Apolipoprotein D (APOD)
The protein contains 189 amino acids for an estimated molecular weight of 21276 Da.
APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts. (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.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs5952 | |
| dbSNP:rs5954 | |
| dbSNP:rs5955 |
Biological Process
Aging
Angiogenesis
Brain development
Glucose metabolic process
Intracellular receptor signaling pathway
Lipid metabolic process
Lipid transport
Negative regulation of cytokine production involved in inflammatory response
Negative regulation of focal adhesion assembly
Negative regulation of lipoprotein lipid oxidation
Negative regulation of monocyte chemotactic protein-1 production
Negative regulation of platelet-derived growth factor receptor signaling pathway
Negative regulation of protein import into nucleus
Negative regulation of smooth muscle cell proliferation
Negative regulation of smooth muscle cell-matrix adhesion
Negative regulation of T cell migration
Peripheral nervous system axon regeneration
Response to axon injury
Response to drug
Response to reactive oxygen species
Tissue regeneration
The reference OMIM entry for this protein is 107740
Apolipoprotein d; apod
DESCRIPTION
Apolipoprotein D (ApoD) is a member of the alpha(2mu)-microglobulin superfamily of carrier proteins also known as lipocalins (e.g., lipocalin-1; 151675). It is a protein component of high-density lipoprotein in human plasma, comprising about 5% of total high-density lipoprotein (Fielding and Fielding, 1980). It is a glycoprotein of estimated molecular weight 33,000 Da. ApoD is closely associated with the enzyme lecithin:cholesterol acyltransferase (LCAT; 606967) (summary by Drayna et al., 1986).CLONING
Drayna et al. (1986) reported the amino acid sequence of apoD based on the nucleotide sequence of the coding portion of the APOD gene and on the cloned cDNA sequence. The 169-amino acid protein bore little similarity to other lipoprotein sequences but had a high degree of homology to plasma retinol-binding protein (180250, 180260, 180280, 180290), a member of the alpha(2mu)-globulin superfamily. This structural similarity may indicate some functional homology of these proteins. ApoD mRNA has been detected in many tissues. Drayna et al. (1987) described multiple RFLPs at the APOD locus. Kamboh et al. (1989) demonstrated for the first time polymorphism of apolipoprotein D by an isoelectric focusing-immunoblotting technique. Zeng et al. (1996) identified apoD as apocrine secretion odor-binding protein-2 (ASOB2), 1 of 2 glycoproteins that bind E-3-methyl-2-hexenoic acid (E-3M2H), the most abundant axillary odor component in human males. The authors used mass spectrometry to determine the amino acid sequence and glycosylation pattern of ASOB2. The pattern of glycosylation for axillary apoD differs from that reported for plasma apoD, suggesting to Zeng et al. (1996) that there are different sites of expression for the 2 glycoproteins. In situ hybridization of an oligonucleotide probe against apoD mRNA with axillary tissue demonstrated that the message for synthesis of this protein is specific to the apocrine glands. These results suggested a remarkable similarity between human axillary secretions and nonhuman mammalian odor sources, where lipocalins have been shown to carry the odoriferous signals used in pheromonal communication.GENE FUNCTION
Zeng et al. (1996) noted several studies in humans suggesting that axillary odors and secretions from both males and females are a source of chemical signals containing physiologically active components capable of altering the female menstrual cycle. These alterations include the menstrual synchrony effect first documented by McClintock (1971) in an all-female living group and later replicated by others in coeducational facilities (Graham and McGrew, 1980; Quadagno et al., 1981). In nonhuman mammals such as rodents, estrous synchrony has been shown to be mediated by airborne chemical signals (McClintock, 1978). Certain axillary components currently function as chemical signals involved in the regulation of reproductive function via alteration of the hypothalamic-pituitary-gonadal axis; chemical signals for this mode of action are termed primer pheromones. Characterization of the source of the odor in the human axillary region is not only of commercial interest but is also important biologically because axillary extracts can alter the length and timing of the female menstrual cycle. In males, the most abundant odor component is known to be E-3-methyl-2-hexenoic acid (E-3M2H), which is liberated from nonodorous apocrine secretions by axillary microorganisms. In ... More on the omim web site
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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 107740 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed