Apolipoprotein A-I (APOA1)
The protein contains 267 amino acids for an estimated molecular weight of 30778 Da.
Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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Biological Process
Adrenal gland development
Amyloid fibril formation
Animal organ regeneration
Blood coagulation
Blood vessel endothelial cell migration
Cellular lipid metabolic process
Cellular protein metabolic process
Cholesterol biosynthetic process
Cholesterol efflux
Cholesterol homeostasis
Cholesterol import
Cholesterol metabolic process
Cholesterol transport
Chylomicron assembly
Chylomicron remodeling
Endothelial cell proliferation
G protein-coupled receptor signaling pathway
Glucocorticoid metabolic process
High-density lipoprotein particle assembly
High-density lipoprotein particle clearance
High-density lipoprotein particle remodeling
Integrin-mediated signaling pathway
Lipid storage
Lipid transport
Lipoprotein biosynthetic process
Lipoprotein metabolic process
Negative chemotaxis
Negative regulation of cell adhesion molecule production
Negative regulation of cytokine production involved in immune response
Negative regulation of cytokine secretion involved in immune response
Negative regulation of heterotypic cell-cell adhesion
Negative regulation of inflammatory response
Negative regulation of interleukin-1 beta production
Negative regulation of interleukin-1 beta secretion
Negative regulation of lipase activity
Negative regulation of response to cytokine stimulus
Negative regulation of tumor necrosis factor-mediated signaling pathway
Negative regulation of very-low-density lipoprotein particle remodeling
Neuron projection regeneration
Peptidyl-methionine modification
Peripheral nervous system axon regeneration
Phosphatidylcholine biosynthetic process
Phosphatidylcholine metabolic process
Phospholipid efflux
Phospholipid homeostasis
Phototransduction, visible light
Platelet activation
Platelet degranulation
Positive regulation of cholesterol efflux
Positive regulation of cholesterol esterification
Positive regulation of fatty acid biosynthetic process
Positive regulation of hydrolase activity
Positive regulation of lipid biosynthetic process
Positive regulation of lipoprotein lipase activity
Positive regulation of phagocytosis
Positive regulation of phospholipid efflux
Positive regulation of Rho protein signal transduction
Positive regulation of stress fiber assembly
Positive regulation of substrate adhesion-dependent cell spreading
Positive regulation of transferase activity
Positive regulation of triglyceride catabolic process
Post-translational protein modification
Protein oxidation
Protein stabilization
Receptor-mediated endocytosis
Regulation of Cdc42 protein signal transduction
Regulation of cholesterol transport
Regulation of intestinal cholesterol absorption
Regulation of lipid metabolic process
Regulation of metabolic process
Regulation of protein phosphorylation
Response to drug
Response to estrogen
Response to nutrient
Retinoid metabolic process
Reverse cholesterol transport
Small molecule metabolic process
Transmembrane transport
Triglyceride catabolic process
Triglyceride homeostasis
Very-low-density lipoprotein particle remodeling
Vitamin transport
Cellular Component
Blood microparticle
Cell surface
Chylomicron
Collagen-containing extracellular matrix
Cytoplasmic vesicle
Cytosol
Discoidal high-density lipoprotein particle
Early endosome
Endocytic vesicle
Endocytic vesicle lumen
Endoplasmic reticulum lumen
Extracellular exosome
Extracellular matrix
Extracellular region
Extracellular space
Extracellular vesicle
High-density lipoprotein particle
Intermediate-density lipoprotein particle
Low-density lipoprotein particle
Nucleus
Plasma membrane
Secretory granule lumen
Spherical high-density lipoprotein particle
Very-low-density lipoprotein particle
Vesicle
Molecular Function
Amyloid-beta binding
Apolipoprotein A-I receptor binding
Apolipoprotein receptor binding
Chemorepellent activity
Cholesterol binding
Cholesterol transfer activity
Cholesterol transporter activity
Enzyme binding
Heat shock protein binding
High-density lipoprotein particle binding
High-density lipoprotein particle receptor binding
Identical protein binding
Lipase inhibitor activity
Phosphatidylcholine binding
Phosphatidylcholine-sterol O-acyltransferase activator activity
Phospholipid binding
Phospholipid transporter activity
Signaling receptor binding
The reference OMIM entry for this protein is 105200
Amyloidosis, familial visceral
Amyloidosis viii
Ostertag type amyloidosis
German type amyloidosis
Amyloidosis, familial renal
Amyloidosis, systemic nonneuropathic
A number sign (#) is used with this entry because of the evidence that systemic nonneuropathic amyloidosis is the result of mutation in the apolipoprotein A1 gene (APOA1; 107680), the fibrinogen alpha-chain gene (FGA; 134820), the lysozyme gene (LYZ; 153450), or the gene encoding beta-2-microglobulin (B2M; 109700).
