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Database: UniProt
Entry: P11276
LinkDB: P11276
Original site: P11276 
ID   FINC_MOUSE              Reviewed;        2477 AA.
AC   P11276; G5E8B8; Q61567; Q61568; Q61569; Q64233; Q80UI4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 4.
DT   13-FEB-2019, entry version 206.
DE   RecName: Full=Fibronectin;
DE            Short=FN;
DE   Contains:
DE     RecName: Full=Anastellin;
DE   Flags: Precursor;
GN   Name=Fn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-920.
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC   TISSUE=Liver;
RX   PubMed=8299972; DOI=10.1016/0378-1119(93)90036-3;
RA   Polly P., Nicholson R.C.;
RT   "Sequence of the mouse fibronectin-encoding gene promoter region.";
RL   Gene 137:353-354(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 562-834.
RC   STRAIN=NMRI;
RX   PubMed=7673336;
RA   Talts J.F., Weller A., Timpl R., Ekblom M., Ekblom P.;
RT   "Regulation of mesenchymal extracellular matrix protein synthesis by
RT   transforming growth factor-beta and glucocorticoids in tumor stroma.";
RL   J. Cell Sci. 108:2153-2162(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 899-2376.
RA   Gorski G., Aros M., Norton P.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
RX   PubMed=3124113; DOI=10.1073/pnas.85.4.1119;
RA   Blatti S.P., Foster D.N., Ranganthan G., Moses H.L., Getz M.J.;
RT   "Induction of fibronectin gene transcription and mRNA is a primary
RT   response to growth-factor stimulation of AKR-2B cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1119-1123(1988).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
RX   PubMed=2521606; DOI=10.1016/0014-4827(89)90080-3;
RA   Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.;
RT   "Coordinate induction of fibronectin, fibronectin receptor,
RT   tropomyosin, and actin genes in serum-stimulated fibroblasts.";
RL   Exp. Cell Res. 180:537-545(1989).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
RC   TISSUE=Kidney;
RX   PubMed=1327855; DOI=10.1016/0014-4827(92)90100-M;
RA   Khandjian E.W., Salomon C., Leonard N., Tremblay S., Turler H.;
RT   "Fibronectin gene expression in proliferating, quiescent, and SV40-
RT   infected mouse kidney cells.";
RL   Exp. Cell Res. 202:464-470(1992).
RN   [10]
RP   TRANSGLUTAMINATION AT GLN-35; GLN-36 AND GLN-48, AND MUTAGENESIS OF
RP   GLN-35; GLN-36 AND GLN-48.
RX   PubMed=9312106; DOI=10.1074/jbc.272.40.24999;
RA   Corbett S.A., Lee L., Wilson C.L., Schwarzbauer J.E.;
RT   "Covalent cross-linking of fibronectin to fibrin is required for
RT   maximal cell adhesion to a fibronectin-fibrin matrix.";
RL   J. Biol. Chem. 272:24999-25005(1997).
RN   [11]
RP   DOWN-REGULATION BY GLUCOCORTICOIDS.
RX   PubMed=11737251; DOI=10.1034/j.1600-0609.2001.5790528.x;
RA   Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.;
RT   "Glucocorticoids down-regulate the extracellular matrix proteins
RT   fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma.";
RL   Eur. J. Haematol. 67:176-184(2001).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [13]
RP   INTERACTION WITH FBLN7.
RX   PubMed=17699513; DOI=10.1074/jbc.M705847200;
RA   de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A.,
RA   Fisher L.W., Fukumoto S., Yamada Y.;
RT   "TM14 is a new member of the fibulin family (fibulin-7) that interacts
RT   with extracellular matrix molecules and is active for cell binding.";
RL   J. Biol. Chem. 282:30878-30888(2007).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-
RT   containing tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [17]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528; ASN-1006; ASN-1290
RP   AND ASN-2198.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [19]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006 AND ASN-1290.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-2475, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [21]
RP   FUNCTION.
RX   PubMed=21768292; DOI=10.1083/jcb.201007108;
RA   Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
RA   Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
RT   "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT   fibronectin deposition.";
RL   J. Cell Biol. 194:307-322(2011).
RN   [22]
RP   OXIDATION.
