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Fibronectin (FN) (Cold-insoluble globulin) (CIG) [Cleaved into: Anastellin; Ugl-Y1; Ugl-Y2; Ugl-Y3]

 FINC_HUMAN              Reviewed;        2386 AA.
P02751; B7ZLF0; E9PE77; E9PG29; O95609; O95610; Q14312; Q14325;
Q14326; Q17RV7; Q564H7; Q585T2; Q59EH1; Q60FE4; Q68DP8; Q68DP9;
Q68DT4; Q6LDP6; Q6MZS0; Q6MZU5; Q6N025; Q6N0A6; Q7Z391; Q86T27;
Q8IVI8; Q96KP7; Q96KP8; Q96KP9; Q9H1B8; Q9HAP3; Q9UMK2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 4.
25-OCT-2017, entry version 235.
RecName: Full=Fibronectin;
Short=FN;
AltName: Full=Cold-insoluble globulin;
Short=CIG;
Contains:
RecName: Full=Anastellin;
Contains:
RecName: Full=Ugl-Y1;
Contains:
RecName: Full=Ugl-Y2;
Contains:
RecName: Full=Ugl-Y3;
Flags: Precursor;
Name=FN1; Synonyms=FN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS PRO-817 AND
ILE-2170.
PubMed=11737888; DOI=10.1186/bcr325;
Schor S.L., Schor A.M.;
"Phenotypic and genetic alterations in mammary stroma: implications
for tumour progression.";
Breast Cancer Res. 3:373-379(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 16).
PubMed=16322219; DOI=10.1158/0008-5472.CAN-05-2038;
Kay R.A., Ellis I.R., Jones S.J., Perrier S., Florence M.M.,
Schor A.M., Schor S.L.;
"The expression of migration stimulating factor, a potent oncofetal
cytokine, is uniquely controlled by 3'-untranslated region-dependent
nuclear sequestration of its precursor messenger RNA.";
Cancer Res. 65:10742-10749(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), AND VARIANTS PRO-817 AND
ILE-2170.
TISSUE=Retinal pigment epithelium;
PubMed=16106752; DOI=10.1093/dnares/12.1.53;
Kato S., Ohtoko K., Ohtake H., Kimura T.;
"Vector-capping: a simple method for preparing a high-quality full-
length cDNA library.";
DNA Res. 12:53-62(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 14), AND VARIANTS
LEU-15; PRO-817 AND ILE-2170.
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 7; 8; 9; 10; 13;
14; 15 AND 16), AND VARIANTS LEU-15; PRO-817 AND ILE-2170.
TISSUE=Amygdala, Cervix, Endometrial tumor, and Uterine endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), AND VARIANTS
LEU-15; PRO-817 AND ILE-2170.
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-38.
PubMed=3770189; DOI=10.1016/0014-5793(86)80029-1;
Gutman A., Yamada K.M., Kornblihtt A.R.;
"Human fibronectin is synthesized as a pre-propolypeptide.";
FEBS Lett. 207:145-148(1986).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, AND VARIANT LEU-15.
PubMed=3031656; DOI=10.1073/pnas.84.7.1876;
Dean D.C., Bowlus C.L., Bourgeois S.;
"Cloning and analysis of the promotor region of the human fibronectin
gene.";
Proc. Natl. Acad. Sci. U.S.A. 84:1876-1880(1987).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-2386 (ISOFORM 3), AND VARIANTS
PRO-817 AND ILE-2170.
PubMed=2992939;
Kornblihtt A.R., Umezawa K., Vibe-Pedersen K., Baralle F.E.;
"Primary structure of human fibronectin: differential splicing may
generate at least 10 polypeptides from a single gene.";
EMBO J. 4:1755-1759(1985).
[12]
PROTEIN SEQUENCE OF 32-290, AND PYROGLUTAMATE FORMATION AT GLN-32.
PubMed=6630202;
Garcia-Pardo A., Pearlstein E., Frangione B.;
"Primary structure of human plasma fibronectin. The 29,000-dalton NH2-
terminal domain.";
J. Biol. Chem. 258:12670-12674(1983).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 103-481 (ISOFORMS
1/3/4/5/6/7/8/9/10/11/12/13/14/15), NUCLEOTIDE SEQUENCE [MRNA] OF
1116-1422 (ISOFORMS 1/3/4/5/6/8/9/10/14), NUCLEOTIDE SEQUENCE [MRNA]
OF 1238-2160 (ISOFORMS 9 AND 12), NUCLEOTIDE SEQUENCE [MRNA] OF
1449-1825 (ISOFORMS 8/9/10/13/14), NUCLEOTIDE SEQUENCE [MRNA] OF
1919-2161 (ISOFORMS 3/7/14), AND NUCLEOTIDE SEQUENCE [MRNA] OF
2228-2386 (ISOFORMS 1/3/6/7/8/9/10/11/12/13/14/15).
TISSUE=Peripheral blood T-cell, and Umbilical vein endothelial cell;
Godfrey H.P., Ebrahim A.A.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[14]
PROTEIN SEQUENCE OF 291-302, AND BINDING TO M.BOVIS ANTIGEN 85B
(FBPB).
PubMed=8406884;
Peake P., Gooley A., Britton W.J.;
"Mechanism of interaction of the 85B secreted protein of Mycobacterium
bovis with fibronectin.";
Infect. Immun. 61:4828-4834(1993).
[15]
PROTEIN SEQUENCE OF 309-608, AND COLLAGEN-BINDING.
PubMed=3024962;
Owens R.J., Baralle F.E.;
"Mapping the collagen-binding site of human fibronectin by expression
in Escherichia coli.";
EMBO J. 5:2825-2830(1986).
[16]
PROTEIN SEQUENCE OF 616-705.
PubMed=3900070;
Calaycay J., Pande H., Lee T., Borsi L., Siri A., Shively J.E.,
Zardi L.;
"Primary structure of a DNA- and heparin-binding domain (Domain III)
in human plasma fibronectin.";
J. Biol. Chem. 260:12136-12141(1985).
[17]
PROTEIN SEQUENCE OF 723-911, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
GLYCOSYLATION AT ASN-877, AND VARIANT PRO-817.
TISSUE=Urine;
PubMed=17614963; DOI=10.1111/j.1742-4658.2007.05926.x;
Iida R., Yasuda T., Kishi K.;
"Identification of novel fibronectin fragments detected specifically
in juvenile urine.";
FEBS J. 274:3939-3947(2007).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 973-2386 (ISOFORM 3), AND VARIANT
ILE-2170.
PubMed=6462919; DOI=10.1093/nar/12.14.5853;
Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.;
"Human fibronectin: cell specific alternative mRNA splicing generates
polypeptide chains differing in the number of internal repeats.";
Nucleic Acids Res. 12:5853-5868(1984).
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1232-1782 (ISOFORMS 7/15).
PubMed=3375063; DOI=10.1093/nar/16.8.3545;
Paolella G., Henchcliffe C., Sebastio G., Baralle F.E.;
"Sequence analysis and in vivo expression show that alternative
splicing of ED-B and ED-A regions of the human fibronectin gene are
independent events.";
Nucleic Acids Res. 16:3545-3557(1988).
[20]
PROTEIN SEQUENCE OF 1234-1286 (ISOFORM 7).
PubMed=2822387;
Zardi L., Carnemolla B., Siri A., Petersen T.E., Paolella G.,
Sebastio G., Baralle F.E.;
"Transformed human cells produce a new fibronectin isoform by
preferential alternative splicing of a previously unobserved exon.";
EMBO J. 6:2337-2342(1987).
[21]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1257-1365 (ISOFORM 11).
PubMed=3478690; DOI=10.1073/pnas.84.20.7179;
Gutman A., Kornblihtt A.R.;
"Identification of a third region of cell-specific alternative
splicing in human fibronectin mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 84:7179-7182(1987).
[22]
PROTEIN SEQUENCE OF 1441-1548.
PubMed=7050098;
Pierschbacher M.D., Ruoslahti E., Sundelin J., Lind P., Peterson P.A.;
"The cell attachment domain of fibronectin. Determination of the
primary structure.";
J. Biol. Chem. 257:9593-9597(1982).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 1448-1540.
PubMed=6688418;
Oldberg A., Linney E., Ruoslahti E.;
"Molecular cloning and nucleotide sequence of a cDNA clone coding for
the cell attachment domain in human fibronectin.";
J. Biol. Chem. 258:10193-10196(1983).
[24]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1448-1540.
PubMed=3003095;
Oldberg A., Ruoslahti E.;
"Evolution of the fibronectin gene. Exon structure of cell attachment
domain.";
J. Biol. Chem. 261:2113-2116(1986).
[25]
PROTEIN SEQUENCE OF 1589-2058.
PubMed=3593230; DOI=10.1042/bj2410923;
Garcia-Pardo A., Rostagno A., Frangione B.;
"Primary structure of human plasma fibronectin. Characterization of a
38 kDa domain containing the C-terminal heparin-binding site (Hep III
site) and a region of molecular heterogeneity.";
Biochem. J. 241:923-928(1987).
[26]
NUCLEOTIDE SEQUENCE [MRNA] OF 1594-2386 (ISOFORMS 1/11/15), AND
VARIANT ILE-2170.
PubMed=2992573; DOI=10.1021/bi00332a016;
Bernard M.P., Kolbe M., Weil D., Chu M.-L.;
"Human cellular fibronectin: comparison of the carboxyl-terminal
portion with rat identifies primary structural domains separated by
hypervariable regions.";
Biochemistry 24:2698-2704(1985).
[27]
PROTEIN SEQUENCE OF 1614-1623; 1730-1748; 1756-1759; 1803-1811;
1860-1923; 1930-1945; 1949-1972; 1982-1989; 1991-2003; 2020-2038;
2060-2131; 2150-2180; 2185-2205 AND 2231-2242, GLYCOSYLATION AT
THR-2064 AND THR-2065, LACK OF GLYCOSYLATION AT ASN-2108, VARIANT
ILE-2170, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=2012601; DOI=10.1042/bj2740731;
Tressel T., McCarthy J.B., Calaycay J., Lee T.D., Legesse K.,
Shively J.E., Pande H.;
"Human plasma fibronectin. Demonstration of structural differences
between the A- and B-chains in the III CS region.";
Biochem. J. 274:731-738(1991).
[28]
NUCLEOTIDE SEQUENCE [MRNA] OF 1624-1727 (ISOFORMS 8/9/10/12/13/14).
PubMed=6200322;
Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.;
"Human fibronectin: molecular cloning evidence for two mRNA species
differing by an internal segment coding for a structural domain.";
EMBO J. 3:221-226(1984).
[29]
NUCLEOTIDE SEQUENCE [MRNA] OF 1712-1739 (ISOFORMS 1/3/4/5/6/7/11/15).
PubMed=3021206; DOI=10.1021/bi00365a032;
Sekiguchi K., Klos A.M., Kurachi K., Yoshitake S., Hakomori S.;
"Human liver fibronectin complementary DNAs: identification of two
different messenger RNAs possibly encoding the alpha and beta subunits
of plasma fibronectin.";
Biochemistry 25:4936-4941(1986).
[30]
NUCLEOTIDE SEQUENCE [MRNA] OF 1788-2386 (ISOFORMS 4; 5 AND 6), AND
VARIANT ILE-2170.
TISSUE=Cartilage;
PubMed=12127832; DOI=10.1053/joca.2002.0792;
Parker A.E., Boutell J., Carr A., Maciewicz R.A.;
"Novel cartilage-specific splice variants of fibronectin.";
Osteoarthritis Cartilage 10:528-534(2002).
[31]
NUCLEOTIDE SEQUENCE [MRNA] OF 1948-2067 (ISOFORMS 1/8/10/11/15).
PubMed=2989004; DOI=10.1016/0014-5793(85)81333-8;
Umezawa K., Kornblihtt A.R., Baralle F.E.;
"Isolation and characterization of cDNA clones for human liver
fibronectin.";
FEBS Lett. 186:31-34(1985).
[32]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1992-2147.
PubMed=3770201; DOI=10.1016/0014-5793(86)81506-X;
Vibe-Pedersen K., Magnusson S., Baralle F.E.;
"Donor and acceptor splice signals within an exon of the human
fibronectin gene: a new type of differential splicing.";
FEBS Lett. 207:287-291(1986).
[33]
PROTEIN SEQUENCE OF 2071-2356 (ISOFORM 3), AND VARIANT ILE-2170.
PubMed=4019516;
Garcia-Pardo A., Pearlstein E., Frangione B.;
"Primary structure of human plasma fibronectin. Characterization of a
31,000-dalton fragment from the COOH-terminal region containing a free
sulfhydryl group and a fibrin-binding site.";
J. Biol. Chem. 260:10320-10325(1985).
[34]
NUCLEOTIDE SEQUENCE [MRNA] OF 2291-2386.
PubMed=6304699; DOI=10.1073/pnas.80.11.3218;
Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.;
"Isolation and characterization of cDNA clones for human and bovine
fibronectins.";
Proc. Natl. Acad. Sci. U.S.A. 80:3218-3222(1983).
[35]
SULFATION.
PubMed=2414772; DOI=10.1073/pnas.82.21.7160;
Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.;
"Tyrosine sulfation of proteins from the human hepatoma cell line
HepG2.";
Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985).
[36]
IDENTIFICATION OF UGL-Y1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
GLYCOSYLATION.
PubMed=3584091; DOI=10.1093/oxfordjournals.jbchem.a121920;
Iida R., Yasuda T., Kishi K.;
"Purification of a young age-related glycoprotein (Ugl-Y) from normal
human urine.";
J. Biochem. 101:357-363(1987).
[37]
INTERACTION WITH FBLN1.
PubMed=1400330;
Balbona K., Tran H., Godyna S., Ingham K.C., Strickland D.K.,
Argraves W.S.;
"Fibulin binds to itself and to the carboxyl-terminal heparin-binding
region of fibronectin.";
J. Biol. Chem. 267:20120-20125(1992).
[38]
CHARACTERIZATION OF FIBRIN-BINDING SITE 1.
PubMed=7989369;
Rostagno A., Williams M.J., Baron M., Campbell I.D., Gold L.I.;
"Further characterization of the NH2-terminal fibrin-binding site on
fibronectin.";
J. Biol. Chem. 269:31938-31945(1994).
[39]
SUBUNIT, AND FUNCTION OF ANASTELLIN.
PubMed=8114919; DOI=10.1038/367193a0;
Morla A., Zhang Z., Ruoslahti E.;
"Superfibronectin is a functionally distinct form of fibronectin.";
Nature 367:193-196(1994).
[40]
INTERACTION WITH LGALS3BP.
PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
Sasaki T., Brakebusch C., Engel J., Timpl R.;
"Mac-2 binding protein is a cell-adhesive protein of the extracellular
matrix which self-assembles into ring-like structures and binds beta1
integrins, collagens and fibronectin.";
EMBO J. 17:1606-1613(1998).
[41]
FUNCTION OF ANASTELLIN.
PubMed=11209058; DOI=10.1073/pnas.98.2.620;
Yi M., Ruoslahti E.;
"A fibronectin fragment inhibits tumor growth, angiogenesis, and
metastasis.";
Proc. Natl. Acad. Sci. U.S.A. 98:620-624(2001).
[42]
INTERACTION WITH COL13A1.
PubMed=11956183; DOI=10.1074/jbc.M107583200;
Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R.,
Pihlajaniemi T.;
"The type XIII collagen ectodomain is a 150-nm rod and capable of
binding to fibronectin, nidogen-2, perlecan, and heparin.";
J. Biol. Chem. 277:23092-23099(2002).
[43]
INTERACTION WITH COMP.
PubMed=12225811; DOI=10.1016/S0945-053X(02)00015-X;
Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P.,
Perris R., Fang C.;
"Matrix-matrix interaction of cartilage oligomeric matrix protein and
fibronectin.";
Matrix Biol. 21:461-470(2002).
[44]
INTERACTION WITH MYOC.
PubMed=11773026;
Filla M.S., Liu X., Nguyen T.D., Polansky J.R., Brandt C.R.,
Kaufman P.L., Peters D.M.;
"In vitro localization of TIGR/MYOC in trabecular meshwork
extracellular matrix and binding to fibronectin.";
Invest. Ophthalmol. Vis. Sci. 43:151-161(2002).
[45]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[46]
FUNCTION OF ANASTELLIN.
PubMed=15665290;
Ambesi A., Klein R.M., Pumiglia K.M., McKeown-Longo P.J.;
"Anastellin, a fragment of the first type III repeat of fibronectin,
inhibits extracellular signal-regulated kinase and causes G(1) arrest
in human microvessel endothelial cells.";
Cancer Res. 65:148-156(2005).
[47]
GLYCOSYLATION AT THR-279; ASN-430; ASN-528; ASN-542; ASN-877;
ASN-1007; ASN-1244 AND ASN-2108.
PubMed=16037490; DOI=10.1093/glycob/cwj019;
Tajiri M., Yoshida S., Wada Y.;
"Differential analysis of site-specific glycans on plasma and cellular
fibronectins: application of a hydrophilic affinity method for
glycopeptide enrichment.";
Glycobiology 15:1332-1340(2005).
[48]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-430; ASN-528; ASN-542;
ASN-1007 AND ASN-1244.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2384, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[50]
INTERACTION WITH FST3.
PubMed=16336961; DOI=10.1016/j.yexcr.2005.11.006;
Maguer-Satta V., Forissier S., Bartholin L., Martel S., Jeanpierre S.,
Bachelard E., Rimokh R.;
"A novel role for fibronectin type I domain in the regulation of human
hematopoietic cell adhesiveness through binding to follistatin domains
of FLRG and follistatin.";
Exp. Cell Res. 312:434-442(2006).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2384, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[52]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-1007.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[53]
GLYCOSYLATION AT ASN-528; ASN-542 AND ASN-1007.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[54]
FUNCTION OF ANASTELLIN, AND MUTAGENESIS OF LEU-663 AND TYR-666.
PubMed=19379667; DOI=10.1016/j.matbio.2009.01.003;
You R., Klein R.M., Zheng M., McKeown-Longo P.J.;
"Regulation of p38 MAP kinase by anastellin is independent of
anastellin's effect on matrix fibronectin.";
Matrix Biol. 28:101-109(2009).
[55]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2363 AND SER-2384, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[57]
PHOSPHORYLATION AT SER-2384.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[58]
STRUCTURE BY NMR OF 1447-1540.
PubMed=1311202; DOI=10.1021/bi00122a025;
Baron M., Main A.L., Driscoll P.C., Mardon H.J., Boyd J.,
Campbell I.D.;
"1H NMR assignment and secondary structure of the cell adhesion type
III module of fibronectin.";
Biochemistry 31:2068-2073(1992).
[59]
STRUCTURE BY NMR OF 1447-1540.
PubMed=1423622; DOI=10.1016/0092-8674(92)90600-H;
Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D.;
"The three-dimensional structure of the tenth type III module of
fibronectin: an insight into RGD-mediated interactions.";
Cell 71:671-678(1992).
[60]
STRUCTURE BY NMR OF 183-275, AND DISULFIDE BONDS.
PubMed=8308892; DOI=10.1006/jmbi.1994.1083;
Williams M.J., Phan I., Harvey T.S., Rostagno A., Gold L.I.,
Campbell I.D.;
"Solution structure of a pair of fibronectin type 1 modules with
fibrin binding activity.";
J. Mol. Biol. 235:1302-1311(1994).
[61]
STRUCTURE BY NMR OF 32-92.
PubMed=7583666; DOI=10.1038/nsb1195-946;
Potts J.R., Phan I., Williams M.J., Campbell I.D.;
"High-resolution structural studies of the factor XIIIa crosslinking
site and the first type 1 module of fibronectin.";
Nat. Struct. Biol. 2:946-950(1995).
[62]
STRUCTURE BY NMR OF 406-464.
PubMed=9514732; DOI=10.1006/jmbi.1997.1528;
Sticht H., Pickford A.R., Potts J.R., Campbell I.D.;
"Solution structure of the glycosylated second type 2 module of
fibronectin.";
J. Mol. Biol. 276:177-187(1998).
[63]
STRUCTURE BY NMR OF EXTRA ED-B DOMAIN FROM ISOFORM 7.
PubMed=10196121; DOI=10.1016/S0969-2126(99)80051-3;
Fattorusso R., Pellecchia M., Viti F., Neri P., Neri D., Wuethrich K.;
"NMR structure of the human oncofoetal fibronectin ED-B domain, a
specific marker for angiogenesis.";
Structure 7:381-390(1999).
[64]
STRUCTURE BY NMR OF 305-405.
PubMed=10647176; DOI=10.1016/S0969-2126(00)88336-7;
Bocquier A.A., Potts J.R., Pickford A.R., Campbell I.D.;
"Solution structure of a pair of modules from the gelatin-binding
domain of fibronectin.";
Structure 7:1451-1460(1999).
[65]
STRUCTURE BY NMR OF 305-464, AND GLYCOSYLATION AT ASN-430.
PubMed=11285216; DOI=10.1093/emboj/20.7.1519;
Pickford A.R., Smith S.P., Staunton D., Boyd J., Campbell I.D.;
"The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human
fibronectin enhances gelatin binding.";
EMBO J. 20:1519-1529(2001).
[66]
STRUCTURE BY NMR OF 1631-1724.
PubMed=11775745; DOI=10.1023/A:1012947209393;
Niimi T., Osawa M., Yamaji N., Yasunaga K., Sakashita H., Mase T.,
Tanaka A., Fujita S.;
"NMR structure of human fibronectin EDA.";
J. Biomol. NMR 21:281-284(2001).
[67]
STRUCTURE BY NMR OF 631-705, AND MUTAGENESIS OF TYR-641; ILE-642;
LEU-663; TYR-666; LEU-681; ILE-682; SER-683; ILE-684; GLU-691;
VAL-692; ARG-694; PHE-695; ASP-696 AND PHE-697.
PubMed=12946358; DOI=10.1016/S0022-2836(03)00890-8;
Briknarova K., Aakerman M.E., Hoyt D.W., Ruoslahti E., Ely K.R.;
"Anastellin, an FN3 fragment with fibronectin polymerization activity,
resembles amyloid fibril precursors.";
J. Mol. Biol. 332:205-215(2003).
[68]
STRUCTURE BY NMR OF 48-140 IN COMPLEX WITH A STAPHYLOCOCCUS
FIBRONECTIN-BINDING PROTEIN.
PubMed=12736686; DOI=10.1038/nature01589;
Schwarz-Linek U., Werner J.M., Pickford A.R., Gurusiddappa S.,
Kim J.H., Pilka E.S., Briggs J.A., Gough T.S., Hoeoek M.,
Campbell I.D., Potts J.R.;
"Pathogenic bacteria attach to human fibronectin through a tandem
beta-zipper.";
Nature 423:177-181(2003).
[69]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1447-1535.
PubMed=8120888; DOI=10.1016/0022-2836(94)90013-2;
Dickinson C.D., Veerapandian B., Dai X.-P., Hamlin R.C., Xuong N.-H.,
Ruoslahti E., Ely K.R.;
"Crystal structure of the tenth type III cell adhesion module of human
fibronectin.";
J. Mol. Biol. 236:1079-1092(1994).
[70]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1173-1540.
PubMed=8548820; DOI=10.1016/S0092-8674(00)81002-8;
Leahy D.J., Aukhil I., Erickson H.P.;
"2.0 A crystal structure of a four-domain segment of human fibronectin
encompassing the RGD loop and synergy region.";
Cell 84:155-164(1996).
[71]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1721-1991.
PubMed=10075919; DOI=10.1093/emboj/18.6.1468;
Sharma A., Askari J.A., Humphries M.J., Jones E.Y., Stuart D.I.;
"Crystal structure of a heparin- and integrin-binding segment of human
fibronectin.";
EMBO J. 18:1468-1479(1999).
[72]
STRUCTURE BY NMR OF 608-701.
PubMed=14657397; DOI=10.1073/pnas.2334390100;
Gao M., Craig D., Lequin O., Campbell I.D., Vogel V., Schulten K.;
"Structure and functional significance of mechanically unfolded
fibronectin type III1 intermediates.";
Proc. Natl. Acad. Sci. U.S.A. 100:14784-14789(2003).
[73]
STRUCTURE BY NMR OF 609-809.
PubMed=17464288; DOI=10.1038/sj.emboj.7601694;
Vakonakis I., Staunton D., Rooney L.M., Campbell I.D.;
"Interdomain association in fibronectin: insight into cryptic sites
and fibrillogenesis.";
EMBO J. 26:2575-2583(2007).
[74]
STRUCTURE BY NMR OF 93-182, X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF
93-182, AND DISULFIDE BONDS.
PubMed=17368672; DOI=10.1016/j.jmb.2007.02.061;
Rudino-Pinera E., Ravelli R.B., Sheldrick G.M., Nanao M.H.,
Korostelev V.V., Werner J.M., Schwarz-Linek U., Potts J.R.,
Garman E.F.;
"The solution and crystal structures of a module pair from the
Staphylococcus aureus-binding site of human fibronectin -- a tale with
a twist.";
J. Mol. Biol. 368:833-844(2007).
[75]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 93-275 IN COMPLEX WITH
STAPHYLOCOCCUS AUREUS FNBA.
PubMed=18713862; DOI=10.1073/pnas.0803556105;
Bingham R.J., Rudino-Pinera E., Meenan N.A.G., Schwarz-Linek U.,
Turkenburg J.P., Hoeoek M., Garman E.F., Potts J.R.;
"Crystal structures of fibronectin-binding sites from Staphylococcus
aureus FnBPA in complex with fibronectin domains.";
Proc. Natl. Acad. Sci. U.S.A. 105:12254-12258(2008).
[76]
STRUCTURE BY NMR OF 2239-2299.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the 11th FN1 domain from human fibronectin 1.";
Submitted (MAR-2008) to the PDB data bank.
[77]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 516-608 IN COMPLEX WITH TYPE
I COLLAGEN.
PubMed=19251642; DOI=10.1073/pnas.0812516106;
Erat M.C., Slatter D.A., Lowe E.D., Millard C.J., Farndale R.W.,
Campbell I.D., Vakonakis I.;
"Identification and structural analysis of type I collagen sites in
complex with fibronectin fragments.";
Proc. Natl. Acad. Sci. U.S.A. 106:4195-4200(2009).
[78]
VARIANTS [LARGE SCALE ANALYSIS] ASN-940; PRO-1120 AND ASN-2380.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[79]
VARIANTS GFND2 CYS-973; ARG-1834 AND ARG-1883, VARIANTS LEU-15 AND
VAL-1960, AND CHARACTERIZATION OF VARIANTS GFND2 ARG-1834 AND
ARG-1883.
PubMed=18268355; DOI=10.1073/pnas.0707730105;
Castelletti F., Donadelli R., Banterla F., Hildebrandt F.,
Zipfel P.F., Bresin E., Otto E., Skerka C., Renieri A., Todeschini M.,
Caprioli J., Caruso R.M., Artuso R., Remuzzi G., Noris M.;
"Mutations in FN1 cause glomerulopathy with fibronectin deposits.";
Proc. Natl. Acad. Sci. U.S.A. 105:2538-2543(2008).
[80]
VARIANT [LARGE SCALE ANALYSIS] ILE-2170, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Fibronectins bind cell surfaces and various compounds
including collagen, fibrin, heparin, DNA, and actin. Fibronectins
are involved in cell adhesion, cell motility, opsonization, wound
healing, and maintenance of cell shape. Involved in osteoblast
compaction through the fibronectin fibrillogenesis cell-mediated
matrix assembly process, essential for osteoblast mineralization.
Participates in the regulation of type I collagen deposition by
osteoblasts.
-!- FUNCTION: Anastellin binds fibronectin and induces fibril
formation. This fibronectin polymer, named superfibronectin,
exhibits enhanced adhesive properties. Both anastellin and
superfibronectin inhibit tumor growth, angiogenesis and
metastasis. Anastellin activates p38 MAPK and inhibits
lysophospholipid signaling.
-!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
variants, connected by 2 disulfide bonds near the carboxyl ends;
to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR,
LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity).
Interacts with COMP (PubMed:12225811). Interacts with TNR; the
interaction inhibits cell adhesion and neurite outgrowth (By
similarity). Interacts with FST3 and MYOC. {ECO:0000250,
ECO:0000269|PubMed:11773026, ECO:0000269|PubMed:11956183,
ECO:0000269|PubMed:12225811, ECO:0000269|PubMed:1400330,
ECO:0000269|PubMed:16336961, ECO:0000269|PubMed:18713862,
ECO:0000269|PubMed:19251642, ECO:0000269|PubMed:8114919,
ECO:0000269|PubMed:9501082}.
-!- SUBUNIT: (Microbial infection) Interacts with S.aureus fnbA
(PubMed:12736686). Interacts with M.bovis fbpB via the collagen-
binding region; also interacts with fibronectin-binding proteins
from other Mycobacteria (PubMed:8406884).
