NLS1_CHICK
ID NLS1_CHICK Reviewed; 528 AA.
AC F1NCD6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 3.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Sodium-dependent lysophosphatidylcholine symporter 1 {ECO:0000305};
DE Short=NLS1;
DE Short=Sodium-dependent LPC symporter 1;
DE AltName: Full=Major facilitator superfamily domain-containing protein 2A {ECO:0000305};
DE Short=GgMFSD2A {ECO:0000303|PubMed:34135507};
GN Name=MFSD2A {ECO:0000303|PubMed:34135507}; Synonyms=NLS1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), TOPOLOGY, DISULFIDE
RP BOND, AND GLYCOSYLATION AT ASN-218 AND ASN-227.
RX PubMed=34135507; DOI=10.1038/s41586-021-03650-9;
RA Cater R.J., Chua G.L., Erramilli S.K., Keener J.E., Choy B.C., Tokarz P.,
RA Chin C.F., Quek D.Q.Y., Kloss B., Pepe J.G., Parisi G., Wong B.H.,
RA Clarke O.B., Marty M.T., Kossiakoff A.A., Khelashvili G., Silver D.L.,
RA Mancia F.;
RT "Structural basis of omega-3 fatty acid transport across the blood-brain
RT barrier.";
RL Nature 595:315-319(2021).
CC -!- FUNCTION: Sodium-dependent lysophosphatidylcholine (LPC) symporter,
CC which plays an essential role for blood-brain barrier formation and
CC function (By similarity). Specifically expressed in endothelium of the
CC blood-brain barrier of micro-vessels and transports LPC into the brain
CC (By similarity). Transport of LPC is essential because it constitutes
CC the major mechanism by which docosahexaenoic acid (DHA), an omega-3
CC fatty acid that is essential for normal brain growth and cognitive
CC function, enters the brain (By similarity). Transports LPC carrying
CC long-chain fatty acids such LPC oleate and LPC palmitate with a minimum
CC acyl chain length of 14 carbons (By similarity). Does not transport
CC docosahexaenoic acid in unesterified fatty acid (By similarity).
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:0000269|PubMed:34135507}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q9DA75}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:34135507}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AADN05000596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_417826.4; XM_417826.5.
DR PDB; 7MJS; EM; 3.03 A; X=1-528.
DR PDBsum; 7MJS; -.
DR SMR; F1NCD6; -.
DR STRING; 9031.ENSGALP00000006158; -.
DR PaxDb; F1NCD6; -.
DR Ensembl; ENSGALT00000006168; ENSGALP00000006158; ENSGALG00000003879.
DR GeneID; 419679; -.
DR KEGG; gga:419679; -.
DR CTD; 84879; -.
DR VEuPathDB; HostDB:geneid_419679; -.
DR eggNOG; KOG4830; Eukaryota.
DR GeneTree; ENSGT00390000005318; -.
DR HOGENOM; CLU_027408_6_1_1; -.
DR InParanoid; F1NCD6; -.
DR OMA; GLYTAWM; -.
DR OrthoDB; 827101at2759; -.
DR TreeFam; TF331194; -.
DR Reactome; R-GGA-1483191; Synthesis of PC.
DR Proteomes; UP000000539; Chromosome 23.
DR Bgee; ENSGALG00000003879; Expressed in liver and 12 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Lipid transport; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..528
FT /note="Sodium-dependent lysophosphatidylcholine symporter
FT 1"
FT /id="PRO_0000455379"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 38..66
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 67..73
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 74..99
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 100..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 130..138
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 139..161
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 162..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 200..241
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 264..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 296..319
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 320..328
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 329..351
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 352..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 377..381
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 405..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 451..467
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT TOPO_DOM 491..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
FT REGION 503..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:34135507, ECO:0007744|PDB:7MJS"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:34135507, ECO:0007744|PDB:7MJS"
FT DISULFID 207..460
FT /evidence="ECO:0000269|PubMed:34135507,
FT ECO:0007744|PDB:7MJS"
SQ SEQUENCE 528 AA; 58423 MW; F3CFA577AFA9D6FC CRC64;
MAGGGGAERV RVGAAAAGLL PPSCRQPRRR ESRERLSVCS KLCYAVGGAP YQTTGCALGF
FLQIYLLDVA QLDPFYASII LFVGRAWDAI TDPMVGFFIS KTPWTRFGRL MPWIIFSTPF
AVISYFLIWF VPDISTGQVM WYLIFYCIFQ TLVTCFHVPY SALTMFISRE QSERDSATAY
RMTVEVLGTV LGTAIQGQIV GKAVTPCIEN PPFLSETNFS VAIRNVNMTH YTGSLADTRN
AYMVAAGVIG GLYILCAVIL SVGVREKRES SELQSDEPVS FFRGLKLVMN HGAYIKLITG
FLFTSLAFML LEGNFALFCT YTLGFRNEFQ NILLAIMLSA TLTIPFWQWF LTRFGKKTAV
YVGISSAVPF LITVVVLDSN LVVTYIVAVA AGISVAAAFL LPWSMLPDVI DDFKLQHPES
RGHEAIFFSF YVFFTKFTSG VSLGISTLSL DFAGYQTRGC SQPSEVNITL KLLVSAVPVG
LILLGLLLFK LYPIDEEKRR ENKKALQDLR EESNSSSESD STELANIV
