NLS1_MOUSE
ID NLS1_MOUSE Reviewed; 534 AA.
AC Q9DA75; Q80ZW8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
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;
DE Short=Mfsd2a {ECO:0000303|PubMed:24828040};
GN Name=Mfsd2a {ECO:0000312|MGI:MGI:1923824}; Synonyms=Mfsd2, Nls1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18694395; DOI=10.1042/bj20080165;
RA Angers M., Uldry M., Kong D., Gimble J.M., Jetten A.M.;
RT "Mfsd2a encodes a novel major facilitator superfamily domain-containing
RT protein highly induced in brown adipose tissue during fasting and adaptive
RT thermogenesis.";
RL Biochem. J. 416:347-355(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
RP GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23209793; DOI=10.1371/journal.pone.0050629;
RA Berger J.H., Charron M.J., Silver D.L.;
RT "Major facilitator superfamily domain-containing protein 2a (MFSD2A) has
RT roles in body growth, motor function, and lipid metabolism.";
RL PLoS ONE 7:E50629-E50629(2012).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-92 AND ASP-96.
RX PubMed=24828044; DOI=10.1038/nature13241;
RA Nguyen L.N., Ma D., Shui G., Wong P., Cazenave-Gassiot A., Zhang X.,
RA Wenk M.R., Goh E.L., Silver D.L.;
RT "Mfsd2a is a transporter for the essential omega-3 fatty acid
RT docosahexaenoic acid.";
RL Nature 509:503-506(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=24828040; DOI=10.1038/nature13324;
RA Ben-Zvi A., Lacoste B., Kur E., Andreone B.J., Mayshar Y., Yan H., Gu C.;
RT "Mfsd2a is critical for the formation and function of the blood-brain
RT barrier.";
RL Nature 509:507-511(2014).
RN [7]
RP 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).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 39-511 OF VARIANT
RP HIS-67, FUNCTION, TRANSMEMBRANE DOMAINS, TOPOLOGY, DISULFIDE BOND, AND
RP MUTAGENESIS OF TYR-55; GLN-56; PHE-64; GLN-67; SER-82; PHE-86; ARG-89;
RP ASP-92; THR-95; ASP-96; GLU-159; THR-163; HIS-166; PRO-168; SER-170;
RP ARG-190; GLU-194; THR-202; GLN-207; CYS-216; ALA-254; PHE-305; SER-309;
RP ARG-330; GLN-334; ASN-335; SER-343; PHE-403; PRO-406; TRP-407; THR-439;
RP LYS-440; THR-451; ASP-455; ARG-461; CYS-464 AND PRO-497.
RX PubMed=34349262; DOI=10.1038/s41586-021-03782-y;
RA Wood C.A.P., Zhang J., Aydin D., Xu Y., Andreone B.J., Langen U.H.,
RA Dror R.O., Gu C., Feng L.;
RT "Structure and mechanism of blood-brain-barrier lipid transporter MFSD2A.";
RL Nature 596:444-448(2021).
CC -!- FUNCTION: Sodium-dependent lysophosphatidylcholine (LPC) symporter,
CC which plays an essential role for blood-brain barrier formation and
CC function (PubMed:18694395, PubMed:23209793, PubMed:24828044,
CC PubMed:24828040, PubMed:34349262). Specifically expressed in
CC endothelium of the blood-brain barrier of micro-vessels and transports
CC LPC into the brain (PubMed:24828044, PubMed:24828040, PubMed:34349262).
CC Transport of LPC is essential because it constitutes the major
CC mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid
CC that is essential for normal brain growth and cognitive function,
CC enters the brain (PubMed:24828044, PubMed:24828040, PubMed:34349262).
CC Transports LPC carrying long-chain fatty acids such LPC oleate and LPC
CC palmitate with a minimum acyl chain length of 14 carbons
CC (PubMed:24828044, PubMed:34349262). Does not transport docosahexaenoic
CC acid in unesterified fatty acid (PubMed:24828044). Not required for
CC central nervous system vascular morphogenesis (PubMed:24828040).
CC {ECO:0000269|PubMed:18694395, ECO:0000269|PubMed:23209793,
CC ECO:0000269|PubMed:24828040, ECO:0000269|PubMed:24828044,
CC ECO:0000269|PubMed:34349262}.
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:0000269|PubMed:24828040};
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:0000269|PubMed:24828040};
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:0000269|PubMed:24828040};
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:0000269|PubMed:24828040};
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:0000269|PubMed:24828040};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209793,
CC ECO:0000269|PubMed:24828040}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:34349262}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18694395}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:34349262}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Exhibits an oscillatory pattern
CC of expression in brown adipose tissue and liver consistent with a
CC circadian rhythm. Enriched in brain micro-vessels, where it is
CC specifically present in endothelium constituting the blood-brain
CC barrier (at protein level) (PubMed:24828044, PubMed:24828040).
CC {ECO:0000269|PubMed:18694395, ECO:0000269|PubMed:23209793,
CC ECO:0000269|PubMed:24828040, ECO:0000269|PubMed:24828044}.
