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Protein

Fibronectin

Gene

FN1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. May be involved in osteoblast compaction (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB-KW
  • cell migration Source: AgBase
  • regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Acute phase, Cell adhesion, Cell shape

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Gene namesi
Name:FN1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: AgBase
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000158529‹1 – ›1256FibronectinAdd BLAST›1256

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi5 ↔ 33PROSITE-ProRule annotation
Disulfide bondi31 ↔ 43PROSITE-ProRule annotation
Glycosylationi122N-linked (GlcNAc...)Sequence analysis1
Glycosylationi169N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1034O-linked (GalNAc...)By similarity1
Glycosylationi1035O-linked (GalNAc...)By similarity1
Glycosylationi1078N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1176 ↔ 1205PROSITE-ProRule annotation
Disulfide bondi1203 ↔ 1215PROSITE-ProRule annotation
Disulfide bondi1221 ↔ 1248PROSITE-ProRule annotation

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).

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiP11722.
PRIDEiP11722.

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 FBLN7 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005654.

Structurei

3D structure databases

ProteinModelPortaliP11722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 46Fibronectin type-I 1PROSITE-ProRule annotationAdd BLAST44
Domaini54 – 148Fibronectin type-III 1Add BLAST95
Domaini149 – 237Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST89
Domaini238 – 330Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST93
Domaini331 – 418Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST88
Domaini419 – 512Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST94
Domaini513 – 604Fibronectin type-III 6; extra domain 1PROSITE-ProRule annotationAdd BLAST92
Domaini605 – 692Fibronectin type-III 7; extra domain 2PROSITE-ProRule annotationAdd BLAST88
Domaini693 – 786Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST94
Domaini787 – 874Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST88
Domaini875 – 966Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST92
Domaini1074 – 1166Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST93
Domaini1174 – 1218Fibronectin type-I 2PROSITE-ProRule annotationAdd BLAST45
Domaini1219 – ›1256Fibronectin type-I 3PROSITE-ProRule annotationAdd BLAST›38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni236 – 509Cell-attachmentAdd BLAST274
Regioni690 – 961Heparin-binding 2Add BLAST272
Regioni962 – 1082Connecting strand 3 (CS-3) (V region)Add BLAST121
Regioni1153 – 1226Fibrin-binding 2By similarityAdd BLAST74

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi493 – 495Cell attachment site3

Sequence similaritiesi

Contains 3 fibronectin type-I domains.PROSITE-ProRule annotation
Contains 11 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IF4N. Eukaryota.
ENOG410Y2NH. LUCA.
HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP11722.
PhylomeDBiP11722.

