ID LAT2_RAT Reviewed; 533 AA. AC Q9WVR6; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=Large neutral amino acids transporter small subunit 2; DE AltName: Full=L-type amino acid transporter 2; DE AltName: Full=Solute carrier family 7 member 8; GN Name=Slc7a8; Synonyms=Lat2, Lat4; 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, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBUNIT, TISSUE SPECIFICITY, AND ACTIVITY REGULATION. RC TISSUE=Small intestine; RX PubMed=10391916; DOI=10.1074/jbc.274.28.19745; RA Segawa H., Fukasawa Y., Miyamoto K., Takeda E., Endou H., Kanai Y.; RT "Identification and functional characterization of a Na+-independent RT neutral amino acid transporter with broad substrate selectivity."; RL J. Biol. Chem. 274:19745-19751(1999). RN [2] 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 [3] RP TISSUE SPECIFICITY. 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). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-29; SER-30 AND RP SER-529, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [5] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15200428; DOI=10.1111/j.1523-1755.2004.00722.x; RA Pinho M.J., Serrao M.P., Gomes P., Hopfer U., Jose P.A., RA Soares-da-Silva P.; RT "Over-expression of renal LAT1 and LAT2 and enhanced L-DOPA uptake in SHR RT immortalized renal proximal tubular cells."; RL Kidney Int. 66:216-226(2004). CC -!- FUNCTION: Associates with SLC3A2 to form a functional heterodimeric CC complex that translocates small and large neutral amino acids with CC broad specificity and a stoichiometry of 1:1 (PubMed:10391916). CC Functions as amino acid antiporter mediating the influx of CC extracellular essential amino acids mainly in exchange with the efflux CC of highly concentrated intracellular amino acids. Has relatively CC symmetrical selectivities but strongly asymmetrical substrate CC affinities at both the intracellular and extracellular sides of the CC transporter. This asymmetry allows SLC7A8 to regulate intracellular CC amino acid pools (mM concentrations) by exchange with external amino CC acids (uM concentration range), equilibrating the relative CC concentrations of different amino acids across the plasma membrane CC instead of mediating their net uptake. May play an essential role in CC the reabsorption of neutral amino acids from the epithelial cells to CC the bloodstream in the kidney. Involved in the uptake of methylmercury CC (MeHg) when administered as the L-cysteine or D,L-homocysteine CC complexes, and hence plays a role in metal ion homeostasis and CC toxicity. Involved in the cellular activity of small molecular weight CC nitrosothiols, via the stereoselective transport of L-nitrosocysteine CC (L-CNSO) across the transmembrane (By similarity). Imports the thyroid CC hormone diiodothyronine (T2) and to a smaller extent triiodothyronine CC (T3) but not rT 3 or thyroxine (T4) (By similarity). Mediates the CC uptake of L-DOPA (PubMed:15200428). May participate in auditory CC function (By similarity). {ECO:0000250|UniProtKB:Q9QXW9, CC ECO:0000250|UniProtKB:Q9UHI5, ECO:0000269|PubMed:10391916, CC ECO:0000269|PubMed:15200428}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-dopa(out) + L-phenylalanine(in) = L-dopa(in) + L- CC phenylalanine(out); Xref=Rhea:RHEA:71439, ChEBI:CHEBI:57504, CC ChEBI:CHEBI:58095; Evidence={ECO:0000305|PubMed:15200428}; 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:Q9QXW9}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71824; CC Evidence={ECO:0000250|UniProtKB:Q9QXW9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidine(in) + L-phenylalanine(out) = L-histidine(out) + L- CC phenylalanine(in); Xref=Rhea:RHEA:71003, ChEBI:CHEBI:57595, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-phenylalanine(out) + L-tryptophan(in) = L-phenylalanine(in) CC + L-tryptophan(out); Xref=Rhea:RHEA:71007, ChEBI:CHEBI:57912, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-isoleucine(in) + L-phenylalanine(out) = L-isoleucine(out) + CC L-phenylalanine(in); Xref=Rhea:RHEA:71011, ChEBI:CHEBI:58045, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-phenylalanine(out) + L-valine(in) = L-phenylalanine(in) + L- CC valine(out); Xref=Rhea:RHEA:71019, ChEBI:CHEBI:57762, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-leucine(in) + L-phenylalanine(out) = L-leucine(out) + L- CC phenylalanine(in); Xref=Rhea:RHEA:71023, ChEBI:CHEBI:57427, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamine(in) + L-phenylalanine(out) = L-glutamine(out) + L- CC phenylalanine(in); Xref=Rhea:RHEA:71027, ChEBI:CHEBI:58095, CC ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cysteine(in) + L-phenylalanine(out) = L-cysteine(out) + L- CC phenylalanine(in); Xref=Rhea:RHEA:71031, ChEBI:CHEBI:35235, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionine(in) + L-phenylalanine(out) = L-methionine(out) + CC L-phenylalanine(in); Xref=Rhea:RHEA:71039, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-leucine(out) + L-methionine(in) = L-leucine(in) + L- CC methionine(out); Xref=Rhea:RHEA:71051, ChEBI:CHEBI:57427, CC ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cysteine(out) + L-methionine(in) = L-cysteine(in) + L- CC methionine(out); Xref=Rhea:RHEA:71055, ChEBI:CHEBI:35235, CC ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionine(in) + S-methylmercury-L-cysteine(out) = L- CC methionine(out) + S-methylmercury-L-cysteine(in); CC Xref=Rhea:RHEA:71103, ChEBI:CHEBI:57844, ChEBI:CHEBI:190186; CC Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-leucine(out) + S-methylmercury-L-cysteine(in) = L- CC leucine(in) + S-methylmercury-L-cysteine(out); Xref=Rhea:RHEA:71107, CC ChEBI:CHEBI:57427, ChEBI:CHEBI:190186; CC Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-phenylalanine(out) + S-methylmercury-L-cysteine(in) = L- CC phenylalanine(in) + S-methylmercury-L-cysteine(out); CC Xref=Rhea:RHEA:71111, ChEBI:CHEBI:58095, ChEBI:CHEBI:190186; CC Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-phenylalanine(out) + L-serine(in) = L-phenylalanine(in) + L- CC serine(out); Xref=Rhea:RHEA:71035, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycine(in) + L-phenylalanine(out) = glycine(out) + L- CC phenylalanine(in); Xref=Rhea:RHEA:71047, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine(in) + L-phenylalanine(out) = L-alanine(out) + L- CC phenylalanine(in); Xref=Rhea:RHEA:71043, ChEBI:CHEBI:57972, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UHI5}; 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:Q9QXW9}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812; CC Evidence={ECO:0000250|UniProtKB:Q9QXW9}; CC -!- ACTIVITY REGULATION: Leucine transport activity is inhibited by 2- CC amino-bicyclo-(2,2,1)-heptane-2-carboxylate (BCH), glycine, L-isomers CC of the neutral amino acids and histidine. CC {ECO:0000269|PubMed:10391916}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=119 uM for L-leucine {ECO:0000269|PubMed:10391916}; CC KM=265 uM for glycine {ECO:0000269|PubMed:10391916}; CC KM=187 uM for L-alanine {ECO:0000269|PubMed:10391916}; CC KM=116 uM for L-serine {ECO:0000269|PubMed:10391916}; CC KM=68.6 uM for L-threonine {ECO:0000269|PubMed:10391916}; CC KM=109 uM for L-cysteine {ECO:0000269|PubMed:10391916}; CC KM=80.7 uM for L-asparagine {ECO:0000269|PubMed:10391916}; CC KM=151 uM for L-glutamine {ECO:0000269|PubMed:10391916}; CC KM=96.7 uM for L-isoleucine {ECO:0000269|PubMed:10391916}; CC KM=124 uM for L-valine {ECO:0000269|PubMed:10391916}; CC KM=204 uM for L-methionine {ECO:0000269|PubMed:10391916}; CC KM=45 uM for L-phenylalanine {ECO:0000269|PubMed:10391916}; CC KM=35.9 uM for L-tyrosine {ECO:0000269|PubMed:10391916}; CC KM=57.6 uM for L-tryptophan {ECO:0000269|PubMed:10391916}; CC KM=29.3 uM for L-DOPA {ECO:0000269|PubMed:15200428}; CC KM=181 uM for L-histidine {ECO:0000269|PubMed:10391916}; CC pH dependence: CC Optimum pH is 6.25. {ECO:0000269|PubMed:10391916}; CC -!- SUBUNIT: Disulfide-linked heterodimer composed of the catalytic light CC chain subunit SLC7A8 and the heavy chain subunit SLC3A2 CC (PubMed:10391916). SLC3A2 acts as a chaperone for correct plasma CC membrane trafficking and stabilization of SLC7A8 and modulates the CC substrate affinity and specificity of SLC7A8. ICAM-1 associates with CC the heterodimer SLC3A2/SLC7A8; facilitates leucine uptake (By CC similarity). {ECO:0000250|UniProtKB:Q9UHI5, CC ECO:0000269|PubMed:10391916}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UHI5}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UHI5}. Basolateral CC cell membrane {ECO:0000269|PubMed:16027961}; Multi-pass membrane CC protein {ECO:0000250|UniProtKB:Q9UHI5}. Note=Localized to the plasma CC membrane when coexpressed with SLC3A2/4F2hc. Colocalized with CC SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal CC tubules and small intestine epithelia of the villi. CC {ECO:0000250|UniProtKB:Q9UHI5}. CC -!