CC -!- INDUCTION: By fasting in liver and brown adipose tissue as well as by
CC cold exposure in brown adipose tissue. Expression following fasting is
CC dependent on glucagon signaling and Ppara.
CC {ECO:0000269|PubMed:18694395, ECO:0000269|PubMed:23209793}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:23209793}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at Mendelian ratios, but show
CC increased postnatal mortality early in life (PubMed:24828044). Mice are
CC smaller, leaner and have decreased serum, liver and brown adipose
CC triglycerides (PubMed:23209793). After weaning, mice display motor
CC dysfunction with front-paw clasping during tail suspension. Brain size
CC and weight are also significantly lower. Behavioral tests indicate that
CC mice have deficits in learning, and short- and long-term memory, as
CC well as severe anxiety, a phenotype related to omega-3 fatty-acid
CC deficiency. Lipidomic analysis of knockout mice shows strongly reduced
CC levels of docosahexaenoic acid (DHA) in brain accompanied by neuronal
CC cell loss in hippocampus and cerebellum (PubMed:24828044). Mice also
CC show a leaky blood-brain barrier from embryonic stages through to
CC adulthood, while the normal patterning of vascular networks is
CC maintained. Electron microscopy analysis shows an increase in central
CC nervous system-endothelial-cell vesicular transcytosis not associated
CC with tight-junction defects (PubMed:24828040). Mice have an increase in
CC plasma levels of LPC (PubMed:26005868). {ECO:0000269|PubMed:23209793,
CC ECO:0000269|PubMed:24828040, ECO:0000269|PubMed:24828044,
CC ECO:0000269|PubMed:26005868}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AK006096; BAB24407.1; -; mRNA.
DR EMBL; BC046793; AAH46793.1; -; mRNA.
DR EMBL; BC060526; AAH60526.1; -; mRNA.
DR CCDS; CCDS18605.1; -.
DR RefSeq; NP_083938.2; NM_029662.2.
DR PDB; 7N98; EM; 3.50 A; A=1-534.
DR PDBsum; 7N98; -.
DR AlphaFoldDB; Q9DA75; -.
DR SMR; Q9DA75; -.
DR STRING; 10090.ENSMUSP00000030408; -.
DR SwissLipids; SLP:000000999; -.
DR GlyGen; Q9DA75; 2 sites.
DR PhosphoSitePlus; Q9DA75; -.
DR EPD; Q9DA75; -.
DR MaxQB; Q9DA75; -.
DR PaxDb; Q9DA75; -.
DR PRIDE; Q9DA75; -.
DR ProteomicsDB; 293687; -.
DR Antibodypedia; 31983; 105 antibodies from 21 providers.
DR DNASU; 76574; -.
DR Ensembl; ENSMUST00000030408; ENSMUSP00000030408; ENSMUSG00000028655.
DR GeneID; 76574; -.
DR KEGG; mmu:76574; -.
DR UCSC; uc008uoo.2; mouse.
DR CTD; 84879; -.
DR MGI; MGI:1923824; Mfsd2a.
DR VEuPathDB; HostDB:ENSMUSG00000028655; -.
DR eggNOG; KOG4830; Eukaryota.
DR GeneTree; ENSGT00390000005318; -.
DR HOGENOM; CLU_027408_6_1_1; -.
DR InParanoid; Q9DA75; -.
DR OMA; GLYTAWM; -.
DR OrthoDB; 827101at2759; -.
DR PhylomeDB; Q9DA75; -.
DR TreeFam; TF331194; -.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR BioGRID-ORCS; 76574; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mfsd2a; mouse.
DR PRO; PR:Q9DA75; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DA75; protein.
DR Bgee; ENSMUSG00000028655; Expressed in primary oocyte and 152 other tissues.
DR ExpressionAtlas; Q9DA75; baseline and differential.
DR Genevisible; Q9DA75; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:ARUK-UCL.
DR GO; GO:0140348; F:lysophosphatidylcholine flippase activity; IDA:GO_Central.
DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:1901480; F:oleate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015293; F:symporter activity; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:ARUK-UCL.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR GO; GO:0009267; P:cellular response to starvation; IMP:ARUK-UCL.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0097009; P:energy homeostasis; IMP:ARUK-UCL.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IMP:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IMP:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IDA:BHF-UCL.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; IMP:UniProtKB.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:ARUK-UCL.
DR GO; GO:0140329; P:lysophospholipid translocation; ISO:MGI.
DR GO; GO:0051977; P:lysophospholipid transport; IDA:UniProtKB.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0061744; P:motor behavior; IMP:ARUK-UCL.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IMP:ARUK-UCL.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:ARUK-UCL.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:ARUK-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:ARUK-UCL.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:ARUK-UCL.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:ARUK-UCL.
DR GO; GO:0150011; P:regulation of neuron projection arborization; IMP:ARUK-UCL.
DR GO; GO:0150172; P:regulation of phosphatidylcholine metabolic process; IMP:ARUK-UCL.
DR GO; GO:0150175; P:regulation of phosphatidylethanolamine metabolic process; IMP:ARUK-UCL.
