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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y5Y0: Variant p.Asp421Asn

Choline/ethanolamine transporter FLVCR1
Gene: FLVCR1
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Variant information Variant position: help 421 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 Aspartate (D) to Asparagine (N) at position 421 (D421N, p.Asp421Asn). 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 medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 NEDMISH; likely pathogenic; due to a nucleotide substitution that causes missplicing of exon 6 or results in missense variant N-421; missense variant N-421 does not affect choline and ethanolamine transmembrane transporter activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 421 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 555 The length of the canonical sequence.
Location on the sequence: help TTLIVYILSFIGMVIFTFTL D LRYIIIVFVTGGVLGFFMTG 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                         TTLIVYILSFIGMVIFTFTLDLRYIIIVFVTGGVLGFFMTG

Mouse                         TTLIVYVLSFIGMLIFTFTLNLGYIIVVFFTGGILGFFMTG

Cat                           TTLIVYILSFLGMVIFTFTLDLGYGIVVFVTGGVLGFFMTG
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 – 555 Choline/ethanolamine transporter FLVCR1
Topological domain 421 – 423 Extracellular
Helix 420 – 422



Literature citations
Biallelic variation in the choline and ethanolamine transporter FLVCR1 underlies a severe developmental disorder spectrum.
Calame D.G.; Wong J.H.; Panda P.; Nguyen D.T.; Leong N.C.P.; Sangermano R.; Patankar S.G.; Abdel-Hamid M.S.; AlAbdi L.; Safwat S.; Flannery K.P.; Dardas Z.; Fatih J.M.; Murali C.; Kannan V.; Lotze T.E.; Herman I.; Ammouri F.; Rezich B.; Efthymiou S.; Alavi S.; Murphy D.; Firoozfar Z.; Nasab M.E.; Bahreini A.; Ghasemi M.; Haridy N.A.; Goldouzi H.R.; Eghbal F.; Karimiani E.G.; Begtrup A.; Elloumi H.; Srinivasan V.M.; Gowda V.K.; Du H.; Jhangiani S.N.; Coban-Akdemir Z.; Marafi D.; Rodan L.; Isikay S.; Rosenfeld J.A.; Ramanathan S.; Staton M.; Oberg K.C.; Clark R.D.; Wenman C.; Loughlin S.; Saad R.; Ashraf T.; Male A.; Tadros S.; Boostani R.; Abdel-Salam G.M.H.; Zaki M.; Mardi A.; Hashemi-Gorji F.; Abdalla E.; Manzini M.C.; Pehlivan D.; Posey J.E.; Gibbs R.A.; Houlden H.; Alkuraya F.S.; Bujakowska K.; Maroofian R.; Lupski J.R.; Nguyen L.N.;
Genet. Med. 27:101273-101273(2025)
Cited for: VARIANTS NEDMISH VAL-253; ARG-305; PRO-328; ILE-340; 363-TYR--ILE-555 DEL; 390-LEU--ILE-555 DEL; 400-GLN--ILE-555 DEL; PRO-409; ALA-412; ASN-421 AND SER-464; INVOLVEMENT IN NEDMISH; CHARACTERIZATION OF VARIANTS NEDMISH ARG-305; ILE-340; PRO-409; ALA-412; ASN-421 AND SER-464; VARIANTS RETSNS ASN-128 AND VAL-168; CHARACTERIZATION OF VARIANT RETSNS ASN-128; VARIANTS ARG-192; SER-249 AND THR-343; CHARACTERIZATION OF VARIANT THR-343; FUNCTION; MUTAGENESIS OF MET-151 AND LEU-443;
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.