FINC_MOUSE
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 03-AUG-2022, entry version 225.
DE RecName: Full=Fibronectin {ECO:0000305};
DE Short=FN;
DE Contains:
DE RecName: Full=Anastellin;
DE Flags: Precursor;
GN Name=Fn1 {ECO:0000312|MGI:MGI:95566};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT 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; DOI=10.1242/jcs.108.6.2153;
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 response
RT 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, tropomyosin,
RT 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-infected
RT 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 GLN-35;
RP 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 maximal
RT 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., 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., Fisher L.W.,
RA Fukumoto S., Yamada Y.;
RT "TM14 is a new member of the fibulin family (fibulin-7) that interacts with
RT 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-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND IDENTIFICATION BY
RP 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 BY
RP 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 affinity
RT 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 AND
RP ASN-2198.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., 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 BY
RP 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 electron
RT 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-linked
RT 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, Pancreas,
RC 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 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., Mosher D.,
RA 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 stretch
RT and integrin-mediated adhesion.";
RL Dev. Cell 36:550-561(2016).
RN [23]
RP TISSUE SPECIFICITY.
RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA Lako M.;
RT "Extracellular matrix component expression in human pluripotent stem cell-
RT derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT an important role for IMPG1 and CD44 in the development of photoreceptors
RT and interphotoreceptor matrix.";
RL Acta Biomater. 74:207-221(2018).
RN [24]
RP FUNCTION.
RX PubMed=34089617; DOI=10.1093/intimm/dxab028;
RA Su M.T., Inui M., Wong Y.L., Takahashi M., Sugahara-Tobinai A., Ono K.,
RA Miyamoto S., Murakami K., Itoh-Nakadai A., Kezuka D., Itoi S., Endo S.,
RA Hirayasu K., Arase H., Takai T.;
RT "Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin
RT ameliorates autoimmune disease in BXSB/Yaa mice.";
RL Int. Immunol. 33:447-458(2021).
RN [25]
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 mouse
RT fibronectin containing the RGD and synergy regions: comparison with the
RT 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 (By similarity).
CC Fibronectins are involved in cell adhesion, cell motility,
CC opsonization, wound healing, and maintenance of cell shape healing, and
CC maintenance of cell shape (By similarity). Involved in osteoblast
CC compaction through the fibronectin fibrillogenesis cell-mediated matrix
CC assembly process, essential for osteoblast mineralization
CC (PubMed:21768292). Participates in the regulation of type I collagen
CC deposition by osteoblasts (PubMed:21768292). Acts as a ligand for the
CC Lilrb4a receptor, inhibiting Fcgr1/CD64-mediated monocyte activation
CC (PubMed:34089617). {ECO:0000250|UniProtKB:P02751,
CC ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:34089617}.
CC -!- FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation.
CC This fibronectin polymer, named superfibronectin, exhibits enhanced
CC adhesive properties. Both anastellin and superfibronectin inhibit tumor
CC growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and
CC inhibits lysophospholipid signaling. {ECO:0000250|UniProtKB:P02751}.
CC -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC variants, connected by 2 disulfide bonds near the carboxyl ends; to a
CC lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and
CC COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP.
CC Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain);
CC this interaction enhances fibronectin fibril assembly. TNFAIP6 may act
CC as a bridging molecule between FN1 and THBS1 (By similarity). Interacts
CC with TNR; the interaction inhibits cell adhesion and neurite outgrowth
CC (By similarity). Interacts with FST3 and MYOC (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P02751}.
CC -!- INTERACTION:
CC P11276; 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. The diversity of isoforms
CC depends on the V region and either of the two extra domain which can
CC be either included or excluded (partially or completely for the V
CC region). {ECO:0000305};
CC Name=1;
CC IsoId=P11276-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the inner limiting membrane and around
CC blood vessels in the retina (at protein level) (PubMed:29777959).
CC Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular
CC FN (dimeric or cross-linked multimeric forms), made by fibroblasts,
CC epithelial and other cell types, is deposited as fibrils in the
CC extracellular matrix. {ECO:0000269|PubMed:29777959}.
CC -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC synthesis.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.
CC -!- PTM: Forms covalent cross-links mediated by a transglutaminase, such as
CC F13A or TGM2, between a glutamine and the epsilon-amino group of a
CC lysine residue, forming homopolymers and heteropolymers (e.g.
