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P11276

- FINC_MOUSE

UniProt

P11276 - FINC_MOUSE

Protein

Fibronectin

Gene

Fn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 4 (03 Oct 2012)
      Previous versions | rss
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    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 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.1 Publication
    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)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi906 – 1171266Add
    BLAST

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. peptidase activator activity Source: MGI
    3. protein binding Source: IntAct

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. angiogenesis Source: UniProtKB-KW
    3. calcium-independent cell-matrix adhesion Source: MGI
    4. cell adhesion Source: MGI
    5. cell-matrix adhesion Source: MGI
    6. cell-substrate junction assembly Source: MGI
    7. peptide cross-linking Source: Ensembl
    8. positive regulation of axon extension Source: MGI
    9. positive regulation of peptidase activity Source: GOC
    10. regulation of cell shape Source: UniProtKB-KW
    11. substrate adhesion-dependent cell spreading Source: Ensembl
    12. wound healing Source: MGI

    Keywords - Biological processi

    Acute phase, Angiogenesis, Cell adhesion, Cell shape

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_204211. Fibronectin matrix formation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.
    REACT_225233. Cell surface interactions at the vascular wall.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibronectin
    Short name:
    FN
    Cleaved into the following chain:
    Gene namesi
    Name:Fn1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:95566. Fn1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: MGI
    2. basal lamina Source: MGI
    3. basement membrane Source: MGI
    4. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    5. extracellular matrix Source: MGI
    6. fibrinogen complex Source: Ensembl
    7. proteinaceous extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi35 – 351Q → A: 99% decrease in cross-linking efficiency; when associated with A-36 and A-48. 1 Publication
    Mutagenesisi35 – 351Q → L: 65% decrease in cross-linking efficiency; when associated with L-36. 1 Publication
    Mutagenesisi36 – 361Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-48. 1 Publication
    Mutagenesisi36 – 361Q → L: 65% decrease in cross-linking efficiency; when associated with L-35. 1 Publication
    Mutagenesisi48 – 481Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-36. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232By similarityAdd
    BLAST
    Chaini33 – 24772445FibronectinPRO_0000019236Add
    BLAST
    Chaini627 – 70175AnastellinBy similarityPRO_0000390480Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei33 – 331Pyrrolidone carboxylic acidBy similarity
    Cross-linki35 – 35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
    Cross-linki36 – 36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
    Cross-linki48 – 48Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
    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
    Disulfide bondi308 ↔ 335By similarity
    Disulfide bondi333 ↔ 342By similarity
    Disulfide bondi360 ↔ 386By similarity
    Disulfide bondi374 ↔ 401By similarity
    Disulfide bondi420 ↔ 446By similarity
    Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi434 ↔ 461By similarity
    Disulfide bondi470 ↔ 498By similarity
    Disulfide bondi496 ↔ 508By similarity
    Disulfide bondi518 ↔ 545By similarity
    Glycosylationi528 – 5281N-linked (GlcNAc...)2 Publications
    Glycosylationi542 – 5421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi543 ↔ 555By similarity
    Disulfide bondi561 ↔ 589By similarity
    Disulfide bondi587 ↔ 599By similarity
    Modified residuei875 – 8751SulfotyrosineSequence Analysis
    Glycosylationi876 – 8761N-linked (GlcNAc...)Sequence Analysis
    Modified residuei880 – 8801SulfotyrosineSequence Analysis
    Glycosylationi1001 – 10011N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi1006 – 10061N-linked (GlcNAc...)3 Publications
    Glycosylationi1243 – 12431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1290 – 12901N-linked (GlcNAc...)2 Publications
    Glycosylationi2198 – 21981N-linked (GlcNAc...)1 Publication
    Disulfide bondi2296 ↔ 2325By similarity
    Disulfide bondi2323 ↔ 2335By similarity
    Disulfide bondi2341 ↔ 2368By similarity
    Disulfide bondi2366 ↔ 2378By similarity
    Disulfide bondi2385 ↔ 2411By similarity
    Modified residuei2392 – 23921SulfotyrosineSequence Analysis
    Disulfide bondi2409 ↔ 2420By similarity
    Disulfide bondi2458 – 2458Interchain (with C-2462)
    Disulfide bondi2462 – 2462Interchain (with C-2458)
    Modified residuei2475 – 24751Phosphoserine3 Publications

    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).
    Phosphorylation sites are present in the extracellular medium.By similarity
    Proteolytic processing produces the C-terminal NC1 peptide, anastellin.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP11276.
    PRIDEiP11276.

    PTM databases

    PhosphoSiteiP11276.

    Expressioni

    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.

    Inductioni

    Glucocorticoids suppressed mRNA expression and protein synthesis.