Family and domain databases

CDDicd00063. FN3. 11 hits.
Gene3Di2.60.40.10. 11 hits.
InterProiIPR000083. Fibronectin_type1.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00039. fn1. 3 hits.
PF00041. fn3. 11 hits.
[Graphical view]
SMARTiSM00058. FN1. 3 hits.
SM00060. FN3. 11 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 7 hits.
PROSITEiPS01253. FN1_1. 2 hits.
PS51091. FN1_2. 3 hits.
PS50853. FN3. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. Each of the "extra domain" and the connecting strand 3 are present in some forms of fibronectin and absent in others.
Isoform 1 (identifier: P11722-1) [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
PLDQCQDSET RTFYQIGDSW EKYVHGVRYQ CYCYGRGIGE WHCQPLQAYA
60 70 80 90 100
PLSPPTNLRL EPNPDTGILI VSWDRSTTPG ISGYRVTTAP TNGQQGSTLE
110 120 130 140 150
EVVGADQTSC TFENLNPGVE YNVSVYAVKD DQESIPISKT ITQEVPQLTD
160 170 180 190 200
LSFVDITDSS IGLRWTPLNA STIIGYRITV VAAGESVPIF EDFVDSSVGY
210 220 230 240 250
YTVTGLEPGI DYDISVITLI NGGESAPTTL TQQTAVPPPT DLRFTNVGPD
260 270 280 290 300
TMRVTWTAPT SIVLSSFLVR YSPVKKEEDV AELTISPSDN VVVLTNLLPG
310 320 330 340 350
TEYLVRVYSV AEQHESAPLS GIQKTGLDSP TGLDFSDITA NSFTVHWIAP
360 370 380 390 400
RATITGYKIR HHPEHGVGRP KEDRVPPSRN SITLTNLLPG TEYVVSIIAV
410 420 430 440 450
NGREESVPLV GQQTTVSDVP RDLEVNPTSP TSLEISWDAP AVTVRYYRIT
460 470 480 490 500
YGETGGSSPV QEFTVPGTMS RATITGLKPG VDYTITVYAV TGRGDSPASS
510 520 530 540 550
KPVTVTYKTE IDTPSQMQVT DVQDNSISIR WLPSSSPVTG YRVTAVPKKG
560 570 580 590 600
HGPTKTKNVP PDQTQVTIEG LQPTVEYMVS VYAQNQNGES LPLVETAVTN
610 620 630 640 650
IDRPKGLTFT EVDVDSIKIA WESPQGQVTR YRVTYSSPED GIHELLPAPG
660 670 680 690 700
GEEDTAELHG LRPGSEYTIN IVAIYDDMES LPLTGTQSTA IPPPTNLKFT
710 720 730 740 750
QVTPTSLTVN WNAPNVRLTG YRVRVNPKEK TGPMKEINLS PDSTSAVVSG
760 770 780 790 800
LMVATKYEVS VYALKDSLTS RPAQGVVTTL ENVSPPRRAR VTDATETTIT
810 820 830 840 850
ITWRTKTETI TGFQIDAIPA ASGQNPIQRT ISPDVRTYTI TGLQPGNDYK
860 870 880 890 900
IYLYTLNENA RSSPVVIDAS TAIDAPSNLR FLTTTTNSLL ASWQPPRAKI
910 920 930 940 950
TGYIIRYDKP GSPAKELLPR PRPGTTEATI TGLEPGTEYT IYIIAVKNNQ
960 970 980 990 1000
KSEPLVGRKR TDDLPTLITG PHPNQPDMLD VPSVDEGTPY LTNNRYDNGN
1010 1020 1030 1040 1050
GIQLPGTSGH PQTIGHQGQQ VFFEEHGYRR PVPTTATPLR PGSRRQPPNV
1060 1070 1080 1090 1100
DEAIEIPGYQ VPIIVVPSYP HSREPRRNDT TGQEALSQTT ISWRPLLEST
1110 1120 1130 1140 1150
EYIISCQPVS QDEDTLQFRV PGTSSSATLT GLTRGATYNI IVEALKDHRR
1160 1170 1180 1190 1200
QKVLEEVVTV GNTVSEGLNQ PADDTCYDTY TGSFYSIGEE WERLSETGFK
1210 1220 1230 1240 1250
LWCQCLGFGS GHFRCDSSKW CHDNGVNYKI GEKWDRQGEN GQMIDCTCLG

NGKGEF
Length:1,256
Mass (Da):137,436
Last modified:November 1, 1997 - v3
Checksum:i345A4CA0E4D71D9B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-adjacent residuesi50 – 51Curated2
Sequence conflicti516Q → P in CAA29781 (PubMed:2823899).Curated1
Sequence conflicti516Q → P in AAA48772 (PubMed:2823899).Curated1
Sequence conflicti569 – 572EGLQ → QGLE (PubMed:2823899).Curated4
Non-terminal residuei12561

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00432 Genomic DNA. Translation: CAA23714.1.
U21327 mRNA. Translation: AAA73566.1.
X06533 Genomic DNA. Translation: CAA29781.1.
M26186 Genomic DNA. Translation: AAA48772.1. Sequence problems.
U20386 mRNA. Translation: AAB01062.1.
PIRiA28512.
A29355.
S71465.
UniGeneiGga.3994.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00432 Genomic DNA. Translation: CAA23714.1.
U21327 mRNA. Translation: AAA73566.1.
X06533 Genomic DNA. Translation: CAA29781.1.
M26186 Genomic DNA. Translation: AAA48772.1. Sequence problems.
U20386 mRNA. Translation: AAB01062.1.
PIRiA28512.
A29355.
S71465.
UniGeneiGga.3994.

3D structure databases

ProteinModelPortaliP11722.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005654.

Proteomic databases

PaxDbiP11722.
PRIDEiP11722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IF4N. Eukaryota.
ENOG410Y2NH. LUCA.
HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP11722.
PhylomeDBiP11722.

Family and domain databases

CDDicd00063. FN3. 11 hits.
Gene3Di2.60.40.10. 11 hits.
InterProiIPR000083. Fibronectin_type1.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00039. fn1. 3 hits.
PF00041. fn3. 11 hits.
[Graphical view]
SMARTiSM00058. FN1. 3 hits.
SM00060. FN3. 11 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 7 hits.
PROSITEiPS01253. FN1_1. 2 hits.
PS51091. FN1_2. 3 hits.
PS50853. FN3. 11 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFINC_CHICK
AccessioniPrimary (citable) accession number: P11722
Secondary accession number(s): Q90921
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.