UniProtKB/Swiss-Prot P50416: Variant p.Ala275Thr

Carnitine O-palmitoyltransferase 1, liver isoform
Gene: CPT1A
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Variant information Variant position:

275 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Alanine (A) to Threonine (T) at position 275 (A275T, p.Ala275Thr). 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 small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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
Other resources:

Links to websites of interest for the variant.

Variant rs2229738 [ dbSNP | Ensembl ]

Sequence information Variant position:

275 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

773 The length of the canonical sequence.
Location on the sequence:

YAMDLLYILPTHIQAARAGN A IHAILLYRRKLDREEIKPIR 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                         YAMDLLYILPTHIQAARAGNAIHAILLYRRKLDREEIKPIR

Mouse                         YAMEMLYITPTHIQAARAGNTIHAILLYRRTVDREELKPIR

Rat                           YAMEMLYITPTHIQAARAGNTIHAILLYRRTLDREELKPIR

Horse                         YAMDLLYVIPTHLQAATAGNGIHAILLYRHKLDREEIKPIL

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	2 – 773	Carnitine O-palmitoyltransferase 1, liver isoform
Topological domain	123 – 773	Cytoplasmic
Modified residue	282 – 282	3'-nitrotyrosine

Literature citations
Organization of the human liver carnitine palmitoyltransferase 1 gene (CPT1A) and identification of novel mutations in hypoketotic hypoglycaemia.
Gobin S.; Bonnefont J.-P.; Prip-Buus C.; Mugnier C.; Ferrec M.; Demaugre F.; Saudubray J.-M.; Rostane H.; Djouadi F.; Wilcox W.; Cederbaum S.; Haas R.; Nyhan W.L.; Green A.; Gray G.; Girard J.; Thuillier L.;
Hum. Genet. 111:179-189(2002)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS CPT1AD VAL-414 AND CYS-498; VARIANT THR-275; Molecular characterization of L-CPT I deficiency in six patients: insights into function of the native enzyme.
Brown N.F.; Mullur R.S.; Subramanian I.; Esser V.; Bennett M.J.; Saudubray J.-M.; Feigenbaum A.S.; Kobari J.A.; Macleod P.M.; McGarry J.D.; Cohen J.C.;
J. Lipid Res. 42:1134-1142(2001)
Cited for: VARIANTS CPT1AD CYS-123; TRP-304; TRP-357; ARG-395 DEL; LEU-479 AND PRO-484; VARIANT THR-275; Functional and structural basis of carnitine palmitoyltransferase 1A deficiency.
Gobin S.; Thuillier L.; Jogl G.; Faye A.; Tong L.; Chi M.; Bonnefont J.-P.; Girard J.; Prip-Buus C.;
J. Biol. Chem. 278:50428-50434(2003)
Cited for: VARIANT CPT1AD GLU-709; CHARACTERIZATION OF VARIANTS CPT1AD THR-275; VAL-414; CYS-498; GLU-709 AND GLU-710; SUBCELLULAR LOCATION; FUNCTION; CATALYTIC ACTIVITY; ACTIVITY REGULATION; BIOPHYSICOCHEMICAL PROPERTIES;

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.