ID   LAT1_MOUSE              Reviewed;         512 AA.
AC   Q9Z127; Q8R0X8; Q9JMI4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Large neutral amino acids transporter small subunit 1;
DE   AltName: Full=4F2 light chain {ECO:0000303|PubMed:9915839};
DE            Short=4F2 LC;
DE            Short=4F2LC {ECO:0000303|PubMed:9915839};
DE   AltName: Full=L-type amino acid transporter 1 {ECO:0000303|PubMed:9915839};
DE            Short=LAT1 {ECO:0000303|PubMed:11011012};
DE   AltName: Full=Solute carrier family 7 member 5;
GN   Name=Slc7a5; Synonyms=Lat1;
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 [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   INDUCTION, ACTIVITY REGULATION, AND TRANSPORTER ACTIVITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=9915839; DOI=10.1074/jbc.274.5.3009;
RA   Nakamura E., Sato M., Yang H., Miyagawa F., Harasaki M., Tomita K.,
RA   Matsuoka S., Noma A., Iwai K., Minato N.;
RT   "4F2 (CD98) heavy chain is associated covalently with an amino acid
RT   transporter and controls intracellular trafficking and membrane topology of
RT   4F2 heterodimer.";
RL   J. Biol. Chem. 274:3009-3016(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RA   Kanai Y., Watanabe M., Endou H.;
RT   "Localization of expression of system L neutral amino acid transporter LAT1
RT   in brain.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=10574970; DOI=10.1074/jbc.274.49.34948;
RA   Rossier G., Meier C., Bauch C., Summa V., Sordat B., Verrey F., Kuehn L.C.;
RT   "LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of
RT   kidney and intestine.";
RL   J. Biol. Chem. 274:34948-34954(1999).
RN   [5]
RP   FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=11011012; DOI=10.1016/s0006-8993(00)02758-x;
RA   Kageyama T., Nakamura M., Matsuo A., Yamasaki Y., Takakura Y., Hashida M.,
RA   Kanai Y., Naito M., Tsuruo T., Minato N., Shimohama S.;
RT   "The 4F2hc/LAT1 complex transports L-DOPA across the blood-brain barrier.";
RL   Brain Res. 879:115-121(2000).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=11117468; DOI=10.1097/00001756-200011270-00015;
RA   Kageyama T., Imura T., Matsuo A., Minato N., Shimohama S.;
RT   "Distribution of the 4F2 light chain, LAT1, in the mouse brain.";
RL   NeuroReport 11:3663-3666(2000).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: The heterodimer with SLC3A2 functions as a sodium-
CC       independent, high-affinity transporter that mediates uptake of large
CC       neutral amino acids such as phenylalanine, tyrosine, histidine, met
CC       hionine, tryptophan, valine, isoleucine and alanine (By similarity).
CC       The heterodimer with SLC3A2 mediates the uptake of L-DOPA and leucine
CC       (PubMed:9915839, PubMed:11011012). Functions as an amino acid exchanger
CC       (By similarity). May play a role in the transport of L-DOPA across the
CC       blood-brain barrier (PubMed:11011012). May act as the major transporter
CC       of tyrosine in fibroblasts (By similarity). May mediate blood-to-retina
CC       L-leucine transport across the inner blood-retinal barrier (By
CC       similarity). Can mediate the transport of thyroid hormones
CC       diiodothyronine (T2), triiodothyronine (T3) and thyroxine (T4) across
CC       the cell membrane. When associated with LAPTM4B, the heterodimer formed
CC       by SLC3A2 and SLC7A5 is recruited to lysosomes to promote leucine
CC       uptake into these organelles, and thereby mediates mTORC1 activation.
