ID   LAT1_RAT                Reviewed;         512 AA.
AC   Q63016; Q9QWL4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Large neutral amino acids transporter small subunit 1;
DE   AltName: Full=4F2 light chain;
DE            Short=4F2 LC;
DE            Short=4F2LC;
DE   AltName: Full=Integral membrane protein E16;
DE            Short=Protein TA1 {ECO:0000303|PubMed:7532544};
DE   AltName: Full=L-type amino acid transporter 1 {ECO:0000303|PubMed:15980244};
DE            Short=LAT-1 {ECO:0000303|PubMed:15120633};
DE   AltName: Full=Solute carrier family 7 member 5;
GN   Name=Slc7a5;
GN   Synonyms=Lat1 {ECO:0000303|PubMed:9726963}, Mpe16, Ta1
GN   {ECO:0000303|PubMed:7532544};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY,
RP   TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9726963; DOI=10.1074/jbc.273.37.23629;
RA   Kanai Y., Segawa H., Miyamoto K., Uchino H., Takeda E., Endou H.;
RT   "Expression cloning and characterization of a transporter for large neutral
RT   amino acids activated by the heavy chain of 4F2 antigen (CD98).";
RL   J. Biol. Chem. 273:23629-23632(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 272-512, AND TISSUE SPECIFICITY.
RC   TISSUE=Hepatoma;
RX   PubMed=7532544;
RA   Sang J., Lim Y.P., Panzica M., Finch P., Thompson N.L.;
RT   "TA1, a highly conserved oncofetal complementary DNA from rat hepatoma,
RT   encodes an integral membrane protein associated with liver development,
RT   carcinogenesis, and cell activation.";
RL   Cancer Res. 55:1152-1159(1995).
RN   [3]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11095508; DOI=10.1097/00001756-200011090-00021;
RA   Matsuo H., Tsukada S., Nakata T., Chairoungdua A., Kim D.K., Cha S.H.,
RA   Inatomi J., Yorifuji H., Fukuda J., Endou H., Kanai Y.;
RT   "Expression of a system L neutral amino acid transporter at the blood-brain
RT   barrier.";
RL   NeuroReport 11:3507-3511(2000).
RN   [4]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11311135; DOI=10.1042/bj3550725;
RA   Broeer A., Friedrich B., Wagner C.A., Fillon S., Ganapathy V., Lang F.,
RA   Broeer S.;
RT   "Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires
RT   different domains.";
RL   Biochem. J. 355:725-731(2001).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TRANSPORTER ACTIVITY.
RX   PubMed=12614332; DOI=10.1046/j.1471-4159.2003.01622.x;
RA   Boado R.J., Li J.Y., Pardridge W.M.;
RT   "Site-directed mutagenesis of rabbit LAT1 at amino acids 219 and 234.";
RL   J. Neurochem. 84:1322-1331(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15120633; DOI=10.1016/j.bbrc.2004.04.062;
RA   Padbury J.F., Diah S.K., McGonnigal B., Miller C., Fugere C., Kuzniar M.,
RA   Thompson N.L.;
RT   "Transcriptional regulation of the LAT-1/CD98 light chain.";
RL   Biochem. Biophys. Res. Commun. 318:529-534(2004).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16027961; DOI=10.1007/s00726-005-0221-x;
RA   Fraga S., Pinho M.J., Soares-da-Silva P.;
RT   "Expression of LAT1 and LAT2 amino acid transporters in human and rat
RT   intestinal epithelial cells.";
RL   Amino Acids 29:229-233(2005).
RN   [8]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, TRANSPORTER
RP   ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=15980244; DOI=10.1167/iovs.04-1175;
RA   Tomi M., Mori M., Tachikawa M., Katayama K., Terasaki T., Hosoya K.;
RT   "L-type amino acid transporter 1-mediated L-leucine transport at the inner
RT   blood-retinal barrier.";
RL   Invest. Ophthalmol. Vis. Sci. 46:2522-2530(2005).
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, L-DOPA, histidine,
CC       methionine, valine and alanine (By similarity). The heterodimer with
CC       SLC3A2 mediates the uptake of leucine, isoleucine and tryptophan
CC       (PubMed:9726963, PubMed:11311135, PubMed:12614332, PubMed:15980244).
