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Entry version 159 (16 Jan 2019)
Sequence version 4 (16 Dec 2008)
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Protein

Fibronectin

Gene

FN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity).By similarity
Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi908 – 1173Add BLAST266

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • disordered domain specific binding Source: CAFA
  • heparin binding Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHeparin-binding
Biological processAcute phase, Angiogenesis, Cell adhesion, Cell shape

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Cleaved into the following chain:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FN1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 32By similarityAdd BLAST32
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000015852733 – 2478FibronectinAdd BLAST2446
ChainiPRO_0000390478628 – 702AnastellinBy similarityAdd BLAST75

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei33Pyrrolidone carboxylic acidBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki48Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi53 ↔ 79By similarity
Disulfide bondi77 ↔ 88By similarity
Disulfide bondi98 ↔ 126By similarity
Disulfide bondi124 ↔ 136By similarity
Disulfide bondi142 ↔ 170By similarity
Disulfide bondi168 ↔ 180By similarity
Disulfide bondi187 ↔ 216By similarity
Disulfide bondi214 ↔ 226By similarity
Disulfide bondi232 ↔ 261By similarity
Disulfide bondi259 ↔ 271By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi280O-linked (GalNAc...) threonine1 Publication1
Modified residuei286PhosphoserineBy similarity1
Disulfide bondi309 ↔ 336By similarity
Disulfide bondi334 ↔ 343By similarity
Disulfide bondi361 ↔ 387By similarity
Disulfide bondi375 ↔ 402By similarity
Disulfide bondi421 ↔ 447By similarity
Glycosylationi431N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 462By similarity
Disulfide bondi471 ↔ 499By similarity
Disulfide bondi497 ↔ 509By similarity
Disulfide bondi519 ↔ 546By similarity
Glycosylationi529N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi543N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi544 ↔ 556By similarity
Disulfide bondi562 ↔ 590By similarity
Disulfide bondi588 ↔ 600By similarity
Modified residuei877SulfotyrosineSequence analysis1
Glycosylationi878N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei882SulfotyrosineSequence analysis1
Glycosylationi1008N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1245N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1292N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2156O-linked (GalNAc...) threonine1 Publication1
Glycosylationi2157O-linked (GalNAc...) threonine1 Publication1
Glycosylationi2200N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2298 ↔ 2327By similarity
Disulfide bondi2325 ↔ 2337By similarity
Disulfide bondi2343 ↔ 2370By similarity
Disulfide bondi2368 ↔ 2380By similarity
Disulfide bondi2387 ↔ 2413By similarity
Modified residuei2394SulfotyrosineSequence analysis1
Disulfide bondi2411 ↔ 2422By similarity
Modified residuei2455PhosphothreonineBy similarity1
Disulfide bondi2459Interchain (with C-2462)PROSITE-ProRule annotation
Disulfide bondi2463Interchain (with C-2458)PROSITE-ProRule annotation
Modified residuei2476Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sulfated.By similarity
Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.By similarity
Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Oxidation, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P07589

PeptideAtlas

More...
PeptideAtlasi
P07589

PRoteomics IDEntifications database

More...
PRIDEi
P07589

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
721

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07589

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P07589

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, FBLN7, AMBP, TNR, LGALS3BP, COL13A1 and COMP (By similarity). Interacts with TNR; the interaction mediates inhibition of cell adhesion and neurite outgrowth. Interacts with FST3 and MYOC (By similarity).By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
PCOLCEQ151132EBI-11147184,EBI-8869614From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P07589, 7 interactors

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000010925

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P07589

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P07589

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini51 – 91Fibronectin type-I 1PROSITE-ProRule annotationAdd BLAST41
Domaini96 – 139Fibronectin type-I 2PROSITE-ProRule annotationAdd BLAST44
Domaini140 – 183Fibronectin type-I 3PROSITE-ProRule annotationAdd BLAST44
Domaini185 – 229Fibronectin type-I 4PROSITE-ProRule annotationAdd BLAST45
Domaini230 – 274Fibronectin type-I 5PROSITE-ProRule annotationAdd BLAST45
Domaini307 – 344Fibronectin type-I 6PROSITE-ProRule annotationAdd BLAST38
Domaini356 – 404Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini416 – 464Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini469 – 517Fibronectin type-I 7PROSITE-ProRule annotationAdd BLAST49
Domaini517 – 559Fibronectin type-I 8PROSITE-ProRule annotationAdd BLAST43
Domaini560 – 603Fibronectin type-I 9PROSITE-ProRule annotationAdd BLAST44
Domaini611 – 706Fibronectin type-III 1Add BLAST96
Domaini718 – 813Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini814 – 903Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST90
Domaini910 – 1001Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST92
Domaini1002 – 1089Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST88
Domaini1090 – 1176Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST87
Domaini1177 – 1271Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST95
Domaini1272 – 1360Fibronectin type-III 8; extra domain 1PROSITE-ProRule annotationAdd BLAST89
Domaini1361 – 1452Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST92
Domaini1453 – 1541Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST89
Domaini1542 – 1635Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST94
Domaini1636 – 1727Fibronectin type-III 12PROSITE-ProRule annotationAdd BLAST92
Domaini1728 – 1815Fibronectin type-III 13; extra domain 2PROSITE-ProRule annotationAdd BLAST88
Domaini1816 – 1909Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST94
Domaini1910 – 1996Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST87
Domaini1997 – 2087Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST91
Domaini2195 – 2289Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST95
Domaini2296 – 2340Fibronectin type-I 10PROSITE-ProRule annotationAdd BLAST45
Domaini2341 – 2383Fibronectin type-I 11PROSITE-ProRule annotationAdd BLAST43
Domaini2385 – 2428Fibronectin type-I 12PROSITE-ProRule annotationAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni53 – 273Fibrin- and heparin-binding 1Add BLAST221
Regioni309 – 609Collagen-bindingAdd BLAST301
Regioni1359 – 1632Cell-attachmentAdd BLAST274
Regioni1813 – 2083Heparin-binding 2Add BLAST271
Regioni2084 – 2203Connecting strand 3 (CS-3) (V region)Add BLAST120
Regioni2298 – 2429Fibrin-binding 2Add BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1616 – 1618Cell attachment siteBy similarity3
Motifi2183 – 2185Cell attachment siteBy similarity3

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IF4N Eukaryota
ENOG410Y2NH LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234344

