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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q96NT5: Variant p.Gly147Arg

Proton-coupled folate transporter
Gene: SLC46A1
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Variant information Variant position: help 147 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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: help From Glycine (G) to Arginine (R) at position 147 (G147R, p.Gly147Arg). 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: help Change from glycine (G) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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: help In HFM; reduces folate uptake to 13% of normal levels. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 147 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 459 The length of the canonical sequence.
Location on the sequence: help QALVSVFVVQLQLHVGYFVL G RILCALLGDFGGLLAASFAS 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         QALVSVFVVQLQLHVGYFVLGRILCALLGDFGGLLAASFAS

Mouse                         QAVVSIFVVQLELHVGFFVLGRALCALLGDFNGLLAASFAS

Rat                           QAVVSIFVVQLQLHIGFFVLGRALCALLGDFNGLLAASFAS

Bovine                        QTVLSIFVVQLHLHIGYLVLGRILCALLGDFSGLLAASFAS

Chicken                       QAAVYLLVMYLRLHVAYLLLGRIISGLLGDYNLILAGCFAS

Xenopus laevis                QAAVYLLVMYQELHVGYFLIGRFISGISGDFNMILAGCFAY

Zebrafish                     QAAVYLTVMYLKLPVFWFLIGRICSGLSGDFNAILAGCFAY
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 459 Proton-coupled folate transporter
Transmembrane 141 – 154 Helical; Name=TM4
Binding site 156 – 156 reversibly protonated residue during proton transport
Disulfide bond 66 – 298
Mutagenesis 156 – 156 D -> E. Does not affect methotrexate uptake.
Mutagenesis 156 – 156 D -> FKNVW. Loss of methotrexate uptake.
Mutagenesis 156 – 156 D -> G. 2-fold reduction of methotrexate uptake.
Mutagenesis 156 – 156 D -> S. 8-fold reduction of methotrexate uptake.
Mutagenesis 158 – 158 G -> N. Abolished sensitivity to myricetin inhibitor.



Literature citations
The spectrum of mutations in the PCFT gene, coding for an intestinal folate transporter, that are the basis for hereditary folate malabsorption.
Zhao R.; Min S.H.; Qiu A.; Sakaris A.; Goldberg G.L.; Sandoval C.; Malatack J.J.; Rosenblatt D.S.; Goldman I.D.;
Blood 110:1147-1152(2007)
Cited for: FUNCTION; SUBCELLULAR LOCATION; VARIANTS HFM SER-113; ARG-147; ARG-318; TRP-376 AND ARG-425;
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.