UniProtKB - P04937 (FINC_RAT)
Fibronectin
Fn1
Functioni
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 906 – 1171 | Add BLAST | 266 |
GO - Molecular functioni
- chaperone binding Source: RGD
- disordered domain specific binding Source: RGD
- enzyme binding Source: RGD
- extracellular matrix structural constituent Source: RGD
- heparin binding Source: UniProtKB-KW
- identical protein binding Source: RGD
- integrin binding Source: RGD
- mercury ion binding Source: RGD
- peptidase activator activity Source: RGD
- protease binding Source: RGD
- protein C-terminus binding Source: RGD
- proteoglycan binding Source: RGD
- signaling receptor binding Source: RGD
GO - Biological processi
- acute-phase response Source: UniProtKB-KW
- angiogenesis Source: UniProtKB-KW
- blood coagulation, fibrin clot formation Source: GO_Central
- calcium-independent cell-matrix adhesion Source: RGD
- cell activation Source: RGD
- cell adhesion Source: RGD
- cell-matrix adhesion Source: RGD
- cell-substrate junction assembly Source: RGD
- cellular response to amyloid-beta Source: RGD
- cellular response to angiotensin 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
- endodermal cell differentiation Source: RGD
- extracellular matrix organization Source: RGD
- glial cell migration Source: RGD
- heart development Source: GO_Central
- integrin activation Source: RGD
- integrin-mediated signaling pathway Source: RGD
- interaction with symbiont Source: RGD
- negative regulation of apoptotic process Source: RGD
- negative regulation of collagen biosynthetic process Source: RGD
- negative regulation of transforming growth factor-beta secretion Source: RGD
- nervous system development Source: GO_Central
- neural crest cell migration involved in autonomic nervous system development Source: RGD
- ossification Source: RGD
- peptide cross-linking Source: RGD
- platelet aggregation Source: GO_Central
- positive regulation of axon extension Source: RGD
- positive regulation of cell migration Source: RGD
- positive regulation of cell population proliferation Source: RGD
- positive regulation of chemotaxis Source: RGD
- positive regulation of fibroblast proliferation Source: RGD
- positive regulation of gene expression Source: RGD
- positive regulation of substrate-dependent cell migration, cell attachment to substrate Source: RGD
- regulation of cell shape Source: UniProtKB-KW
- regulation of ERK1 and ERK2 cascade Source: RGD
- regulation of gene expression Source: RGD
- regulation of protein phosphorylation Source: RGD
- 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
- substrate adhesion-dependent cell spreading Source: RGD
- wound healing Source: RGD
Keywordsi
Molecular function | Heparin-binding |
Biological process | Acute phase, Angiogenesis, Cell adhesion, Cell shape |
Enzyme and pathway databases
Reactomei | R-RNO-114608, Platelet degranulation R-RNO-1474228, Degradation of the extracellular matrix R-RNO-1474244, Extracellular matrix organization R-RNO-1566977, Fibronectin matrix formation R-RNO-202733, Cell surface interactions at the vascular wall R-RNO-2129379, Molecules associated with elastic fibres R-RNO-216083, Integrin cell surface interactions R-RNO-3000170, Syndecan interactions R-RNO-3000171, Non-integrin membrane-ECM interactions R-RNO-3000178, ECM proteoglycans R-RNO-354192, Integrin signaling R-RNO-354194, GRB2:SOS provides linkage to MAPK signaling for Integrins R-RNO-372708, p130Cas linkage to MAPK signaling for integrins R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-RNO-5674135, MAP2K and MAPK activation R-RNO-8874081, MET activates PTK2 signaling R-RNO-8957275, Post-translational protein phosphorylation |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Fn1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2624, Fn1 |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- basement membrane Source: RGD
- collagen-containing extracellular matrix Source: RGD
