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Protein

Fibronectin

Gene

Fn1

Organism
Rattus norvegicus (Rat)
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. 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 (By similarity).By similarity
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

  • extracellular matrix structural constituent Source: RGD
  • heparin binding Source: UniProtKB-KW
  • mercury ion binding Source: RGD
  • protease binding Source: RGD

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • angiogenesis Source: UniProtKB-KW
  • cell activation Source: RGD
  • cell-matrix adhesion Source: RGD
  • cellular response to angiotensin Source: RGD
  • cellular response to beta-amyloid Source: RGD
  • cellular response to BMP stimulus Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to mercury ion Source: RGD
  • cellular response to platelet-derived growth factor stimulus Source: RGD
  • cellular response to prostaglandin E stimulus Source: RGD
  • cellular response to transforming growth factor beta stimulus Source: RGD
  • cellular response to vascular endothelial growth factor stimulus Source: RGD
  • extracellular matrix organization Source: RGD
  • glial cell migration Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • ossification Source: RGD
  • positive regulation of cell migration Source: RGD
  • positive regulation of chemotaxis Source: RGD
  • regulation of cell shape Source: UniProtKB-KW
  • response to activity Source: RGD
  • response to drug Source: RGD
  • response to glucocorticoid Source: RGD
  • response to iron ion Source: RGD
  • response to ischemia Source: RGD
  • response to ozone Source: RGD
  • response to wounding Source: RGD
Complete GO annotation...

Keywords - Biological processi

Acute phase, Angiogenesis, Cell adhesion, Cell shape

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Cleaved into the following chain:
Gene namesi
Name:Fn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2624. Fn1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: RGD
  • extracellular space Source: RGD
  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 24772453FibronectinPRO_0000019237Add
BLAST
Chaini627 – 70175AnastellinBy similarityPRO_0000390481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki35 – 35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki36 – 36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki48 – 48Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
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 residuei285 – 2851PhosphoserineCombined sources
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...)Sequence analysis
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
Glycosylationi1006 – 10061N-linked (GlcNAc...)Sequence analysis
Glycosylationi1243 – 12431N-linked (GlcNAc...)Sequence analysis
Glycosylationi1290 – 12901N-linked (GlcNAc...)Sequence analysis
Glycosylationi2154 – 21541O-linked (GalNAc...)By similarity
Glycosylationi2198 – 21981N-linked (GlcNAc...)Sequence analysis
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
Modified residuei2454 – 24541PhosphothreonineBy similarity
Disulfide bondi2458 – 2458Interchain (with C-2462)
Disulfide bondi2462 – 2462Interchain (with C-2458)
Modified residuei2475 – 24751PhosphoserineCombined sources

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, Sulfation

Proteomic databases

PaxDbiP04937.
PRIDEiP04937.

PTM databases

iPTMnetiP04937.
PhosphoSiteiP04937.

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.

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, FBLN7, AMBP, LGALS3BP, COL13A1 and COMP (By similarity). Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth. Interacts with FST3 and MYOC (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Sdc4P349012EBI-6127274,EBI-1173182

GO - Molecular functioni

  • protease binding Source: RGD

Protein-protein interaction databases

IntActiP04937. 2 interactions.
MINTiMINT-5024668.
STRINGi10116.ENSRNOP00000019772.

Structurei

3D structure databases

ProteinModelPortaliP04937.
SMRiP04937. Positions 49-274, 305-464, 609-808, 1172-1630, 1721-2081, 2332-2389.
ModBaseiSearch...
MobiDBiSearch...

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 – 34540Fibronectin type-I 6PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 40349Fibronectin type-II 1PROSITE-ProRule annotationAdd
BLAST
Domaini415 – 46349Fibronectin type-II 2PROSITE-ProRule annotationAdd
BLAST
Domaini468 – 51144Fibronectin 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 – 90190Fibronectin 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 – 228694Fibronectin 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

HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP04937.
PhylomeDBiP04937.

Family and domain databases

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. 11 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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Each of the "extra domain" and the connecting strand 3 are present in some forms of fibronectin and absent in others.

