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 EMDB; EMD-12634; -. DR SMR; P02751; -. DR BioGRID; 108621; 807. DR ComplexPortal; CPX-6232; Fibronectin complex. DR CORUM; P02751; -. DR DIP; DIP-29547N; -. DR ELM; P02751; -. DR IntAct; P02751; 544. DR MINT; P02751; -. DR STRING; 9606.ENSP00000346839; -. DR BindingDB; P02751; -. 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 GlyCosmos; P02751; 20 sites, 130 glycans. DR GlyGen; P02751; 30 sites, 132 N-linked glycans (8 sites), 7 O-linked glycans (18 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 PaxDb; 9606-ENSP00000346839; -. DR PeptideAtlas; 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 Pumba; P02751; -. DR ABCD; P02751; 17 sequenced antibodies. DR Antibodypedia; 3522; 3120 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 AGR; HGNC:3778; -. 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; VHWLAPQ; -. DR OrthoDB; 5399734at2759; -. 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; 11 hits in 1162 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 202 other cell types or tissues. DR ExpressionAtlas; P02751; baseline and differential. 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:0005518; F:collagen binding; NAS:UniProtKB. 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: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: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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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 GO; GO:0042060; P:wound healing; IEA:Ensembl. DR CDD; cd00061; FN1; 12. DR CDD; cd00062; FN2; 2. DR CDD; cd00063; FN3; 17. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 12. DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR46708:SF8; FIBRONECTIN; 1. DR PANTHER; PTHR46708; TENASCIN; 1. DR Pfam; PF00039; fn1; 11. DR Pfam; PF00040; fn2; 2. DR Pfam; PF00041; fn3; 17. DR PRINTS; PR00013; FNTYPEII. DR SMART; SM00058; FN1; 12. DR SMART; SM00059; FN2; 2. DR SMART; SM00060; FN3; 17. DR SUPFAM; SSF49265; Fibronectin type III; 11. DR SUPFAM; SSF57603; FnI-like domain; 12. DR SUPFAM; SSF57440; Kringle-like; 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; 17. DR Genevisible; P02751; HS. 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; uncertain significance; FT 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 FT A-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 FT A-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 FT A-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 FT A-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 FT A-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; FT CAE45714/CAH18171/CAH18172/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 //