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005731

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07589

Database of Orthologous Groups

More...
OrthoDBi
6580at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 16 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.10.10.10, 2 hits
2.60.40.10, 17 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000083 Fibronectin_type1
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR013783 Ig-like_fold
IPR013806 Kringle-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00039 fn1, 12 hits
PF00040 fn2, 2 hits
PF00041 fn3, 16 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 17 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265 SSF49265, 11 hits
SSF57440 SSF57440, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00022 EGF_1, 2 hits
PS01253 FN1_1, 12 hits
PS51091 FN1_2, 12 hits
PS00023 FN2_1, 2 hits
PS51092 FN2_2, 2 hits
PS50853 FN3, 17 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoform i produced by alternative splicing. AlignAdd to basket
Note: A number of isoforms are produced. Each of the "extra domain" and the connecting strand 3 are present in some forms of fibronectin and absent in others.
Isoform 1 (identifier: P07589-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLGGPGPGLL LLLAVLSLGT AVPSAGASKS RRQAQQIVQP QSPLTVSQSK
60 70 80 90 100
PGCYDNGKHY QINQQWERTY LGSALVCTCY GGSRGFNCES KPEPEETCFD
110 120 130 140 150
KYTGNTYRVG DTYERPKDSM IWDCTCIGAG RGRISCTIAN RCHEGGQSYK
160 170 180 190 200
IGDTWRRPHE TGGYMLECVC LGNGKGEWTC KPIAEKCFDQ AAGTSYVVGE
210 220 230 240 250
TWEKPYQGWM MVDCTCLGEG SGRITCTSRN RCNDQDTRTS YRIGDTWSKK
260 270 280 290 300
DNRGNLLQCI CTGNGRGEWK CERHTSLQTT SAGSGSFTDV RTAIYQPQPH
310 320 330 340 350
PQPPPYGHCV TDSGVVYSVG MQWLKTQGNK QMLCTCLGNG VSCQETAVTQ
360 370 380 390 400
TYGGNSNGEP CVLPFTYNGK TFYSCTTEGR QDGHLWCSTT SNYEQDQKYS
410 420 430 440 450
FCTDHTVLVQ TRGGNSNGAL CHFPFLYNNH NYTDCTSEGR RDNMKWCGTT
460 470 480 490 500
QNYDADQKFG FCPMAAHEEI CTTNEGVMYR IGDQWDKQHD MGHMMRCTCV
510 520 530 540 550
GNGRGEWTCV AYSQLRDQCI VDGITYNVND TFHKRHEEGH MLNCTCFGQG
560 570 580 590 600
RGRWKCDPVD QCQDSETRTF YQIGDSWEKY LQGVRYQCYC YGRGIGEWAC
610 620 630 640 650
QPLQTYPDTS GPVQVIITET PSQPNSHPIQ WSAPESSHIS KYILRWKPKN
660 670 680 690 700
SPDRWKEATI PGHLNSYTIK GLRPGVVYEG QLISVQHYGQ REVTRFDFTT
710 720 730 740 750
TSTSPAVTSN TVTGETTPLS PVVATSESVT EITASSFVVS WVSASDTVSG
760 770 780 790 800
FRVEYELSEE GDEPQYLDLP STATSVNIPD LLPGRKYTVN VYEISEEGEQ
810 820 830 840 850
NLILSTSQTT APDAPPDPTV DQVDDTSIVV RWSRPRAPIT GYRIVYSPSV
860 870 880 890 900
EGSSTELNLP ETANSVTLSD LQPGVQYNIT IYAVEENQES TPVFIQQETT
910 920 930 940 950
GVPRSDKVPP PRDLQFVEVT DVKITIMWTP PESPVTGYRV DVIPVNLPGE
960 970 980 990 1000
HGQRLPVSRN TFAEVTGLSP GVTYHFKVFA VNQGRESKPL TAQQATKLDA
1010 1020 1030 1040 1050
PTNLQFINET DTTVIVTWTP PRARIVGYRL TVGLTRGGQP KQYNVGPAAS
1060 1070 1080 1090 1100
QYPLRNLQPG SEYAVSLVAV KGNQQSPRVT GVFTTLQPLG SIPHYNTEVT
1110 1120 1130 1140 1150
ETTIVITWTP APRIGFKLGV RPSQGGEAPR EVTSESGSIV VSGLTPGVEY
1160 1170 1180 1190 1200
VYTISVLRDG QERDAPIVKK VVTPLSPPTN LHLEANPDTG VLTVSWERST
1210 1220 1230 1240 1250
TPDITGYRIT TTPTNGQQGY SLEEVVHADQ SSCTFENLSP GLEYNVSVYT
1260 1270 1280 1290 1300
VKDDKESVPI SDTIIPEVPQ LTDLSFVDIT DSSIGLRWTP LNSSTIIGYR
1310 1320 1330 1340 1350
ITVVAAGEGI PIFEDFVDSS VGYYTVTGLE PGIDYDISVI TLINGGESAP
1360 1370 1380 1390 1400
TTLTQQTAVP PPTDLRFTNV GPDTMRVTWA PPSSIELTNL LVRYSPVKNE
1410 1420 1430 1440 1450
EDVAELSISP SDNAVVLTNL LPGTEYLVSV SSVYEQHESI PLRGRQKTAL
1460 1470 1480 1490 1500
DSPSGIDFSD ITANSFTVHW IAPRATITGY RIRHHPENMG GRPREDRVPP
1510 1520 1530 1540 1550
SRNSITLTNL NPGTEYVVSI VALNSKEESL PLVGQQSTVS DVPRDLEVIA
1560 1570 1580 1590 1600
ATPTSLLISW DAPAVTVRYY RITYGETGGS SPVQEFTVPG SKSTATISGL
1610 1620 1630 1640 1650
KPGVDYTITV YAVTGRGDSP ASSKPVSINY RTEIDKPSQM QVTDVQDNSI
1660 1670 1680 1690 1700
SVRWLPSSSP VTGYRVTTAP KNGPGPSKTK TVGPDQTEMT IEGLQPTVEY
1710 1720 1730 1740 1750
VVSVYAQNQN GESQPLVQTA VTNIDRPKGL AFTDVDVDSI KIAWESPQGQ
1760 1770 1780 1790 1800
VSRYRVTYSS PEDGIHELFP APDGEEETAE LQGLRPGSEY TVSVVALHDD
1810 1820 1830 1840 1850
MESQPLIGTQ STTIPAPTNL KFTQVTPTSL TAQWTAPNVQ LTGYRVRVTP
1860 1870 1880 1890 1900
KEKTGPMKEI NLAPDSSSVV VSGLMVATKY EVSVYALKDT LTSRPAQGVV
1910 1920 1930 1940 1950
TTLENVSPPR RARVTDATET TITISWRTKT ETITGFQVDA IPANGQTPIQ
1960 1970 1980 1990 2000
RTIRPDVRSY TITGLQPGTD YKIHLYTLND NARSSPVVID ASTAIDAPSN
2010 2020 2030 2040 2050
LRFLATTPNS LLVSWQPPRA RITGYIIKYE KPGSPPREVV PRPRPGVTEA
2060 2070 2080 2090 2100
TITGLEPGTE YTIQVIALKN NQKSEPLIGR KKTDELPQLV TLPHPNLHGP
2110 2120 2130 2140 2150
EILDVPSTVQ KTPFITNPGY DTGNGIQLPG TSGQQPSLGQ QMIFEEHGFR
2160 2170 2180 2190 2200
RTTPPTTATP VRHRPRPYPP NVNEEIQIGH VPRGDVDHHL YPHVVGLNPN
2210 2220 2230 2240 2250
ASTGQEALSQ TTISWTPFQE SSEYIISCHP VGIDEEPLQF RVPGTSASAT
2260 2270 2280 2290 2300
LTGLTRGATY NIIVEAVKDQ QRQKVREEVV TVGNSVDQGL SQPTDDSCFD
2310 2320 2330 2340 2350
PYTVSHYAIG EEWERLSDSG FKLSCQCLGF GSGHFRCDSS KWCHDNGVNY
2360 2370 2380 2390 2400
KIGEKWDRQG ENGQMMSCTC LGNGKGEFKC DPHEATCYDD GKTYHVGEQW
2410 2420 2430 2440 2450
QKEYLGAICS CTCFGGQRGW RCDNCRRPGA EPGNEGSTAH SYNQYSQRYH
2460 2470
QRTNTNVNCP IECFMPLDVQ ADREDSRE
Length:2,478
Mass (Da):272,154
Last modified:December 16, 2008 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2BAD301A8112FEDC
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AAFC03125045 Genomic DNA No translation available.
AAFC03065407 Genomic DNA No translation available.
K00800 mRNA Translation: AAA30521.2

