P11276 (FINC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibronectin
Short name=FN

Cleaved into the following chain:

1. Anastellin

Gene names

Name:

Fn1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2477 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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.
Subunit structure	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 By similarity. Ref.13
Subcellular location	Secreted › extracellular space › extracellular matrix.
Tissue specificity	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. Ref.11
Post-translational modification	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.
Sequence similarities	Contains 12 fibronectin type-I domains. Contains 2 fibronectin type-II domains. Contains 17 fibronectin type-III domains.

Ontologies

Keywords
Biological process	Acute phase Angiogenesis Cell adhesion Cell shape
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal
Ligand	Heparin-binding
PTM	Disulfide bond Glycoprotein Isopeptide bond Phosphoprotein Pyrrolidone carboxylic acid Sulfation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW calcium-independent cell-matrix adhesion Inferred from direct assay PubMed 19651211. Source: MGI cell-substrate junction assembly Inferred from direct assay PubMed 12867986. Source: MGI peptide cross-linking Inferred from electronic annotation. Source: Compara regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW substrate adhesion-dependent cell spreading Inferred from electronic annotation. Source: Compara wound healing Inferred from mutant phenotype PubMed 12847088. Source: MGI
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 10742111. Source: MGI basement membrane Inferred from direct assay PubMed 11511678PubMed 8984825. Source: MGI endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: Compara fibrinogen complex Inferred from electronic annotation. Source: Compara
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW peptidase activator activity Inferred from direct assay PubMed 16061471. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Plcg2	Q8CIH5	6	EBI-641955,EBI-617954

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

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)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

By similarity

Chain

33 – 2477

2445

Fibronectin

PRO_0000019236

Chain

627 – 701

75

Anastellin By similarity

PRO_0000390480

Regions

Domain

51 – 91

41

Fibronectin type-I 1

Domain

96 – 139

44

Fibronectin type-I 2

Domain

140 – 183

44

Fibronectin type-I 3

Domain

185 – 229

45

Fibronectin type-I 4

Domain

230 – 274

45

Fibronectin type-I 5

Domain

306 – 343

38

Fibronectin type-I 6

Domain

355 – 403

49

Fibronectin type-II 1

Domain

415 – 463

49

Fibronectin type-II 2

Domain

468 – 516

49

Fibronectin type-I 7

Domain

516 – 558

43

Fibronectin type-I 8

Domain

559 – 602

44

Fibronectin type-I 9

Domain

607 – 699

93

Fibronectin type-III 1

Domain

719 – 808

90

Fibronectin type-III 2

Domain

810 – 897

88

Fibronectin type-III 3

Domain

905 – 994

90

Fibronectin type-III 4

Domain

995 – 1083

89

Fibronectin type-III 5

Domain

1091 – 1171

81

Fibronectin type-III 6

Domain

1172 – 1264

93

Fibronectin type-III 7

Domain

1265 – 1355

91

Fibronectin type-III 8; extra domain 1

Domain

1356 – 1446

91

Fibronectin type-III 9

Domain

1447 – 1536

90

Fibronectin type-III 10

Domain

1537 – 1626

90

Fibronectin type-III 11

Domain

1631 – 1720

90

Fibronectin type-III 12

Domain

1721 – 1810

90

Fibronectin type-III 13; extra domain 2

Domain

1813 – 1900

88

Fibronectin type-III 14

Domain

1903 – 1991

89

Fibronectin type-III 15

Domain

1992 – 2081

90

Fibronectin type-III 16

Domain

2190 – 2280

91

Fibronectin type-III 17

Domain

2294 – 2338

45

Fibronectin type-I 10

Domain

2339 – 2381

43

Fibronectin type-I 11

Domain

2383 – 2426

44

Fibronectin type-I 12

DNA binding

906 – 1171

266

Region

53 – 273

221

Fibrin- and heparin-binding 1

Region

308 – 608

301

Collagen-binding

Region

1357 – 1630

274

Cell-attachment

Region

1811 – 2081

271

Heparin-binding 2

Region

2082 – 2201

120

Connecting strand 3 (CS-3) (V region)

