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Protein

Fibronectin

Gene

Fn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
DNA bindingi906 – 1171Add BLAST266

GO - Molecular functioni

  • heparin binding Source: UniProtKB-KW
  • integrin binding Source: MGI
  • peptidase activator activity Source: MGI
  • protease binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Acute phase, Angiogenesis, Cell adhesion, Cell shape

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1474244. Extracellular matrix organization.
R-MMU-1566977. Fibronectin matrix formation.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-2129379. Molecules associated with elastic fibres.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000170. Syndecan interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.
R-MMU-8874081. MET activates PTK2 signaling.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:95566. Fn1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • basal lamina Source: MGI
  • basement membrane Source: MGI
  • blood microparticle Source: MGI
  • endoplasmic reticulum-Golgi intermediate compartment Source: MGI
  • extracellular exosome Source: MGI
  • extracellular matrix Source: UniProtKB
  • extracellular space Source: MGI
  • fibrinogen complex Source: MGI
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35Q → A: 99% decrease in cross-linking efficiency; when associated with A-36 and A-48. 1 Publication1
Mutagenesisi35Q → L: 65% decrease in cross-linking efficiency; when associated with L-36. 1 Publication1
Mutagenesisi36Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-48. 1 Publication1
Mutagenesisi36Q → L: 65% decrease in cross-linking efficiency; when associated with L-35. 1 Publication1
Mutagenesisi48Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-36. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32By similarityAdd BLAST32
ChainiPRO_000001923633 – 2477FibronectinAdd BLAST2445
ChainiPRO_0000390480627 – 701AnastellinBy similarityAdd BLAST75

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei33Pyrrolidone carboxylic acidBy similarity1
Cross-linki35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-linki36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-linki48Isoglutamyl 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
Modified residuei285PhosphoserineCombined sources1
Disulfide bondi308 ↔ 335By similarity
Disulfide bondi333 ↔ 342By similarity
Disulfide bondi360 ↔ 386By similarity
Disulfide bondi374 ↔ 401By similarity
Disulfide bondi420 ↔ 446By similarity
Glycosylationi430N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi434 ↔ 461By similarity
Disulfide bondi470 ↔ 498By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi518 ↔ 545By similarity
Glycosylationi528N-linked (GlcNAc...)2 Publications1
Glycosylationi542N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi543 ↔ 555By similarity
Disulfide bondi561 ↔ 589By similarity
Disulfide bondi587 ↔ 599By similarity
Modified residuei875SulfotyrosineSequence analysis1
Glycosylationi876N-linked (GlcNAc...)Sequence analysis1
Modified residuei880SulfotyrosineSequence analysis1
Glycosylationi1001N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi1006N-linked (GlcNAc...)3 Publications1
Glycosylationi1243N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1290N-linked (GlcNAc...)2 Publications1
Glycosylationi2198N-linked (GlcNAc...)1 Publication1
Disulfide bondi2296 ↔ 2325By similarity
Disulfide bondi2323 ↔ 2335By similarity
Disulfide bondi2341 ↔ 2368By similarity
Disulfide bondi2366 ↔ 2378By similarity
Disulfide bondi2385 ↔ 2411By similarity
Modified residuei2392SulfotyrosineSequence analysis1
Disulfide bondi2409 ↔ 2420By similarity
Modified residuei2454PhosphothreonineBy similarity1
Disulfide bondi2458Interchain (with C-2462)
Disulfide bondi2462Interchain (with C-2458)
Modified residuei2475PhosphoserineCombined sources1

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).
Phosphorylated by FAM20C 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

EPDiP11276.
MaxQBiP11276.
PaxDbiP11276.
PeptideAtlasiP11276.
PRIDEiP11276.

PTM databases

iPTMnetiP11276.
PhosphoSitePlusiP11276.
SwissPalmiP11276.

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

BgeeiENSMUSG00000026193.
CleanExiMM_FN1.
ExpressionAtlasiP11276. baseline and differential.
GenevisibleiP11276. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199719. 1 interactor.
IntActiP11276. 6 interactors.
MINTiMINT-202764.
STRINGi10090.ENSMUSP00000054499.

Structurei

Secondary structure

12477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1455 – 1459Combined sources5
Beta strandi1461 – 1467Combined sources7
Beta strandi1476 – 1484Combined sources9
Beta strandi1492 – 1496Combined sources5
Beta strandi1501 – 1507Combined sources7
Beta strandi1510 – 1521Combined sources12
Beta strandi1530 – 1536Combined sources7
Beta strandi1545 – 1550Combined sources6
Beta strandi1553 – 1557Combined sources5
Beta strandi1567 – 1580Combined sources14
Beta strandi1582 – 1586Combined sources5
Beta strandi1591 – 1594Combined sources4
Beta strandi1600 – 1612Combined sources13
Beta strandi1615 – 1617Combined sources3
Beta strandi1624 – 1630Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MFNNMR-A1447-1630[»]
2MFNNMR-A1447-1630[»]
ProteinModelPortaliP11276.
SMRiP11276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11276.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Domaini306 – 343Fibronectin type-I 6PROSITE-ProRule annotationAdd BLAST38
Domaini355 – 403Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini415 – 463Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini468 – 516Fibronectin type-I 7PROSITE-ProRule annotationAdd BLAST49
Domaini516 – 558Fibronectin type-I 8PROSITE-ProRule annotationAdd BLAST43
Domaini559 – 602Fibronectin type-I 9PROSITE-ProRule annotationAdd BLAST44
Domaini610 – 717Fibronectin type-III 1Add BLAST108
Domaini721 – 811Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST91
Domaini812 – 903Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini908 – 997Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST90
Domaini998 – 1087Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST90
Domaini1088 – 1174Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST87
Domaini1175 – 1269Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST95
Domaini1270 – 1358Fibronectin type-III 8; extra domain 1PROSITE-ProRule annotationAdd BLAST89
Domaini1359 – 1451Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST93
Domaini1452 – 1539Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST88
Domaini1540 – 1633Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST94
Domaini1634 – 1725Fibronectin type-III 12PROSITE-ProRule annotationAdd BLAST92
Domaini1726 – 1813Fibronectin type-III 13; extra domain 2PROSITE-ProRule annotationAdd BLAST88
Domaini1814 – 1907Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST94
Domaini1908 – 1994Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST87
Domaini1995 – 2085Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST91
Domaini2193 – 2287Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST95
Domaini2294 – 2338Fibronectin type-I 10PROSITE-ProRule annotationAdd BLAST45
Domaini2339 – 2381Fibronectin type-I 11PROSITE-ProRule annotationAdd BLAST43
Domaini2383 – 2426Fibronectin type-I 12PROSITE-ProRule annotationAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 273Fibrin- and heparin-binding 1Add BLAST221
Regioni308 – 608Collagen-bindingAdd BLAST301
Regioni1357 – 1630Cell-attachmentAdd BLAST274
Regioni1811 – 2081Heparin-binding 2Add BLAST271
Regioni2082 – 2201Connecting strand 3 (CS-3) (V region)Add BLAST120
Regioni2296 – 2427Fibrin-binding 2Add BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1614 – 1616Cell attachment site3
Motifi2181 – 2183Cell attachment site3

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

eggNOGiENOG410IF4N. Eukaryota.
ENOG410Y2NH. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP11276.
KOiK05717.
OMAiVTLPHPN.
OrthoDBiEOG091G116D.
TreeFamiTF329915.

Family and domain databases

CDDicd00062. FN2. 2 hits.
cd00063. FN3. 17 hits.
Gene3Di2.10.10.10. 2 hits.
2.60.40.10. 17 hits.
InterProiIPR000083. Fibronectin_type1.
IPR003961. FN3_dom.
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. 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: 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)DescriptionActionsGraphical viewLength
Sequence conflicti1063V → A in CAA63654 (Ref. 6) Curated1
Sequence conflicti1820F → L in CAA63654 (Ref. 6) Curated1
Sequence conflicti2440T → N in AAA37636 (PubMed:3124113).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. mouse. [P11276-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MFNNMR-A1447-1630[»]
2MFNNMR-A1447-1630[»]
ProteinModelPortaliP11276.
SMRiP11276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199719. 1 interactor.
IntActiP11276. 6 interactors.
MINTiMINT-202764.
STRINGi10090.ENSMUSP00000054499.

PTM databases

iPTMnetiP11276.
PhosphoSitePlusiP11276.
SwissPalmiP11276.

Proteomic databases

EPDiP11276.
MaxQBiP11276.
PaxDbiP11276.
PeptideAtlasiP11276.
PRIDEiP11276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193. [P11276-1]
GeneIDi14268.
KEGGimmu:14268.
UCSCiuc007bju.2. mouse. [P11276-1]

Organism-specific databases

CTDi2335.
MGIiMGI:95566. Fn1.

Phylogenomic databases

eggNOGiENOG410IF4N. Eukaryota.
ENOG410Y2NH. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP11276.
KOiK05717.
OMAiVTLPHPN.
OrthoDBiEOG091G116D.
TreeFamiTF329915.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1474244. Extracellular matrix organization.
R-MMU-1566977. Fibronectin matrix formation.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-2129379. Molecules associated with elastic fibres.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000170. Syndecan interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.
R-MMU-8874081. MET activates PTK2 signaling.

Miscellaneous databases

ChiTaRSiFn1. mouse.
EvolutionaryTraceiP11276.
PROiP11276.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026193.
CleanExiMM_FN1.
ExpressionAtlasiP11276. baseline and differential.
GenevisibleiP11276. MM.

Family and domain databases

CDDicd00062. FN2. 2 hits.
cd00063. FN3. 17 hits.
Gene3Di2.10.10.10. 2 hits.
2.60.40.10. 17 hits.
InterProiIPR000083. Fibronectin_type1.
IPR003961. FN3_dom.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 186 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.