RX   PubMed=26954549; DOI=10.1016/j.devcel.2016.02.009;
RA   Kraft-Sheleg O., Zaffryar-Eilot S., Genin O., Yaseen W.,
RA   Soueid-Baumgarten S., Kessler O., Smolkin T., Akiri G., Neufeld G.,
RA   Cinnamon Y., Hasson P.;
RT   "Localized LoxL3-dependent fibronectin oxidation regulates myofiber
RT   stretch and integrin-mediated adhesion.";
RL   Dev. Cell 36:550-561(2016).
RN   [23]
RP   STRUCTURE BY NMR OF 1447-1630.
RX   PubMed=9533887; DOI=10.1006/jmbi.1998.1616;
RA   Copie V., Tomita Y., Akiyama S.K., Aota S., Yamada K.M., Venable R.M.,
RA   Pastor R.W., Krueger S., Torchia D.A.;
RT   "Solution structure and dynamics of linked cell attachment modules of
RT   mouse fibronectin containing the RGD and synergy regions: comparison
RT   with the human fibronectin crystal structure.";
RL   J. Mol. Biol. 277:663-682(1998).
CC   -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC       including collagen, fibrin, heparin, DNA, and actin. Fibronectins
CC       are involved in cell adhesion, cell motility, opsonization, wound
CC       healing, and maintenance of cell shape healing, and maintenance of
CC       cell shape. Involved in osteoblast compaction through the
CC       fibronectin fibrillogenesis cell-mediated matrix assembly process,
CC       essential for osteoblast mineralization. Participates in the
CC       regulation of type I collagen deposition by osteoblasts.
CC       {ECO:0000269|PubMed:21768292}.
CC   -!- FUNCTION: Anastellin binds fibronectin and induces fibril
CC       formation. This fibronectin polymer, named superfibronectin,
CC       exhibits enhanced adhesive properties. Both anastellin and
CC       superfibronectin inhibit tumor growth, angiogenesis and
CC       metastasis. Anastellin activates p38 MAPK and inhibits
CC       lysophospholipid signaling (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC       variants, connected by 2 disulfide bonds near the carboxyl ends;
CC       to a lesser extent homodimers. Interacts with FBLN1, AMBP,
CC       LGALS3BP and COL13A1 and COMP (By similarity). Interacts with TNR;
CC       interaction mediates inhibition of cell adhesion and neurite
CC       outgrowth. Interacts with FBLN7. Interacts with FST3 and MYOC (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8CIH5:Plcg2; NbExp=6; IntAct=EBI-641955, EBI-617954;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. Each of the "extra
CC         domain" and the connecting strand 3 are present in some forms of
CC         fibronectin and absent in others.;
CC       Name=1;
CC         IsoId=P11276-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted
CC       by hepatocytes. Cellular FN (dimeric or cross-linked multimeric
CC       forms), made by fibroblasts, epithelial and other cell types, is
CC       deposited as fibrils in the extracellular matrix.
CC   -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC       synthesis.
CC   -!- PTM: Sulfated. {ECO:0000250}.
CC   -!- PTM: Forms covalent cross-links mediated by a transglutaminase,
CC       such as F13A or TGM2, between a glutamine and the epsilon-amino
CC       group of a lysine residue, forming homopolymers and heteropolymers
CC       (e.g. fibrinogen-fibronectin, collagen-fibronectin
CC       heteropolymers). {ECO:0000269|PubMed:9312106}.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P02751}.
CC   -!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
CC       anastellin. {ECO:0000250}.
CC   -!- PTM: Some lysine residues are oxidized to allysine by LOXL3,
CC       promoting fibronectin activation and matrix formation.
CC       {ECO:0000269|PubMed:26954549}.
DR   EMBL; AC124821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466548; EDL00265.1; -; Genomic_DNA.
DR   EMBL; BC051082; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; Z22729; CAA80422.1; -; Genomic_DNA.
DR   EMBL; X82402; CAA57796.1; -; mRNA.
DR   EMBL; X93167; CAA63654.1; -; mRNA.
DR   EMBL; M18194; AAA37636.1; -; mRNA.
DR   EMBL; S45680; AAB23491.1; -; mRNA.
DR   CCDS; CCDS15031.1; -. [P11276-1]
DR   PIR; A49173; A49173.
DR   PIR; I48349; I48349.
DR   RefSeq; NP_034363.1; NM_010233.2. [P11276-1]
DR   UniGene; Mm.193099; -.
