View source for Biology:Fibronectin type II domain

{{Pfam_box
| Symbol = fn2
| Name = Fibronectin type II domain
| image =1h8p_opm.png
| width =250
| caption =Collagen-binding type II domain of seminal plasma protein PDC-109.<ref name="pmid11937055">{{cite journal |vauthors=Wah DA, Fernández-Tornero C, Sanz L, Romero A, Calvete JJ |title=Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex |journal=Structure |volume=10 |issue=4 |pages=505–14 |date=April 2002 |pmid=11937055 |doi= 10.1016/S0969-2126(02)00751-7|doi-access=free }}</ref>
| Pfam= PF00040
| InterPro= IPR000562
| SMART= SM00059
| PROSITE = PDOC00022
| SCOP = 1pdc
| TCDB =
| OPM family= 115
| OPM protein= 1h8p
| CDD = cd00062
| PDB=
}}

'''Fibronectin type II domain ''' is a [[Biology:Collagen|collagen]]-binding [[Biology:Protein domain|protein domain]]. Fibronectin is a multi-domain [[Chemistry:Glycoprotein|glycoprotein]], found in a soluble form in plasma, and in an insoluble form in loose connective tissue and basement membranes, that binds cell surfaces and various compounds including [[Biology:Collagen|collagen]], [[Biology:Fibrin|fibrin]], [[Chemistry:Heparin|heparin]], [[Biology:DNA|DNA]], and [[Biology:Actin|actin]]. Fibronectins are involved in a number of important functions e.g., [[Biology:Wound healing|wound healing]]; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular [[Biology:Cytoskeleton|cytoskeleton]]; and tumour [[Medicine:Metastasis|metastasis]].<ref name="PUB00004633">{{cite journal |vauthors=Dean DC, Bowlus CL, Bourgeois S |title=Cloning and analysis of the {{sic|promotor|hide=y}} region of the human fibronectin gene |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue=7 |pages=1876–1880 |year=1987 |pmid=3031656 |doi=10.1073/pnas.84.7.1876 |pmc=304544|doi-access=free }}</ref> The major part of the sequence of fibronectin consists of the repetition of three types of domains, which are called type I, II, and III.<ref name="PUB00001346">{{cite journal |vauthors=Skorstengaard K, Jensen MS, Sahl P, Petersen TE, Magnusson S |title=Complete primary structure of bovine plasma fibronectin |journal=Eur. J. Biochem. |volume=161 |issue=2 |pages=441–453 |year=1986 |pmid=3780752 |doi=10.1111/j.1432-1033.1986.tb10464.x}}</ref>