CC fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
CC {ECO: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|UniProtKB:P02751}.
CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting
CC fibronectin activation and matrix formation.
CC {ECO:0000269|PubMed:26954549}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia.
CC {ECO:0000250|UniProtKB:P07589}.
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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 PDB; 1MFN; NMR; -; A=1447-1630.
DR PDB; 2MFN; NMR; -; A=1447-1630.
DR PDBsum; 1MFN; -.
DR PDBsum; 2MFN; -.
DR AlphaFoldDB; P11276; -.
DR SMR; P11276; -.
DR BioGRID; 199719; 28.
DR CORUM; P11276; -.
DR ELM; P11276; -.
DR IntAct; P11276; 5.
DR MINT; P11276; -.
DR STRING; 10090.ENSMUSP00000054499; -.
DR GlyGen; P11276; 8 sites.
DR iPTMnet; P11276; -.
DR PhosphoSitePlus; P11276; -.
DR SwissPalm; P11276; -.
DR CPTAC; non-CPTAC-3296; -.
DR CPTAC; non-CPTAC-3538; -.
DR EPD; P11276; -.
DR jPOST; P11276; -.
DR MaxQB; P11276; -.
DR PaxDb; P11276; -.
DR PeptideAtlas; P11276; -.
DR PRIDE; P11276; -.
DR ProteomicsDB; 271764; -. [P11276-1]
DR ABCD; P11276; 8 sequenced antibodies.
DR Antibodypedia; 3522; 2765 antibodies from 49 providers.
DR DNASU; 14268; -.
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 VEuPathDB; HostDB:ENSMUSG00000026193; -.
DR eggNOG; ENOG502QPTS; Eukaryota.
DR GeneTree; ENSGT00940000155126; -.
DR InParanoid; P11276; -.
DR OMA; TTNPPMG; -.
DR PhylomeDB; P11276; -.
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 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 Reactome; R-MMU-9634597; GPER1 signaling.
DR BioGRID-ORCS; 14268; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Fn1; mouse.
DR EvolutionaryTrace; P11276; -.
DR PRO; PR:P11276; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P11276; protein.
DR Bgee; ENSMUSG00000026193; Expressed in vault of skull and 284 other tissues.
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: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; IDA:UniProtKB.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; ISO:MGI.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
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:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0150102; P:negative regulation of monocyte activation; IDA:UniProtKB.
DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISO:MGI.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; 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:0010468; P:regulation of gene expression; 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; 11.
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; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparin-binding; Isopeptide bond; Oxidation; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..32
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT CHAIN 33..2477
FT /note="Fibronectin"
FT /id="PRO_0000019236"
FT CHAIN 627..701
FT /note="Anastellin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390480"
FT DOMAIN 51..91
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 96..139
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 140..183
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 185..229
FT /note="Fibronectin type-I 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 230..274
FT /note="Fibronectin type-I 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 306..343
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 355..403
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 415..463
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 468..516
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 516..558
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 559..602
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 610..717
FT /note="Fibronectin type-III 1"
FT DOMAIN 721..811
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 812..903
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 908..997
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 998..1087
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1088..1174
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1175..1269
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1270..1358
FT /note="Fibronectin type-III 8; extra domain B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1359..1451
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1452..1539
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1540..1633
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1634..1725
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1726..1813
FT /note="Fibronectin type-III 13; extra domain A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1814..1907
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1908..1994
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1995..2085
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2193..2287
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2294..2338
FT /note="Fibronectin type-I 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2339..2381
