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Gene Review

MCFD2  -  multiple coagulation factor deficiency 2

Homo sapiens

Synonyms: F5F8D, F5F8D2, LMAN1IP, Multiple coagulation factor deficiency protein 2, Neural stem cell-derived neuronal survival protein, ...
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Disease relevance of MCFD2


High impact information on MCFD2

  • These findings suggest that the MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins [3].
  • Here we show that inactivating mutations in MCFD2 cause F5F8D with a phenotype indistinguishable from that caused by mutations in LMAN1 [3].
  • LMAN1 and MCFD2 form a protein complex that functions as a cargo receptor ferrying FV and FVIII from the endoplasmic reticulum to the Golgi [4].
  • MCFD2 is a soluble EF-hand-containing protein that is retained in the endoplasmic reticulum through its interaction with LMAN1 [5].
  • Their efficient secretion requires the membrane lectin ER Golgi intermediate compartment protein-53 (ERGIC-53) and its soluble luminal interaction partner multiple coagulation factor deficiency protein 2 (MCFD2), which form a cargo receptor complex in the early secretory pathway [6].

Biological context of MCFD2

  • YFP PCA analysis revealed the oligomerization of ERGIC-53 and its interaction with MCFD2, as well as its lectin-mediated interaction with cathepsin Z [1].
  • The results indicate that ERGIC-53 can bind cargo glycoproteins in an MCFD2-independent fashion and suggest that MCFD2 is a recruitment factor for blood coagulation factors V and VIII [6].

Other interactions of MCFD2

  • Combined deficiency of factor (F)V and FVIII (F5F8D) and combined deficiency of vitamin K-dependent clotting factors (VKCFD) comprise the vast majority of reported cases of familial multiple coagulation factor deficiencies [7].


  1. Capturing protein interactions in the secretory pathway of living cells. Nyfeler, B., Michnick, S.W., Hauri, H.P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  2. Combined factor V - factor VIII deficiency (F5F8D): Compound heterozygosity for two novel truncating mutations in LMAN1 in a consanguineous patient. Farah, R.A., de Moerloose, P., Bouchardy, I., Morris, M.A., Barakat, W., Sayad, A.E., Neerman-Arbez, M. Thromb. Haemost. (2006) [Pubmed]
  3. Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex. Zhang, B., Cunningham, M.A., Nichols, W.C., Bernat, J.A., Seligsohn, U., Pipe, S.W., McVey, J.H., Schulte-Overberg, U., de Bosch, N.B., Ruiz-Saez, A., White, G.C., Tuddenham, E.G., Kaufman, R.J., Ginsburg, D. Nat. Genet. (2003) [Pubmed]
  4. Combined deficiency of factor V and factor VIII is due to mutations in either LMAN1 or MCFD2. Zhang, B., McGee, B., Yamaoka, J.S., Guglielmone, H., Downes, K.A., Minoldo, S., Jarchum, G., Peyvandi, F., de Bosch, N.B., Ruiz-Saez, A., Chatelain, B., Olpinski, M., Bockenstedt, P., Sperl, W., Kaufman, R.J., Nichols, W.C., Tuddenham, E.G., Ginsburg, D. Blood (2006) [Pubmed]
  5. LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. Zhang, B., Kaufman, R.J., Ginsburg, D. J. Biol. Chem. (2005) [Pubmed]
  6. Cargo Selectivity of the ERGIC-53/MCFD2 Transport Receptor Complex. Nyfeler, B., Zhang, B., Ginsburg, D., Kaufman, R.J., Hauri, H.P. Traffic (2006) [Pubmed]
  7. Familial multiple coagulation factor deficiencies: new biologic insight from rare genetic bleeding disorders. Zhang, B., Ginsburg, D. J. Thromb. Haemost. (2004) [Pubmed]
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