Type II domain is approximately sixty amino acids long,<ref name="PUB12244123">{{cite journal |vauthors=Pankov R, Yamada KM |title=Fibronectin at a glance.|journal=J Cell Sci |volume=115|pages=3861–3863 |year=2002 |issue=20|pmid=12244123 |doi=10.1242/jcs.00059|doi-access=free }}</ref> contains four conserved cysteines involved in disulfide bonds and is part of the collagen-binding region of fibronectin.  Type II domains occur two times in fibronectin. Type II domains have also been found in a range of proteins including blood coagulation factor XII; bovine seminal plasma proteins PDC-109 (BSP-A1/A2) and BSP-A3;<ref name="PUB00000461">{{cite journal |vauthors=Chretien M, Seidah NG, Manjunath P, Rochemont J, Sairam MR |title=Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin |journal=Biochem. J. |volume=243 |issue=1 |pages=195–203 |year=1987 |doi=10.1042/bj2430195 |pmid=3606570 |pmc=1147832}}</ref> cation-independent mannose-6-phosphate receptor;<ref name="PUB00000084">{{cite journal |author=Kornfeld S |title=Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors |journal=Annu. Rev. Biochem. |volume=61 |issue= 1|pages=307–330 |year=1992 |pmid=1323236 |doi=10.1146/annurev.bi.61.070192.001515}}</ref> mannose receptor of macrophages;<ref name="PUB00002562">{{cite journal |vauthors=Drickamer K, Taylor ME, Conary JT, Lennartz MR, Stahl PD |title=Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains|journal=J. Biol. Chem. |volume=265 |issue=21 |pages=12156–12162 |year=1990 |doi=10.1016/S0021-9258(19)38325-5|pmid=2373685|doi-access=free}}</ref> 180 Kd secretory phospholipase A2 receptor;<ref name="PUB00002849">{{cite journal |vauthors=Lazdunski M, Barhanin J, Lambeau G, Ancian P |title=Cloning and expression of a membrane receptor for secretory phospholipases A2 |journal=J. Biol. Chem. |volume=269 |issue=3|pages=1575–1578 |year=1994 |doi=10.1016/S0021-9258(17)42060-6 |pmid=8294398|doi-access=free }}</ref> DEC-205 receptor;<ref name="PUB00004209">{{cite journal |vauthors=Jiang W, Swiggard WJ, Heufler C, Peng M, Mirza A, Steinman RM, Nussenzweig MC |title=The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing |journal=Nature |volume=375 |issue=6527 |pages=151–155 |year=1995 |pmid=7753172 |doi=10.1038/375151a0|bibcode=1995Natur.375..151J |s2cid=4244472 }}</ref> 72 Kd and 92 Kd type IV collagenase ({{EC number|3.4.24.24}});<ref name="PUB00002483">{{cite journal |vauthors=Grant GA, Collier IE, Wilhelm SM, Eisen AZ, Marmer BL, Seltzer JL, Kronberger A, Bauer EA, Goldberg GI, He CS |title=H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen |journal=J. Biol. Chem. |volume=263 |issue=14 |pages=6579–6587 |year=1988 |doi=10.1016/S0021-9258(18)68680-6 |pmid=2834383|doi-access=free }}</ref> and hepatocyte growth factor activator.<ref name="PUB00002776">{{cite journal |vauthors=Miyazawa K, Shimomura T, Kitamura A, Kondo J, Morimoto Y, Kitamura N |title=Molecular cloning and sequence analysis of the cDNA for a human serine protease responsible for activation of hepatocyte growth factor. Structural similarity of the protease precursor to blood coagulation factor XII |journal=J. Biol. Chem. |volume=268 |issue=14 |pages=10024–10028 |year=1993 |doi=10.1016/S0021-9258(18)82167-6 |pmid=7683665|doi-access=free }}</ref>

== Fibronectin type II domain and Lipid bilayer interaction ==

Fibronectin type II domain is part of the extracellular portions of EphA2 receptor proteins. FN2 domain on EphA2 receptors bears positively-charged components, namely K441 and R443, which attract and almost exclusively bind to anionic lipids such as anionic membrane lipid phosphatidylglycerol.<ref name="Chavent_2016" /> K441 and R443 together make up a membrane-binding motif that allows EphA2 receptors to attach to the cell membrane.<ref name="Chavent_2016">{{cite journal | vauthors = Chavent M, Seiradake E, Jones EY, Sansom MS | title = Structures of the EphA2 Receptor at the Membrane: Role of Lipid Interactions | journal = Structure | volume = 24 | issue = 2 | pages = 337–47 | date = February 2016 | pmid = 26724997 | pmc = 4744086 | doi = 10.1016/j.str.2015.11.008 }}</ref>

==Human proteins containing this domain ==
BSPH1;     ELSPBP1;   [[Biology:Factor XII|F12]];       FN1;       HGFAC;     IGF2R;     [[Biology:LY75|LY75]];      [[Biology:MMP2|MMP2]];
[[Biology:MMP9|MMP9]];      MRC1;      MRC1L1;    MRC2;      PLA2R1;    SEL1L;

*Fibronectin type I domain: [[Biology:Factor XII|F12]];       FN1;       HGFAC;     [[Biology:Tissue plasminogen activator|PLAT]];

==References==
{{reflist|2}}

==External links==
* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC00022 Fibronectin type-II collagen-binding domain] in [[Biology:PROSITE|PROSITE]]

[[Category:Protein domains]]
[[Category:Peripheral membrane proteins]]



{{Sourceattribution|Fibronectin type II domain}}