Microsomal triglyceride transfer protein

Microsomal triglyceride transfer protein
Identifiers
Symbols	MTTP; ABL; MGC149819; MGC149820; MTP
External IDs	OMIM: 157147 MGI: 106926 HomoloGene: 212 GeneCards: MTTP Gene
Gene Ontology Molecular function • lipid transporter activity • binding • lipid binding Cellular component • endoplasmic reticulum • endoplasmic reticulum lumen Biological process • lipid metabolic process • transport • lipid transport • lipoprotein metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4547	17777
Ensembl	ENSG00000138823	ENSMUSG00000028158
UniProt	P55157	Q3TVF2
RefSeq (mRNA)	NM_000253	NM_008642
RefSeq (protein)	NP_000244	NP_032668
Location (UCSC)	Chr 4: 100.48 – 100.55 Mb	Chr 3: 137.75 – 137.81 Mb
PubMed search	[1]	[2]

Microsomal triglyceride transfer protein large subunit is a protein that in humans is encoded by the MTTP gene.^[1][2]

MTP encodes the large subunit of the heterodimeric microsomal triglyceride transfer protein. Protein disulfide isomerase (PDI) completes the heterodimeric microsomal triaglyceride transfer protein, which has been shown to play a central role in lipoprotein assembly. Mutations in MTP can cause abetalipoproteinemia.^[2]

Apoprotein B48 on chylomicra and Apoprotein B100 on LDL, IDL, and VLDL are important for MTP binding.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.^[3]

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Statin Pathway edit

References

1. ^ Shoulders CC, Brett DJ, Bayliss JD, Narcisi TM, Jarmuz A, Grantham TT, Leoni PR, Bhattacharya S, Pease RJ, Cullen PM, et al. (Mar 1994). "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein". Hum Mol Genet 2 (12): 2109–16. doi:10.1093/hmg/2.12.2109. PMID 8111381. 
2. ^ ^{a b} "Entrez Gene: MTTP microsomal triglyceride transfer protein". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4547. 
3. ^ The interactive pathway map can be edited at WikiPathways: "StatinPathway_WP430". http://www.wikipathways.org/index.php/Pathway:WP430. 

Further reading

• Luz JM, Lennarz WJ (1996). "Protein disulfide isomerase: a multifunctional protein of the endoplasmic reticulum.". EXS 77: 97–117. PMID 8856971. 
• Wetterau JR, Lin MC, Jamil H (1997). "Microsomal triaglyceride transfer protein.". Biochim. Biophys. Acta 1345 (2): 136–50. PMID 9106493. 
• Gordon DA (1997). "Recent advances in elucidating the role of the microsomal triaglyceride transfer protein in apolipoprotein B lipoprotein assembly.". Curr. Opin. Lipidol. 8 (3): 131–7. doi:10.1097/00041433-199706000-00002. PMID 9211060. 
• Ye J (2007). "Reliance of Host Cholesterol Metabolic Pathways for the Life Cycle of Hepatitis C Virus". PLoS Pathog. 3 (8): e108. doi:10.1371/journal.ppat.0030108. PMC 1959368. PMID 17784784. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1959368. 
• Wetterau JR, Aggerbeck LP, Bouma ME, et al. (1992). "Absence of microsomal triaglyceride transfer protein in individuals with abetalipoproteinemia". Science 258 (5084): 999–1001. doi:10.1126/science.1439810. PMID 1439810. 
• Sharp D, Ricci B, Kienzle B, et al. (1994). "Human microsomal triaglyceride transfer protein large subunit gene structure". Biochemistry 33 (31): 9057–61. doi:10.1021/bi00197a005. PMID 7545943. 
• Shoulders CC, Narcisi TM, Read J, et al. (1995). "The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an alpha-helical domain". Nat. Struct. Biol. 1 (5): 285–6. doi:10.1038/nsb0594-285. PMID 7664034. 
• Hagan DL, Kienzle B, Jamil H, Hariharan N (1994). "Transcriptional regulation of human and hamster microsomal triaglyceride transfer protein genes. Cell type-specific expression and response to metabolic regulators". J. Biol. Chem. 269 (46): 28737–44. PMID 7961826. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Sharp D, Blinderman L, Combs KA, et al. (1993). "Cloning and gene defects in microsomal triaglyceride transfer protein associated with abetalipoproteinaemia". Nature 365 (6441): 65–9. doi:10.1038/365065a0. PMID 8361539. 
• Narcisi TM, Shoulders CC, Chester SA, et al. (1996). "Mutations of the Microsomal Triglyceride-Transfer–Protein Gene in Abetalipoproteinemia". Am. J. Hum. Genet. 57 (6): 1298–310. PMC 1801399. PMID 8533758. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1801399. 
• Rehberg EF, Samson-Bouma ME, Kienzle B, et al. (1997). "A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triaglyceride transfer protein that prevents complex formation with protein disulfide isomerase". J. Biol. Chem. 271 (47): 29945–52. doi:10.1074/jbc.271.47.29945. PMID 8939939. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Linnik KM, Herscovitz H (1998). "Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state". J. Biol. Chem. 273 (33): 21368–73. doi:10.1074/jbc.273.33.21368. PMID 9694898. 
• Bradbury P, Mann CJ, Köchl S, et al. (1999). "A common binding site on the microsomal triaglyceride transfer protein for apolipoprotein B and protein disulfide isomerase". J. Biol. Chem. 274 (5): 3159–64. doi:10.1074/jbc.274.5.3159. PMID 9915855. 
• Wang J, Hegele RA (2000). "Microsomal triaglyceride transfer protein (MTP) gene mutations in Canadian subjects with abetalipoproteinemia". Hum. Mutat. 15 (3): 294–5. doi:10.1002/(SICI)1098-1004(200003)15:3<294::AID-HUMU14>3.0.CO;2-E. PMID 10679949.