Vitellogenin lipid transport domain
| Lipoprotein amino terminal region | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Vitellogenin_N | ||||||||
| Pfam | PF01347 | ||||||||
| InterPro | IPR001747 | ||||||||
| SCOP | 1llv | ||||||||
| SUPERFAMILY | 1llv | ||||||||
| OPM superfamily | 340 | ||||||||
| OPM protein | 1lsh | ||||||||
| |||||||||
This domain represents a conserved region found in several lipid transport proteins, including vitellogenin, microsomal triglyceride transfer protein and apolipoprotein B-100.[1]
Vitellogenin precursors provide the major egg yolk proteins that are a source of nutrients during early development of oviparous vertebrates and invertebrates. Vitellinogen precursors are multi-domain apolipoproteins that are cleaved into distinct yolk proteins. Different vitellinogen precursors exist, which are composed of variable combinations of yolk protein components; however, the cleavage sites are conserved. In vertebrates, a complete vitellinogen is composed of an N-terminal signal peptide for export, followed by four regions that can be cleaved into yolk proteins: lipovitellin-1, phosvitin, lipovitellin-2, and a von Willebrand factor type D domain (YGP40).[2][3]
Microsomal triglyceride transfer protein (MTTP) is an endoplasmic reticulum lipid transfer protein involved in the biosynthesis and lipid loading of apolipoprotein B. MTTP is also involved in the late stage of CD1d trafficking in the lysosomal compartment, CD1d being the MHC I-like lipid antigen presenting molecule.[4]
Apolipoprotein B can exist in two forms: B-100 and B-48. Apoliporotein B-100 is present on several lipoproteins, including very low-density lipoproteins (VLDL), intermediate density lipoproteins (IDL) and low density lipoproteins (LDL), and can assemble VLDL particles in the liver.[5] Apolipoprotein B-100 has been linked to the development of atherosclerosis.
Human proteins containing this domain
APOB ( [6] see native LDL-ApoB structure at 37°C on YouTube); MTTP;
References
- ↑ Banaszak LJ, Anderson TA, Levitt DG (1998). "The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein". Structure. 6 (7): 895–909. doi:10.1016/S0969-2126(98)00091-4. PMID 9687371.
- ↑ Finn RN (2007). "Vertebrate Yolk Complexes and the Functional Implications of Phosvitins and Other Subdomains in Vitellogenins". Biol. Reprod. 76 (6): –. doi:10.1095/biolreprod.106.059766. PMID 17314313.
- ↑ Banaszak LJ, Thompson JR (2002). "Lipid-protein interactions in lipovitellin". Biochemistry. 41 (30): 9398–9409. doi:10.1021/bi025674w. PMID 12135361.
- ↑ Agami R, Sagiv Y, Teyton L, Bai L, Wei DG, Savage PB, Bendelac A (2007). "A distal effect of microsomal triglyceride transfer protein deficiency on the lysosomal recycling of CD1d". J. Exp. Med. 204 (4): –. doi:10.1084/jem.20061568. PMC 2118556
. PMID 17403933. - ↑ Olofsson SO, Boren J (2005). "Apolipoprotein B: a clinically important apolipoprotein which assembles atherogenic lipoproteins and promotes the development of atherosclerosis". J. Intern. Med. 258 (5): –. doi:10.1111/j.1365-2796.2005.01556.x. PMID 16238675.
- ↑ Kumar V, Butcher SJ, Öörni K, Engelhardt P, Heikkonen J, et al. (2011) Three-Dimensional cryoEM Reconstruction of Native LDL Particles to 16Å Resolution at Physiological Body Temperature.
This article incorporates text from the public domain Pfam and InterPro IPR001747