Summary: Apolipoprotein M (ApoM)
This is the Wikipedia entry entitled "APOM". More...
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Rendering based on PDB .
|RNA expression pattern|
The protein encoded by this gene is an apolipoprotein and member of the lipocalin protein family. It is found associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. The encoded protein is secreted through the plasma membrane but remains membrane-bound, where it is involved in lipid transport. Two transcript variants encoding two different isoforms have been found for this gene, but only one of them has been fully characterized.
- Xu N, Dahlback B (Dec 1999). "A novel human apolipoprotein (apoM)". J Biol Chem 274 (44): 31286–90. doi:10.1074/jbc.274.44.31286. PMID 10531326.
- Duan J, Dahlback B, Villoutreix BO (Jun 2001). "Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis". FEBS Lett 499 (1–2): 127–32. doi:10.1016/S0014-5793(01)02544-3. PMID 11418126.
- "Entrez Gene: APOM apolipoprotein M".
- Albertella MR, Jones H, Thomson W, et al. (1997). "Localization of eight additional genes in the human major histocompatibility complex, including the gene encoding the casein kinase II beta subunit (CSNK2B)". Genomics 36 (2): 240–51. doi:10.1006/geno.1996.0459. PMID 8812450.
- Xu N, Zhang XY, Dong X, et al. (2002). "Effects of platelet-activating factor, tumor necrosis factor, and interleukin-1alpha on the expression of apolipoprotein M in HepG2 cells". Biochem. Biophys. Res. Commun. 292 (4): 944–50. doi:10.1006/bbrc.2002.6755. PMID 11944906.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Zhang XY, Dong X, Zheng L, et al. (2003). "Specific tissue expression and cellular localization of human apolipoprotein M as determined by in situ hybridization". Acta Histochem. 105 (1): 67–72. doi:10.1078/0065-1281-00687. PMID 12666989.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
- Richter S, Shih DQ, Pearson ER, et al. (2004). "Regulation of apolipoprotein M gene expression by MODY3 gene hepatocyte nuclear factor-1alpha: haploinsufficiency is associated with reduced serum apolipoprotein M levels". Diabetes 52 (12): 2989–95. doi:10.2337/diabetes.52.12.2989. PMID 14633861.
- Xie T, Rowen L, Aguado B, et al. (2004). "Analysis of the Gene-Dense Major Histocompatibility Complex Class III Region and Its Comparison to Mouse". Genome Res. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMC 403804. PMID 14656967.
- Zhang XY, Jiao GQ, Hurtig M, et al. (2005). "Expression pattern of apolipoprotein M during mouse and human embryogenesis". Acta Histochem. 106 (2): 123–8. doi:10.1016/j.acthis.2003.11.004. PMID 15147633.
- Kabbara A, Payet N, Cottel D, et al. (2004). "Exclusion of CYP46 and APOM as candidate genes for Alzheimer's disease in a French population". Neurosci. Lett. 363 (2): 139–43. doi:10.1016/j.neulet.2004.03.066. PMID 15172102.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Xu N, Nilsson-Ehle P, Ahrén B (2005). "Correlation of apolipoprotein M with leptin and cholesterol in normal and obese subjects". J. Nutr. Biochem. 15 (10): 579–82. doi:10.1016/j.jnutbio.2004.03.001. PMID 15542348.
- Luo G, Hurtig M, Zhang X, et al. (2005). "Leptin inhibits apolipoprotein M transcription and secretion in human hepatoma cell line, HepG2 cells". Biochim. Biophys. Acta 1734 (2): 198–202. doi:10.1016/j.bbalip.2005.02.005. PMID 15904876.
- Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human Plasma N-Glycoproteome Analysis by Immunoaffinity Subtraction, Hydrazide Chemistry, and Mass Spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
- Niu N, Zhu X, Liu Y, et al. (2007). "Single nucleotide polymorphisms in the proximal promoter region of apolipoprotein M gene (apoM) confer the susceptibility to development of type 2 diabetes in Han Chinese". Diabetes Metab. Res. Rev. 23 (1): 21–5. doi:10.1002/dmrr.641. PMID 16572495.
- Christoffersen C, Nielsen LB, Axler O, et al. (2006). "Isolation and characterization of human apolipoprotein M-containing lipoproteins". J. Lipid Res. 47 (8): 1833–43. doi:10.1194/jlr.M600055-JLR200. PMID 16682745.
- Karlsson H, Lindqvist H, Tagesson C, Lindahl M (2006). "Characterization of apolipoprotein M isoforms in low-density lipoprotein". J. Proteome Res. 5 (10): 2685–90. doi:10.1021/pr060180x. PMID 17022639.
- Xu X, Ye Q, Xu N, et al. (2007). "Effects of ischemia-reperfusion injury on apolipoprotein M expression in the liver". Transplant. Proc. 38 (9): 2769–73. doi:10.1016/j.transproceed.2006.08.133. PMID 17112825.
- Ahnström J, Faber K, Axler O, Dahlbäck B (2007). "Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M". J. Lipid Res. 48 (8): 1754–62. doi:10.1194/jlr.M700103-JLR200. PMID 17525477.
|This article on a gene on chromosome 6 is a stub. You can help Wikipedia by expanding it.|
Apolipoprotein M (ApoM) Provide feedback
ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells . Lipoproteins consist of lipids solubilized by apolipoproteins. ApoM lacks an external amphipathic motif and is uniquely secreted to plasma without cleavage of its terminal signal peptide .
Ahnstrom J, Axler O, Jauhiainen M, Salomaa V, Havulinna AS, Ehnholm C, Frikke-Schmidt R, Tybjaerg-Hansen A, Dahlback B; , J Lipid Res. 2008; [Epub ahead of print]: Levels of apolipoprotein M are not associated with the risk of coronary heart disease in two independent case-control studies. PUBMED:18490703 EPMC:18490703
Christoffersen C, Ahnstrom J, Axler O, Christensen EI, Dahlback B, Nielsen LB; , J Biol Chem. 2008; [Epub ahead of print]: The signal peptide anchors apolipoprotein M in plasma lipoproteins and prevents rapid clearance of apolipoprotein M from plasma. PUBMED:18460466 EPMC:18460466
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR022734
ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells [PUBMED:18490703]. Lipoproteins consist of lipids solubilized by apolipoproteins. ApoM lacks an external amphipathic motif and is uniquely secreted to plasma without cleavage of its terminal signal peptide [PUBMED:18460466].
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The calycin structural superfamily [1-3] includes the lipocalins, the fatty acid-binding proteins (FABPs).
The clan contains the following 16 members:ApoM DUF3642 His_binding Lipocalin Lipocalin_2 Lipocalin_3 Lipocalin_4 Lipocalin_5 Lipocalin_6 Lipocalin_7 META Nitrophorin NlpE Triabin VDE YodA
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Curation and family details
|Author:||Pollington J, Finn RD|
|Number in seed:||4|
|Number in full:||77|
|Average length of the domain:||164.30 aa|
|Average identity of full alignment:||37 %|
|Average coverage of the sequence by the domain:||93.66 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ApoM domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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