{ECO:0000269|PubMed:12736686, ECO:0000269|PubMed:8406884}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-1220319, EBI-1220319;
Q99IB8:- (xeno); NbExp=3; IntAct=EBI-1220319, EBI-6927928;
P02452:COL1A1; NbExp=2; IntAct=EBI-1220319, EBI-982999;
P29279:CTGF; NbExp=5; IntAct=EBI-1220319, EBI-2835375;
P07585:DCN; NbExp=9; IntAct=EBI-1220319, EBI-9663608;
P35555:FBN1; NbExp=2; IntAct=EBI-1220319, EBI-2505934;
P35556:FBN2; NbExp=2; IntAct=EBI-1220319, EBI-6164392;
P14738:fnbA (xeno); NbExp=20; IntAct=EBI-1220319, EBI-8398157;
Q53682:fnbB (xeno); NbExp=19; IntAct=EBI-1220319, EBI-8398005;
Q93ED6:fne (xeno); NbExp=8; IntAct=EBI-1220319, EBI-9826140;
P06241:FYN; NbExp=2; IntAct=EBI-7133890, EBI-515315;
P75358:gapA (xeno); NbExp=3; IntAct=EBI-1220319, EBI-2259469;
P08519:LPA; NbExp=2; IntAct=EBI-1220319, EBI-9232288;
Q4AAD6:MHJ_0194 (xeno); NbExp=3; IntAct=EBI-1220319, EBI-14034164;
Q601D1:mhp271 (xeno); NbExp=2; IntAct=EBI-1220319, EBI-13948049;
P75392:pdhC (xeno); NbExp=2; IntAct=EBI-1220319, EBI-2259593;
Q9CKF6:PM1665 (xeno); NbExp=5; IntAct=EBI-1220319, EBI-11164515;
P11684:SCGB1A1; NbExp=3; IntAct=EBI-1220319, EBI-7797649;
P21980:TGM2; NbExp=4; IntAct=EBI-1220319, EBI-727668;
P07996:THBS1; NbExp=2; IntAct=EBI-1220319, EBI-2530274;
P98066:TNFAIP6; NbExp=8; IntAct=EBI-1220319, EBI-11700693;
P23568:tuf (xeno); NbExp=2; IntAct=EBI-1220319, EBI-2259072;
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-1220319, EBI-741480;
P40337:VHL; NbExp=2; IntAct=EBI-1220319, EBI-301246;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=17;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=P02751-1; Sequence=Displayed;
Name=2; Synonyms=MSF-FN70, Migration stimulation factor FN70;
IsoId=P02751-2; Sequence=VSP_003255, VSP_003256, VSP_003257;
Name=3; Synonyms=V89;
IsoId=P02751-3; Sequence=VSP_008110;
Name=4; Synonyms=Fibronectin III-15X;
IsoId=P02751-4; Sequence=VSP_008107, VSP_008111, VSP_008112;
Name=5; Synonyms=Fibronectin (V+I-10)-;
IsoId=P02751-5; Sequence=VSP_008107, VSP_008113;
Name=6; Synonyms=Fibronectin (V+III-15)-;
IsoId=P02751-6; Sequence=VSP_008109;
Name=7; Synonyms=Fibronectin containing extra ED-B domain;
IsoId=P02751-7; Sequence=VSP_008104, VSP_008110;
Name=8; Synonyms=Fibronectin not containing EIIIA domain;
IsoId=P02751-8; Sequence=VSP_008106;
Name=9; Synonyms=Fibronectin not containing EIIIA and EIIIB and
uses V64 variant of IIICS region;
IsoId=P02751-9; Sequence=VSP_008106, VSP_008108, VSP_008110;
Name=10;
IsoId=P02751-10; Sequence=VSP_008106, VSP_008107;
Name=11; Synonyms=Fibronectin containing extra type III repeat
(EDII), exon x+2;
IsoId=P02751-11; Sequence=VSP_008105;
Name=12;
IsoId=P02751-12; Sequence=VSP_013681, VSP_008106, VSP_008108,
VSP_008110;
Name=13;
IsoId=P02751-13; Sequence=VSP_008104, VSP_008106, VSP_008107;
Note=No experimental confirmation available.;
Name=14;
IsoId=P02751-14; Sequence=VSP_008106, VSP_008110;
Name=15;
IsoId=P02751-15; Sequence=VSP_008104;
Note=No experimental confirmation available.;
Name=16; Synonyms=Migration stimulation factor, MSF;
IsoId=P02751-16; Sequence=VSP_003256, VSP_003257;
Note=Expressed by fetal and tumor-associated cells.;
Name=17;
IsoId=P02751-17; Sequence=VSP_047310, VSP_047311;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted
by hepatocytes. Cellular FN (dimeric or cross-linked multimeric
forms), made by fibroblasts, epithelial and other cell types, is
deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2
and Ugl-Y3 are found in urine. {ECO:0000269|PubMed:17614963,
ECO:0000269|PubMed:3584091}.
-!- DEVELOPMENTAL STAGE: Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the
urine from 0 to 17 years of age. {ECO:0000269|PubMed:17614963,
ECO:0000269|PubMed:3584091}.
-!- PTM: Sulfated. {ECO:0000269|PubMed:2414772}.
-!- PTM: It is not known whether both or only one of Thr-2064 and Thr-
2065 are/is glycosylated. {ECO:0000269|PubMed:11285216,
ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16037490,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17614963,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2012601, ECO:0000269|PubMed:3584091}.
-!- PTM: Forms covalent cross-links mediated by a transglutaminase,
such as F13A or TGM2, between a glutamine and the epsilon-amino
group of a lysine residue, forming homopolymers and heteropolymers
(e.g. fibrinogen-fibronectin, collagen-fibronectin
heteropolymers).
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
anastellin.
-!- PTM: Some lysine residues are oxidized to allysine by LOXL3,
promoting fibronectin activation and matrix formation.
{ECO:0000250|UniProtKB:P11276}.
-!- DISEASE: Glomerulopathy with fibronectin deposits 2 (GFND2)
[MIM:601894]: Genetically heterogeneous autosomal dominant
disorder characterized clinically by proteinuria, microscopic
hematuria, and hypertension that leads to end-stage renal failure
in the second to fifth decade of life.
{ECO:0000269|PubMed:18268355}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAX76513.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAD93077.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD91166.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD97964.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD97965.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD97984.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAH18136.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Fibronectin entry;
URL="https://en.wikipedia.org/wiki/Fibronectin";
-----------------------------------------------------------------------
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EMBL; AJ276395; CAC20427.1; -; mRNA.
EMBL; AJ535086; CAD59389.1; -; mRNA.
EMBL; AJ849445; CAH60958.1; -; mRNA.
EMBL; AB191261; BAD52437.1; -; mRNA.
EMBL; AB209840; BAD93077.1; ALT_INIT; mRNA.
EMBL; AL832202; CAD91166.1; ALT_INIT; mRNA.
EMBL; BX537590; CAD97791.1; -; mRNA.
EMBL; BX538017; CAD97964.1; ALT_INIT; mRNA.
EMBL; BX538018; CAD97965.1; ALT_INIT; mRNA.
EMBL; BX538045; CAD97984.1; ALT_INIT; mRNA.
EMBL; BX640608; CAE45714.1; -; mRNA.
EMBL; BX640731; CAE45847.1; -; mRNA.
EMBL; BX640875; CAE45932.1; -; mRNA.
EMBL; BX640920; CAE45958.1; -; mRNA.
EMBL; CR749281; CAH18136.1; ALT_INIT; mRNA.
EMBL; CR749316; CAH18171.1; -; mRNA.
EMBL; CR749317; CAH18172.1; -; mRNA.
EMBL; AC012462; AAX76513.1; ALT_SEQ; Genomic_DNA.
EMBL; AC073284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471063; EAW70536.1; -; Genomic_DNA.
EMBL; BC117176; AAI17177.1; -; mRNA.
EMBL; BC143763; AAI43764.1; -; mRNA.
EMBL; M15801; AAA53376.1; -; Genomic_DNA.
EMBL; AF312399; AAG30571.1; -; mRNA.
EMBL; X02761; CAA26536.1; -; mRNA.
EMBL; U41850; AAD00014.1; -; mRNA.
EMBL; U42404; AAD00015.1; -; mRNA.
EMBL; U42592; AAD00017.1; -; mRNA.
EMBL; U42593; AAD00018.1; -; mRNA.
EMBL; U42594; AAD00019.1; -; mRNA.
EMBL; U42455; AAD09448.1; -; mRNA.
EMBL; U42456; AAD09449.1; -; mRNA.
EMBL; U42458; AAD09450.1; -; mRNA.
EMBL; U42457; AAD04751.1; -; mRNA.
EMBL; X07718; CAB52436.1; ALT_TERM; Genomic_DNA.
EMBL; X07717; CAB52437.1; -; Genomic_DNA.
EMBL; M18179; AAA52461.1; -; Genomic_DNA.
EMBL; M18177; AAA52461.1; JOINED; Genomic_DNA.
EMBL; M18178; AAA52461.1; JOINED; Genomic_DNA.
EMBL; M12549; AAA58483.1; -; Genomic_DNA.
EMBL; M10905; AAA52462.1; -; mRNA.
EMBL; M14059; AAA52463.1; -; mRNA.
EMBL; AJ320525; CAC86914.1; -; mRNA.
EMBL; AJ320526; CAC86915.1; -; mRNA.
EMBL; AJ320527; CAC86916.1; -; mRNA.
EMBL; M27589; AAA52465.1; -; mRNA.
EMBL; X04530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS2399.1; -. [P02751-3]
CCDS; CCDS2400.1; -. [P02751-10]
CCDS; CCDS42813.1; -. [P02751-8]
CCDS; CCDS42814.1; -. [P02751-15]
CCDS; CCDS46510.1; -. [P02751-17]
CCDS; CCDS46512.1; -. [P02751-16]
CCDS; CCDS77522.1; -. [P02751-9]
CCDS; CCDS77523.1; -. [P02751-14]
CCDS; CCDS77525.1; -. [P02751-13]
CCDS; CCDS77526.1; -. [P02751-7]
PIR; A26460; FNHU.
PIR; I52394; I52394.
PIR; S00848; S00848.
RefSeq; NP_001293058.1; NM_001306129.1.
RefSeq; NP_001293059.1; NM_001306130.1.
RefSeq; NP_001293060.1; NM_001306131.1.
RefSeq; NP_001293061.1; NM_001306132.1.
RefSeq; NP_002017.1; NM_002026.3.
RefSeq; NP_473375.2; NM_054034.2. [P02751-16]
RefSeq; NP_997639.1; NM_212474.2.
RefSeq; NP_997641.1; NM_212476.2.
RefSeq; NP_997643.1; NM_212478.2.
RefSeq; NP_997647.1; NM_212482.2.
RefSeq; XP_005246463.1; XM_005246406.1. [P02751-1]
UniGene; Hs.203717; -.
PDB; 1E88; NMR; -; A=305-464.
PDB; 1E8B; NMR; -; A=305-464.
PDB; 1FBR; NMR; -; A=183-275.
PDB; 1FNA; X-ray; 1.80 A; A=1452-1542.
PDB; 1FNF; X-ray; 2.00 A; A=1173-1540.
PDB; 1FNH; X-ray; 2.80 A; A=1721-1991.
PDB; 1J8K; NMR; -; A=1631-1724.
PDB; 1O9A; NMR; -; A=48-140.
PDB; 1OWW; NMR; -; A=608-701.
PDB; 1Q38; NMR; -; A=631-705.
PDB; 1QGB; NMR; -; A=48-140.
PDB; 1QO6; NMR; -; A=305-405.
PDB; 1TTF; NMR; -; A=1447-1540.
PDB; 1TTG; NMR; -; A=1447-1540.
PDB; 2CG6; X-ray; 1.55 A; A=93-182.
PDB; 2CG7; X-ray; 1.20 A; A=93-182.
PDB; 2CK2; X-ray; 2.00 A; A/B=1447-1542.
PDB; 2CKU; NMR; -; A=93-182.
PDB; 2EC3; NMR; -; A=2239-2299.
