ID NLS1A_DANRE Reviewed; 532 AA. AC Q5U3U7; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 07-OCT-2020, entry version 83. DE RecName: Full=Sodium-dependent lysophosphatidylcholine symporter 1-A; DE Short=NLS1-A; DE Short=Sodium-dependent LPC symporter 1-A; DE AltName: Full=Major facilitator superfamily domain-containing protein 2A-A; GN Name=mfsd2aa; Synonyms=mfsd2a, nls1a; ORFNames=zgc:101615; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=26005868; DOI=10.1038/ng.3311; RA Guemez-Gamboa A., Nguyen L.N., Yang H., Zaki M.S., Kara M., Ben-Omran T., RA Akizu N., Rosti R.O., Rosti B., Scott E., Schroth J., Copeland B., RA Vaux K.K., Cazenave-Gassiot A., Quek D.Q., Wong B.H., Tan B.C., Wenk M.R., RA Gunel M., Gabriel S., Chi N.C., Silver D.L., Gleeson J.G.; RT "Inactivating mutations in MFSD2A, required for omega-3 fatty acid RT transport in brain, cause a lethal microcephaly syndrome."; RL Nat. Genet. 47:809-813(2015). 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. Specifically CC required for blood-brain barrier formation and function, probably by CC mediating lipid transport (By similarity). {ECO:0000250}. 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 -!- TISSUE SPECIFICITY: Expressed in the developing nervous system. CC {ECO:0000269|PubMed:26005868}. CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the gene results in early CC postnatal lethality and microcephaly. {ECO:0000269|PubMed:26005868}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC085388; AAH85388.1; -; mRNA. DR RefSeq; NP_001007452.1; NM_001007451.1. DR STRING; 7955.ENSDARP00000046114; -. DR PaxDb; Q5U3U7; -. DR GeneID; 492810; -. DR KEGG; dre:492810; -. DR CTD; 492810; -. DR ZFIN; ZDB-GENE-041114-166; mfsd2aa. DR eggNOG; KOG4830; Eukaryota. DR InParanoid; Q5U3U7; -. DR KO; K23894; -. DR OrthoDB; 827101at2759; -. DR PhylomeDB; Q5U3U7; -. DR PRO; PR:Q5U3U7; -. DR Proteomes; UP000000437; Unplaced. 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; IBA:GO_Central. 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; IDA:ZFIN. DR GO; GO:0035633; P:maintenance of blood-brain barrier; IMP:ZFIN. DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central. DR GO; GO:0045056; P:transcytosis; ISS:UniProtKB. 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; Endoplasmic reticulum; Glycoprotein; Lipid transport; KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..532 FT /note="Sodium-dependent lysophosphatidylcholine symporter FT 1-A" FT /id="PRO_0000273390" FT TOPO_DOM 1..46 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 47..67 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 68 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 69..89 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 90..118 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 119..139 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 140..143 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 144..164 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 165..247 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 269..302 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 303..323 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 324..335 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 336..356 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 357..361 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 362..382 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 383..384 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 385..405 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 406..428 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 429..449 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 450..475 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 476..496 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 497..532 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 214 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 229 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 471 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 532 AA; 59266 MW; 387709380163A7F2 CRC64; MARGEGAEQF SSGLLPTAKS VTQNEIKMVK LPKQQERKRA LTVWSKVCFA IGGAPYQITG TALGFFLQIF LLDVAQLNPL NASVILFVGR AWDAVTDPTV GFLVSRTPWT RHGRMMPWIL VSTIPAVLCY FLIWVVPPIE QGKMMWYLLF YCLFQTLQTC FHVPYSALTM FISTEQRERD SATAYRMTVE VFGTVVGTAI QGQIVGMANT PCKNNTSPNN SSNDLIQSNN SHIPLKSNIF DERCAYMIAS AVISLIYVVC AAVLFFGVRE QDVQGELKAQ KRVSFQKGLR LVMGHGPYVK LVLAFLFTSL AFMLLEGNFA VFIKYTLGFR EDFQNILLVI MVSATVSIPM WQWFLCRFGK KTAVYIGITW AVPFMILVVS VNSSLIVSYI VSIAAGVSVG AAFLLPWSML PDVVDDFKLQ NPTSQGHEAI FYSFYVFFTK FASGVSLGVS TLALSFAGYE TGVCVQSDSV NLTLKLLVSA APVSLIALGL LIFMTYPIDE ERREYNNKQL QLLLRNEEEE DEMEVLKPDI TA //