P11276 · FINC_MOUSE

  • Protein
    Fibronectin
  • Gene
    Fn1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (By similarity).
Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape (By similarity).
Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (PubMed:21768292).
Participates in the regulation of type I collagen deposition by osteoblasts (PubMed:21768292).
Acts as a ligand for the Lilrb4a receptor, inhibiting Fcgr1/CD64-mediated monocyte activation (PubMed:34089617).
Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling.

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.

Features

Showing features for dna binding.

TypeIDPosition(s)Description
DNA binding906-1171

GO annotations

AspectTerm
Cellular Componentapical plasma membrane
Cellular Componentbasement membrane
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentendoplasmic reticulum-Golgi intermediate compartment
Cellular Componentextracellular exosome
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Cellular Componentfibrinogen complex
Molecular Functionheparin binding
Molecular Functionidentical protein binding
Molecular Functionintegrin binding
Molecular Functionmercury ion binding
Molecular Functionpeptidase activator activity
Molecular Functionprotease binding
Molecular Functionproteoglycan binding
Molecular Functionreceptor ligand activity
Molecular Functionsignaling receptor binding
Biological Processacute-phase response
Biological Processangiogenesis
Biological Processbiological process involved in interaction with symbiont
Biological Processcalcium-independent cell-matrix adhesion
Biological Processcell adhesion
Biological Processcell-matrix adhesion
Biological Processcell-substrate junction assembly
Biological Processcellular response to interleukin-1
Biological Processcellular response to mercury ion
Biological Processendodermal cell differentiation
Biological Processextracellular matrix organization
Biological Processglial cell migration
Biological Processheart development
Biological Processintegrin activation
Biological Processintegrin-mediated signaling pathway
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of collagen biosynthetic process
Biological Processnegative regulation of monocyte activation
Biological Processnegative regulation of transforming growth factor beta production
Biological Processnervous system development
Biological Processneural crest cell migration involved in autonomic nervous system development
Biological Processpositive regulation of axon extension
Biological Processpositive regulation of cell migration
Biological Processpositive regulation of chemotaxis
Biological Processpositive regulation of fibroblast proliferation
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processpositive regulation of substrate-dependent cell migration, cell attachment to substrate
Biological Processregulation of cell shape
Biological Processregulation of ERK1 and ERK2 cascade
Biological Processregulation of protein phosphorylation
Biological Processresponse to muscle activity
Biological Processsubstrate adhesion-dependent cell spreading
Biological Processwound healing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fibronectin
  • Short names
    FN
  • Cleaved into 1 chains

Gene names

    • Name
      Fn1

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N-3
    • NMRI
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P11276
  • Secondary accessions
    • G5E8B8
    • Q61567
    • Q61568
    • Q61569
    • Q64233
    • Q80UI4

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Muscle-specific mutant mice show comparable body weight, glucose tolerance test (GTT) and insulin tolerance test (ITT) with control mice. After high fat diet (HFD) feeding and exercise training, control and mutant mice have a similar body weight and liver and muscle tissue weight but daily exercise training improves GTT and ITT values in HFD-fed control mice but not in HFD-fed mutants.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis3599% decrease in cross-linking efficiency; when associated with A-36 and A-48.
Mutagenesis3565% decrease in cross-linking efficiency; when associated with L-36.
Mutagenesis3699% decrease in cross-linking efficiency; when associated with A-35 and A-48.
Mutagenesis3665% decrease in cross-linking efficiency; when associated with L-35.
Mutagenesis4899% decrease in cross-linking efficiency; when associated with A-35 and A-36.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 94 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, modified residue, chain, cross-link, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-32
Modified residue33Pyrrolidone carboxylic acid
ChainPRO_000001923633-2477Fibronectin
Cross-link35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-link36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-link48Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Disulfide bond53↔79
Disulfide bond77↔88
Disulfide bond98↔126
Disulfide bond124↔136
Disulfide bond142↔170
Disulfide bond168↔180
Disulfide bond187↔216
Disulfide bond214↔226
Disulfide bond232↔261
Disulfide bond259↔271
Modified residue285Phosphoserine
Disulfide bond308↔335
Disulfide bond333↔342
Disulfide bond360↔386
Disulfide bond374↔401
Disulfide bond420↔446
Glycosylation430N-linked (GlcNAc...) asparagine
Disulfide bond434↔461
Disulfide bond470↔498
Disulfide bond496↔508
Disulfide bond518↔545
Glycosylation528N-linked (GlcNAc...) asparagine
Glycosylation542N-linked (GlcNAc...) asparagine
Disulfide bond543↔555
Disulfide bond561↔589
Disulfide bond587↔599
ChainPRO_0000390480627-701Anastellin
Modified residue875Sulfotyrosine
Glycosylation876N-linked (GlcNAc...) asparagine
Modified residue880Sulfotyrosine
Glycosylation1006N-linked (GlcNAc...) asparagine
Glycosylation1243N-linked (GlcNAc...) asparagine
Glycosylation1290N-linked (GlcNAc...) asparagine
Glycosylation2198N-linked (GlcNAc...) asparagine
Disulfide bond2296↔2325
Disulfide bond2323↔2335
Disulfide bond2341↔2368
Disulfide bond2366↔2378
Disulfide bond2385↔2411
Modified residue2392Sulfotyrosine
Disulfide bond2409↔2420
Modified residue2454Phosphothreonine
Disulfide bond2458Interchain (with C-2462)
Disulfide bond2462Interchain (with C-2458)
Modified residue2475Phosphoserine

Post-translational modification

Sulfated.
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).
Phosphorylated by FAM20C in the extracellular medium.
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.
Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.
Serotonylated on Gln residues by TGM2 in response to hypoxia.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level) (PubMed:29777959).
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

Induction

Glucocorticoids suppressed mRNA expression and protein synthesis.

