Search by BoMiProt ID - Bomi163


Primary Information

BoMiProt ID Bomi163
Protein Name Lactadherin
Organism Bos taurus
Uniprot IdQ95114
Milk FractionWhey
Ref Sequence Id NP_788783.1
Amino Acid Lenth 427
Molecular Weight 47411
Fasta Sequence http://www.uniprot.org/uniprot/Q95114.fasta
Gene Name MFGE8
Gene Id 281913
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

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)

N-glycosylation, O-glycosylation,
Phosphorylation
>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