UniProt functional annotation for P11276



	UniProt functional annotation for P11276

UniProt code: P11276.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (By similarity). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (PubMed:21768292). Participates in the regulation of type I collagen deposition by osteoblasts (PubMed:21768292). {ECO:0000250|UniProtKB:P02751, ECO:0000269|PubMed:21768292}.

Function: [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. {ECO:0000250|UniProtKB:P02751}.

Subunit: 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, AMBP, LGALS3BP and COL13A1 and COMP (By similarity). Interacts with TNR; interaction mediates inhibition of cell adhesion and neurite outgrowth. Interacts with FBLN7. Interacts with FST3 and MYOC (By similarity). {ECO:0000250}.

Subcellular location: Secreted, extracellular space, extracellular matrix.

Tissue specificity: Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level) (PubMed:29777959). 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. {ECO:0000269|PubMed:29777959}.

Induction: Glucocorticoids suppressed mRNA expression and protein synthesis.

Ptm: Sulfated. {ECO:0000250|UniProtKB:P02751}.

Ptm: 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). {ECO:0000269|PubMed:9312106}.

Ptm: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02751}.

Ptm: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000250|UniProtKB:P02751}.

Ptm: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000269|PubMed:26954549}.

Ptm: Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000250|UniProtKB:P07589}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (By similarity). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (PubMed:21768292). Participates in the regulation of type I collagen deposition by osteoblasts (PubMed:21768292). {ECO:0000250\|UniProtKB:P02751, ECO:0000269\|PubMed:21768292}.



Function:		[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. {ECO:0000250\|UniProtKB:P02751}.


Subunit:		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, AMBP, LGALS3BP and COL13A1 and COMP (By similarity). Interacts with TNR; interaction mediates inhibition of cell adhesion and neurite outgrowth. Interacts with FBLN7. Interacts with FST3 and MYOC (By similarity). {ECO:0000250}.
Subcellular location:		Secreted, extracellular space, extracellular matrix.
Tissue specificity:		Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level) (PubMed:29777959). 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. {ECO:0000269\|PubMed:29777959}.
Induction:		Glucocorticoids suppressed mRNA expression and protein synthesis.
Ptm:		Sulfated. {ECO:0000250\|UniProtKB:P02751}.
Ptm:		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). {ECO:0000269\|PubMed:9312106}.
Ptm:		Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250\|UniProtKB:P02751}.
Ptm:		Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000250\|UniProtKB:P02751}.
Ptm:		Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000269\|PubMed:26954549}.
Ptm:		Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000250\|UniProtKB:P07589}.