Gene expression databases

Interaction

Subunit

Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity).
Interacts with COMP. Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain); this interaction enhances fibronectin fibril assembly. TNFAIP6 may act as a bridging molecule between FN1 and THBS1 (By similarity).
Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity).
Interacts with FST3 and MYOC (By similarity).
Interacts with SVEP1 (PubMed:36792666).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P11276Plcg2 Q8CIH56EBI-641955, EBI-617954

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, motif.

TypeIDPosition(s)Description
Domain51-91Fibronectin type-I 1
Region53-273Fibrin- and heparin-binding 1
Domain96-139Fibronectin type-I 2
Region124-143Required for binding to Lilrb4a
Domain140-183Fibronectin type-I 3
Domain185-229Fibronectin type-I 4
Domain230-274Fibronectin type-I 5
Domain306-343Fibronectin type-I 6
Region308-608Collagen-binding
Domain355-403Fibronectin type-II 1
Domain415-463Fibronectin type-II 2
Domain468-516Fibronectin type-I 7
Domain516-558Fibronectin type-I 8
Domain559-602Fibronectin type-I 9
Domain610-717Fibronectin type-III 1
Domain721-811Fibronectin type-III 2
Domain812-903Fibronectin type-III 3
Domain908-997Fibronectin type-III 4
Domain998-1087Fibronectin type-III 5
Domain1088-1174Fibronectin type-III 6
Domain1175-1269Fibronectin type-III 7
Domain1270-1358Fibronectin type-III 8; extra domain B
Region1357-1630Cell-attachment
Domain1359-1451Fibronectin type-III 9
Domain1452-1539Fibronectin type-III 10
Domain1540-1633Fibronectin type-III 11
Motif1614-1616Cell attachment site
Domain1634-1725Fibronectin type-III 12
Region1661-1684Disordered
Domain1726-1813Fibronectin type-III 13; extra domain A
Region1811-2081Heparin-binding 2
Domain1814-1907Fibronectin type-III 14
Domain1908-1994Fibronectin type-III 15
Domain1995-2085Fibronectin type-III 16
Region2082-2201V region (type III connecting segment, IIICS)
Motif2181-2183Cell attachment site
Domain2193-2287Fibronectin type-III 17
Domain2294-2338Fibronectin type-I 10
Region2296-2427Fibrin-binding 2
Domain2339-2381Fibronectin type-I 11
Domain2383-2426Fibronectin type-I 12

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. The diversity of isoforms depends on the V region and either of the two extra domain which can be either included or excluded (partially or completely for the V region).

P11276-1

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.

  • Length
    2,477
  • Mass (Da)
    272,538
  • Last updated
    2012-10-03 v4
  • Checksum
    24A207BE67F85585
MLRGPGPGRLLLLAVLCLGTSVRCTEAGKSKRQAQQIVQPQSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHALQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSASTPVTSNTVTGETAPYSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGTPRSDNVPPPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTSLEEVVHADQSSCTFENLNPGLEYNVSVYTVKDDKESAPISDTVVPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSDIPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTTPKNGLGPSKTKTASPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIRELFPAPDGEDDTAELQGLRPGSEYTVSVVALHDDMESQPLIGIQSTAIPAPTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTENGIQLPGTTHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALQNQRRHKVREEVVTVGNAVSEGLNQPTDDSCFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYNQRTNTNVNCPIECFMPLDVQADRDDSRE

Computationally mapped potential isoform sequences

There are 11 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q4KL80Q4KL80_MOUSEFn1383
Q3UHL6Q3UHL6_MOUSEFn12361
B7ZNJ1B7ZNJ1_MOUSEFn12176
A0A087WQE0A0A087WQE0_MOUSEFn171
A0A087WR50A0A087WR50_MOUSEFn12386
A0A087WQW8A0A087WQW8_MOUSEFn1160
A0A087WS56A0A087WS56_MOUSEFn12266
A0A087WS99A0A087WS99_MOUSEFn1200
A0A087WSU6A0A087WSU6_MOUSEFn167
A0A087WSN6A0A087WSN6_MOUSEFn12296
B9EHT6B9EHT6_MOUSEFn12271

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict1063in Ref. 6; CAA63654
Sequence conflict1820in Ref. 6; CAA63654
Sequence conflict2440in Ref. 7; AAA37636

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC124821
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466548
EMBL· GenBank· DDBJ
EDL00265.1
EMBL· GenBank· DDBJ
Genomic DNA
BC051082
EMBL· GenBank· DDBJ
-mRNA No translation available.
Z22729
EMBL· GenBank· DDBJ
CAA80422.1
EMBL· GenBank· DDBJ
Genomic DNA
X82402
EMBL· GenBank· DDBJ
CAA57796.1
EMBL· GenBank· DDBJ
mRNA
X93167
EMBL· GenBank· DDBJ
CAA63654.1
EMBL· GenBank· DDBJ
mRNA
M18194
EMBL· GenBank· DDBJ
AAA37636.1
EMBL· GenBank· DDBJ
mRNA
S45680
EMBL· GenBank· DDBJ
AAB23491.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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