Sequence information
Variant position: 172 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 543 The length of the canonical sequence.
Location on the sequence:
FPHGQTYWYLLFYCLFETMV
T CFHVPYSALTMFISTEQTER
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 FPHGQT-----YWYLLFYCLFETMVT CFHVPYSALTMFISTEQTER
Mouse FPSGTESSHGFLWYLLFYCLFETLVT CFHVPYSALTMFIST
Xenopus tropicalis FSGVSM----VIWYLVFYCLFQTLVT CFHVPYSALTMFISK
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
1 – 543
Sodium-dependent lysophosphatidylcholine symporter 1
Transmembrane
158 – 182
Helical
Alternative sequence
1 – 186
MAKGEGAESGSAAGLLPTSILQSTERPAQVKKEPKKKKQQLSVCNKLCYALGGAPYQVTGCALGFFLQIYLLDVAQKDEEVVFCFSSFQVGPFSASIILFVGRAWDAITDPLVGLCISKSPWTCLGRLMPWIIFSTPLAVIAYFLIWFVPDFPHGQTYWYLLFYCLFETMVTCFHVPYSALTMFIS -> MWLRWALSLPPSSCLWAEPGMPSQTPWWASASANPPGPAWVALCPGSSSPRPWPSLPTSSSGSCPTSHTARPIGTCFSIASLKQWSRVSMFPTRLSPCSSA. In isoform 3.
Mutagenesis
177 – 177
P -> T. Reduced expression; no effect on cell membrane localization; decreased LPC transport activity.
Literature citations
Inactivating mutations in MFSD2A, required for omega-3 fatty acid transport in brain, cause a lethal microcephaly syndrome.
Guemez-Gamboa A.; Nguyen L.N.; Yang H.; Zaki M.S.; Kara M.; Ben-Omran T.; Akizu N.; Rosti R.O.; Rosti B.; Scott E.; Schroth J.; Copeland B.; Vaux K.K.; Cazenave-Gassiot A.; Quek D.Q.; Wong B.H.; Tan B.C.; Wenk M.R.; Gunel M.; Gabriel S.; Chi N.C.; Silver D.L.; Gleeson J.G.;
Nat. Genet. 47:809-813(2015)
Cited for: INVOLVEMENT IN NEDMISBA; VARIANTS NEDMISBA MET-172 AND LEU-179; CHARACTERIZATION OF VARIANTS NEDMISBA MET-172 AND LEU-179; FUNCTION; SUBCELLULAR LOCATION;
Biallelic MFSD2A variants associated with congenital microcephaly, developmental delay, and recognizable neuroimaging features.
Scala M.; Chua G.L.; Chin C.F.; Alsaif H.S.; Borovikov A.; Riazuddin S.; Riazuddin S.; Chiara Manzini M.; Severino M.; Kuk A.; Fan H.; Jamshidi Y.; Toosi M.B.; Doosti M.; Karimiani E.G.; Salpietro V.; Dadali E.; Baydakova G.; Konovalov F.; Lozier E.; O'Connor E.; Sabr Y.; Alfaifi A.; Ashrafzadeh F.; Striano P.; Zara F.; Alkuraya F.S.; Houlden H.; Maroofian R.; Silver D.L.;
Eur. J. Hum. Genet. 28:1509-1519(2020)
Cited for: VARIANTS NEDMISBA MET-172; MET-211; PHE-263; HIS-339 AND LEU-506; CHARACTERIZATION OF VARIANTS MET-211; PHE-263; HIS-339 AND LEU-506; MUTAGENESIS OF PRO-177; FUNCTION; SUBCELLULAR LOCATION;
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.