CC       Involved in the uptake of toxic methylmercury (MeHg) when administered
CC       as the L-cysteine or D,L-homocysteine complexes. Involved in the
CC       cellular activity of small molecular weight nitrosothiols, via the
CC       stereoselective transport of L-nitrosocysteine (L-CNSO) across the
CC       membrane (By similarity). {ECO:0000250|UniProtKB:Q01650,
CC       ECO:0000250|UniProtKB:Q63016, ECO:0000269|PubMed:11011012,
CC       ECO:0000269|PubMed:9915839}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine(in) = L-phenylalanine(out);
CC         Xref=Rhea:RHEA:27950, ChEBI:CHEBI:58095;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27952;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan(in) = L-tryptophan(out); Xref=Rhea:RHEA:70947,
CC         ChEBI:CHEBI:57912; Evidence={ECO:0000250|UniProtKB:Q01650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70949;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidine(out) = L-histidine(in); Xref=Rhea:RHEA:72807,
CC         ChEBI:CHEBI:57595; Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine(in) = L-leucine(out); Xref=Rhea:RHEA:73011,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:9915839};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73013;
CC         Evidence={ECO:0000305|PubMed:9915839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-isoleucine(in) = L-isoleucine(out); Xref=Rhea:RHEA:70943,
CC         ChEBI:CHEBI:58045; Evidence={ECO:0000250|UniProtKB:Q01650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70945;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-valine(in) = L-valine(out); Xref=Rhea:RHEA:29703,
CC         ChEBI:CHEBI:57762; Evidence={ECO:0000250|UniProtKB:Q01650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29705;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine(in) = L-tyrosine(out); Xref=Rhea:RHEA:68572,
CC         ChEBI:CHEBI:58315; Evidence={ECO:0000250|UniProtKB:Q01650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68574;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionine(in) = L-methionine(out); Xref=Rhea:RHEA:70939,
CC         ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q01650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70941;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) = L-alanine(out); Xref=Rhea:RHEA:70719,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q01650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70721;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,3'-diiodo-L-thyronine(out) = 3,3'-diiodo-L-thyronine(in);
CC         Xref=Rhea:RHEA:71823, ChEBI:CHEBI:176514;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L-
CC         thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015;
CC         Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819,
CC         ChEBI:CHEBI:58448; Evidence={ECO:0000250|UniProtKB:Q01650};
CC   -!- ACTIVITY REGULATION: Leucine uptake was inhibited by ileum, valine
CC       histidine and phenylalanine as well as by 2-amino-bicyclo-(2,2,1)-
CC       heptane-2-carboxylate (BCH) (a specific inhibitor of system L
CC       transport). {ECO:0000269|PubMed:9915839}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25 uM for leucine {ECO:0000269|PubMed:9915839};
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC       protein SLC3A2/4F2hc (PubMed:9915839, PubMed:11011012). Interacts with
CC       LAPTM4B; this recruits the heterodimer formed by SLC3A2 and SLC7A5 to
CC       lysosomes to promote leucine uptake into these organelles and is
CC       required for mTORC1 activation (By similarity).
CC       {ECO:0000250|UniProtKB:Q01650, ECO:0000269|PubMed:11011012,
CC       ECO:0000269|PubMed:9915839}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q01650}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q01650}. Cell membrane
CC       {ECO:0000269|PubMed:9915839}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q01650}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q01650}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q01650}. Note=Located to the plasma membrane by
CC       SLC3A2/4F2hc (PubMed:9915839). Localized to the apical membrane of
CC       placental syncytiotrophoblastic cells. Recruited to lysosomes by
CC       LAPTM4B (By similarity). Expressed in both luminal and abluminal
CC       membranes of brain capillary endothelial cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q01650, ECO:0000250|UniProtKB:Q63016,
CC       ECO:0000269|PubMed:9915839}.
CC   -!- TISSUE SPECIFICITY: Detected in brain, spleen, liver and testis (at
CC       protein level) (PubMed:9915839). Predominantly expressed in the
CC       microvessels in the brain parenchyma of the central nervous system.
CC       Also detected in the subfornical organ, the subcommissural organ,
CC       ventromedial nucleus of the hypothalamus, subgranular zone of the
CC       dentate gyrus in hippocampus, ependymal layer of the lateral
CC       ventricles, and the olfactory bulb. Very strong expression also seen in
CC       testis, ovary, and placenta with weaker expression in spleen, skin,
CC       brain, thymus, stomach, lung, heart, kidney, small intestine, uterus
CC       and skeletal muscle. {ECO:0000269|PubMed:10574970,
CC       ECO:0000269|PubMed:11011012, ECO:0000269|PubMed:11117468,
CC       ECO:0000269|PubMed:9915839}.
CC   -!- DEVELOPMENTAL STAGE: Strong expression in the liver of 14 dpc embryo.
CC       In embryo of 18 dpc expressed strongly in brain, moderate expression in
CC       spleen and brain and weak expression in liver.
CC       {ECO:0000269|PubMed:9915839}.
CC   -!- INDUCTION: Expression induced by concanavalin-A stimulation.
CC       {ECO:0000269|PubMed:9915839}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
CC       {ECO:0000305}.
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DR   EMBL; AB017189; BAA75520.1; -; mRNA.
DR   EMBL; AB023409; BAA90556.1; -; mRNA.
DR   EMBL; BC026131; AAH26131.1; -; mRNA.
DR   CCDS; CCDS22730.1; -.
DR   RefSeq; NP_035534.2; NM_011404.3.
DR   AlphaFoldDB; Q9Z127; -.
DR   SMR; Q9Z127; -.
DR   BioGRID; 203318; 44.
DR   STRING; 10090.ENSMUSP00000041557; -.
DR   ChEMBL; CHEMBL4523516; -.
DR   GlyGen; Q9Z127; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Z127; -.
DR   PhosphoSitePlus; Q9Z127; -.
DR   SwissPalm; Q9Z127; -.
DR   EPD; Q9Z127; -.
DR   MaxQB; Q9Z127; -.
DR   PaxDb; 10090-ENSMUSP00000041557; -.
DR   ProteomicsDB; 265046; -.
DR   Pumba; Q9Z127; -.
DR   Antibodypedia; 17241; 451 antibodies from 39 providers.
DR   DNASU; 20539; -.
DR   Ensembl; ENSMUST00000045557.10; ENSMUSP00000041557.9; ENSMUSG00000040010.11.