DR   PDB; 1MFN; NMR; -; A=1447-1630.
DR   PDB; 2MFN; NMR; -; A=1447-1630.
DR   PDBsum; 1MFN; -.
DR   PDBsum; 2MFN; -.
DR   ProteinModelPortal; P11276; -.
DR   SMR; P11276; -.
DR   BioGrid; 199719; 2.
DR   CORUM; P11276; -.
DR   ELM; P11276; -.
DR   IntAct; P11276; 6.
DR   MINT; P11276; -.
DR   STRING; 10090.ENSMUSP00000054499; -.
DR   iPTMnet; P11276; -.
DR   PhosphoSitePlus; P11276; -.
DR   SwissPalm; P11276; -.
DR   EPD; P11276; -.
DR   jPOST; P11276; -.
DR   MaxQB; P11276; -.
DR   PaxDb; P11276; -.
DR   PeptideAtlas; P11276; -.
DR   PRIDE; P11276; -.
DR   Ensembl; ENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193. [P11276-1]
DR   GeneID; 14268; -.
DR   KEGG; mmu:14268; -.
DR   UCSC; uc007bju.2; mouse. [P11276-1]
DR   CTD; 2335; -.
DR   MGI; MGI:95566; Fn1.
DR   eggNOG; ENOG410IF4N; Eukaryota.
DR   eggNOG; ENOG410Y2NH; LUCA.
DR   GeneTree; ENSGT00940000155126; -.
DR   HOGENOM; HOG000234344; -.
DR   HOVERGEN; HBG005731; -.
DR   InParanoid; P11276; -.
DR   KO; K05717; -.
DR   OrthoDB; 6580at2759; -.
DR   TreeFam; TF329915; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-1474244; Extracellular matrix organization.
DR   Reactome; R-MMU-1566977; Fibronectin matrix formation.
DR   Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-3000170; Syndecan interactions.
DR   Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
DR   Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR   Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   ChiTaRS; Fn1; mouse.
DR   EvolutionaryTrace; P11276; -.
DR   PRO; PR:P11276; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026193; Expressed in 313 organ(s), highest expression level in vault of skull.
DR   ExpressionAtlas; P11276; baseline and differential.
DR   Genevisible; P11276; MM.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005577; C:fibrinogen complex; ISO:MGI.
DR   GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR   GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0045340; F:mercury ion binding; ISO:MGI.
DR   GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IDA:MGI.
DR   GO; GO:0001775; P:cell activation; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR   GO; GO:0007044; P:cell-substrate junction assembly; IDA:MGI.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR   GO; GO:0071288; P:cellular response to mercury ion; ISO:MGI.
DR   GO; GO:0035987; P:endodermal cell differentiation; ISO:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; ISO:MGI.
DR   GO; GO:0008347; P:glial cell migration; ISO:MGI.
DR   GO; GO:0033622; P:integrin activation; ISO:MGI.
DR   GO; GO:0052047; P:interaction with other organism via secreted substance involved in symbiotic interaction; ISO:MGI.
DR   GO; GO:0051702; P:interaction with symbiont; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:2001202; P:negative regulation of transforming growth factor-beta secretion; ISO:MGI.
DR   GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISO:MGI.
DR   GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR   GO; GO:0045773; P:positive regulation of axon extension; IDA:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; ISO:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:0042060; P:wound healing; IMP:MGI.
DR   CDD; cd00061; FN1; 12.
DR   CDD; cd00062; FN2; 2.
DR   CDD; cd00063; FN3; 17.
DR   Gene3D; 2.10.10.10; -; 2.
DR   Gene3D; 2.60.40.10; -; 17.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013806; Kringle-like.
DR   Pfam; PF00039; fn1; 12.
DR   Pfam; PF00040; fn2; 2.
DR   Pfam; PF00041; fn3; 17.
DR   SMART; SM00058; FN1; 12.
DR   SMART; SM00059; FN2; 2.
DR   SMART; SM00060; FN3; 17.
DR   SUPFAM; SSF49265; SSF49265; 11.
DR   SUPFAM; SSF57440; SSF57440; 2.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01253; FN1_1; 12.
DR   PROSITE; PS51091; FN1_2; 12.
DR   PROSITE; PS00023; FN2_1; 2.
DR   PROSITE; PS51092; FN2_2; 2.
DR   PROSITE; PS50853; FN3; 17.