PDB; 2FN2; NMR; -; A=406-464.
PDB; 2FNB; NMR; -; A=1265-1355.
PDB; 2GEE; X-ray; 2.01 A; A=1205-1356.
PDB; 2H41; NMR; -; A=721-809.
PDB; 2H45; NMR; -; A=721-809.
PDB; 2HA1; NMR; -; A=609-809.
PDB; 2MNU; NMR; -; A=907-995.
PDB; 2N1K; NMR; -; A=808-905.
PDB; 2OCF; X-ray; 2.95 A; D=1447-1540.
PDB; 2RKY; X-ray; 1.80 A; A/C=183-275.
PDB; 2RKZ; X-ray; 2.00 A; A/B/C/D/E/F=93-182.
PDB; 2RL0; X-ray; 2.00 A; A/B/D/F/I/K=184-272.
PDB; 3CAL; X-ray; 1.70 A; A/C=93-182.
PDB; 3EJH; X-ray; 2.10 A; A/B=516-608.
PDB; 3GXE; X-ray; 2.60 A; A/B=516-608.
PDB; 3M7P; X-ray; 2.50 A; A=297-604.
PDB; 3MQL; X-ray; 3.00 A; A=308-515.
PDB; 3R8Q; X-ray; 2.40 A; A=1721-1991.
PDB; 3T1W; X-ray; 2.40 A; A=1173-1448.
PDB; 3ZRZ; X-ray; 1.70 A; A/B=93-182.
PDB; 4GH7; X-ray; 2.60 A; B/D=1173-1427.
PDB; 4JE4; X-ray; 2.31 A; B=1450-1540.
PDB; 4JEG; X-ray; 2.30 A; B=1450-1540.
PDB; 4LXO; X-ray; 1.42 A; A/B=1357-1540.
PDB; 4MMX; X-ray; 3.32 A; C=1448-1540.
PDB; 4MMY; X-ray; 3.18 A; C=1448-1540.
PDB; 4MMZ; X-ray; 3.10 A; C=1448-1540.
PDB; 4PZ5; X-ray; 1.96 A; A=93-182.
PDB; 5DC0; X-ray; 2.23 A; A=1447-1540.
PDB; 5DC4; X-ray; 1.48 A; B=1445-1540.
PDB; 5DC9; X-ray; 1.56 A; B=1445-1540.
PDB; 5DFT; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1539-1635.
PDB; 5J6Z; NMR; -; A=806-834, B=631-705.
PDB; 5J7C; X-ray; 2.54 A; C/D=1447-1540.
PDBsum; 1E88; -.
PDBsum; 1E8B; -.
PDBsum; 1FBR; -.
PDBsum; 1FNA; -.
PDBsum; 1FNF; -.
PDBsum; 1FNH; -.
PDBsum; 1J8K; -.
PDBsum; 1O9A; -.
PDBsum; 1OWW; -.
PDBsum; 1Q38; -.
PDBsum; 1QGB; -.
PDBsum; 1QO6; -.
PDBsum; 1TTF; -.
PDBsum; 1TTG; -.
PDBsum; 2CG6; -.
PDBsum; 2CG7; -.
PDBsum; 2CK2; -.
PDBsum; 2CKU; -.
PDBsum; 2EC3; -.
PDBsum; 2FN2; -.
PDBsum; 2FNB; -.
PDBsum; 2GEE; -.
PDBsum; 2H41; -.
PDBsum; 2H45; -.
PDBsum; 2HA1; -.
PDBsum; 2MNU; -.
PDBsum; 2N1K; -.
PDBsum; 2OCF; -.
PDBsum; 2RKY; -.
PDBsum; 2RKZ; -.
PDBsum; 2RL0; -.
PDBsum; 3CAL; -.
PDBsum; 3EJH; -.
PDBsum; 3GXE; -.
PDBsum; 3M7P; -.
PDBsum; 3MQL; -.
PDBsum; 3R8Q; -.
PDBsum; 3T1W; -.
PDBsum; 3ZRZ; -.
PDBsum; 4GH7; -.
PDBsum; 4JE4; -.
PDBsum; 4JEG; -.
PDBsum; 4LXO; -.
PDBsum; 4MMX; -.
PDBsum; 4MMY; -.
PDBsum; 4MMZ; -.
PDBsum; 4PZ5; -.
PDBsum; 5DC0; -.
PDBsum; 5DC4; -.
PDBsum; 5DC9; -.
PDBsum; 5DFT; -.
PDBsum; 5J6Z; -.
PDBsum; 5J7C; -.
ProteinModelPortal; P02751; -.
SMR; P02751; -.
BioGrid; 108621; 739.
CORUM; P02751; -.
DIP; DIP-29547N; -.
ELM; P02751; -.
IntAct; P02751; 502.
MINT; MINT-1779779; -.
BindingDB; P02751; -.
ChEMBL; CHEMBL3810; -.
DrugBank; DB08888; Ocriplasmin.
iPTMnet; P02751; -.
PhosphoSitePlus; P02751; -.
SwissPalm; P02751; -.
UniCarbKB; P02751; -.
BioMuta; FN1; -.
DMDM; 300669710; -.
DOSAC-COBS-2DPAGE; P02751; -.
EPD; P02751; -.
MaxQB; P02751; -.
PeptideAtlas; P02751; -.
PRIDE; P02751; -.
DNASU; 2335; -.
Ensembl; ENST00000323926; ENSP00000323534; ENSG00000115414. [P02751-7]
Ensembl; ENST00000336916; ENSP00000338200; ENSG00000115414. [P02751-3]
Ensembl; ENST00000354785; ENSP00000346839; ENSG00000115414. [P02751-15]
Ensembl; ENST00000356005; ENSP00000348285; ENSG00000115414. [P02751-8]
Ensembl; ENST00000357867; ENSP00000350534; ENSG00000115414. [P02751-10]
Ensembl; ENST00000359671; ENSP00000352696; ENSG00000115414. [P02751-1]
Ensembl; ENST00000421182; ENSP00000394423; ENSG00000115414. [P02751-9]
Ensembl; ENST00000426059; ENSP00000398907; ENSG00000115414. [P02751-16]
Ensembl; ENST00000432072; ENSP00000399538; ENSG00000115414. [P02751-13]
Ensembl; ENST00000443816; ENSP00000415018; ENSG00000115414. [P02751-14]
Ensembl; ENST00000446046; ENSP00000410422; ENSG00000115414. [P02751-17]
GeneID; 2335; -.
KEGG; hsa:2335; -.
UCSC; uc002vfa.4; human. [P02751-1]
CTD; 2335; -.
DisGeNET; 2335; -.
EuPathDB; HostDB:ENSG00000115414.18; -.
GeneCards; FN1; -.
HGNC; HGNC:3778; FN1.
HPA; CAB000126; -.
HPA; HPA027066; -.
MalaCards; FN1; -.
MIM; 135600; gene.
MIM; 601894; phenotype.
neXtProt; NX_P02751; -.
OpenTargets; ENSG00000115414; -.
Orphanet; 84090; Fibronectin glomerulopathy.
PharmGKB; PA28194; -.
GeneTree; ENSGT00830000128240; -.
HOGENOM; HOG000234344; -.
HOVERGEN; HBG005731; -.
InParanoid; P02751; -.
KO; K05717; -.
OMA; ITISWRT; -.
OrthoDB; EOG091G116D; -.
PhylomeDB; P02751; -.
TreeFam; TF329915; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1474244; Extracellular matrix organization.
Reactome; R-HSA-1566977; Fibronectin matrix formation.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P02751; -.
ChiTaRS; FN1; human.
EvolutionaryTrace; P02751; -.
GeneWiki; Fibronectin; -.
GenomeRNAi; 2335; -.
PRO; PR:P02751; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115414; -.
ExpressionAtlas; P02751; baseline and differential.
Genevisible; P02751; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005605; C:basal lamina; IEA:Ensembl.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0005577; C:fibrinogen complex; IDA:BHF-UCL.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0051087; F:chaperone binding; IPI:CAFA.
GO; GO:0005518; F:collagen binding; NAS:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
GO; GO:0005102; F:receptor binding; IPI:CAFA.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0035987; P:endodermal cell differentiation; IDA:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0033622; P:integrin activation; IMP:UniProtKB.
GO; GO:0052047; P:interaction with other organism via secreted substance involved in symbiotic interaction; IDA:CAFA.
GO; GO:0051702; P:interaction with symbiont; IDA:CAFA.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:2001202; P:negative regulation of transforming growth factor-beta secretion; IDA:UniProtKB.
GO; GO:0018149; P:peptide cross-linking; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0009611; P:response to wounding; NAS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
CDD; cd00062; FN2; 2.
CDD; cd00063; FN3; 16.
Gene3D; 2.10.10.10; -; 2.
Gene3D; 2.60.40.10; -; 16.
InterPro; IPR000083; Fibronectin_type1.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013806; Kringle-like.
Pfam; PF00039; fn1; 12.
Pfam; PF00040; fn2; 2.
Pfam; PF00041; fn3; 16.
SMART; SM00058; FN1; 12.
SMART; SM00059; FN2; 2.
SMART; SM00060; FN3; 16.
SUPFAM; SSF49265; SSF49265; 10.
SUPFAM; SSF57440; SSF57440; 2.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01253; FN1_1; 12.
PROSITE; PS51091; FN1_2; 12.
PROSITE; PS00023; FN2_1; 2.
PROSITE; PS51092; FN2_2; 2.
PROSITE; PS50853; FN3; 16.
1: Evidence at protein level;
3D-structure; Acute phase; Alternative splicing; Angiogenesis;
Cell adhesion; Cell shape; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Extracellular matrix; Glycoprotein; Heparin-binding; Isopeptide bond;
Oxidation; Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Signal; Sulfation.
SIGNAL 1 31 {ECO:0000269|PubMed:6630202}.
CHAIN 32 2386 Fibronectin.
/FTId=PRO_0000019235.
CHAIN 627 702 Anastellin.
/FTId=PRO_0000390479.
CHAIN 723 911 Ugl-Y1.
/FTId=PRO_0000300249.
CHAIN 723 903 Ugl-Y2.
/FTId=PRO_0000300250.
CHAIN 723 ? Ugl-Y3.
/FTId=PRO_0000300251.