Region

2296 – 2427

132

Fibrin-binding 2

Motif

1614 – 1616

3

Cell attachment site

Motif

2181 – 2183

3

Cell attachment site

Amino acid modifications

Modified residue

33

1

Pyrrolidone carboxylic acid By similarity

Modified residue

875

1

Sulfotyrosine Potential

Modified residue

880

1

Sulfotyrosine Potential

Modified residue

2392

1

Sulfotyrosine Potential

Modified residue

2475

1

Phosphoserine Ref.15 Ref.16 Ref.18

Glycosylation

430

1

N-linked (GlcNAc...) Potential

Glycosylation

528

1

N-linked (GlcNAc...) Ref.14 Ref.17

Glycosylation

542

1

N-linked (GlcNAc...) Potential

Glycosylation

876

1

N-linked (GlcNAc...) Potential

Glycosylation

1001

1

N-linked (GlcNAc...) Ref.17

Glycosylation

1006

1

N-linked (GlcNAc...) Ref.12 Ref.17 Ref.19

Glycosylation

1243

1

N-linked (GlcNAc...) Potential

Glycosylation

1290

1

N-linked (GlcNAc...) Ref.17 Ref.19

Glycosylation

2198

1

N-linked (GlcNAc...) Ref.17

Disulfide bond

53 ↔ 79

By similarity

Disulfide bond

77 ↔ 88

By similarity

Disulfide bond

98 ↔ 126

By similarity

Disulfide bond

124 ↔ 136

By similarity

Disulfide bond

142 ↔ 170

By similarity

Disulfide bond

168 ↔ 180

By similarity

Disulfide bond

187 ↔ 216

By similarity

Disulfide bond

214 ↔ 226

By similarity

Disulfide bond

232 ↔ 261

By similarity

Disulfide bond

259 ↔ 271

By similarity

Disulfide bond

308 ↔ 335

By similarity

Disulfide bond

333 ↔ 342

By similarity

Disulfide bond

360 ↔ 386

By similarity

Disulfide bond

374 ↔ 401

By similarity

Disulfide bond

420 ↔ 446

By similarity

Disulfide bond

434 ↔ 461

By similarity

Disulfide bond

470 ↔ 498

By similarity

Disulfide bond

496 ↔ 508

By similarity

Disulfide bond

518 ↔ 545

By similarity

Disulfide bond

543 ↔ 555

By similarity

Disulfide bond

561 ↔ 589

By similarity

Disulfide bond

587 ↔ 599

By similarity

Disulfide bond

2296 ↔ 2325

By similarity

Disulfide bond

2323 ↔ 2335

By similarity

Disulfide bond

2341 ↔ 2368

By similarity

Disulfide bond

2366 ↔ 2378

By similarity

Disulfide bond

2385 ↔ 2411

By similarity

Disulfide bond

2409 ↔ 2420

By similarity

Disulfide bond

2458

Interchain (with C-2462)

Disulfide bond

2462

Interchain (with C-2458)

Cross-link

35

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Cross-link

36

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Cross-link

48

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Experimental info

Mutagenesis

35

1

Q → A: 99% decrease in cross-linking efficiency; when associated with A-36 and A-48. Ref.10

Mutagenesis

35

1

Q → L: 65% decrease in cross-linking efficiency; when associated with L-36. Ref.10

Mutagenesis

36

1

Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-48. Ref.10

Mutagenesis

36

1

Q → L: 65% decrease in cross-linking efficiency; when associated with L-35. Ref.10

Mutagenesis

48

1

Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-36. Ref.10

Sequence conflict

1063

1

V → A in CAA63654. Ref.6

Sequence conflict

1820

1

F → L in CAA63654. Ref.6

Sequence conflict

2440

1

T → N in AAA37636. Ref.7

Secondary structure

1

.

.

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.

.

.

.

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2477

Helix Strand Turn

Details...