FT /note="Fibronectin type-I 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2383..2426
FT /note="Fibronectin type-I 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND 906..1171
FT REGION 53..273
FT /note="Fibrin- and heparin-binding 1"
FT REGION 124..143
FT /note="Required for binding to Lilrb4a"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 308..608
FT /note="Collagen-binding"
FT REGION 1357..1630
FT /note="Cell-attachment"
FT REGION 1661..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..2081
FT /note="Heparin-binding 2"
FT REGION 2082..2201
FT /note="V region (type III connecting segment, IIICS)"
FT REGION 2296..2427
FT /note="Fibrin-binding 2"
FT MOTIF 1614..1616
FT /note="Cell attachment site"
FT MOTIF 2181..2183
FT /note="Cell attachment site"
FT MOD_RES 33
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 875
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 880
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2392
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2454
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 2475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 876
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770"
FT CARBOHYD 1243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 2198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT DISULFID 53..79
FT /evidence="ECO:0000250"
FT DISULFID 77..88
FT /evidence="ECO:0000250"
FT DISULFID 98..126
FT /evidence="ECO:0000250"
FT DISULFID 124..136
FT /evidence="ECO:0000250"
FT DISULFID 142..170
FT /evidence="ECO:0000250"
FT DISULFID 168..180
FT /evidence="ECO:0000250"
FT DISULFID 187..216
FT /evidence="ECO:0000250"
FT DISULFID 214..226
FT /evidence="ECO:0000250"
FT DISULFID 232..261
FT /evidence="ECO:0000250"
FT DISULFID 259..271
FT /evidence="ECO:0000250"
FT DISULFID 308..335
FT /evidence="ECO:0000250"
FT DISULFID 333..342
FT /evidence="ECO:0000250"
FT DISULFID 360..386
FT /evidence="ECO:0000250"
FT DISULFID 374..401
FT /evidence="ECO:0000250"
FT DISULFID 420..446
FT /evidence="ECO:0000250"
FT DISULFID 434..461
FT /evidence="ECO:0000250"
FT DISULFID 470..498
FT /evidence="ECO:0000250"
FT DISULFID 496..508
FT /evidence="ECO:0000250"
FT DISULFID 518..545
FT /evidence="ECO:0000250"
FT DISULFID 543..555
FT /evidence="ECO:0000250"
FT DISULFID 561..589
FT /evidence="ECO:0000250"
FT DISULFID 587..599
FT /evidence="ECO:0000250"
FT DISULFID 2296..2325
FT /evidence="ECO:0000250"
FT DISULFID 2323..2335
FT /evidence="ECO:0000250"
FT DISULFID 2341..2368
FT /evidence="ECO:0000250"
FT DISULFID 2366..2378
FT /evidence="ECO:0000250"
FT DISULFID 2385..2411
FT /evidence="ECO:0000250"
FT DISULFID 2409..2420
FT /evidence="ECO:0000250"
FT DISULFID 2458
FT /note="Interchain (with C-2462)"
FT DISULFID 2462
FT /note="Interchain (with C-2458)"
FT CROSSLNK 35
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000269|PubMed:9312106"
FT CROSSLNK 36
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000269|PubMed:9312106"
FT CROSSLNK 48
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000269|PubMed:9312106"
FT MUTAGEN 35
FT /note="Q->A: 99% decrease in cross-linking efficiency; when
FT associated with A-36 and A-48."
FT /evidence="ECO:0000269|PubMed:9312106"
FT MUTAGEN 35
FT /note="Q->L: 65% decrease in cross-linking efficiency; when
FT associated with L-36."
FT /evidence="ECO:0000269|PubMed:9312106"
FT MUTAGEN 36
FT /note="Q->A: 99% decrease in cross-linking efficiency; when
FT associated with A-35 and A-48."
FT /evidence="ECO:0000269|PubMed:9312106"
FT MUTAGEN 36
FT /note="Q->L: 65% decrease in cross-linking efficiency; when
FT associated with L-35."
FT /evidence="ECO:0000269|PubMed:9312106"
FT MUTAGEN 48
FT /note="Q->A: 99% decrease in cross-linking efficiency; when
FT associated with A-35 and A-36."
FT /evidence="ECO:0000269|PubMed:9312106"
FT CONFLICT 1063
FT /note="V -> A (in Ref. 6; CAA63654)"
FT /evidence="ECO:0000305"
FT CONFLICT 1820
FT /note="F -> L (in Ref. 6; CAA63654)"
FT /evidence="ECO:0000305"
FT CONFLICT 2440
FT /note="T -> N (in Ref. 7; AAA37636)"
FT /evidence="ECO:0000305"
FT STRAND 1455..1459
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1461..1467
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1476..1484
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1492..1496
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1501..1507
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1510..1521
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1530..1536
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1545..1550
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1553..1557
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1567..1580
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1582..1586
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1591..1594
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1600..1612
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1615..1617
FT /evidence="ECO:0007829|PDB:1MFN"
FT STRAND 1624..1630
FT /evidence="ECO:0007829|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
