Summary: Lipoprotein amino terminal region
This is the Wikipedia entry entitled "Vitellogenin lipid transport domain". More...
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Vitellogenin lipid transport domain Edit Wikipedia article
|Lipoprotein amino terminal region|
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).
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.
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. Apolipoprotein B-100 has been linked to the development of atherosclerosis.
Human proteins containing this domain
- 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. 
Lipoprotein amino terminal region Provide feedback
This family contains regions from: Vitellogenin, Microsomal triglyceride transfer protein and apolipoprotein B-100. These proteins are all involved in lipid transport . This family contains the LV1n chain from lipovitellin, that contains two structural domains.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001747
This entry represents a conserved region found in several lipid transport proteins, including vitellogenin, microsomal triglyceride transfer protein and apolipoprotein B-100 [PUBMED:9687371].
Vitellinogen 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) [PUBMED:17314313, PUBMED:12135361].
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 [PUBMED:17403933].
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 [PUBMED:16238675]. Apolipoprotein B-100 has been linked to the development of atherosclerosis.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||lipid transporter activity (GO:0005319)|
|Biological process||lipid transport (GO:0006869)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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- the UniProt description of the protein sequence
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Tetratricopeptide-like repeats are found in a numerous and diverse proteins involved in such functions as cell cycle regulation, transcriptional control, mitochondrial and peroxisomal protein transport, neurogenesis and protein folding.
The clan contains the following 132 members:Adaptin_N Alkyl_sulf_dimr ANAPC3 ANAPC5 API5 Arm Arm_2 Arm_3 Avirulence B56 BTAD CAS_CSE1 ChAPs CLASP_N Clathrin Clathrin-link Clathrin_H_link Clathrin_propel Cnd1 Cnd3 Coatomer_E Cohesin_HEAT Cohesin_load COPI_C CRM1_C Cse1 DNA_alkylation Drf_FH3 Drf_GBD DUF1822 DUF2019 DUF2225 DUF3385 DUF3458 DUF3808 DUF3856 DUF4042 DUF924 EST1 EST1_DNA_bind FAT Fis1_TPR_C Fis1_TPR_N Foie-gras_1 GUN4_N HAT HEAT HEAT_2 HEAT_EZ HEAT_PBS HemY_N IBB IBN_N IFRD KAP Leuk-A4-hydro_C LRV LRV_FeS MA3 MIF4G MIF4G_like MIF4G_like_2 Mo25 MRP-S27 NARP1 Neurochondrin Nipped-B_C Nro1 NSF Paf67 ParcG PC_rep PHAT PI3Ka PknG_TPR PPP5 PPR PPR_1 PPR_2 PPR_3 PPR_long PPTA Proteasom_PSMB PUF Rab5-bind Rapsyn_N RPN7 Sel1 SHNi-TPR SNAP SPO22 SRP_TPR_like ST7 Suf SusD SusD-like SusD-like_2 SusD-like_3 TAF6_C TAtT Tcf25 TIP120 TOM20_plant TPR_1 TPR_10 TPR_11 TPR_12 TPR_14 TPR_15 TPR_16 TPR_17 TPR_18 TPR_19 TPR_2 TPR_20 TPR_21 TPR_3 TPR_4 TPR_5 TPR_6 TPR_7 TPR_8 TPR_9 Upf2 V-ATPase_H_C V-ATPase_H_N Vac14_Fab1_bd Vitellogenin_N Vps39_1 W2 Xpo1 YfiO
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_1280 (release 3.0)|
|Number in seed:||43|
|Number in full:||729|
|Average length of the domain:||442.70 aa|
|Average identity of full alignment:||16 %|
|Average coverage of the sequence by the domain:||27.30 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||19|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Vitellogenin_N domain has been found. There are 3 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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