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UniProtKB - P04937 (FINC_RAT)

Protein

Fibronectin

Gene

Fn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
DNA bindingi906 – 1171Add BLAST266

GO - Molecular functioni

  • extracellular matrix structural constituent Source: RGD
  • heparin binding Source: UniProtKB-KW
  • mercury ion binding Source: RGD
  • protease binding Source: RGD
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHeparin-binding
Biological processAcute phase, Angiogenesis, Cell adhesion, Cell shape

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Cleaved into the following chain:
Anastellin
Gene namesi
Name:Fn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2624 Fn1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001923725 – 2477FibronectinAdd BLAST2453
ChainiPRO_0000390481627 – 701AnastellinBy similarityAdd BLAST75

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki48Isoglutamyl 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 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...) asparagineSequence analysis1
Disulfide bondi434 ↔ 461By similarity
Disulfide bondi470 ↔ 498By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi518 ↔ 545By similarity
Glycosylationi528N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi542N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi543 ↔ 555By similarity
Disulfide bondi561 ↔ 589By similarity
Disulfide bondi587 ↔ 599By similarity
Modified residuei875SulfotyrosineSequence analysis1
Glycosylationi876N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei880SulfotyrosineSequence analysis1
Glycosylationi1006N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1243N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1290N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2154O-linked (GalNAc...) threonineBy similarity1
Glycosylationi2198N-linked (GlcNAc...) asparagineSequence analysis1
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
Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Oxidation, Phosphoprotein, Sulfation

Proteomic databases

PaxDbiP04937
PeptideAtlasiP04937
PRIDEiP04937

PTM databases

CarbonylDBiP04937
iPTMnetiP04937
PhosphoSitePlusiP04937

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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActiP04937, 2 interactors
MINTiP04937
STRINGi10116.ENSRNOP00000019772

Structurei

3D structure databases

ProteinModelPortaliP04937
SMRiP04937
ModBaseiSearch...
MobiDBiSearch...

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 – 345Fibronectin type-I 6PROSITE-ProRule annotationAdd BLAST40
Domaini355 – 403Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini415 – 463Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini468 – 511Fibronectin type-I 7PROSITE-ProRule annotationAdd BLAST44
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 – 901Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST90
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 – 2286Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST94
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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000234344
HOVERGENiHBG005731
InParanoidiP04937
PhylomeDBiP04937

Family and domain databases

CDDicd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 17 hits
Gene3Di2.10.10.10, 2 hits
2.60.40.10, 17 hits
InterProiView 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
PfamiView protein in Pfam
PF00039 fn1, 11 hits
PF00040 fn2, 2 hits
PF00041 fn3, 17 hits
SMARTiView protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 17 hits
SUPFAMiSSF49265 SSF49265, 11 hits
SSF57440 SSF57440, 2 hits
PROSITEiView 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

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.

This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A096P6L8A0A096P6L8_RAT
Fibronectin
Fn1 rCG_25006
2,477Annotation score:
F1LST1F1LST1_RAT
Fibronectin
Fn1 rCG_25006
2,387Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2318G → A in AAA41166 (PubMed:6317187).Curated1
Sequence conflicti2318G → A in AAA41167 (PubMed:6317187).Curated1
Sequence conflicti2318G → A in AAA41168 (PubMed:6317187).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0032581720 – 1809Missing in isoform 2. CuratedAdd BLAST90
Alternative sequenceiVSP_0032602082 – 2200Missing in isoform 4. CuratedAdd BLAST119
Alternative sequenceiVSP_0032592082 – 2106Missing in isoform 3. CuratedAdd BLAST25

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

Similar 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
PIRiS14428
UniGeneiRn.1604

3D structure databases

ProteinModelPortaliP04937
SMRiP04937
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04937, 2 interactors
MINTiP04937
STRINGi10116.ENSRNOP00000019772

PTM databases

CarbonylDBiP04937
iPTMnetiP04937
PhosphoSitePlusiP04937

Proteomic databases

PaxDbiP04937
PeptideAtlasiP04937
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

PROiPR:P04937

Family and domain databases

CDDicd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 17 hits
Gene3Di2.10.10.10, 2 hits
2.60.40.10, 17 hits
InterProiView 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
PfamiView protein in Pfam
PF00039 fn1, 11 hits
PF00040 fn2, 2 hits
PF00041 fn3, 17 hits
SMARTiView protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 17 hits
SUPFAMiSSF49265 SSF49265, 11 hits
SSF57440 SSF57440, 2 hits
PROSITEiView 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
ProtoNetiSearch...

Entry informationi

Entry nameiFINC_RAT
AccessioniPrimary (citable) accession number: P04937
Secondary accession number(s): Q6LDX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1990
Last modified: July 18, 2018
This is version 171 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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