PE   1: Evidence at protein level;
KW   3D-structure; Acute phase; Alternative splicing; Angiogenesis;
KW   Cell adhesion; Cell shape; Complete proteome; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Heparin-binding; Isopeptide bond;
KW   Oxidation; Phosphoprotein; Pyrrolidone carboxylic acid;
KW   Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL        1     32       {ECO:0000250|UniProtKB:P02751}.
FT   CHAIN        33   2477       Fibronectin.
FT                                /FTId=PRO_0000019236.
FT   CHAIN       627    701       Anastellin. {ECO:0000250}.
FT                                /FTId=PRO_0000390480.
FT   DOMAIN       51     91       Fibronectin type-I 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN       96    139       Fibronectin type-I 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      140    183       Fibronectin type-I 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      185    229       Fibronectin type-I 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      230    274       Fibronectin type-I 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      306    343       Fibronectin type-I 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      355    403       Fibronectin type-II 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      415    463       Fibronectin type-II 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      468    516       Fibronectin type-I 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      516    558       Fibronectin type-I 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      559    602       Fibronectin type-I 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      610    717       Fibronectin type-III 1.
FT   DOMAIN      721    811       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      812    903       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      908    997       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      998   1087       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1088   1174       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1175   1269       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1270   1358       Fibronectin type-III 8; extra domain 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1359   1451       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1452   1539       Fibronectin type-III 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1540   1633       Fibronectin type-III 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1634   1725       Fibronectin type-III 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1726   1813       Fibronectin type-III 13; extra domain 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1814   1907       Fibronectin type-III 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1908   1994       Fibronectin type-III 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1995   2085       Fibronectin type-III 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2193   2287       Fibronectin type-III 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2294   2338       Fibronectin type-I 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN     2339   2381       Fibronectin type-I 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN     2383   2426       Fibronectin type-I 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DNA_BIND    906   1171
FT   REGION       53    273       Fibrin- and heparin-binding 1.
FT   REGION      308    608       Collagen-binding.
FT   REGION     1357   1630       Cell-attachment.
FT   REGION     1811   2081       Heparin-binding 2.
FT   REGION     2082   2201       Connecting strand 3 (CS-3) (V region).
FT   REGION     2296   2427       Fibrin-binding 2.
FT   MOTIF      1614   1616       Cell attachment site.
FT   MOTIF      2181   2183       Cell attachment site.
FT   MOD_RES      33     33       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P02751}.
FT   MOD_RES     285    285       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     875    875       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     880    880       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES    2392   2392       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES    2454   2454       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P02751}.
FT   MOD_RES    2475   2475       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:18630941,
FT                                ECO:0000244|PubMed:19131326,
FT                                ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    430    430       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    528    528       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17330941,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    542    542       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    876    876       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1006   1006       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16944957,
FT                                ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD   1243   1243       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1290   1290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD   2198   2198       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19656770}.
FT   DISULFID     53     79       {ECO:0000250}.
FT   DISULFID     77     88       {ECO:0000250}.
FT   DISULFID     98    126       {ECO:0000250}.
FT   DISULFID    124    136       {ECO:0000250}.
FT   DISULFID    142    170       {ECO:0000250}.
FT   DISULFID    168    180       {ECO:0000250}.
FT   DISULFID    187    216       {ECO:0000250}.
FT   DISULFID    214    226       {ECO:0000250}.
FT   DISULFID    232    261       {ECO:0000250}.
FT   DISULFID    259    271       {ECO:0000250}.
FT   DISULFID    308    335       {ECO:0000250}.
FT   DISULFID    333    342       {ECO:0000250}.
FT   DISULFID    360    386       {ECO:0000250}.
FT   DISULFID    374    401       {ECO:0000250}.
FT   DISULFID    420    446       {ECO:0000250}.
FT   DISULFID    434    461       {ECO:0000250}.
FT   DISULFID    470    498       {ECO:0000250}.
FT   DISULFID    496    508       {ECO:0000250}.
FT   DISULFID    518    545       {ECO:0000250}.
FT   DISULFID    543    555       {ECO:0000250}.
FT   DISULFID    561    589       {ECO:0000250}.
FT   DISULFID    587    599       {ECO:0000250}.
FT   DISULFID   2296   2325       {ECO:0000250}.
FT   DISULFID   2323   2335       {ECO:0000250}.