DOMAIN 50 90 Fibronectin type-I 1.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 95 138 Fibronectin type-I 2.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 139 182 Fibronectin type-I 3.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 184 228 Fibronectin type-I 4.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 229 273 Fibronectin type-I 5.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 306 345 Fibronectin type-I 6.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 355 403 Fibronectin type-II 1.
{ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 415 463 Fibronectin type-II 2.
{ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 468 511 Fibronectin type-I 7.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 516 558 Fibronectin type-I 8.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 559 602 Fibronectin type-I 9.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 610 702 Fibronectin type-III 1.
DOMAIN 722 812 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 813 904 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 909 998 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 999 1088 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 1089 1175 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 1176 1266 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 1269 1361 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 1362 1449 Fibronectin type-III 9.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 1450 1543 Fibronectin type-III 10.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1544 1635 Fibronectin type-III 11.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1636 1723 Fibronectin type-III 12; extra domain.
{ECO:0000255|PROSITE-ProRule:PRU00316,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 1724 1817 Fibronectin type-III 13.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1818 1904 Fibronectin type-III 14.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1905 1995 Fibronectin type-III 15.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 2103 2197 Fibronectin type-III 16.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 2204 2248 Fibronectin type-I 10.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 2249 2291 Fibronectin type-I 11.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DOMAIN 2293 2336 Fibronectin type-I 12.
{ECO:0000255|PROSITE-ProRule:PRU00478}.
DNA_BIND 907 1172
REGION 52 272 Fibrin- and heparin-binding 1.
REGION 308 608 Collagen-binding.
REGION 464 477 Critical for collagen binding.
REGION 1267 1540 Cell-attachment.
REGION 1721 1991 Heparin-binding 2.
REGION 1813 1991 Binds to FBLN1.
REGION 1992 2102 Connecting strand 3 (CS-3) (V region).
REGION 2206 2337 Fibrin-binding 2.
MOTIF 1524 1526 Cell attachment site.
SITE 663 663 Important for superfibronectin formation.
SITE 666 666 Important for superfibronectin formation.
SITE 2108 2108 Not glycosylated.
{ECO:0000269|PubMed:2012601}.
MOD_RES 32 32 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:6630202}.
MOD_RES 876 876 Sulfotyrosine. {ECO:0000255}.
MOD_RES 881 881 Sulfotyrosine. {ECO:0000255}.
MOD_RES 2363 2363 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2384 2384 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
CARBOHYD 279 279 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:16037490}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11285216,
ECO:0000269|PubMed:16037490,
ECO:0000269|PubMed:16335952}.
CARBOHYD 528 528 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16037490,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 542 542 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16037490,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
CARBOHYD 877 877 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16037490,
ECO:0000269|PubMed:17614963}.
CARBOHYD 1007 1007 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16037490,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 1244 1244 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16037490,
ECO:0000269|PubMed:16335952}.
CARBOHYD 2064 2064 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:2012601}.
CARBOHYD 2065 2065 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:2012601}.
CARBOHYD 2108 2108 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16037490}.
DISULFID 52 78
DISULFID 76 87
DISULFID 97 125
DISULFID 123 135
DISULFID 141 169
DISULFID 167 179
DISULFID 186 215
DISULFID 213 225
DISULFID 231 260
DISULFID 258 270
DISULFID 308 335
DISULFID 333 342
DISULFID 360 386
DISULFID 374 401
DISULFID 420 446
DISULFID 434 461
DISULFID 470 498 {ECO:0000250}.
DISULFID 496 508 {ECO:0000250}.
DISULFID 518 545 {ECO:0000250}.
DISULFID 543 555 {ECO:0000250}.
DISULFID 561 589 {ECO:0000250}.
DISULFID 587 599 {ECO:0000250}.
DISULFID 2206 2235 {ECO:0000250}.
DISULFID 2233 2245 {ECO:0000250}.
DISULFID 2251 2278 {ECO:0000250}.
DISULFID 2276 2288 {ECO:0000250}.
DISULFID 2295 2319 {ECO:0000250}.
DISULFID 2317 2333 {ECO:0000250}.
DISULFID 2367 2367 Interchain (with C-2371).
DISULFID 2371 2371 Interchain (with C-2367).
CROSSLNK 34 34 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-?). {ECO:0000250}.
CROSSLNK 35 35 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-?). {ECO:0000250}.
CROSSLNK 47 47 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-?). {ECO:0000250}.
VAR_SEQ 368 388 GRTFYSCTTEGRQDGHLWCST -> DRTDST (in
isoform 2).
{ECO:0000303|PubMed:11737888}.
/FTId=VSP_003255.
VAR_SEQ 648 657 KNSVGRWKEA -> VSIPPRNLGY (in isoform 2
and isoform 16).
{ECO:0000303|PubMed:11737888,
ECO:0000303|PubMed:16322219,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_003256.
VAR_SEQ 658 2386 Missing (in isoform 2 and isoform 16).
{ECO:0000303|PubMed:11737888,
ECO:0000303|PubMed:16322219,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_003257.
VAR_SEQ 1256 1487 Missing (in isoform 12).
{ECO:0000303|Ref.13}.
/FTId=VSP_013681.
VAR_SEQ 1265 1265 P -> PEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRI
TVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITL
INGGESAPTTLTQQT (in isoform 7, isoform 13
and isoform 15).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_008104.
VAR_SEQ 1266 1365 AVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVK
NEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHES
TPLRGRQKTGLDSPTGID -> EVPQLTDLSFVDITDSSIG
LRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTV
TGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLR
(in isoform 11). {ECO:0000305}.
/FTId=VSP_008105.
VAR_SEQ 1631 1721 NIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPED
GIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQ
PLIGTQSTA -> T (in isoform 8, isoform 9,
isoform 10, isoform 12, isoform 13 and
isoform 14).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16106752,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.13, ECO:0000303|Ref.4}.
/FTId=VSP_008106.
VAR_SEQ 1991 2110 Missing (in isoform 4, isoform 5, isoform
10 and isoform 13).
{ECO:0000303|PubMed:12127832,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_008107.
VAR_SEQ 1991 2015 Missing (in isoform 9 and isoform 12).
{ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.13}.
/FTId=VSP_008108.
VAR_SEQ 1992 2193 Missing (in isoform 6).
{ECO:0000303|PubMed:12127832}.
/FTId=VSP_008109.
VAR_SEQ 1992 2016 Missing (in isoform 17). {ECO:0000305}.
/FTId=VSP_047310.
VAR_SEQ 2081 2111 Missing (in isoform 3, isoform 7, isoform
9, isoform 12 and isoform 14).
{ECO:0000303|PubMed:16106752,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:2992939,
ECO:0000303|PubMed:6462919,
ECO:0000303|Ref.13, ECO:0000303|Ref.4}.
/FTId=VSP_008110.
VAR_SEQ 2082 2112 Missing (in isoform 17). {ECO:0000305}.
/FTId=VSP_047311.
VAR_SEQ 2148 2151 FRVP -> STKA (in isoform 4).
{ECO:0000303|PubMed:12127832}.
/FTId=VSP_008111.
VAR_SEQ 2152 2386 Missing (in isoform 4).
{ECO:0000303|PubMed:12127832}.
/FTId=VSP_008112.
VAR_SEQ 2193 2247 Missing (in isoform 5).
{ECO:0000303|PubMed:12127832}.
/FTId=VSP_008113.
VARIANT 15 15 Q -> L (in dbSNP:rs1250259).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:18268355,
ECO:0000269|PubMed:3031656,
ECO:0000269|Ref.4}.
/FTId=VAR_043917.
VARIANT 817 817 T -> P (in dbSNP:rs2577301).
{ECO:0000269|PubMed:11737888,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16106752,
ECO:0000269|PubMed:17614963,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:2992939,
ECO:0000269|Ref.4}.
/FTId=VAR_059529.
VARIANT 940 940 D -> N (in a breast cancer sample;
somatic mutation; dbSNP:rs752106647).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036018.
VARIANT 973 973 Y -> C (in GFND2; dbSNP:rs137854488).
{ECO:0000269|PubMed:18268355}.
/FTId=VAR_043918.
VARIANT 1120 1120 R -> P (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036019.
VARIANT 1467 1467 S -> R (in dbSNP:rs11687611).
/FTId=VAR_056576.
VARIANT 1834 1834 W -> R (in GFND2; reduced binding to
heparin, endothelial cells and podocytes;
impaired capability to induce stress-
fiber formation; dbSNP:rs137854486).
{ECO:0000269|PubMed:18268355}.
/FTId=VAR_043919.
VARIANT 1883 1883 L -> R (in GFND2; reduced binding to
heparin, endothelial cells and podocytes;
impaired capability to induce stress-
fiber formation; dbSNP:rs137854487).
{ECO:0000269|PubMed:18268355}.
/FTId=VAR_043920.
VARIANT 1960 1960 I -> V (in dbSNP:rs1250209).
{ECO:0000269|PubMed:18268355}.
/FTId=VAR_043921.
VARIANT 2121 2121 I -> V (in dbSNP:rs17449032).
/FTId=VAR_056577.
VARIANT 2170 2170 V -> I (in dbSNP:rs1250209).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:11737888,
ECO:0000269|PubMed:12127832,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16106752,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:2012601,
ECO:0000269|PubMed:2992573,
ECO:0000269|PubMed:2992939,
ECO:0000269|PubMed:4019516,
ECO:0000269|PubMed:6462919,
ECO:0000269|Ref.4}.
/FTId=VAR_061486.
VARIANT 2380 2380 D -> N (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036020.
MUTAGEN 641 641 Y->A: Severely compromised ability to
form fibronectin aggregates; when
associated with A-681 and A-683.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 642 642 I->A: Little effect on ability to form
fibronectin aggregates; when associated
with A-682; A-684 and A-692.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 663 663 L->A: No effect on secondary structure
nor on fibronectin binding nor on
activation of p38 K but abolishes
polymerization activity; when associated
with A-666. {ECO:0000269|PubMed:12946358,
ECO:0000269|PubMed:19379667}.
MUTAGEN 666 666 Y->A: No effect on secondary structure
nor on fibronectin binding nor on
activation of p38 kinase but abolishes
polymerization activity; when associated
with A-663. {ECO:0000269|PubMed:12946358,
ECO:0000269|PubMed:19379667}.