CC       Functions as an amino acid exchanger (By similarity). May play a role
CC       in the transport of L-DOPA across the blood-brain barrier (By
CC       similarity). May act as the major transporter of tyrosine in
CC       fibroblasts (By similarity). May mediate blood-to-retina L-leucine
CC       transport across the inner blood-retinal barrier (Probable). Can
CC       mediate the transport of thyroid hormones diiodothyronine (T2),
CC       triiodothyronine (T3) and thyroxine (T4) across the cell membrane. When
CC       associated with LAPTM4B, the heterodimer formed by SLC3A2 and SLC7A5 is
CC       recruited to lysosomes to promote leucine uptake into these organelles,
CC       and thereby mediates mTORC1 activation. Involved in the uptake of toxic
CC       methylmercury (MeHg) when administered as the L-cysteine or D,L-
CC       homocysteine complexes. Involved in the cellular activity of small
CC       molecular weight nitrosothiols, via the stereoselective transport of L-
CC       nitrosocysteine (L-CNSO) across the membrane (By similarity).
CC       {ECO:0000250|UniProtKB:Q01650, ECO:0000250|UniProtKB:Q9Z127,
CC       ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:12614332,
CC       ECO:0000269|PubMed:9726963, ECO:0000305|PubMed:15980244}.
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:0000269|PubMed:12614332};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70949;
CC         Evidence={ECO:0000305|PubMed:12614332};
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:15980244,
CC         ECO:0000269|PubMed:9726963};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73013;
CC         Evidence={ECO:0000305|PubMed:9726963};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-isoleucine(in) = L-isoleucine(out); Xref=Rhea:RHEA:70943,
CC         ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:11311135};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70945;
CC         Evidence={ECO:0000305|PubMed:11311135};
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: L-leucine uptake by TR-iBRB2 cells was inhibited
CC       by L-leucine, L-phenylalanine, L-methionine, L-isoleucine, L-valine, L-
CC       tyrosine, L-tryptophan, D-leucine, D-phenylalanine, D-methionine and by
CC       2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid (BCH) (a specific
CC       inhibitor of system L transport). {ECO:0000269|PubMed:15980244}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14.1 uM for L-leucine {ECO:0000269|PubMed:15980244};
CC         KM=18.5 uM for tryptophan (in frog oocytes)
CC         {ECO:0000269|PubMed:12614332};
CC         KM=18.1 uM for leucine {ECO:0000269|PubMed:9726963};
CC         Note=Km values in PubMed:9726963, PubMed:12614332 were determined for
CC         the heterodimer of SLC7A5/LAT1 and SLC3A2/4F2hc.;
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC       protein SLC3A2/4F2hc (PubMed:9726963, PubMed:11311135). 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:11311135,
CC       ECO:0000269|PubMed:9726963}.
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:11311135, ECO:0000269|PubMed:16027961}; Multi-pass
CC       membrane protein {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. Localized to the apical membrane of placental
CC       syncytiotrophoblastic cells. Recruited to lysosomes by LAPTM4B (By
CC       similarity). Expressed in both luminal and abluminal membranes of brain
CC       capillary endothelial cells (PubMed:11095508).
CC       {ECO:0000250|UniProtKB:Q01650, ECO:0000269|PubMed:11095508}.
CC   -!- TISSUE SPECIFICITY: Expressed in hepatoma but not in normal liver. Also
CC       expressed in placenta, testis, brain, ovary, spleen, mammary gland, and
CC       uterus. In brain expressed on capillary endothelia in cerebral cortex.
CC       Expressed in jejunum mucosa and the epithelial cells of the jejunum,
CC       ileum and colon. Also expressed in the intestinal epithelial cell line
CC       IEC-6. Expressed in the brain, retina, inner blood-retinal barrier of
CC       retina, retinal vascular endothelial cells, and in the retinal
CC       capillary endothelial cell line TR-iBRB2. {ECO:0000269|PubMed:11095508,
CC       ECO:0000269|PubMed:15120633, ECO:0000269|PubMed:15980244,
CC       ECO:0000269|PubMed:16027961, ECO:0000269|PubMed:7532544,
CC       ECO:0000269|PubMed:9726963}.
CC   -!- INDUCTION: Expression induced in normal hepatic cells cultured in
CC       arginine-depleted medium. {ECO:0000269|PubMed:15120633}.
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; AB015432; BAA33035.1; -; mRNA.
DR   EMBL; U00995; AAA74411.1; -; mRNA.
DR   RefSeq; NP_059049.1; NM_017353.1.
DR   AlphaFoldDB; Q63016; -.
DR   SMR; Q63016; -.
DR   BioGRID; 248432; 1.
DR   IntAct; Q63016; 1.
DR   STRING; 10116.ENSRNOP00000025784; -.
DR   BindingDB; Q63016; -.
DR   ChEMBL; CHEMBL4149; -.
DR   DrugCentral; Q63016; -.
DR   TCDB; 2.A.3.8.1; the amino acid-polyamine-organocation (apc) family.
DR   PhosphoSitePlus; Q63016; -.
DR   jPOST; Q63016; -.
DR   PaxDb; 10116-ENSRNOP00000025784; -.
