afamin; alpha-albumin; alpha-Alb (AFM, ALB2, ALBA)

Function: - vitamin E binding protein - may transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient - may be involved in the regulation & transport of vitamin E at the blood-brain barrier (putative) Structure: - N-glycosylated; more than 90% of the glycans are sialylated - belongs to the ALB/AFP/VDB family - contains 3 albumin domains Compartment: secreted Expression: - high level detected in plasma - also detected in extravascular fluids such as follicular & cerebrospinal fluids (at protein level)

General

glycoprotein secreted protein

Properties

SIZE: entity length = 599 aa MW = 69 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-21} Albumin 1 {22-210} MOTIF: N-glycosylation site {N33} cysteine residue {C77} MODIFICATION: cysteine residue {C86} cysteine residue {C86} MODIFICATION: cysteine residue {C77} cysteine residue {C99} MODIFICATION: cysteine residue {C114} N-glycosylation site {N109} cysteine residue {C113} MODIFICATION: cysteine residue {C124} cysteine residue {C114} MODIFICATION: cysteine residue {C99} cysteine residue {C124} MODIFICATION: cysteine residue {C113} cysteine residue {C148} MODIFICATION: cysteine residue {C193} cysteine residue {C192} MODIFICATION: cysteine residue {C201} cysteine residue {C193} MODIFICATION: cysteine residue {C148} cysteine residue {C201} MODIFICATION: cysteine residue {C192} Albumin 2 {211-403} MOTIF: cysteine residue {C224} MODIFICATION: cysteine residue {C270} cysteine residue {C269} MODIFICATION: cysteine residue {C277} cysteine residue {C270} MODIFICATION: cysteine residue {C224} cysteine residue {C277} MODIFICATION: cysteine residue {C269} cysteine residue {C289} MODIFICATION: cysteine residue {C303} cysteine residue {C302} MODIFICATION: cysteine residue {C313} cysteine residue {C303} MODIFICATION: cysteine residue {C289} cysteine residue {C313} MODIFICATION: cysteine residue {C302} cysteine residue {C340} MODIFICATION: cysteine residue {C385} N-glycosylation site {N383} cysteine residue {C384} MODIFICATION: cysteine residue {C393} cysteine residue {C385} MODIFICATION: cysteine residue {C340} cysteine residue {C393} MODIFICATION: cysteine residue {C384} N-glycosylation site {N402} Albumin 3 {404-599} MOTIF: cysteine residue {C416} MODIFICATION: cysteine residue {C462} cysteine residue {C461} MODIFICATION: cysteine residue {C470} cysteine residue {C462} MODIFICATION: cysteine residue {C416} cysteine residue {C470} MODIFICATION: cysteine residue {C461} cysteine residue {C483} MODIFICATION: cysteine residue {C499} N-glycosylation site {N488} cysteine residue {C498} MODIFICATION: cysteine residue {C509} cysteine residue {C499} MODIFICATION: cysteine residue {C483} cysteine residue {C509} MODIFICATION: cysteine residue {C498} cysteine residue {C536} MODIFICATION: cysteine residue {C581} cysteine residue {C580} MODIFICATION: cysteine residue {C589} cysteine residue {C581} MODIFICATION: cysteine residue {C536} cysteine residue {C589} MODIFICATION: cysteine residue {C580}

Database Correlations

OMIM 104145 UniProt P43652 Pfam PF00273 Entrez Gene 173 Kegg hsa:173

References

UniProt :accession P43652