DR GO; GO:0150178; P:regulation of phosphatidylserine metabolic process; IMP:ARUK-UCL.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ARUK-UCL.
DR GO; GO:0003406; P:retinal pigment epithelium development; IMP:ARUK-UCL.
DR GO; GO:0045056; P:transcytosis; IMP:UniProtKB.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:ARUK-UCL.
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..534
FT /note="Sodium-dependent lysophosphatidylcholine symporter
FT 1"
FT /id="PRO_0000273388"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 40..69
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 70..80
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 102..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 134..148
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 149..173
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 174..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 181..212
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 213..232
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 233..266
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 267..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 298..324
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 325..335
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 355..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 381..383
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 384..420
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 421..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 431..457
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 458..469
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TRANSMEM 470..493
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT TOPO_DOM 494..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 216..464
FT /evidence="ECO:0000269|PubMed:34349262,
FT ECO:0007744|PDB:7N98"
FT MUTAGEN 55
FT /note="Y->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 56
FT /note="Q->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 64
FT /note="F->A: Slightly increased LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 67
FT /note="Q->H: Abolishes LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 82
FT /note="S->A: No effect on LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 86
FT /note="F->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 89
FT /note="R->A: No effect on LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 92
FT /note="D->A: Significant reduction in LPC transport.
FT Abolishes LPC transport; when associated with A-96."
FT /evidence="ECO:0000269|PubMed:24828044,
FT ECO:0000269|PubMed:34349262"
FT MUTAGEN 95
FT /note="T->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 96
FT /note="D->A: Abolishes LPC transport. Abolishes LPC
FT transport; when associated with A-92."
FT /evidence="ECO:0000269|PubMed:24828044,
FT ECO:0000269|PubMed:34349262"
FT MUTAGEN 159
FT /note="E->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 163
FT /note="T->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 163
FT /note="T->M: Abolishes LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 166
FT /note="H->A: Abolishes LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 168
FT /note="P->T: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 170
FT /note="S->L: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 190
FT /note="R->A: Abolishes LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 194
FT /note="E->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 202
FT /note="T->A: Slightly increased LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 202
FT /note="T->F: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 202
FT /note="T->M: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 207
FT /note="Q->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 216
FT /note="C->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 254
FT /note="A->F: Abolishes LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 305
FT /note="F->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 309
FT /note="S->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 330
FT /note="R->H: No effect on LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 334
FT /note="Q->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 335
FT /note="N->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 343
FT /note="S->L: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 403
FT /note="F->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 406
FT /note="P->H: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 407
FT /note="W->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 439
FT /note="T->A: No effect on LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 440
FT /note="K->A: Abolishes LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 451
FT /note="T->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 455
FT /note="D->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 461
FT /note="R->A: Slightly reduced LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 464
FT /note="C->A: Significant reduction in LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT MUTAGEN 497
FT /note="P->L: Abolishes LPC transport."
FT /evidence="ECO:0000269|PubMed:34349262"
FT CONFLICT 67
FT /note="Q -> H (in Ref. 2; AAH46793)"
FT /evidence="ECO:0000305"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:7N98"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 78..104
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 149..171
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 180..208
FT /evidence="ECO:0007829|PDB:7N98"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:7N98"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:7N98"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 236..265
FT /evidence="ECO:0007829|PDB:7N98"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 297..322
FT /evidence="ECO:0007829|PDB:7N98"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:7N98"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:7N98"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:7N98"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 364..378
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 387..408
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 410..419
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 428..455
FT /evidence="ECO:0007829|PDB:7N98"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:7N98"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 470..492
FT /evidence="ECO:0007829|PDB:7N98"
FT HELIX 499..508
FT /evidence="ECO:0007829|PDB:7N98"
SQ SEQUENCE 534 AA; 58984 MW; 2DE15EBBB2C1F396 CRC64;
MAKGEGAESG SAAGLLPTSI LQASERPVQV KKEPKKKQQL SICNKLCYAV GGAPYQLTGC
ALGFFLQIYL LDVAKVEPLP ASIILFVGRA WDAFTDPLVG FCISKSSWTR LGRLMPWIIF
STPLAIIAYF LIWFVPDFPS GTESSHGFLW YLLFYCLFET LVTCFHVPYS ALTMFISTEQ
SERDSATAYR MTVEVLGTVI GTAIQGQIVG QAKAPCLQDQ NGSVVVSEVA NRTQSTASLK
DTQNAYLLAA GIIASIYVLC AFILILGVRE QRELYESQQA ESMPFFQGLR LVMGHGPYVK
LIAGFLFTSL AFMLVEGNFA LFCTYTLDFR NEFQNLLLAI MLSATFTIPI WQWFLTRFGK
KTAVYIGISS AVPFLILVAL MERNLIVTYV VAVAAGVSVA AAFLLPWSML PDVIDDFHLK
HPHSPGTEPI FFSFYVFFTK FASGVSLGVS TLSLDFANYQ RQGCSQPEQV KFTLKMLVTM
APIILILLGL LLFKLYPIDE EKRRQNKKAL QALREEASSS GCSDTDSTEL ASIL