CLINICAL FEATURES
Ostertag (1932, 1950) reported on a family with visceral amyloidosis. A woman, 3 of her children, and 1 of her grandchildren were affected with chronic nephropathy, arterial hypertension, and hepatosplenomegaly. Albuminuria, hematuria and pitting edema were early signs. The age of onset was variable. Death occurred about 10 years after onset. The visceral involvement by amyloid was found to be extensive. Maxwell and Kimbell (1936) described 3 brothers who died of visceral, especially renal, amyloidosis in their 40s. Chronic weakness, edema, proteinuria, and hepatosplenomegaly were features. McKusick (1974) followed up on the family reported by Maxwell and Kimbell (1936). The father of the 3 affected brothers died at age 72 after an automobile accident and their mother died suddenly at age 87 after being in apparent good health. A son of one of the brothers had frequent bouts of unexplained fever in childhood (as did his father and 2 uncles), accompanied at times by nonspecific rash. At the age of 35, proteinuria was discovered and renal amyloidosis was diagnosed by renal biopsy. For 2 years thereafter he displayed the nephrotic syndrome, followed in the next 2 years by uremia from which he died at age 39. Autopsy revealed amyloidosis, most striking in the kidneys but also involving the adrenal glands and spleen. Although some features of the family of Maxwell and Kimbell (1936) are similar to those of urticaria, deafness and amyloidosis (191900), no deafness was present in their family. Weiss and Page (1974) reported a family with 2 definite and 4 probable cases in 3 generations. Mornaghi et al. (1981, 1982) reported rapidly progressive biopsy-proved renal amyloidosis in 3 brothers, aged 49, 52 and 55, of Irish-American origin. None had evidence of a plasma cell dyscrasia, a monoclonal serum or urine protein, or any underlying chronic disease. Immunoperoxidase staining of 1 pulmonary and 1 renal biopsy specimen was negative for amyloid A (AA), amyloid L (AL) and prealbumin. The authors concluded that the disorder in the 3 brothers closely resembled that described by Ostertag (1932). Studying the proband of a kindred with the familial amyloidosis of Ostertag, Lanham et al. (1982) demonstrated permanganate-sensitive congophilia of the amyloid but found no immunofluorescent staining for amyloid A or prealbumin. They concluded that this amyloid may be chemically distinct from previously characterized forms. Libbey and Talbert (1987) described a case of nephropathic amyloidosis, presumably of the Ostertag type. In their case, the amyloid showed no staining for light chains or prealbumin. Involvement of the liver was associated with cholestasis. In the kindred reported by Lanham et al. (1982), 6 members in 2 generations showed the onset of renal disease between ages 23 and 45 years. The deposition of amyloid is characteristically interstitial rather than glomerular as seen in other forms of amyloidosis. The proband had the sicca syndrome. The details of their patient's family history were not given by Libbey and Talbert (1987). Zalin et al. (1991) described yet another family with the Ostertag type of f ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 16, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 26, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 105200 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed