FINC_RAT
ID FINC_RAT Reviewed; 2477 AA.
AC P04937; Q6LDX9;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Fibronectin {ECO:0000305};
DE Short=FN;
DE Contains:
DE RecName: Full=Anastellin;
DE Flags: Precursor;
GN Name=Fn1 {ECO:0000312|RGD:2624};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=2445560; DOI=10.1002/j.1460-2075.1987.tb02547.x;
RA Scwarzbauer J.E., Patel R.S., Fonda D., Hynes R.O.;
RT "Multiple sites of alternative splicing of the rat fibronectin gene
RT transcript.";
RL EMBO J. 6:2573-2580(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139 AND 2382-2477.
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=3119323; DOI=10.1002/j.1460-2075.1987.tb02545.x;
RA Patel R.S., Odermatt E., Schwarzbauer J.E., Hynes R.O.;
RT "Organization of the fibronectin gene provides evidence for exon shuffling
RT during evolution.";
RL EMBO J. 6:2565-2572(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1586-2477.
RX PubMed=6317187; DOI=10.1016/0092-8674(83)90175-7;
RA Schwarzbauer J.E., Tamkun J.W., Lemischka I.R., Hynes R.O.;
RT "Three different fibronectin mRNAs arise by alternative splicing within the
RT coding region.";
RL Cell 35:421-431(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1722-1810, AND ALTERNATIVE SPLICING.
RX PubMed=3863113; DOI=10.1073/pnas.82.19.6571;
RA Odermatt E., Tamkun J.W., Hynes R.O.;
RT "Repeating modular structure of the fibronectin gene: relationship to
RT protein structure and subunit variation.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6571-6575(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2052-2237, AND ALTERNATIVE SPLICING.
RX PubMed=6089177; DOI=10.1073/pnas.81.16.5140;
RA Tamkun J.W., Schwarzbauer J.E., Hynes R.O.;
RT "A single rat fibronectin gene generates three different mRNAs by
RT alternative splicing of a complex exon.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5140-5144(1984).
RN [6]
RP PROTEIN SEQUENCE OF 1183-1192; 1385-1399 AND 2287-2300, AND INTERACTION
RP WITH AMBP.
RX PubMed=7519849; DOI=10.1042/bj3010745;
RA Falkenberg C., Enghild J.J., Thoegersen I.B., Salvesen G., Aakerstroem B.;
RT "Isolation and characterization of fibronectin-alpha 1-microglobulin
RT complex in rat plasma.";
RL Biochem. J. 301:745-751(1994).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-2475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER CYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC including collagen, fibrin, heparin, DNA, and actin. Fibronectins are
CC involved in cell adhesion, cell motility, opsonization, wound healing,
CC and 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. Participates
CC in the regulation of type I collagen deposition by osteoblasts (By
CC similarity). {ECO:0000250|UniProtKB:P02751,
CC ECO:0000250|UniProtKB:P11276}.
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 P04937; P34901: Sdc4; NbExp=2; IntAct=EBI-6127274, EBI-1173182;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
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=P04937-1; Sequence=Displayed;
CC Name=2; Synonyms=FNIII-13-less;
CC IsoId=P04937-2; Sequence=VSP_003258;
CC Name=3; Synonyms=Lambda-RLF4-5;
CC IsoId=P04937-3; Sequence=VSP_003259;
CC Name=4; Synonyms=Lambda-RLF6;
CC IsoId=P04937-4; Sequence=VSP_003260;
CC -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by
CC hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms),
CC made by fibroblasts, epithelial and other cell types, is deposited as
CC fibrils in the extracellular matrix.
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:0000250|UniProtKB:P11276}.
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:0000250|UniProtKB:P11276}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia.
CC {ECO:0000250|UniProtKB:P07589}.
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DR EMBL; X15906; CAA34020.1; -; mRNA.
DR EMBL; L29191; AAA41166.1; -; Genomic_DNA.
DR EMBL; L00191; AAA41166.1; JOINED; Genomic_DNA.
DR EMBL; L29191; AAA41167.1; -; Genomic_DNA.
DR EMBL; L00191; AAA41167.1; JOINED; Genomic_DNA.
DR EMBL; L29191; AAA41168.1; -; Genomic_DNA.
DR EMBL; L00191; AAA41168.1; JOINED; Genomic_DNA.
DR EMBL; M11750; AAA41170.1; -; Genomic_DNA.
DR EMBL; X05831; CAA29278.1; -; Genomic_DNA.
DR EMBL; X05832; CAA29279.1; -; Genomic_DNA.
DR EMBL; X05833; CAA29280.1; -; Genomic_DNA.
DR EMBL; X05834; CAA29281.1; -; Genomic_DNA.
DR PIR; S14428; S14428.
DR AlphaFoldDB; P04937; -.
DR SMR; P04937; -.
DR IntAct; P04937; 3.
DR MINT; P04937; -.
DR STRING; 10116.ENSRNOP00000019772; -.
DR CarbonylDB; P04937; -.
DR GlyGen; P04937; 9 sites.
DR iPTMnet; P04937; -.
DR PhosphoSitePlus; P04937; -.
DR jPOST; P04937; -.
DR PaxDb; P04937; -.
DR PeptideAtlas; P04937; -.
DR PRIDE; P04937; -.
DR ABCD; P04937; 2 sequenced antibodies.
DR UCSC; RGD:2624; rat. [P04937-1]
DR RGD; 2624; Fn1.
DR eggNOG; ENOG502QPTS; Eukaryota.
DR InParanoid; P04937; -.
DR PhylomeDB; P04937; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1474244; Extracellular matrix organization.
DR Reactome; R-RNO-1566977; Fibronectin matrix formation.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-354192; Integrin signaling.
DR Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-9634597; GPER1 signaling.
DR PRO; PR:P04937; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005577; C:fibrinogen complex; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:RGD.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0045340; F:mercury ion binding; IDA:RGD.
DR GO; GO:0016504; F:peptidase activator activity; ISO:RGD.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
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:RGD.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; ISO:RGD.
DR GO; GO:0001775; P:cell activation; IMP:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:RGD.
DR GO; GO:0007044; P:cell-substrate junction assembly; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IMP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071288; P:cellular response to mercury ion; IDA:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEP:RGD.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:RGD.
DR GO; GO:0008347; P:glial cell migration; IDA:RGD.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:0150102; P:negative regulation of monocyte activation; ISO:RGD.
DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; ISO:RGD.
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:RGD.
DR GO; GO:0001503; P:ossification; TAS:RGD.
DR GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0010193; P:response to ozone; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
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 Acute phase; Alternative splicing; Angiogenesis; Cell adhesion; Cell shape;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparin-binding; Isopeptide bond; Oxidation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:26479776"
FT CHAIN 25..2477
FT /note="Fibronectin"
FT /id="PRO_0000019237"
FT CHAIN 627..701
FT /note="Anastellin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390481"
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..345
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 355..403
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 415..463
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 468..511
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 516..558
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 559..602
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 610..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..901
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..2286
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 308..608
FT /note="Collagen-binding"
FT REGION 1357..1630
FT /note="Cell-attachment"
FT REGION 1661..1685
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 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
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:0000255"
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:0000255"
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:0000255"
FT CARBOHYD 2154
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:P11276"
FT CROSSLNK 36
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 48
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT VAR_SEQ 1720..1809
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003258"
FT VAR_SEQ 2082..2200
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003260"
FT VAR_SEQ 2082..2106
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003259"
FT CONFLICT 2318
FT /note="G -> A (in Ref. 3; AAA41166/AAA41167/AAA41168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2477 AA; 272511 MW; B4391A472ECEDEB5 CRC64;
MLRGPGPGRL LLLAVLCLGT SVRCTETGKS KRQAQQIVQP PSPVAVSQSK PGCFDNGKHY
QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYKVG DTYERPKDSM
IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDKWRRPHE TGGYMLECLC LGNGKGEWTC
KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS
YRIGDTWSKK DNRGNLLQCV CTGNGRGEWK CERHVLQSAS AGSGSFTDVR TAIYQPQTHP
QPAPYGHCVT DSGVVYSVGM QWLKSQGDKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
VLPFHYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHAVLVQT RGGNSNGALC
HFPFLYSNRN YSDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI
GDQWDKQHDL GHMMRCTCVG NGRGQWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
LNCTCFGQGR GRWKCDPIDR CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS TGRWKEATIP
GHLNSYTIKG LTPGVIYEGQ LISIQQYGHQ EVTRFDFTTS ASTPVTSNTV TGETAPFSPV
VATSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL
PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY
RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGV
PRSDDVPAPK DLQFVEVTDV KVTIMWTPPN SAVTGYRVDV LPVNLPGEHG QRLPVNRNTF
AEVTGLSPGV TYLFKVFAVH QGRESKPLTA QQTTKLDAPT NLQFVNETDR TVLVTWTPPR
ARIAGYRLTV GLTRGGQPKQ YNVGPMASKY PLRNLQPGSE YTVTLMAVKG NQQSPKATGV
FTTLQPLRSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS
GLTPGVEYTY TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP
DITGYRITTT PTNGQQGTAL EEVVHADQSS CTFENRNPGL EYNVSVYTVK DDKESAPISD
TVIPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT VVAAGEGIPI FEDFVDSSVG
YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP
PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL
RGRQKTGLDS PTGFDSSDVT ANSFTVHWVA PRAPITGYII RHHAEHSAGR PRQDRVPPSR
NSITLTNLNP GTEYIVTIIA VNGREESPPL IGQQSTVSDV PRDLEVIAST PTSLLISWEP
PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP GADYTITLYA VTGRGDSPAS
SKPVSINYQT EIDKPSQMQV TDVQDNSISV RWLPSTSPVT GYRVTTAPKN GLGPTKSQTV
SPDQTEMTIE GLQPTVEYVV SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI
AWESPQGQVS RYRVTYSSPE DGIHELFPAP DGDEDTAELH GLRPGSEYTV SVVALHGGME
SQPLIGVQST AIPAPTNLKF TQVSPTTLTA QWTAPSVKLT GYRVRVTPKE KTGPMKEINL
SPDSTSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVVTT LENVSPPRRA RVTDATETTI
TISWRTKTET ITGFQVDAIP ANGQTPVQRT ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA
RSSPVVIDAS TAIDAPSNLR FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR
PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI
LDVPSTVQKT PFVTNPGYDT ENGIQLPGTS HQQPSVGQQM IFEEHGFRRT TPPTAATPVR
LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT ISWTPFQESS
EYIISCQPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALHNQRR HKVREEVVTV
GNTVNEGLNQ PTDDSCFDPY TVSHYAVGEE WERLSDSGFK LTCQCLGFGS GHFRCDSSKW
CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYHQ RTNTNVNCPI
ECFMPLDVQA DRDDSRE
