NLS1_XENTR
ID NLS1_XENTR Reviewed; 525 AA.
AC Q0IHM1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Sodium-dependent lysophosphatidylcholine symporter 1;
DE Short=NLS1;
DE Short=Sodium-dependent LPC symporter 1;
DE AltName: Full=Major facilitator superfamily domain-containing protein 2A;
GN Name=mfsd2a; Synonyms=mfsd2, nls1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sodium-dependent lysophosphatidylcholine (LPC) symporter,
CC which plays an essential role for blood-brain barrier formation and
CC function. Specifically expressed in endothelium of the blood-brain
CC barrier of micro-vessels and transports LPC into the brain. Transport
CC of LPC is essential because it constitutes the major mechanism by which
CC docosahexaenoic acid (DHA), an omega-3 fatty acid that is essential for
CC normal brain growth and cognitive function, enters the brain.
CC Transports LPC carrying long-chain fatty acids such LPC oleate and LPC
CC palmitate with a minimum acyl chain length of 14 carbons. Does not
CC transport docosahexaenoic acid in unesterified fatty acid.
CC {ECO:0000250|UniProtKB:Q9DA75}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) = a 1-
CC acyl-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:44376, ChEBI:CHEBI:29101, ChEBI:CHEBI:58168;
CC Evidence={ECO:0000250|UniProtKB:Q9DA75};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phosphocholine(in) + Na(+)(in) = 1-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43860, ChEBI:CHEBI:29101, ChEBI:CHEBI:73873;
CC Evidence={ECO:0000250|UniProtKB:Q9DA75};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(in) +
CC Na(+)(in) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(out) +
CC Na(+)(out); Xref=Rhea:RHEA:43856, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q9DA75};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43864, ChEBI:CHEBI:29101, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:Q9DA75};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine(in) + Na(+)(in) = a
CC 1-acyl-sn-glycero-3-phosphoethanolamine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43868, ChEBI:CHEBI:29101, ChEBI:CHEBI:64381;
CC Evidence={ECO:0000250|UniProtKB:Q9DA75};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9DA75};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q9DA75}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; BC123088; AAI23089.1; -; mRNA.
DR RefSeq; NP_001072635.1; NM_001079167.1.
DR AlphaFoldDB; Q0IHM1; -.
DR SMR; Q0IHM1; -.
DR STRING; 8364.ENSXETP00000002564; -.
DR PaxDb; Q0IHM1; -.
DR DNASU; 780091; -.
DR GeneID; 780091; -.
DR KEGG; xtr:780091; -.
DR CTD; 84879; -.
DR Xenbase; XB-GENE-951402; mfsd2a.
DR eggNOG; KOG4830; Eukaryota.
DR HOGENOM; CLU_027408_6_1_1; -.
DR InParanoid; Q0IHM1; -.
DR OMA; DIPYWSM; -.
DR OrthoDB; 827101at2759; -.
DR PhylomeDB; Q0IHM1; -.
DR TreeFam; TF331194; -.
DR Reactome; R-XTR-1483191; Synthesis of PC.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000001185; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; Q0IHM1; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; ISS:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR GO; GO:0060856; P:establishment of blood-brain barrier; ISS:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; ISS:UniProtKB.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISS:UniProtKB.
DR GO; GO:0051977; P:lysophospholipid transport; ISS:UniProtKB.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR GO; GO:0045056; P:transcytosis; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR039672; MFS_2.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11328; PTHR11328; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Lipid transport; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..525
FT /note="Sodium-dependent lysophosphatidylcholine symporter
FT 1"
FT /id="PRO_0000273391"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 33..62
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 63..73
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 95..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 127..137
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 138..162
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 163..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 170..201
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 202..226
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 227..260
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 261..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 292..318
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 319..329
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 349..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 353..374
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 375..377
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 378..414
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 415..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 425..451
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 452..463
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 464..487
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 488..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 205..458
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
SQ SEQUENCE 525 AA; 58591 MW; 8EC34983EC43073A CRC64;
MEKESENASC AGLLGQKNEP GSPTQSRSGK HKLSVCSKIC FAIGGAPYQI TGCALGFFLQ
IFLLDIAQVP PFYASIILFS GRVWDAITDP LVGFFVSKSS WTRLGRLLPW VVFSTPFAVV
SYLLIWFVPG FSGVSMVIWY LVFYCLFQTL VTCFHVPYSA LTMFISKEQS DRDSATGYRM
TVEVLGTVLG TAIQGQIVGR ENTPCVEHIR ETHLYNTSVI MEDLNITHDV ESLSSTRDAY
MIAAGVICAI YVLCAIILTL GVREKRDAYE LLSDQPFSFW QGLKLVMSHK PYIKLITGFL
FTSLAFMLLE GNFALFLTYT MGFRRDFQNI LLVVMLSATL TVPFWQWFLT RFGKKTAVYF
GISSVIPFLI LVVLMESNLI LAYVVAVAAG LSVAAAFLLP WSMLPDVIDD FILKNPDSHG
HEPIFFSFYV FFTKFASGVS LGISTLSLDF AGYQTRACSQ PEQVNLTLKM LICVAPVILI
LLGLLLFILY PINEEKRKQN KKALQLIRES NRDSDSDSLE LASNV
