UniProtKB/Swiss-Prot P55157 : Variant p.Asp169Val
Microsomal triglyceride transfer protein large subunit
Gene: MTTP
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Variant information
Variant position:
169
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
LP/P [Disclaimer : Variants classification is intended for research purposes only, not for clinical and diagnostic use . The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant. ]
The variants are classified into three categories: LP/P, LB/B and US.LP/P: likely pathogenic or pathogenic. LB/B: likely benign or benign. US: uncertain significance
Residue change:
From Aspartate (D) to Valine (V) at position 169 (D169V, p.Asp169Val).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:
Change from medium size and acidic (D) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
-3
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another: Lowest score: -4 (low probability of substitution).Highest score: 11 (high probability of substitution). More information can be found on the following page
Variant description:
In ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with APOB; inhibits interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion.
Any additional useful information about the variant.
Sequence information
Variant position:
169
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:
894
The length of the canonical sequence.
Location on the sequence:
KRGLASLFQTQLSSGTTNEV
D ISGNCKVTYQAHQDKVIKIK
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:
The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KRGLASLFQTQLSSGTTNEVD IS---GNCKVTYQAHQDKVIKIK
Mouse KRGLASLFQMQLSSGTTNEVD IS---GDCKVTYQAQQDKVV
Rat KRGLASLFQMQLTSGTTNEVD IS---GDCKVTYQAQQDKVV
Pig KRGLASLFQMQLSSGTTNEVD IS---GDCKVTYQAHQDKVT
Zebrafish KRGVASMLMMQLKSGKMSEAD AS---GKCLVEYKVNKHQVI
Caenorhabditis elegans LYAIVNTIYTPAEYGEGDEQT VDTIYGRCFVNFGRPEDKRF
Drosophila ERGIASLLQLRLDASQEEELD VS---GLCRVSYNVKSSTKV
Sequence annotation in neighborhood:
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
19 – 894
Microsomal triglyceride transfer protein large subunit
Domain
28 – 659
Vitellogenin
Alternative sequence
152 – 894
Missing. In isoform 2.
Mutagenesis
169 – 169
D -> E. No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB or P4HB/PDI, does partially reduce phospholipid or triglyceride transfer activity and apolipoprotein B secretion.
Mutagenesis
187 – 187
K -> L. No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB, but inhibits interaction with P4HB/PDI, phospholipid or triglyceride transfer activity and apolipoprotein B secretion.
Mutagenesis
187 – 187
K -> R. No loss on localization to the endoplasmic reticulum, does not reduce interaction with APOB or P4HB/PDI, partially inhibits triglyceride transfer activity, does not inhibit phospholipid transfer activity and apolipoprotein B secretion.
Mutagenesis
189 – 189
K -> L. No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB, but inhibits interaction with P4HB/PDI, phospholipid or triglyceride transfer activity and apolipoprotein B secretion.
Mutagenesis
189 – 189
K -> R. No loss on localization to the endoplasmic reticulum, does not reduce interaction with APOB or P4HB/PDI, partially inhibits triglyceride transfer activity, does not inhibit phospholipid transfer activity and apolipoprotein B secretion.
Beta strand
169 – 171
Literature citations
A novel abetalipoproteinemia missense mutation highlights the importance of N-Terminal beta-barrel in microsomal triglyceride transfer protein function.
Walsh M.T.; Iqbal J.; Josekutty J.; Soh J.; Di Leo E.; Oezaydin E.; Guenduez M.; Tarugi P.; Hussain M.M.;
Circ. Cardiovasc. Genet. 8:677-687(2015)
Cited for: VARIANT ABL VAL-169; CHARACTERIZATION OF VARIANT ABL VAL-169; FUNCTION; INTERACTION WITH APOB AND P4HB; SUBCELLULAR LOCATION; MUTAGENESIS OF ASP-169; LYS-187 AND LYS-189;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.