- extracellular exosome Source: RGD
- extracellular matrix Source: RGD
- extracellular space Source: RGD
- fibrinogen complex Source: RGD
Plasma Membrane
- apical plasma membrane Source: RGD
Other locations
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | 1 PublicationAdd BLAST | 24 | |
ChainiPRO_0000019237 | 25 – 2477 | FibronectinAdd BLAST | 2453 | |
ChainiPRO_0000390481 | 627 – 701 | AnastellinBy similarityAdd BLAST | 75 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 35 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity | ||
Cross-linki | 36 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity | ||
Cross-linki | 48 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity | ||
Disulfide bondi | 53 ↔ 79 | By similarity | ||
Disulfide bondi | 77 ↔ 88 | By similarity | ||
Disulfide bondi | 98 ↔ 126 | By similarity | ||
Disulfide bondi | 124 ↔ 136 | By similarity | ||
Disulfide bondi | 142 ↔ 170 | By similarity | ||
Disulfide bondi | 168 ↔ 180 | By similarity | ||
Disulfide bondi | 187 ↔ 216 | By similarity | ||
Disulfide bondi | 214 ↔ 226 | By similarity | ||
Disulfide bondi | 232 ↔ 261 | By similarity | ||
Disulfide bondi | 259 ↔ 271 | By similarity | ||
Modified residuei | 285 | PhosphoserineCombined sources | 1 | |
Disulfide bondi | 308 ↔ 335 | By similarity | ||
Disulfide bondi | 333 ↔ 342 | By similarity | ||
Disulfide bondi | 360 ↔ 386 | By similarity | ||
Disulfide bondi | 374 ↔ 401 | By similarity | ||
Disulfide bondi | 420 ↔ 446 | By similarity | ||
Glycosylationi | 430 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 434 ↔ 461 | By similarity | ||
Disulfide bondi | 470 ↔ 498 | By similarity | ||
Disulfide bondi | 496 ↔ 508 | By similarity | ||
Disulfide bondi | 518 ↔ 545 | By similarity | ||
Glycosylationi | 528 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 542 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 543 ↔ 555 | By similarity | ||
Disulfide bondi | 561 ↔ 589 | By similarity | ||
Disulfide bondi | 587 ↔ 599 | By similarity | ||
Modified residuei | 875 | SulfotyrosineSequence analysis | 1 | |
Glycosylationi | 876 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 880 | SulfotyrosineSequence analysis | 1 | |
Glycosylationi | 1006 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1243 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1290 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2154 | O-linked (GalNAc...) threonineBy similarity | 1 | |
Glycosylationi | 2198 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2296 ↔ 2325 | By similarity | ||
Disulfide bondi | 2323 ↔ 2335 | By similarity | ||
Disulfide bondi | 2341 ↔ 2368 | By similarity | ||
Disulfide bondi | 2366 ↔ 2378 | By similarity | ||
Disulfide bondi | 2385 ↔ 2411 | By similarity | ||
Modified residuei | 2392 | SulfotyrosineSequence analysis | 1 | |
Disulfide bondi | 2409 ↔ 2420 | By similarity | ||
Modified residuei | 2454 | PhosphothreonineBy similarity | 1 | |
Disulfide bondi | 2458 | Interchain (with C-2462) | ||
Disulfide bondi | 2462 | Interchain (with C-2458) | ||
Modified residuei | 2475 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Isopeptide bond, Oxidation, Phosphoprotein, SulfationProteomic databases
jPOSTi | P04937 |
PaxDbi | P04937 |
PeptideAtlasi | P04937 |
PRIDEi | P04937 |
PTM databases
CarbonylDBi | P04937 |
GlyGeni | P04937, 9 sites |
iPTMneti | P04937 |
PhosphoSitePlusi | P04937 |
Expressioni
Tissue specificityi
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 similarityBinary interactionsi
P04937
With | #Exp. | IntAct |
---|---|---|
Sdc4 [P34901] | 2 | EBI-6127274,EBI-1173182 |
GO - Molecular functioni
- chaperone binding Source: RGD
- disordered domain specific binding Source: RGD
- enzyme binding Source: RGD
- identical protein binding Source: RGD
- integrin binding Source: RGD
- protease binding Source: RGD
- protein C-terminus binding Source: RGD
- proteoglycan binding Source: RGD
- signaling receptor binding Source: RGD
Protein-protein interaction databases
IntActi | P04937, 3 interactors |
MINTi | P04937 |
STRINGi | 10116.ENSRNOP00000019772 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 51 – 91 | Fibronectin type-I 1PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 96 – 139 | Fibronectin type-I 2PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 140 – 183 | Fibronectin type-I 3PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 185 – 229 | Fibronectin type-I 4PROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 230 – 274 | Fibronectin type-I 5PROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 306 – 345 | Fibronectin type-I 6PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 355 – 403 | Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST | 49 | |
Domaini | 415 – 463 | Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST | 49 | |
Domaini | 468 – 511 | Fibronectin type-I 7PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 516 – 558 | Fibronectin type-I 8PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 559 – 602 | Fibronectin type-I 9PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 610 – 717 | Fibronectin type-III 1Add BLAST | 108 | |
Domaini | 721 – 811 | Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST | 91 | |
Domaini | 812 – 901 | Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST | 90 | |
Domaini | 908 – 997 | Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST | 90 | |
Domaini | 998 – 1087 | Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST | 90 | |
Domaini | 1088 – 1174 | Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST | 87 | |
Domaini | 1175 – 1269 | Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST | 95 | |
Domaini | 1270 – 1358 | Fibronectin type-III 8; extra domain 1PROSITE-ProRule annotationAdd BLAST | 89 | |
Domaini | 1359 – 1451 | Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST | 93 | |
Domaini | 1452 – 1539 | Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST | 88 | |
Domaini | 1540 – 1633 | Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST | 94 | |
Domaini | 1634 – 1725 | Fibronectin type-III 12PROSITE-ProRule annotationAdd BLAST | 92 | |
Domaini | 1726 – 1813 | Fibronectin type-III 13; extra domain 2PROSITE-ProRule annotationAdd BLAST | 88 | |
Domaini | 1814 – 1907 | Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST | 94 | |
Domaini | 1908 – 1994 | Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST | 87 | |
Domaini | 1995 – 2085 | Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST | 91 | |
Domaini | 2193 – 2286 | Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST | 94 | |
Domaini | 2294 – 2338 | Fibronectin type-I 10PROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 2339 – 2381 | Fibronectin type-I 11PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 2383 – 2426 | Fibronectin type-I 12PROSITE-ProRule annotationAdd BLAST | 44 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 53 – 273 | Fibrin- and heparin-binding 1Add BLAST | 221 | |
Regioni | 308 – 608 | Collagen-bindingAdd BLAST | 301 | |
Regioni | 1357 – 1630 | Cell-attachmentAdd BLAST | 274 | |
Regioni | 1811 – 2081 | Heparin-binding 2Add BLAST | 271 | |
Regioni | 2082 – 2201 | Connecting strand 3 (CS-3) (V region)Add BLAST | 120 | |
Regioni | 2296 – 2427 | Fibrin-binding 2Add BLAST | 132 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 1614 – 1616 | Cell attachment site | 3 | |
Motifi | 2181 – 2183 | Cell attachment site | 3 |
Keywords - Domaini
Repeat, SignalPhylogenomic databases
eggNOGi | ENOG502QPTS, Eukaryota |
InParanoidi | P04937 |
PhylomeDBi | P04937 |
Family and domain databases
CDDi | cd00061, FN1, 12 hits cd00062, FN2, 2 hits cd00063, FN3, 17 hits |
Gene3Di | 2.10.10.10, 2 hits 2.60.40.10, 17 hits |
