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MGP001097

UniProt Annotations

Entry Information
Gene Namefibronectin 1
Protein EntryFINC_HUMAN
UniProt IDP02751
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=17; Comment=Additional isoforms seem to exist.; Name=1; IsoId=P02751-1; Sequence=Displayed; Name=2; Synonyms=MSF-FN70, Migration stimulation factor FN70; IsoId=P02751-2; Sequence=VSP_003255, VSP_003256, VSP_003257; Name=3; Synonyms=V89; IsoId=P02751-3; Sequence=VSP_008110; Name=4; Synonyms=Fibronectin III-15X; IsoId=P02751-4; Sequence=VSP_008107, VSP_008111, VSP_008112; Name=5; Synonyms=Fibronectin (V+I-10)-; IsoId=P02751-5; Sequence=VSP_008107, VSP_008113; Name=6; Synonyms=Fibronectin (V+III-15)-; IsoId=P02751-6; Sequence=VSP_008109; Name=7; Synonyms=Fibronectin containing extra ED-B domain; IsoId=P02751-7; Sequence=VSP_008104, VSP_008110; Name=8; Synonyms=Fibronectin not containing EIIIA domain; IsoId=P02751-8; Sequence=VSP_008106; Name=9; Synonyms=Fibronectin not containing EIIIA and EIIIB and uses V64 variant of IIICS region; IsoId=P02751-9; Sequence=VSP_008106, VSP_008108, VSP_008110; Name=10; IsoId=P02751-10; Sequence=VSP_008106, VSP_008107; Name=11; Synonyms=Fibronectin containing extra type III repeat (EDII), exon x+2; IsoId=P02751-11; Sequence=VSP_008105; Name=12; IsoId=P02751-12; Sequence=VSP_013681, VSP_008106, VSP_008108, VSP_008110; Name=13; IsoId=P02751-13; Sequence=VSP_008104, VSP_008106, VSP_008107; Note=No experimental confirmation available.; Name=14; IsoId=P02751-14; Sequence=VSP_008106, VSP_008110; Name=15; IsoId=P02751-15; Sequence=VSP_008104; Note=No experimental confirmation available.; Name=16; Synonyms=Migration stimulation factor, MSF; IsoId=P02751-16; Sequence=VSP_003256, VSP_003257; Note=Expressed by fetal and tumor-associated cells.; Name=17; IsoId=P02751-17; Sequence=VSP_047310, VSP_047311; Note=Gene prediction based on EST data.;
Developmental StageUgl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age. {ECO:0000269|PubMed:17614963, ECO:0000269|PubMed:3584091}.
DiseaseGlomerulopathy with fibronectin deposits 2 (GFND2) [MIM:601894]: Genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life. {ECO:0000269|PubMed:18268355}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionAnastellin 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.
FunctionFibronectins 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.
InteractionQ99IB8:- (xeno); NbExp=3; IntAct=EBI-1220319, EBI-6927928; P29279:CTGF; NbExp=5; IntAct=EBI-1220319, EBI-2835375; P35555:FBN1; NbExp=2; IntAct=EBI-1220319, EBI-2505934; P35556:FBN2; NbExp=2; IntAct=EBI-1220319, EBI-6164392; P14738:fnbA (xeno); NbExp=18; IntAct=EBI-1220319, EBI-8398157; Q53682:fnbB (xeno); NbExp=19; IntAct=EBI-1220319, EBI-8398005; Q93ED6:fne (xeno); NbExp=8; IntAct=EBI-1220319, EBI-9826140; P06241:FYN; NbExp=2; IntAct=EBI-7133890, EBI-515315; P08519:LPA; NbExp=2; IntAct=EBI-1220319, EBI-9232288; P11684:SCGB1A1; NbExp=3; IntAct=EBI-1220319, EBI-7797649; P21980:TGM2; NbExp=3; IntAct=EBI-1220319, EBI-727668; P40337:VHL; NbExp=2; IntAct=EBI-1220319, EBI-301246;
PtmForms 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).
PtmIt is not known whether both or only one of Thr-2064 and Thr- 2065 are/is glycosylated. {ECO:0000269|PubMed:11285216, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16037490, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17614963, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2012601, ECO:0000269|PubMed:3584091}.
PtmPhosphorylation sites are present in the extracellular medium. {ECO:0000269|PubMed:17081983, ECO:0000269|PubMed:18318008}.
PtmProteolytic processing produces the C-terminal NC1 peptide, anastellin.
PtmSulfated. {ECO:0000269|PubMed:2414772}.
Sequence CautionSequence=AAX76513.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=BAD93077.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=CAD91166.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=CAD97964.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=CAD97965.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=CAD97984.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=CAH18136.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
SimilarityContains 12 fibronectin type-I domains. {ECO:0000255|PROSITE-ProRule:PRU00478}.
SimilarityContains 16 fibronectin type-III domains. {ECO:0000255|PROSITE-ProRule:PRU00316}.
SimilarityContains 2 fibronectin type-II domains. {ECO:0000255|PROSITE-ProRule:PRU00479}.
Subcellular LocationSecreted, extracellular space, extracellular matrix.
SubunitMostly 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, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP. Interacts with S.aureus fnbA. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3 and MYOC. {ECO:0000250, ECO:0000269|PubMed:11773026, ECO:0000269|PubMed:11956183, ECO:0000269|PubMed:12225811, ECO:0000269|PubMed:12736686, ECO:0000269|PubMed:1400330, ECO:0000269|PubMed:16336961, ECO:0000269|PubMed:18713862, ECO:0000269|PubMed:19251642, ECO:0000269|PubMed:8114919, ECO:0000269|PubMed:9501082}.
Tissue SpecificityPlasma 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. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine. {ECO:0000269|PubMed:17614963, ECO:0000269|PubMed:3584091}.
Web ResourceName=Wikipedia; Note=Fibronectin entry; URL="http://en.wikipedia.org/wiki/Fibronectin";
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