    Gene expression databases

    ArrayExpressiP11276.
    CleanExiMM_FN1.
    GenevestigatoriP11276.

    Interactioni

    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, AMBP, LGALS3BP and COL13A1 and COMP By similarity. Interacts with TNR; interaction mediates inhibition of cell adhesion and neurite outgrowth. Interacts with FBLN7. Interacts with FST3 and MYOC By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Plcg2Q8CIH56EBI-641955,EBI-617954

    Protein-protein interaction databases

    IntActiP11276. 3 interactions.
    MINTiMINT-202764.

    Structurei

    Secondary structure

    1
    2477
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1455 – 14595
    Beta strandi1461 – 14677
    Beta strandi1476 – 14849
    Beta strandi1492 – 14965
    Beta strandi1501 – 15077
    Beta strandi1510 – 152112
    Beta strandi1530 – 15367
    Beta strandi1545 – 15506
    Beta strandi1553 – 15575
    Beta strandi1567 – 158014
    Beta strandi1582 – 15865
    Beta strandi1591 – 15944
    Beta strandi1600 – 161213
    Beta strandi1615 – 16173
    Beta strandi1624 – 16307

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MFNNMR-A1447-1630[»]
    2MFNNMR-A1447-1630[»]
    ProteinModelPortaliP11276.
    SMRiP11276. Positions 49-274, 297-606, 609-808, 1172-1630, 1721-2081, 2332-2389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11276.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini51 – 9141Fibronectin type-I 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini96 – 13944Fibronectin type-I 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 18344Fibronectin type-I 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini185 – 22945Fibronectin type-I 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini230 – 27445Fibronectin type-I 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini306 – 34338Fibronectin type-I 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini355 – 40349Fibronectin type-II 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini415 – 46349Fibronectin type-II 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini468 – 51649Fibronectin type-I 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini516 – 55843Fibronectin type-I 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini559 – 60244Fibronectin type-I 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini610 – 717108Fibronectin type-III 1Add
    BLAST
    Domaini721 – 81191Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini812 – 90392Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini908 – 99790Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini998 – 108790Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1088 – 117487Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1175 – 126995Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1270 – 135889Fibronectin type-III 8; extra domain 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1359 – 145193Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1452 – 153988Fibronectin type-III 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1540 – 163394Fibronectin type-III 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1634 – 172592Fibronectin type-III 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1726 – 181388Fibronectin type-III 13; extra domain 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1814 – 190794Fibronectin type-III 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1908 – 199487Fibronectin type-III 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1995 – 208591Fibronectin type-III 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2193 – 228795Fibronectin type-III 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2294 – 233845Fibronectin type-I 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini2339 – 238143Fibronectin type-I 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2383 – 242644Fibronectin type-I 12PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 273221Fibrin- and heparin-binding 1Add
    BLAST
    Regioni308 – 608301Collagen-bindingAdd
    BLAST
    Regioni1357 – 1630274Cell-attachmentAdd
    BLAST
    Regioni1811 – 2081271Heparin-binding 2Add
    BLAST
    Regioni2082 – 2201120Connecting strand 3 (CS-3) (V region)Add
    BLAST
    Regioni2296 – 2427132Fibrin-binding 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1614 – 16163Cell attachment site
    Motifi2181 – 21833Cell attachment site

    Sequence similaritiesi

    Contains 12 fibronectin type-I domains.PROSITE-ProRule annotation
    Contains 2 fibronectin type-II domains.PROSITE-ProRule annotation
    Contains 17 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00750000117415.
    HOGENOMiHOG000234344.
    HOVERGENiHBG005731.
    InParanoidiP11276.
    KOiK05717.
    OMAiIPGHLNS.
    OrthoDBiEOG7X9G60.
    TreeFamiTF329915.

    Family and domain databases

    Gene3Di2.10.10.10. 2 hits.
    2.60.40.10. 17 hits.
    InterProiIPR000083. Fibronectin_type1.
    IPR003961. Fibronectin_type3.
    IPR000562. FN_type2_col-bd.
    IPR013783. Ig-like_fold.
    IPR013806. Kringle-like.
    [Graphical view]
    PfamiPF00039. fn1. 12 hits.
    PF00040. fn2. 2 hits.
    PF00041. fn3. 17 hits.
    [Graphical view]
    SMARTiSM00058. FN1. 12 hits.
    SM00059. FN2. 2 hits.
    SM00060. FN3. 17 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 11 hits.
    SSF57440. SSF57440. 2 hits.
    PROSITEiPS00022. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 1 isoform i produced by alternative splicing. Align

    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: P11276-1) [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

    MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK     50
    PGCFDNGKHY QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD 100
    KYTGNTYKVG DTYERPKDSM IWDCTCIGAG RGRISCTIAN RCHEGGQSYK 150
    IGDKWRRPHE TGGYMLECLC LGNGKGEWTC KPIAEKCFDH AAGTSYVVGE 200
    TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS YRIGDTWSKK 250
    DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP 300
    QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT 350
    YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF 400
    CTDHAVLVQT RGGNSNGALC HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ 450
    NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDL GHMMRCTCVG 500
    NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR 550
    GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ 600
    PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS 650
    TGRWKEATIP GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS 700
    ASTPVTSNTV TGETAPYSPV VATSESVTEI TASSFVVSWV SASDTVSGFR 750
    VEYELSEEGD EPQYLDLPST ATSVNIPDLL PGRKYIVNVY QISEEGKQSL 800
    ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY RIVYSPSVEG 850
    SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT 900
    PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG 950
    QRLPVNRNTF AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT 1000
    NLQFVNETDR TVLVTWTPPR ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY 1050
    PLRNLQPGSE YTVTLVAVKG NQQSPKATGV FTTLQPLRSI PPYNTEVTET 1100
    TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS GLTPGVEYTY 1150
    TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP 1200
    DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK 1250
    DDKESAPISD TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT 1300
    VVAAGEGIPI FEDFVDSSVG YYTVTGLEPG IDYDISVITL INGGESAPTT 1350
    LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP PSIELTNLLV RYSPVKNEED 1400
    VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL RGRQKTGLDS 1450
    PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR 1500
    NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST 1550
    PTSLLISWEP PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP 1600
    GADYTITLYA VTGRGDSPAS SKPVSINYKT EIDKPSQMQV TDVQDNSISV 1650
    RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA SPDQTEMTIE GLQPTVEYVV 1700
    SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI AWESPQGQVS 1750
    RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME 1800
    SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE 1850
    KTGPMKEINL SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT 1900
    LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAIP ANGQTPVQRS 1950
    ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA RSSPVIIDAS TAIDAPSNLR 2000
    FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR PRPGVTEATI 2050
    TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI 2100
    LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT 2150
    TPPTAATPVR LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS 2200
    TGQEALSQTT ISWTPFQESS EYIISCQPVG TDEEPLQFQV PGTSTSATLT 2250
    GLTRGVTYNI IVEALQNQRR HKVREEVVTV GNAVSEGLNQ PTDDSCFDPY 2300
    TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW CHDNGVNYKI 2350
    GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK 2400
    EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ 2450
    RTNTNVNCPI ECFMPLDVQA DRDDSRE 2477
    Length:2,477
    Mass (Da):272,538
    Last modified:October 3, 2012 - v4
    Checksum:i24A207BE67F85585
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1063 – 10631V → A in CAA63654. 1 PublicationCurated
    Sequence conflicti1820 – 18201F → L in CAA63654. 1 PublicationCurated
    Sequence conflicti2440 – 24401T → N in AAA37636. (PubMed:3124113)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC124821 Genomic DNA. No translation available.
    CH466548 Genomic DNA. Translation: EDL00265.1.
    BC051082 mRNA. No translation available.
    Z22729 Genomic DNA. Translation: CAA80422.1.
    X82402 mRNA. Translation: CAA57796.1.
    X93167 mRNA. Translation: CAA63654.1.
    M18194 mRNA. Translation: AAA37636.1.
    S45680 mRNA. Translation: AAB23491.1.
    CCDSiCCDS15031.1. [P11276-1]
    PIRiA49173.
    I48349.
    RefSeqiNP_034363.1. NM_010233.2. [P11276-1]
    UniGeneiMm.193099.

    Genome annotation databases

    EnsembliENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193. [P11276-1]
    GeneIDi14268.
    KEGGimmu:14268.
    UCSCiuc007bju.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC124821 Genomic DNA. No translation available.
    CH466548 Genomic DNA. Translation: EDL00265.1 .
    BC051082 mRNA. No translation available.
    Z22729 Genomic DNA. Translation: CAA80422.1 .
    X82402 mRNA. Translation: CAA57796.1 .
    X93167 mRNA. Translation: CAA63654.1 .
    M18194 mRNA. Translation: AAA37636.1 .
    S45680 mRNA. Translation: AAB23491.1 .
    CCDSi CCDS15031.1. [P11276-1 ]
    PIRi A49173.
    I48349.
    RefSeqi NP_034363.1. NM_010233.2. [P11276-1 ]
    UniGenei Mm.193099.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MFN NMR - A 1447-1630 [» ]
    2MFN NMR - A 1447-1630 [» ]
    ProteinModelPortali P11276.
    SMRi P11276. Positions 49-274, 297-606, 609-808, 1172-1630, 1721-2081, 2332-2389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11276. 3 interactions.
    MINTi MINT-202764.

    PTM databases

    PhosphoSitei P11276.

    Proteomic databases

    PaxDbi P11276.
    PRIDEi P11276.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000055226 ; ENSMUSP00000054499 ; ENSMUSG00000026193 . [P11276-1 ]
    GeneIDi 14268.
    KEGGi mmu:14268.
    UCSCi uc007bju.1. mouse.

    Organism-specific databases

    CTDi 2335.
    MGIi MGI:95566. Fn1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00750000117415.
    HOGENOMi HOG000234344.
    HOVERGENi HBG005731.
    InParanoidi P11276.
    KOi K05717.
    OMAi IPGHLNS.
    OrthoDBi EOG7X9G60.
    TreeFami TF329915.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_204211. Fibronectin matrix formation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.
    REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    ChiTaRSi FN1. mouse.
    EvolutionaryTracei P11276.
    NextBioi 285629.
    PROi P11276.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11276.
    CleanExi MM_FN1.
    Genevestigatori P11276.

    Family and domain databases

    Gene3Di 2.10.10.10. 2 hits.
    2.60.40.10. 17 hits.
    InterProi IPR000083. Fibronectin_type1.
    IPR003961. Fibronectin_type3.
    IPR000562. FN_type2_col-bd.
    IPR013783. Ig-like_fold.
    IPR013806. Kringle-like.
    [Graphical view ]
    Pfami PF00039. fn1. 12 hits.
    PF00040. fn2. 2 hits.
    PF00041. fn3. 17 hits.
    [Graphical view ]
    SMARTi SM00058. FN1. 12 hits.
    SM00059. FN2. 2 hits.
    SM00060. FN3. 17 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 11 hits.
    SSF57440. SSF57440. 2 hits.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-920.
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    4. "Sequence of the mouse fibronectin-encoding gene promoter region."
      Polly P., Nicholson R.C.
      Gene 137:353-354(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
      Tissue: Liver.
    5. "Regulation of mesenchymal extracellular matrix protein synthesis by transforming growth factor-beta and glucocorticoids in tumor stroma."
      Talts J.F., Weller A., Timpl R., Ekblom M., Ekblom P.
      J. Cell Sci. 108:2153-2162(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 562-834.
      Strain: NMRI.
    6. Gorski G., Aros M., Norton P.
      Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 899-2376.
    7. "Induction of fibronectin gene transcription and mRNA is a primary response to growth-factor stimulation of AKR-2B cells."
      Blatti S.P., Foster D.N., Ranganthan G., Moses H.L., Getz M.J.
      Proc. Natl. Acad. Sci. U.S.A. 85:1119-1123(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
    8. "Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts."
      Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.
      Exp. Cell Res. 180:537-545(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
    9. "Fibronectin gene expression in proliferating, quiescent, and SV40-infected mouse kidney cells."
      Khandjian E.W., Salomon C., Leonard N., Tremblay S., Turler H.
      Exp. Cell Res. 202:464-470(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
      Tissue: Kidney.
    10. "Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix."
      Corbett S.A., Lee L., Wilson C.L., Schwarzbauer J.E.
      J. Biol. Chem. 272:24999-25005(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSGLUTAMINATION AT GLN-35; GLN-36 AND GLN-48, MUTAGENESIS OF GLN-35; GLN-36 AND GLN-48.
    11. "Glucocorticoids down-regulate the extracellular matrix proteins fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma."
      Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.
      Eur. J. Haematol. 67:176-184(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOWN-REGULATION BY GLUCOCORTICOIDS.
    12. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006.
      Strain: C57BL/6.
      Tissue: Plasma.
    13. "TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding."
      de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A., Fisher L.W., Fukumoto S., Yamada Y.
      J. Biol. Chem. 282:30878-30888(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBLN7.
    14. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
      Bernhard O.K., Kapp E.A., Simpson R.J.
      J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528.
      Strain: C57BL/6.
      Tissue: Plasma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    17. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528; ASN-1001; ASN-1006; ASN-1290 AND ASN-2198.
      Tissue: Myoblast.
    18. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    19. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006 AND ASN-1290.
    20. "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
      Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
      J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure."
      Copie V., Tomita Y., Akiyama S.K., Aota S., Yamada K.M., Venable R.M., Pastor R.W., Krueger S., Torchia D.A.
      J. Mol. Biol. 277:663-682(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1447-1630.

    Entry informationi

    Entry nameiFINC_MOUSE
    AccessioniPrimary (citable) accession number: P11276
    Secondary accession number(s): G5E8B8
    , Q61567, Q61568, Q61569, Q64233, Q80UI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 162 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3