DR   Ensembl; ENSRNOT00000025784.3; ENSRNOP00000025784.1; ENSRNOG00000018824.3.
DR   Ensembl; ENSRNOT00055034039; ENSRNOP00055027649; ENSRNOG00055019934.
DR   Ensembl; ENSRNOT00060032021; ENSRNOP00060026042; ENSRNOG00060018608.
DR   Ensembl; ENSRNOT00065010492; ENSRNOP00065007715; ENSRNOG00065006751.
DR   GeneID; 50719; -.
DR   KEGG; rno:50719; -.
DR   UCSC; RGD:620639; rat.
DR   AGR; RGD:620639; -.
DR   CTD; 8140; -.
DR   RGD; 620639; Slc7a5.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000155581; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; Q63016; -.
DR   OMA; WCQKVME; -.
DR   OrthoDB; 1103451at2759; -.
DR   PhylomeDB; Q63016; -.
DR   TreeFam; TF313355; -.
DR   Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-RNO-71240; Tryptophan catabolism.
DR   SABIO-RK; Q63016; -.
DR   PRO; PR:Q63016; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000018824; Expressed in pancreas and 20 other cell types or tissues.
DR   GO; GO:1990184; C:amino acid transport complex; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0098591; C:external side of apical plasma membrane; IDA:ARUK-UCL.
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:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IMP:ARUK-UCL.
DR   GO; GO:0015297; F:antiporter activity; ISS:UniProtKB.
DR   GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; ISO:RGD.
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:RGD.
DR   GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
DR   GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0032328; P:alanine transport; ISO:RGD.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IMP:ARUK-UCL.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IEP:RGD.
DR   GO; GO:1903577; P:cellular response to L-arginine; IEP:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0015818; P:isoleucine transport; IDA:UniProtKB.
DR   GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; ISO:RGD.
DR   GO; GO:0015807; P:L-amino acid transport; IMP:RGD.
DR   GO; GO:1902024; P:L-histidine transport; ISO:RGD.
DR   GO; GO:1903801; P:L-leucine import across plasma membrane; ISO:RGD.
DR   GO; GO:1904556; P:L-tryptophan transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0098713; P:leucine import across plasma membrane; ISO:RGD.
DR   GO; GO:0015820; P:leucine transport; IDA:UniProtKB.
DR   GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR   GO; GO:0015821; P:methionine transport; ISO:RGD.
DR   GO; GO:0010507; P:negative regulation of autophagy; IMP:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; IDA:RGD.
DR   GO; GO:0015804; P:neutral amino acid transport; ISS:UniProtKB.
DR   GO; GO:0015823; P:phenylalanine transport; ISO:RGD.
DR   GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
DR   GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:RGD.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:RGD.
DR   GO; GO:1905534; P:positive regulation of leucine import across plasma membrane; IMP:RGD.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; ISO:RGD.
DR   GO; GO:0015824; P:proline transport; ISO:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR   GO; GO:0070327; P:thyroid hormone transport; ISO:RGD.
DR   GO; GO:0015827; P:tryptophan transport; IDA:UniProtKB.
DR   GO; GO:0015828; P:tyrosine transport; ISO:RGD.
DR   GO; GO:0015829; P:valine transport; IMP:RGD.
DR   GO; GO:0042908; P:xenobiotic transport; ISO:RGD.
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; Q63016; RN.
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_0000054272"
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"
SQ   SEQUENCE   512 AA;  55903 MW;  B487CE0B58D73A02 CRC64;
     MAVAGAKRRA VAAPATTAAE EERQAREKML EARRGDGADP EGEGVTLQRN ITLINGVAII
     VGTIIGSGIF VTPTGVLKEA GSPGLSLVVW AVCGVFSIVG ALCYAELGTT ISKSGGDYAY
     MLEVYGSLPA FLKLWIELLI IRPSSQYIVA LVFATYLLKP VFPTCPVPEE AAKLVACLCV
     LLLTAVNCYS VKAATRVQDA FAAAKLLALA LIILLGFIQM GKDIGQGDAS NLHQKLSFEG
     TNLDVGNIVL ALYSGLFAYG GWNYLNFVTE EMINPYRNLP LAIIISLPIV TLVYVLTNLA
     YFTTLSTNQM LTSEAVAVDF GNYHLGVMSW IIPVFVGLSC FGSVNGSLFT SSRLFFVGSR
     EGHLPSILSM IHPQLLTPVP SLVFTCVMTL MYAFSRDIFS IINFFSFFNW LCVALAIIGM
     MWLRFKKPEL ERPIKVNLAL PVFFILACLF LIAVSFWKTP LECGIGFAII LSGLPVYFFG
     VWWKNKPKWI LQVIFSVTVL CQKLMQVVPQ ET
//