Lectin, Mannose-Binding, 1 (LMAN1) Antibody – Rabbit Polyclonal

The protein encoded by this gene is a type I integral membrane protein localized in the intermediate region between the endoplasmic reticulum and the Golgi, presumably recycling between the two compartments. The protein is a mannose-specific lectin and is a member of a novel family of plant lectin homologs in the secretory pathway of animal cells. Mutations in the gene are associated with a coagulation defect. Using positional cloning, the gene was identified as the disease gene leading to combined factor V-factor VIII deficiency, a rare, autosomal recessive disorder in which both coagulation factors V and VIII are diminished. [provided by RefSeq, Jul 2008]

LMAN1: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1); also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.

Protein type: Membrane protein, integral

Chromosomal Location of Human Ortholog: 18q21.3-q22

Cellular Component: Golgi membrane; endoplasmic reticulum membrane; ER-Golgi intermediate compartment membrane; sarcomere; membrane; integral to membrane; ER-Golgi intermediate compartment

Molecular Function: mannose binding; protein binding; metal ion binding; unfolded protein binding

Biological Process: endoplasmic reticulum organization and biogenesis; ER to Golgi vesicle-mediated transport; cellular protein metabolic process; protein folding; protein exit from endoplasmic reticulum; protein amino acid N-linked glycosylation via asparagine; blood coagulation; post-translational protein modification; Golgi organization and biogenesis

Disease: Factor V And Factor Viii, Combined Deficiency Of, 1