Isoform 1 (identifier: P04937-1) [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 SVRCTETGKS KRQAQQIVQP PSPVAVSQSK
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 CERHVLQSAS AGSGSFTDVR TAIYQPQTHP
310 320 330 340 350
QPAPYGHCVT DSGVVYSVGM QWLKSQGDKQ MLCTCLGNGV SCQETAVTQT
360 370 380 390 400
YGGNSNGEPC VLPFHYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF
410 420 430 440 450
CTDHAVLVQT RGGNSNGALC HFPFLYSNRN YSDCTSEGRR DNMKWCGTTQ
460 470 480 490 500
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDL GHMMRCTCVG
510 520 530 540 550
NGRGQWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR
560 570 580 590 600
GRWKCDPIDR CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ
610 620 630 640 650
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS
660 670 680 690 700
TGRWKEATIP GHLNSYTIKG LTPGVIYEGQ LISIQQYGHQ EVTRFDFTTS
710 720 730 740 750
ASTPVTSNTV TGETAPFSPV 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 VFIQQETTGV
910 920 930 940 950
PRSDDVPAPK DLQFVEVTDV KVTIMWTPPN SAVTGYRVDV LPVNLPGEHG
960 970 980 990 1000
QRLPVNRNTF AEVTGLSPGV TYLFKVFAVH QGRESKPLTA QQTTKLDAPT
1010 1020 1030 1040 1050
NLQFVNETDR TVLVTWTPPR ARIAGYRLTV GLTRGGQPKQ YNVGPMASKY
1060 1070 1080 1090 1100
PLRNLQPGSE YTVTLMAVKG 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 PTNGQQGTAL EEVVHADQSS CTFENRNPGL EYNVSVYTVK
1260 1270 1280 1290 1300
DDKESAPISD TVIPEVPQLT 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
PTGFDSSDVT ANSFTVHWVA PRAPITGYII RHHAEHSAGR PRQDRVPPSR
1510 1520 1530 1540 1550
NSITLTNLNP GTEYIVTIIA VNGREESPPL IGQQSTVSDV PRDLEVIAST
1560 1570 1580 1590 1600
PTSLLISWEP PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP
1610 1620 1630 1640 1650
GADYTITLYA VTGRGDSPAS SKPVSINYQT EIDKPSQMQV TDVQDNSISV
1660 1670 1680 1690 1700
RWLPSTSPVT GYRVTTAPKN GLGPTKSQTV SPDQTEMTIE GLQPTVEYVV
1710 1720 1730 1740 1750
SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI AWESPQGQVS
1760 1770 1780 1790 1800
RYRVTYSSPE DGIHELFPAP DGDEDTAELH GLRPGSEYTV SVVALHGGME
1810 1820 1830 1840 1850
SQPLIGVQST AIPAPTNLKF TQVSPTTLTA QWTAPSVKLT GYRVRVTPKE
1860 1870 1880 1890 1900
KTGPMKEINL SPDSTSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVVTT
1910 1920 1930 1940 1950
LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAIP ANGQTPVQRT
1960 1970 1980 1990 2000
ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA RSSPVVIDAS 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 PFVTNPGYDT ENGIQLPGTS 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 IVEALHNQRR HKVREEVVTV GNTVNEGLNQ PTDDSCFDPY
2310 2320 2330 2340 2350
TVSHYAVGEE WERLSDSGFK LTCQCLGFGS GHFRCDSSKW CHDNGVNYKI
2360 2370 2380 2390 2400
GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
2410 2420 2430 2440 2450
EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYHQ
2460 2470
RTNTNVNCPI ECFMPLDVQA DRDDSRE
Length:2,477
Mass (Da):272,511
Last modified:November 1, 1990 - v2
Checksum:iB4391A472ECEDEB5
GO
Isoform 2 (identifier: P04937-2) [UniParc]FASTAAdd to basket

Also known as: FNIII-13-less

The sequence of this isoform differs from the canonical sequence as follows:
     1720-1809: Missing.

Show »
Length:2,387
Mass (Da):262,791
Checksum:i6C6CC67A23FD3D61
GO
Isoform 3 (identifier: P04937-3) [UniParc]FASTAAdd to basket

Also known as: Lambda-RLF4-5

The sequence of this isoform differs from the canonical sequence as follows:
     2082-2106: Missing.

Show »
Length:2,452
Mass (Da):269,797
Checksum:iCCCE09E02AD38F38
GO
Isoform 4 (identifier: P04937-4) [UniParc]FASTAAdd to basket

Also known as: Lambda-RLF6

The sequence of this isoform differs from the canonical sequence as follows:
     2082-2200: Missing.

Show »
Length:2,358
Mass (Da):259,350
Checksum:iACB4C7070092F5F0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2318 – 23181G → A in AAA41166 (PubMed:6317187).Curated
Sequence conflicti2318 – 23181G → A in AAA41167 (PubMed:6317187).Curated
Sequence conflicti2318 – 23181G → A in AAA41168 (PubMed:6317187).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1720 – 180990Missing in isoform 2. CuratedVSP_003258Add
BLAST
Alternative sequencei2082 – 2200119Missing in isoform 4. CuratedVSP_003260Add
BLAST
Alternative sequencei2082 – 210625Missing in isoform 3. CuratedVSP_003259Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15906 mRNA. Translation: CAA34020.1.
L29191, L00191 Genomic DNA. Translation: AAA41166.1.
L29191, L00191 Genomic DNA. Translation: AAA41167.1.
L29191, L00191 Genomic DNA. Translation: AAA41168.1.
M11750 Genomic DNA. Translation: AAA41170.1.
X05831 Genomic DNA. Translation: CAA29278.1.
X05832 Genomic DNA. Translation: CAA29279.1.
X05833 Genomic DNA. Translation: CAA29280.1.
X05834 Genomic DNA. Translation: CAA29281.1.
PIRiS14428.
UniGeneiRn.1604.

Genome annotation databases

UCSCiRGD:2624. rat. [P04937-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15906 mRNA. Translation: CAA34020.1.
L29191, L00191 Genomic DNA. Translation: AAA41166.1.
L29191, L00191 Genomic DNA. Translation: AAA41167.1.
L29191, L00191 Genomic DNA. Translation: AAA41168.1.
M11750 Genomic DNA. Translation: AAA41170.1.
X05831 Genomic DNA. Translation: CAA29278.1.
X05832 Genomic DNA. Translation: CAA29279.1.
X05833 Genomic DNA. Translation: CAA29280.1.
X05834 Genomic DNA. Translation: CAA29281.1.
PIRiS14428.
UniGeneiRn.1604.

3D structure databases

ProteinModelPortaliP04937.
SMRiP04937. Positions 49-274, 305-464, 609-808, 1172-1630, 1721-2081, 2332-2389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04937. 2 interactions.
MINTiMINT-5024668.
STRINGi10116.ENSRNOP00000019772.

PTM databases

iPTMnetiP04937.
PhosphoSiteiP04937.

Proteomic databases

PaxDbiP04937.
PRIDEiP04937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2624. rat. [P04937-1]

Organism-specific databases

RGDi2624. Fn1.

Phylogenomic databases

HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP04937.
PhylomeDBiP04937.

Miscellaneous databases

PROiP04937.

Family and domain databases

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. 11 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...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple sites of alternative splicing of the rat fibronectin gene transcript."
    Scwarzbauer J.E., Patel R.S., Fonda D., Hynes R.O.
    EMBO J. 6:2573-2580(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer.
    Tissue: Liver.
  2. "Organization of the fibronectin gene provides evidence for exon shuffling during evolution."
    Patel R.S., Odermatt E., Schwarzbauer J.E., Hynes R.O.
    EMBO J. 6:2565-2572(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139 AND 2382-2477.
    Strain: Fischer.
    Tissue: Liver.
  3. "Three different fibronectin mRNAs arise by alternative splicing within the coding region."
    Schwarzbauer J.E., Tamkun J.W., Lemischka I.R., Hynes R.O.
    Cell 35:421-431(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1586-2477.
  4. "Repeating modular structure of the fibronectin gene: relationship to protein structure and subunit variation."
    Odermatt E., Tamkun J.W., Hynes R.O.
    Proc. Natl. Acad. Sci. U.S.A. 82:6571-6575(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1722-1810, ALTERNATIVE SPLICING.
  5. "A single rat fibronectin gene generates three different mRNAs by alternative splicing of a complex exon."
    Tamkun J.W., Schwarzbauer J.E., Hynes R.O.
    Proc. Natl. Acad. Sci. U.S.A. 81:5140-5144(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2052-2237, ALTERNATIVE SPLICING.
  6. "Isolation and characterization of fibronectin-alpha 1-microglobulin complex in rat plasma."
    Falkenberg C., Enghild J.J., Thoegersen I.B., Salvesen G., Aakerstroem B.
    Biochem. J. 301:745-751(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1183-1192; 1385-1399 AND 2287-2300, INTERACTION WITH AMBP.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: CLEAVAGE OF SIGNAL PEPTIDE AFTER CYS-24, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFINC_RAT
AccessioniPrimary (citable) accession number: P04937
Secondary accession number(s): Q6LDX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1990
Last modified: June 8, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.