Protein sequence database of the Protein Information Resource

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PIRi
A26452 FNBO

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Bt.23418

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFC03125045 Genomic DNA No translation available.
AAFC03065407 Genomic DNA No translation available.
K00800 mRNA Translation: AAA30521.2
PIRiA26452 FNBO
UniGeneiBt.23418

3D structure databases

ProteinModelPortaliP07589
SMRiP07589
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07589, 7 interactors
STRINGi9913.ENSBTAP00000010925

PTM databases

GlyConnecti721
iPTMnetiP07589
UniCarbKBiP07589

Proteomic databases

PaxDbiP07589
PeptideAtlasiP07589
PRIDEiP07589

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IF4N Eukaryota
ENOG410Y2NH LUCA
HOGENOMiHOG000234344
HOVERGENiHBG005731
InParanoidiP07589
OrthoDBi6580at2759

Family and domain databases

CDDicd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 16 hits
Gene3Di2.10.10.10, 2 hits
2.60.40.10, 17 hits
InterProiView protein in InterPro
IPR000083 Fibronectin_type1
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR013783 Ig-like_fold
IPR013806 Kringle-like
PfamiView protein in Pfam
PF00039 fn1, 12 hits
PF00040 fn2, 2 hits
PF00041 fn3, 16 hits
SMARTiView protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 17 hits
SUPFAMiSSF49265 SSF49265, 11 hits
SSF57440 SSF57440, 2 hits
PROSITEiView protein in PROSITE
PS00022 EGF_1, 2 hits
PS01253 FN1_1, 12 hits
PS51091 FN1_2, 12 hits
PS00023 FN2_1, 2 hits
PS51092 FN2_2, 2 hits
PS50853 FN3, 17 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFINC_BOVIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07589
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 16, 2008
Last modified: January 16, 2019
This is version 159 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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