Beta strand

1455 – 1459

5

Beta strand

1461 – 1467

7

Beta strand

1476 – 1484

9

Beta strand

1492 – 1496

5

Beta strand

1501 – 1507

7

Beta strand

1510 – 1521

12

Beta strand

1530 – 1536

7

Beta strand

1545 – 1550

6

Beta strand

1553 – 1557

5

Beta strand

1567 – 1580

14

Beta strand

1582 – 1586

5

Beta strand

1591 – 1594

4

Beta strand

1600 – 1612

13

Beta strand

1615 – 1617

3

Beta strand

1624 – 1630

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2012. Version 4. Checksum: 24A207BE67F85585	FASTA	2,477	272,538
	10 20 30 40 50 60 MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK PGCFDNGKHY 70 80 90 100 110 120 QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYKVG DTYERPKDSM 130 140 150 160 170 180 IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDKWRRPHE TGGYMLECLC LGNGKGEWTC 190 200 210 220 230 240 KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS 250 260 270 280 290 300 YRIGDTWSKK DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP 310 320 330 340 350 360 QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC 370 380 390 400 410 420 VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHAVLVQT RGGNSNGALC 430 440 450 460 470 480 HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI 490 500 510 520 530 540 GDQWDKQHDL GHMMRCTCVG NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM 550 560 570 580 590 600 LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ 610 620 630 640 650 660 PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS TGRWKEATIP 670 680 690 700 710 720 GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS ASTPVTSNTV TGETAPYSPV 730 740 750 760 770 780 VATSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL 790 800 810 820 830 840 PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY 850 860 870 880 890 900 RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT 910 920 930 940 950 960 PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG QRLPVNRNTF 970 980 990 1000 1010 1020 AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT NLQFVNETDR TVLVTWTPPR 1030 1040 1050 1060 1070 1080 ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY PLRNLQPGSE YTVTLVAVKG NQQSPKATGV 1090 1100 1110 1120 1130 1140 FTTLQPLRSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS 1150 1160 1170 1180 1190 1200 GLTPGVEYTY TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP 1210 1220 1230 1240 1250 1260 DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK DDKESAPISD 1270 1280 1290 1300 1310 1320 TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT VVAAGEGIPI FEDFVDSSVG 1330 1340 1350 1360 1370 1380 YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP 1390 1400 1410 1420 1430 1440 PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL 1450 1460 1470 1480 1490 1500 RGRQKTGLDS PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR 1510 1520 1530 1540 1550 1560 NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST PTSLLISWEP 1570 1580 1590 1600 1610 1620 PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP GADYTITLYA VTGRGDSPAS 1630 1640 1650 1660 1670 1680 SKPVSINYKT EIDKPSQMQV TDVQDNSISV RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA 1690 1700 1710 1720 1730 1740 SPDQTEMTIE GLQPTVEYVV SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI 1750 1760 1770 1780 1790 1800 AWESPQGQVS RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME 1810 1820 1830 1840 1850 1860 SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE KTGPMKEINL 1870 1880 1890 1900 1910 1920 SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT LENVSPPRRA RVTDATETTI 1930 1940 1950 1960 1970 1980 TISWRTKTET ITGFQVDAIP ANGQTPVQRS ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA 1990 2000 2010 2020 2030 2040 RSSPVIIDAS TAIDAPSNLR FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR 2050 2060 2070 2080 2090 2100 PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI 2110 2120 2130 2140 2150 2160 LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT TPPTAATPVR 2170 2180 2190 2200 2210 2220 LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT ISWTPFQESS 2230 2240 2250 2260 2270 2280 EYIISCQPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALQNQRR HKVREEVVTV 2290 2300 2310 2320 2330 2340 GNAVSEGLNQ PTDDSCFDPY TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW 2350 2360 2370 2380 2390 2400 CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK 2410 2420 2430 2440 2450 2460 EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ RTNTNVNCPI 2470 ECFMPLDVQA DRDDSRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
[15]	"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, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, MASS SPECTROMETRY. Tissue: Melanoma.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[20]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00113539.

PIR

A49173.
I48349.

RefSeq

NP_034363.1. NM_010233.2.

UniGene

Mm.193099.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MFN	NMR	-	A	1447-1630	[»]
2MFN	NMR	-	A	1447-1630	[»]

ProteinModelPortal

P11276.

SMR

P11276. Positions 49-274, 297-606, 609-808, 1172-1630, 1721-2081, 2332-2389.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11276. 1 interaction.

MINT

MINT-202764.

PTM databases

PhosphoSite

P11276.

Proteomic databases

PaxDb

P11276.

PRIDE

P11276.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193.

GeneID

14268.

KEGG

mmu:14268.

UCSC

uc007bju.1. mouse.

Organism-specific databases

CTD

2335.

MGI

MGI:95566. Fn1.

Phylogenomic databases

eggNOG

NOG12793.

GeneTree

ENSGT00700000104067.

HOGENOM

HOG000234344.

HOVERGEN

HBG005731.

InParanoid

P11276.

KO

K05717.

OMA

IPGHLNS.

Gene expression databases

CleanEx

MM_FN1.

Genevestigator

P11276.

GermOnline

ENSMUSG00000026193. Mus musculus.

Family and domain databases

Gene3D

2.10.10.10. 2 hits.
2.60.40.10. 17 hits.

InterPro

IPR000083. Fibronectin_type1.
IPR003961. Fibronectin_type3.
IPR000562. FN_type2_col-bd.
IPR013783. Ig-like_fold.
IPR013806. Kringle-like.
[Graphical view]

Pfam

PF00039. fn1. 12 hits.
PF00040. fn2. 2 hits.
PF00041. fn3. 17 hits.
[Graphical view]

SMART

SM00058. FN1. 12 hits.
SM00059. FN2. 2 hits.
SM00060. FN3. 17 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 17 hits.
SSF57440. Kringle-like. 2 hits.

PROSITE

PS00022. EGF_1. 2 hits.
PS01253. FN1_1. 12 hits.
PS51091. FN1_2. 12 hits.
PS00023. FN2_1. 2 hits.
PS51092. FN2_2. 2 hits.
PS50853. FN3. 17 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FN1. mouse.

EvolutionaryTrace

P11276.

NextBio

285629.

SOURCE

Search...

Entry information

Entry name

FINC_MOUSE

Accession

Primary (citable) accession number: P11276
Secondary accession number(s): G5E8B8 , Q61567, Q61568, Q61569, Q64233, Q80UI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 147 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program