InterProi | View protein in InterPro IPR000083, Fibronectin_type1 IPR003961, FN3_dom IPR036116, FN3_sf IPR000562, FN_type2_dom IPR036943, FN_type2_sf IPR013783, Ig-like_fold IPR013806, Kringle-like |
Pfami | View protein in Pfam PF00039, fn1, 11 hits PF00040, fn2, 2 hits PF00041, fn3, 17 hits |
SMARTi | View protein in SMART SM00058, FN1, 12 hits SM00059, FN2, 2 hits SM00060, FN3, 17 hits |
SUPFAMi | SSF49265, SSF49265, 11 hits SSF57440, SSF57440, 2 hits |
PROSITEi | View protein in 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 |
s (4+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A096P6L8 | A0A096P6L8_RAT | Fibronectin | Fn1 rCG_25006 | 2,477 | Annotation score: | ||
F1LST1 | F1LST1_RAT | Fibronectin | Fn1 rCG_25006 | 2,387 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2318 | G → A in AAA41166 (PubMed:6317187).Curated | 1 | |
Sequence conflicti | 2318 | G → A in AAA41167 (PubMed:6317187).Curated | 1 | |
Sequence conflicti | 2318 | G → A in AAA41168 (PubMed:6317187).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_003258 | 1720 – 1809 | Missing in isoform 2. CuratedAdd BLAST | 90 | |
Alternative sequenceiVSP_003260 | 2082 – 2200 | Missing in isoform 4. CuratedAdd BLAST | 119 | |
Alternative sequenceiVSP_003259 | 2082 – 2106 | Missing in isoform 3. CuratedAdd BLAST | 25 |
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 |
PIRi | S14428 |
Genome annotation databases
UCSCi | RGD:2624, rat [P04937-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
PIRi | S14428 |
3D structure databases
SMRi | P04937 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | P04937, 3 interactors |
MINTi | P04937 |
STRINGi | 10116.ENSRNOP00000019772 |
PTM databases
CarbonylDBi | P04937 |
GlyGeni | P04937, 9 sites |
iPTMneti | P04937 |
PhosphoSitePlusi | P04937 |
Proteomic databases
jPOSTi | P04937 |
PaxDbi | P04937 |
PeptideAtlasi | P04937 |
PRIDEi | P04937 |
Protocols and materials databases
ABCDi | P04937, 2 sequenced antibodies |
Genome annotation databases
UCSCi | RGD:2624, rat [P04937-1] |
Organism-specific databases
RGDi | 2624, Fn1 |
Phylogenomic databases
eggNOGi | ENOG502QPTS, Eukaryota |
InParanoidi | P04937 |
PhylomeDBi | P04937 |
Enzyme and pathway databases
Reactomei | R-RNO-114608, Platelet degranulation R-RNO-1474228, Degradation of the extracellular matrix R-RNO-1474244, Extracellular matrix organization R-RNO-1566977, Fibronectin matrix formation R-RNO-202733, Cell surface interactions at the vascular wall R-RNO-2129379, Molecules associated with elastic fibres R-RNO-216083, Integrin cell surface interactions R-RNO-3000170, Syndecan interactions R-RNO-3000171, Non-integrin membrane-ECM interactions R-RNO-3000178, ECM proteoglycans R-RNO-354192, Integrin signaling R-RNO-354194, GRB2:SOS provides linkage to MAPK signaling for Integrins R-RNO-372708, p130Cas linkage to MAPK signaling for integrins R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-RNO-5674135, MAP2K and MAPK activation R-RNO-8874081, MET activates PTK2 signaling R-RNO-8957275, Post-translational protein phosphorylation |
Miscellaneous databases
PROi | PR:P04937 |
Family and domain databases
CDDi | cd00061, FN1, 12 hits cd00062, FN2, 2 hits cd00063, FN3, 17 hits |
Gene3Di | 2.10.10.10, 2 hits 2.60.40.10, 17 hits |
InterProi | View protein in InterPro IPR000083, Fibronectin_type1 IPR003961, FN3_dom IPR036116, FN3_sf IPR000562, FN_type2_dom IPR036943, FN_type2_sf IPR013783, Ig-like_fold IPR013806, Kringle-like |
Pfami | View protein in Pfam PF00039, fn1, 11 hits PF00040, fn2, 2 hits PF00041, fn3, 17 hits |
SMARTi | View protein in SMART SM00058, FN1, 12 hits SM00059, FN2, 2 hits SM00060, FN3, 17 hits |
SUPFAMi | SSF49265, SSF49265, 11 hits SSF57440, SSF57440, 2 hits |
PROSITEi | View protein in 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FINC_RAT | |
Accessioni | P04937Primary (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: | December 2, 2020 | |
This is version 182 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |