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P11276

- FINC_MOUSE

UniProt

P11276 - FINC_MOUSE

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Protein

Fibronectin

Gene

Fn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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. blood microparticle Source: Ensembl
  5. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  6. extracellular matrix Source: UniProtKB
  7. extracellular vesicular exosome Source: Ensembl
  8. fibrinogen complex Source: Ensembl
  9. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

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

CleanExiMM_FN1.
ExpressionAtlasiP11276. baseline and differential.
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.
GeneTreeiENSGT00760000118861.
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

        10         20         30         40         50
MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK
60 70 80 90 100
PGCFDNGKHY QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD
110 120 130 140 150
KYTGNTYKVG DTYERPKDSM IWDCTCIGAG RGRISCTIAN RCHEGGQSYK
160 170 180 190 200
IGDKWRRPHE TGGYMLECLC LGNGKGEWTC KPIAEKCFDH AAGTSYVVGE
210 220 230 240 250
TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS YRIGDTWSKK
260 270 280 290 300
DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP
310 320 330 340 350
QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT
360 370 380 390 400
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF
410 420 430 440 450
CTDHAVLVQT RGGNSNGALC HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ
460 470 480 490 500
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDL GHMMRCTCVG
510 520 530 540 550
NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR
560 570 580 590 600
GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ
610 620 630 640 650
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS
660 670 680 690 700
TGRWKEATIP GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS
710 720 730 740 750
ASTPVTSNTV TGETAPYSPV VATSESVTEI TASSFVVSWV SASDTVSGFR
760 770 780 790 800
VEYELSEEGD EPQYLDLPST ATSVNIPDLL PGRKYIVNVY QISEEGKQSL
810 820 830 840 850
ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY RIVYSPSVEG
860 870 880 890 900
SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT
910 920 930 940 950
PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG
960 970 980 990 1000
QRLPVNRNTF AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT
1010 1020 1030 1040 1050
NLQFVNETDR TVLVTWTPPR ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY
1060 1070 1080 1090 1100
PLRNLQPGSE YTVTLVAVKG NQQSPKATGV FTTLQPLRSI PPYNTEVTET
1110 1120 1130 1140 1150
TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS GLTPGVEYTY
1160 1170 1180 1190 1200
TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP
1210 1220 1230 1240 1250
DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK
1260 1270 1280 1290 1300
DDKESAPISD TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT
1310 1320 1330 1340 1350
VVAAGEGIPI FEDFVDSSVG YYTVTGLEPG IDYDISVITL INGGESAPTT
1360 1370 1380 1390 1400
LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP PSIELTNLLV RYSPVKNEED
1410 1420 1430 1440 1450
VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL RGRQKTGLDS
1460 1470 1480 1490 1500
PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR
1510 1520 1530 1540 1550
NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST
1560 1570 1580 1590 1600
PTSLLISWEP PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP
1610 1620 1630 1640 1650
GADYTITLYA VTGRGDSPAS SKPVSINYKT EIDKPSQMQV TDVQDNSISV
1660 1670 1680 1690 1700
RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA SPDQTEMTIE GLQPTVEYVV
1710 1720 1730 1740 1750
SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI AWESPQGQVS
1760 1770 1780 1790 1800
RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME
1810 1820 1830 1840 1850
SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE
1860 1870 1880 1890 1900
KTGPMKEINL SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT
1910 1920 1930 1940 1950
LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAIP ANGQTPVQRS
1960 1970 1980 1990 2000
ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA RSSPVIIDAS TAIDAPSNLR
2010 2020 2030 2040 2050
FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR PRPGVTEATI
2060 2070 2080 2090 2100
TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI
2110 2120 2130 2140 2150
LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT
2160 2170 2180 2190 2200
TPPTAATPVR LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS
2210 2220 2230 2240 2250
TGQEALSQTT ISWTPFQESS EYIISCQPVG TDEEPLQFQV PGTSTSATLT
2260 2270 2280 2290 2300
GLTRGVTYNI IVEALQNQRR HKVREEVVTV GNAVSEGLNQ PTDDSCFDPY
2310 2320 2330 2340 2350
TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW CHDNGVNYKI
2360 2370 2380 2390 2400
GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
2410 2420 2430 2440 2450
EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ
2460 2470
RTNTNVNCPI ECFMPLDVQA DRDDSRE
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 ENSGT00760000118861.
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

CleanExi MM_FN1.
ExpressionAtlasi P11276. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 163 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