DR   GeneID; 20539; -.
DR   KEGG; mmu:20539; -.
DR   UCSC; uc009nsc.2; mouse.
DR   AGR; MGI:1298205; -.
DR   CTD; 8140; -.
DR   MGI; MGI:1298205; Slc7a5.
DR   VEuPathDB; HostDB:ENSMUSG00000040010; -.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000155581; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; Q9Z127; -.
DR   OMA; WCQKVME; -.
DR   OrthoDB; 1103451at2759; -.
DR   PhylomeDB; Q9Z127; -.
DR   TreeFam; TF313355; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-MMU-71240; Tryptophan catabolism.
DR   BioGRID-ORCS; 20539; 18 hits in 78 CRISPR screens.
DR   ChiTaRS; Slc7a5; mouse.
DR   PRO; PR:Q9Z127; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9Z127; Protein.
DR   Bgee; ENSMUSG00000040010; Expressed in lacrimal gland and 259 other cell types or tissues.
DR   GO; GO:1990184; C:amino acid transport complex; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0098591; C:external side of apical plasma membrane; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015297; F:antiporter activity; ISS:UniProtKB.
DR   GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015190; F:L-leucine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015196; F:L-tryptophan transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0032328; P:alanine transport; ISO:MGI.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR   GO; GO:1903577; P:cellular response to L-arginine; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0015818; P:isoleucine transport; ISO:MGI.
DR   GO; GO:0015807; P:L-amino acid transport; IDA:MGI.
DR   GO; GO:1902024; P:L-histidine transport; ISO:MGI.
DR   GO; GO:1903801; P:L-leucine import across plasma membrane; ISO:MGI.
DR   GO; GO:1904556; P:L-tryptophan transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0098713; P:leucine import across plasma membrane; ISO:MGI.
DR   GO; GO:0015820; P:leucine transport; IDA:UniProtKB.
DR   GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR   GO; GO:0015821; P:methionine transport; ISO:MGI.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0015804; P:neutral amino acid transport; ISO:MGI.
DR   GO; GO:0015823; P:phenylalanine transport; ISO:MGI.
DR   GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR   GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:MGI.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:MGI.
DR   GO; GO:1905534; P:positive regulation of leucine import across plasma membrane; ISO:MGI.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; ISO:MGI.
DR   GO; GO:0015824; P:proline transport; ISO:MGI.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR   GO; GO:0070327; P:thyroid hormone transport; ISO:MGI.
DR   GO; GO:0015827; P:tryptophan transport; ISO:MGI.
DR   GO; GO:0015828; P:tyrosine transport; ISO:MGI.
DR   GO; GO:0015829; P:valine transport; ISO:MGI.
DR   GO; GO:0042908; P:xenobiotic transport; ISO:MGI.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004760; L_AA_transporter.
DR   NCBIfam; TIGR00911; 2A0308; 1.
DR   PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR11785:SF315; LARGE NEUTRAL AMINO ACIDS TRANSPORTER SMALL SUBUNIT 1; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   Genevisible; Q9Z127; MM.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Disulfide bond; Lysosome; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..512
FT                   /note="Large neutral amino acids transporter small subunit
FT                   1"
FT                   /id="PRO_0000054271"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        72..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        106..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        149..170
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        192..193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        194..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        216..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        269..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        303..329
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        351..374
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        396..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        422..435
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        436..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        457..462
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   TOPO_DOM        484..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   DISULFID        165
FT                   /note="Interchain (with C-210 in SLC3A2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q01650"
FT   CONFLICT        8
FT                   /note="R -> M (in Ref. 2; BAA90556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="A -> T (in Ref. 1; BAA75520 and 2; BAA90556)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  55872 MW;  57045EC4DD9DE1A1 CRC64;
     MAVAGAKRRA VATPAAAAAE EERQAREKML EARRGDGADP EGEGVTLQRN ITLLNGVAII
     VGTIIGSGIF VTPTGVLKEA GSPGLSLVVW AVCGVFSIVG ALCYAELGTT ISKSGGDYAY
     MLEVYGSLPA FLKLWIELLI IRPSSQYIVA LVFATYLLKP VFPTCPVPEE AAKLVACLCV
     LLLTAVNCYS VKAATRVQDA FAAAKLLALA LIILLGFIQM GKDMGQGDAS NLQQKLSFEG
     TNLDVGNIVL ALYSGLFAYG GWNYLNFVTE EMINPYRNLP LAIIISLPIV TLVYVLTNLA
     YFTTLSTNQM LTSEAVAVDF GNYHLGVMSW IIPVFVGLSC FGSVNGSLFT SSRLFFVGSR
     EGHLPSVLSM IHPQLLTPVP SLVFTCIMTL MYAFSRDIFS IINFFSFFNW LCVALAIIGM
     MWLRFKKPEL ERPIKVNLAL PVFFILACLF LIAVSFWKTP MECGIGFAII LSGLPVYFFG
     VWWKNKPKWI LQAIFSVTVL CQKLMQVVPQ ET
//