FT   DISULFID   2341   2368       {ECO:0000250}.
FT   DISULFID   2366   2378       {ECO:0000250}.
FT   DISULFID   2385   2411       {ECO:0000250}.
FT   DISULFID   2409   2420       {ECO:0000250}.
FT   DISULFID   2458   2458       Interchain (with C-2462).
FT   DISULFID   2462   2462       Interchain (with C-2458).
FT   CROSSLNK     35     35       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-?).
FT                                {ECO:0000269|PubMed:9312106}.
FT   CROSSLNK     36     36       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-?).
FT                                {ECO:0000269|PubMed:9312106}.
FT   CROSSLNK     48     48       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-?).
FT                                {ECO:0000269|PubMed:9312106}.
FT   MUTAGEN      35     35       Q->A: 99% decrease in cross-linking
FT                                efficiency; when associated with A-36 and
FT                                A-48. {ECO:0000269|PubMed:9312106}.
FT   MUTAGEN      35     35       Q->L: 65% decrease in cross-linking
FT                                efficiency; when associated with L-36.
FT                                {ECO:0000269|PubMed:9312106}.
FT   MUTAGEN      36     36       Q->A: 99% decrease in cross-linking
FT                                efficiency; when associated with A-35 and
FT                                A-48. {ECO:0000269|PubMed:9312106}.
FT   MUTAGEN      36     36       Q->L: 65% decrease in cross-linking
FT                                efficiency; when associated with L-35.
FT                                {ECO:0000269|PubMed:9312106}.
FT   MUTAGEN      48     48       Q->A: 99% decrease in cross-linking
FT                                efficiency; when associated with A-35 and
FT                                A-36. {ECO:0000269|PubMed:9312106}.
FT   CONFLICT   1063   1063       V -> A (in Ref. 6; CAA63654).
FT                                {ECO:0000305}.
FT   CONFLICT   1820   1820       F -> L (in Ref. 6; CAA63654).
FT                                {ECO:0000305}.
FT   CONFLICT   2440   2440       T -> N (in Ref. 7; AAA37636).
FT                                {ECO:0000305}.
FT   STRAND     1455   1459       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1461   1467       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1476   1484       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1492   1496       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1501   1507       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1510   1521       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1530   1536       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1545   1550       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1553   1557       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1567   1580       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1582   1586       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1591   1594       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1600   1612       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1615   1617       {ECO:0000244|PDB:1MFN}.
FT   STRAND     1624   1630       {ECO:0000244|PDB:1MFN}.
SQ   SEQUENCE   2477 AA;  272538 MW;  24A207BE67F85585 CRC64;
     MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK PGCFDNGKHY
     QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYKVG DTYERPKDSM
     IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDKWRRPHE TGGYMLECLC LGNGKGEWTC
     KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS
     YRIGDTWSKK DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP
     QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
     VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHAVLVQT RGGNSNGALC
     HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI
     GDQWDKQHDL GHMMRCTCVG NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
     LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ
     PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS TGRWKEATIP
     GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS ASTPVTSNTV TGETAPYSPV
     VATSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL
     PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY
     RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT
     PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG QRLPVNRNTF
     AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT NLQFVNETDR TVLVTWTPPR
     ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY PLRNLQPGSE YTVTLVAVKG NQQSPKATGV
     FTTLQPLRSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS
     GLTPGVEYTY TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP
     DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK DDKESAPISD
     TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT VVAAGEGIPI FEDFVDSSVG
     YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP
     PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL
     RGRQKTGLDS PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR
     NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST PTSLLISWEP
     PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP GADYTITLYA VTGRGDSPAS
     SKPVSINYKT EIDKPSQMQV TDVQDNSISV RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA
     SPDQTEMTIE GLQPTVEYVV SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI
     AWESPQGQVS RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME
     SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE KTGPMKEINL
     SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT LENVSPPRRA RVTDATETTI
     TISWRTKTET ITGFQVDAIP ANGQTPVQRS ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA
     RSSPVIIDAS TAIDAPSNLR FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR
     PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI
     LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT TPPTAATPVR
     LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT ISWTPFQESS
     EYIISCQPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALQNQRR HKVREEVVTV
     GNAVSEGLNQ PTDDSCFDPY TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW
     CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
     EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ RTNTNVNCPI
     ECFMPLDVQA DRDDSRE
//
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