|Ref Sequence Id||NP_788783.1|
|Amino Acid Lenth||427|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||serum, urine, cerebrospinal fluid|
|Protein Function||Involved in phagocytosis, angiogenesis, atherosclerosis, tissue remodeling, blood coagulation processes and haemostasis regulation; modulate function as a cell adhesion protein in the connection of smooth muscles to fibers in arteries; can inhibit enzymes engaged in coagulation processes such as prothrombinase, factor X, and VIIa; expressed on the acrosomal cap of sperm and helps in fusion with oocyte|
|Biochemical Properties||Exhibits specificity for 3D structure of phosphatidyl serine and high affinity for membrane binding sites, similar to factors VIII and V; lactadherin recognizes many more binding sites on membranes that are highly curved as opposed to the more planar membranes found in larger vesicles|
|Significance in milk||Lines phospholipid bilayer of MFG and stabilises the bilipid structure;|
|PTMs||Glycosylated; contained galactose, N-acetylgalactosamine and fucose, and which was 0- linked to Ser9 in PAS-6 and to Thr16 in PAS-7 as detected in bovine MFG; N and O-glycosylated depending on different isoforms found in mouse mammary gland|
| Site(s) of PTM(s) |
|>sp|Q95114|MFGM_BOVIN Lactadherin OS=Bos taurus OX=9913 GN=MFGE8 PE=1 SV=2
MPCPRLLAALFCSSGLFAASGDFCDSS*27LCLHGGT*34CLLNEDRTPPFYCLCP EGFTGLLCN*59ETEHGPCFPNPCHNDAECQVTDDSHRGDVFIQYICKCPLGY VGIHCETTCTSPLGMQTGAIADSQISASSMHLGFMGLQRWAPELARLHQT GIVNAWTSGNYDKNPWIQVNLMRKMWVTGVVTQGASRAGSAEYLKTFKVA YSTDGRQFQFIQVAGRSGDKIFIGNVNSGLKINLFDTPLETQYVRLVPI ICHRGCTLRFELLGCELNGCTEPLGLKDNTIPNKQITASSYYKTWGLSAF SWFPYYARLDNQGKFNAWTAQTNSASEWLQIDLGSQKRVTGIITQGARDF GHIQYVAAYRVAYGDDGVTWTEYKDPGASESKIFPGNMDNNSHKKNIFET PFQARFVRIQPVAWHNRITLRVELLGC
|PDB ID||2pqs, 3bn6,|
|Bibliography||1. Oshima, K., Aoki, N., Negi, M., Kishi, M., Kitajima, K., and Matsuda, T. (1999) Lactation-Dependent Expression of an mRNA Splice Variant with an Exon for a MultiplyO-Glycosylated Domain of Mouse Milk Fat Globule Glycoprotein MFG-E8. Biochem. Biophys. Res. Commun. 254, 522–528. |
2. Hvarregaard, J., Andersen, M. H., Berglund, L., Rasmussen, J. T., and Petersen, T. E. (1996) Characterization of glycoprotein PAS-6/7 from membranes of bovine milk fat globules. Eur. J. Biochem. 240, 628–636.
3. Shi, J., Heegaard, C. W., Rasmussen, J. T., and Gilbert, G. E. (2004) Lactadherin binds selectively to membranes containing phosphatidyl-L-serine and increased curvature. Biochim. Biophys. Acta 1667, 82–90.
4. Silvestre, J.-S., Théry, C., Hamard, G., Boddaert, J., Aguilar, B., Delcayre, A., Houbron, C., Tamarat, R., Blanc-Brude, O., Heeneman, S., Clergue, M., Duriez, M., Merval, R., Lévy, B., Tedgui, A., Amigorena, S., and Mallat, Z. (2005) Lactadherin promotes VEGF-dependent neovascularization. Nat. Med. 11, 499–506.
5. Shi, J. and Gilbert, G. E. (2003) Lactadherin inhibits enzyme complexes of blood coagulation by competing for phospholipid-binding sites. Blood 101, 2628–2636.
6. Gilbert, G. E., Novakovic, V. A., Shi, J., Rasmussen, J., and Pipe, S. W. (2015) Platelet binding sites for factor VIII in relation to fibrin and phosphatidylserine. Blood 126, 1237–1244