MUTAGEN 681 681 L->A: Severely compromised ability to
form fibronectin aggregates; when
associated with A-641 and A-683.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 682 682 I->A: Little effect on ability to form
fibronectin aggregates; when associated
with A-642; A-684 and A-692.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 683 683 S->A: Severely compromised ability to
form fibronectin aggregates; when
associated with A-641 and A-681.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 684 684 I->A: Little effect on ability to form
fibronectin aggregates; when associated
with A-642; A-682 and A-692.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 691 691 E->A: Slightly enhanced ability to form
fibronectin aggregates; when associated
with A-694 and A-696.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 692 692 V->A: Little effect on ability to form
fibronectin aggregates; when associated
with A-642; A-682 and A-684.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 694 694 R->A: Slightly enhanced ability to form
fibronectin aggregates; when associated
with A-691 and A-696.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 695 695 F->A: Loss of ability to form fibronectin
aggregates; when associated with A-697.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 696 696 D->A: Slightly enhanced ability to form
fibronectin aggregates; when associated
with A-691 and A-694.
{ECO:0000269|PubMed:12946358}.
MUTAGEN 697 697 F->A: Loss of ability to form fibronectin
aggregates; when associated with A-695.
{ECO:0000269|PubMed:12946358}.
CONFLICT 32 32 Q -> R (in Ref. 5; CAH18171).
{ECO:0000305}.
CONFLICT 69 69 Y -> N (in Ref. 5; CAH18172).
{ECO:0000305}.
CONFLICT 73 73 A -> V (in Ref. 11; CAA26536).
{ECO:0000305}.
CONFLICT 126 126 I -> V (in Ref. 5; CAH18136).
{ECO:0000305}.
CONFLICT 199 199 E -> G (in Ref. 5; CAD91166).
{ECO:0000305}.
CONFLICT 247 247 S -> R (in Ref. 1; CAD59389 and 2;
CAH60958). {ECO:0000305}.
CONFLICT 260 260 C -> R (in Ref. 5; CAH18172).
{ECO:0000305}.
CONFLICT 289 289 V -> A (in Ref. 5; CAE45847).
{ECO:0000305}.
CONFLICT 355 355 S -> L (in Ref. 13; AAD00015).
{ECO:0000305}.
CONFLICT 357 357 G -> E (in Ref. 5; CAD97984).
{ECO:0000305}.
CONFLICT 375 375 T -> A (in Ref. 5; CAH18136).
{ECO:0000305}.
CONFLICT 411 411 R -> Q (in Ref. 13; AAD00015).
{ECO:0000305}.
CONFLICT 518 518 C -> R (in Ref. 5; CAD97791).
{ECO:0000305}.
CONFLICT 552 552 R -> K (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 580 580 V -> A (in Ref. 5; CAH18172).
{ECO:0000305}.
CONFLICT 678 678 E -> Q (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 704 705 TP -> PT (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 980 980 V -> L (in Ref. 5; CAD97791).
{ECO:0000305}.
CONFLICT 1030 1030 T -> A (in Ref. 5; CAH18136).
{ECO:0000305}.
CONFLICT 1048 1048 V -> D (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 1134 1134 D -> G (in Ref. 5; CAH18136).
{ECO:0000305}.
CONFLICT 1137 1137 S -> N (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 1152 1152 T -> I (in Ref. 5; CAH18136).
{ECO:0000305}.
CONFLICT 1222 1222 E -> G (in Ref. 5; CAD97791).
{ECO:0000305}.
CONFLICT 1226 1226 H -> Q (in Ref. 5; CAE45932).
{ECO:0000305}.
CONFLICT 1555 1555 D -> G (in Ref. 5; CAE45714).
{ECO:0000305}.
CONFLICT 1601 1601 G -> S (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 1622 1622 Q -> E (in Ref. 27; AA sequence).
{ECO:0000305}.
CONFLICT 1715 1721 IGTQSTA -> VQTAVTT (in Ref. 29;
AAA52463). {ECO:0000305}.
CONFLICT 1726 1726 T -> A (in Ref. 5; CAE45847).
{ECO:0000305}.
CONFLICT 1755 1755 R -> W (in Ref. 5; CAH18136).
{ECO:0000305}.
CONFLICT 1768 1768 I -> V (in Ref. 19; CAB52436).
{ECO:0000305}.
CONFLICT 1783 1783 M -> T (in Ref. 5; CAE45932).
{ECO:0000305}.
CONFLICT 1927 1927 R -> C (in Ref. 13; AAD00014).
{ECO:0000305}.
CONFLICT 1934 1934 I -> V (in Ref. 5; CAH18172).
{ECO:0000305}.
CONFLICT 1992 1992 D -> G (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 2023 2023 V -> A (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 2027 2027 G -> R (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 2251 2251 C -> R (in Ref. 5; CAH18172).
{ECO:0000305}.
CONFLICT 2312 2312 Y -> N (in Ref. 5; CAD97965/CAD97964).
{ECO:0000305}.
CONFLICT 2341 2341 S -> T (in Ref. 5; CAE45714/CAH18171/
CAH18172/CAE45958). {ECO:0000305}.
CONFLICT 2367 2367 C -> Y (in Ref. 5; CAE45932).
{ECO:0000305}.
STRAND 52 54 {ECO:0000244|PDB:1QGB}.
STRAND 57 59 {ECO:0000244|PDB:1QGB}.
STRAND 64 69 {ECO:0000244|PDB:1O9A}.
STRAND 72 78 {ECO:0000244|PDB:1O9A}.
TURN 81 83 {ECO:0000244|PDB:1QGB}.
STRAND 85 89 {ECO:0000244|PDB:1O9A}.
STRAND 96 98 {ECO:0000244|PDB:2CG7}.
TURN 100 102 {ECO:0000244|PDB:2CG7}.
STRAND 105 107 {ECO:0000244|PDB:2CG7}.
STRAND 111 116 {ECO:0000244|PDB:2CG7}.
STRAND 119 127 {ECO:0000244|PDB:2CG7}.
TURN 128 131 {ECO:0000244|PDB:2CG7}.
STRAND 132 136 {ECO:0000244|PDB:2CG7}.
STRAND 140 143 {ECO:0000244|PDB:2CG7}.
STRAND 146 149 {ECO:0000244|PDB:2CG7}.
STRAND 153 157 {ECO:0000244|PDB:2CG7}.
STRAND 161 171 {ECO:0000244|PDB:2CG7}.
TURN 172 175 {ECO:0000244|PDB:2CG7}.
STRAND 176 181 {ECO:0000244|PDB:2CG7}.
STRAND 185 188 {ECO:0000244|PDB:2RKY}.
TURN 189 192 {ECO:0000244|PDB:2RKY}.
STRAND 193 196 {ECO:0000244|PDB:2RKY}.
STRAND 200 205 {ECO:0000244|PDB:2RKY}.
TURN 206 208 {ECO:0000244|PDB:2RKY}.
STRAND 209 217 {ECO:0000244|PDB:2RKY}.
TURN 218 221 {ECO:0000244|PDB:2RKY}.
STRAND 222 226 {ECO:0000244|PDB:2RKY}.
STRAND 230 233 {ECO:0000244|PDB:2RKY}.
TURN 234 237 {ECO:0000244|PDB:2RKY}.
STRAND 238 241 {ECO:0000244|PDB:2RKY}.
STRAND 245 249 {ECO:0000244|PDB:2RKY}.
STRAND 251 253 {ECO:0000244|PDB:2RKY}.
STRAND 255 262 {ECO:0000244|PDB:2RKY}.
TURN 263 266 {ECO:0000244|PDB:2RKY}.
STRAND 267 271 {ECO:0000244|PDB:2RKY}.
STRAND 302 304 {ECO:0000244|PDB:3M7P}.
STRAND 307 309 {ECO:0000244|PDB:3M7P}.
TURN 311 313 {ECO:0000244|PDB:1E88}.
STRAND 315 317 {ECO:0000244|PDB:3M7P}.
STRAND 321 326 {ECO:0000244|PDB:3M7P}.
STRAND 329 336 {ECO:0000244|PDB:3M7P}.
STRAND 339 344 {ECO:0000244|PDB:3M7P}.
TURN 353 356 {ECO:0000244|PDB:3M7P}.
STRAND 360 366 {ECO:0000244|PDB:3M7P}.
STRAND 369 373 {ECO:0000244|PDB:3M7P}.
STRAND 381 383 {ECO:0000244|PDB:1E88}.
STRAND 385 391 {ECO:0000244|PDB:3M7P}.
HELIX 392 395 {ECO:0000244|PDB:3M7P}.
STRAND 398 401 {ECO:0000244|PDB:3M7P}.
HELIX 403 405 {ECO:0000244|PDB:1E8B}.
TURN 413 417 {ECO:0000244|PDB:3M7P}.
STRAND 422 426 {ECO:0000244|PDB:3M7P}.
STRAND 429 433 {ECO:0000244|PDB:3M7P}.
STRAND 440 442 {ECO:0000244|PDB:2FN2}.
STRAND 445 451 {ECO:0000244|PDB:3M7P}.
HELIX 452 455 {ECO:0000244|PDB:3M7P}.
STRAND 458 460 {ECO:0000244|PDB:3M7P}.
HELIX 465 467 {ECO:0000244|PDB:3MQL}.
STRAND 469 471 {ECO:0000244|PDB:3M7P}.
STRAND 477 479 {ECO:0000244|PDB:3M7P}.
STRAND 483 485 {ECO:0000244|PDB:3M7P}.
STRAND 490 492 {ECO:0000244|PDB:3M7P}.
STRAND 495 500 {ECO:0000244|PDB:3M7P}.
TURN 501 504 {ECO:0000244|PDB:3M7P}.
STRAND 505 513 {ECO:0000244|PDB:3M7P}.
STRAND 517 520 {ECO:0000244|PDB:3EJH}.
STRAND 523 526 {ECO:0000244|PDB:3EJH}.
STRAND 529 534 {ECO:0000244|PDB:3EJH}.
STRAND 540 547 {ECO:0000244|PDB:3EJH}.
TURN 548 551 {ECO:0000244|PDB:3EJH}.
STRAND 552 557 {ECO:0000244|PDB:3EJH}.
STRAND 559 562 {ECO:0000244|PDB:3EJH}.
TURN 564 566 {ECO:0000244|PDB:3EJH}.
STRAND 569 571 {ECO:0000244|PDB:3EJH}.
STRAND 575 578 {ECO:0000244|PDB:3EJH}.
STRAND 585 591 {ECO:0000244|PDB:3EJH}.
TURN 592 595 {ECO:0000244|PDB:3EJH}.
STRAND 596 601 {ECO:0000244|PDB:3EJH}.
STRAND 613 615 {ECO:0000244|PDB:1OWW}.
STRAND 626 631 {ECO:0000244|PDB:1OWW}.
STRAND 634 636 {ECO:0000244|PDB:1OWW}.
STRAND 638 647 {ECO:0000244|PDB:1OWW}.
TURN 648 651 {ECO:0000244|PDB:1Q38}.
STRAND 655 659 {ECO:0000244|PDB:1OWW}.
STRAND 661 664 {ECO:0000244|PDB:1Q38}.
STRAND 665 668 {ECO:0000244|PDB:1OWW}.
STRAND 673 688 {ECO:0000244|PDB:1OWW}.
STRAND 690 699 {ECO:0000244|PDB:1OWW}.
HELIX 732 734 {ECO:0000244|PDB:2H41}.
STRAND 736 739 {ECO:0000244|PDB:2H41}.
STRAND 747 756 {ECO:0000244|PDB:2H41}.
TURN 757 759 {ECO:0000244|PDB:2H41}.
STRAND 764 769 {ECO:0000244|PDB:2H41}.
STRAND 774 777 {ECO:0000244|PDB:2H41}.
STRAND 785 794 {ECO:0000244|PDB:2H41}.
STRAND 799 808 {ECO:0000244|PDB:2H41}.
STRAND 818 822 {ECO:0000244|PDB:2N1K}.
STRAND 824 830 {ECO:0000244|PDB:2N1K}.
STRAND 839 847 {ECO:0000244|PDB:2N1K}.
STRAND 854 859 {ECO:0000244|PDB:2N1K}.
STRAND 864 869 {ECO:0000244|PDB:2N1K}.
STRAND 875 883 {ECO:0000244|PDB:2N1K}.
STRAND 892 897 {ECO:0000244|PDB:2N1K}.
STRAND 1178 1184 {ECO:0000244|PDB:1FNF}.
STRAND 1186 1189 {ECO:0000244|PDB:1FNF}.
STRAND 1191 1196 {ECO:0000244|PDB:1FNF}.
STRAND 1205 1212 {ECO:0000244|PDB:1FNF}.
TURN 1213 1215 {ECO:0000244|PDB:1FNF}.
STRAND 1221 1225 {ECO:0000244|PDB:1FNF}.
STRAND 1231 1233 {ECO:0000244|PDB:1FNF}.
STRAND 1243 1251 {ECO:0000244|PDB:1FNF}.
STRAND 1259 1263 {ECO:0000244|PDB:1FNF}.
STRAND 1271 1277 {ECO:0000244|PDB:1FNF}.
STRAND 1283 1288 {ECO:0000244|PDB:1FNF}.
STRAND 1296 1304 {ECO:0000244|PDB:1FNF}.
HELIX 1305 1307 {ECO:0000244|PDB:3T1W}.
HELIX 1308 1310 {ECO:0000244|PDB:2GEE}.
STRAND 1312 1316 {ECO:0000244|PDB:1FNF}.
STRAND 1322 1325 {ECO:0000244|PDB:1FNF}.
STRAND 1333 1342 {ECO:0000244|PDB:1FNF}.
STRAND 1350 1355 {ECO:0000244|PDB:1FNF}.
STRAND 1362 1368 {ECO:0000244|PDB:4LXO}.
STRAND 1374 1379 {ECO:0000244|PDB:4LXO}.
STRAND 1386 1394 {ECO:0000244|PDB:4LXO}.
STRAND 1402 1406 {ECO:0000244|PDB:4LXO}.
STRAND 1412 1415 {ECO:0000244|PDB:4LXO}.
STRAND 1423 1432 {ECO:0000244|PDB:4LXO}.
STRAND 1440 1445 {ECO:0000244|PDB:4LXO}.
STRAND 1452 1460 {ECO:0000244|PDB:4LXO}.
STRAND 1463 1469 {ECO:0000244|PDB:4LXO}.
STRAND 1476 1484 {ECO:0000244|PDB:4LXO}.
STRAND 1487 1489 {ECO:0000244|PDB:5DC9}.
STRAND 1492 1497 {ECO:0000244|PDB:4LXO}.
STRAND 1502 1505 {ECO:0000244|PDB:4LXO}.
STRAND 1513 1522 {ECO:0000244|PDB:4LXO}.
STRAND 1525 1527 {ECO:0000244|PDB:4LXO}.
STRAND 1534 1539 {ECO:0000244|PDB:4LXO}.
STRAND 1548 1553 {ECO:0000244|PDB:5DFT}.
STRAND 1558 1562 {ECO:0000244|PDB:5DFT}.
STRAND 1570 1581 {ECO:0000244|PDB:5DFT}.
STRAND 1586 1590 {ECO:0000244|PDB:5DFT}.
STRAND 1596 1599 {ECO:0000244|PDB:5DFT}.
STRAND 1607 1615 {ECO:0000244|PDB:5DFT}.
STRAND 1621 1630 {ECO:0000244|PDB:5DFT}.
STRAND 1639 1644 {ECO:0000244|PDB:1J8K}.
STRAND 1647 1651 {ECO:0000244|PDB:1J8K}.
STRAND 1662 1668 {ECO:0000244|PDB:1J8K}.
TURN 1669 1671 {ECO:0000244|PDB:1J8K}.
STRAND 1672 1676 {ECO:0000244|PDB:1J8K}.
STRAND 1686 1689 {ECO:0000244|PDB:1J8K}.
STRAND 1696 1704 {ECO:0000244|PDB:1J8K}.
STRAND 1706 1708 {ECO:0000244|PDB:1J8K}.
STRAND 1714 1719 {ECO:0000244|PDB:1J8K}.
STRAND 1726 1733 {ECO:0000244|PDB:3R8Q}.
STRAND 1738 1743 {ECO:0000244|PDB:3R8Q}.
STRAND 1751 1763 {ECO:0000244|PDB:3R8Q}.
STRAND 1766 1770 {ECO:0000244|PDB:3R8Q}.
STRAND 1776 1779 {ECO:0000244|PDB:3R8Q}.
STRAND 1787 1796 {ECO:0000244|PDB:3R8Q}.
STRAND 1804 1809 {ECO:0000244|PDB:3R8Q}.
STRAND 1818 1825 {ECO:0000244|PDB:3R8Q}.
STRAND 1830 1835 {ECO:0000244|PDB:3R8Q}.
STRAND 1843 1853 {ECO:0000244|PDB:3R8Q}.
STRAND 1857 1861 {ECO:0000244|PDB:3R8Q}.
STRAND 1866 1870 {ECO:0000244|PDB:3R8Q}.
STRAND 1878 1887 {ECO:0000244|PDB:3R8Q}.
STRAND 1895 1900 {ECO:0000244|PDB:3R8Q}.
STRAND 1907 1915 {ECO:0000244|PDB:3R8Q}.
STRAND 1918 1924 {ECO:0000244|PDB:3R8Q}.
STRAND 1932 1938 {ECO:0000244|PDB:3R8Q}.
STRAND 1957 1960 {ECO:0000244|PDB:3R8Q}.
STRAND 1968 1977 {ECO:0000244|PDB:3R8Q}.
STRAND 1985 1990 {ECO:0000244|PDB:3R8Q}.
STRAND 2253 2255 {ECO:0000244|PDB:2EC3}.
STRAND 2263 2267 {ECO:0000244|PDB:2EC3}.
STRAND 2269 2280 {ECO:0000244|PDB:2EC3}.
TURN 2281 2284 {ECO:0000244|PDB:2EC3}.
STRAND 2285 2290 {ECO:0000244|PDB:2EC3}.
SEQUENCE 2386 AA; 262625 MW; 5F7EDB9700335098 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
DTIIPAVPPP TDLRFTNIGP DTMRVTWAPP PSIDLTNFLV RYSPVKNEED VAELSISPSD
NAVVLTNLLP GTEYVVSVSS VYEQHESTPL RGRQKTGLDS PTGIDFSDIT ANSFTVHWIA
PRATITGYRI RHHPEHFSGR PREDRVPHSR NSITLTNLTP GTEYVVSIVA LNGREESPLL
IGQQSTVSDV PRDLEVVAAT PTSLLISWDA PAVTVRYYRI TYGETGGNSP VQEFTVPGSK
STATISGLKP GVDYTITVYA VTGRGDSPAS SKPISINYRT EIDKPSQMQV TDVQDNSISV
KWLPSSSPVT GYRVTTTPKN GPGPTKTKTA GPDQTEMTIE GLQPTVEYVV SVYAQNPSGE
SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI AWESPQGQVS RYRVTYSSPE DGIHELFPAP
DGEEDTAELQ GLRPGSEYTV SVVALHDDME SQPLIGTQST AIPAPTDLKF TQVTPTSLSA
QWTPPNVQLT GYRVRVTPKE KTGPMKEINL APDSSSVVVS GLMVATKYEV SVYALKDTLT
SRPAQGVVTT LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAVP ANGQTPIQRT
IKPDVRSYTI TGLQPGTDYK IYLYTLNDNA RSSPVVIDAS TAIDAPSNLR FLATTPNSLL
VSWQPPRARI TGYIIKYEKP GSPPREVVPR PRPGVTEATI TGLEPGTEYT IYVIALKNNQ
KSEPLIGRKK TDELPQLVTL PHPNLHGPEI LDVPSTVQKT PFVTHPGYDT GNGIQLPGTS
GQQPSVGQQM IFEEHGFRRT TPPTTATPIR HRPRPYPPNV GEEIQIGHIP REDVDYHLYP
HGPGLNPNAS TGQEALSQTT ISWAPFQDTS EYIISCHPVG TDEEPLQFRV PGTSTSATLT
GLTRGATYNV IVEALKDQQR HKVREEVVTV GNSVNEGLNQ PTDDSCFDPY TVSHYAVGDE
WERMSESGFK LLCQCLGFGS GHFRCDSSRW CHDNGVNYKI GEKWDRQGEN GQMMSCTCLG
NGKGEFKCDP HEATCYDDGK TYHVGEQWQK EYLGAICSCT CFGGQRGWRC DNCRRPGGEP
SPEGTTGQSY NQYSQRYHQR TNTNVNCPIE CFMPLDVQAD REDSRE


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