- TISSUE SPECIFICITY: Expression is seen in jejunum mucosa and the CC epithelial cells of the jejunum, ileum and colon, as well as in kidney, CC placenta, brain, testis and skeletal muscle. Expressed in retina, inner CC blood-retinal barrier of retina, retinal vascular endothelial cells. CC Also expressed in the intestinal epithelial cell line IEC-6 and in the CC retinal capillary endothelial cell line TR-iBRB2. CC {ECO:0000269|PubMed:10391916, ECO:0000269|PubMed:15980244, CC ECO:0000269|PubMed:16027961}. 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}. 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; AB024400; BAA82517.1; -; mRNA. DR RefSeq; NP_445894.1; NM_053442.1. DR AlphaFoldDB; Q9WVR6; -. DR SMR; Q9WVR6; -. DR STRING; 10116.ENSRNOP00000019618; -. DR TCDB; 2.A.3.8.6; the amino acid-polyamine-organocation (apc) family. DR iPTMnet; Q9WVR6; -. DR PhosphoSitePlus; Q9WVR6; -. DR PaxDb; 10116-ENSRNOP00000019618; -. DR Ensembl; ENSRNOT00000019618.5; ENSRNOP00000019618.3; ENSRNOG00000014311.6. DR Ensembl; ENSRNOT00055020572; ENSRNOP00055016570; ENSRNOG00055012104. DR Ensembl; ENSRNOT00060044749; ENSRNOP00060037100; ENSRNOG00060025856. DR Ensembl; ENSRNOT00065054154; ENSRNOP00065044567; ENSRNOG00065031419. DR GeneID; 84551; -. DR KEGG; rno:84551; -. DR UCSC; RGD:619904; rat. DR AGR; RGD:619904; -. DR CTD; 23428; -. DR RGD; 619904; Slc7a8. DR eggNOG; KOG1287; Eukaryota. DR GeneTree; ENSGT00940000158278; -. DR InParanoid; Q9WVR6; -. DR OMA; WVSNAAL; -. DR OrthoDB; 1103451at2759; -. DR PhylomeDB; Q9WVR6; -. DR TreeFam; TF313355; -. DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane. DR SABIO-RK; Q9WVR6; -. DR PRO; PR:Q9WVR6; -. DR Proteomes; UP000002494; Chromosome 15. DR Bgee; ENSRNOG00000014311; Expressed in ovary and 19 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD. DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD. DR GO; GO:0031528; C:microvillus membrane; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0015297; F:antiporter activity; ISO:RGD. DR GO; GO:0015187; F:glycine transmembrane transporter activity; ISO:RGD. DR GO; GO:0015180; F:L-alanine 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; ISO:RGD. DR GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; ISO:RGD. DR GO; GO:0015101; F:organic cation transmembrane transporter activity; ISO:RGD. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD. DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0019534; F:toxin transmembrane transporter activity; ISO:RGD. DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:RGD. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central. DR GO; GO:0006865; P:amino acid transport; ISO:RGD. DR GO; GO:0015816; P:glycine transport; ISO:RGD. DR GO; GO:1904273; P:L-alanine import across plasma membrane; ISO:RGD. DR GO; GO:0015807; P:L-amino acid transport; ISO:RGD. DR GO; GO:1903801; P:L-leucine import across plasma membrane; ISO:RGD. DR GO; GO:0098713; P:leucine import across plasma membrane; ISO:RGD. DR GO; GO:0015820; P:leucine transport; ISO:RGD. DR GO; GO:0015804; P:neutral amino acid transport; ISS:UniProtKB. DR GO; GO:0035524; P:proline transmembrane transport; ISO:RGD. DR GO; GO:0070327; P:thyroid hormone transport; ISS:UniProtKB. DR GO; GO:0015827; P:tryptophan transport; ISO:RGD. DR GO; GO:0015829; P:valine 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:SF113; LARGE NEUTRAL AMINO ACIDS TRANSPORTER SMALL SUBUNIT 2; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. DR Genevisible; Q9WVR6; RN. PE 1: Evidence at protein level; KW Amino-acid transport; Antiport; Cell membrane; Disulfide bond; Membrane; KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..533 FT /note="Large neutral amino acids transporter small subunit FT 2" FT /id="PRO_0000054275" FT TOPO_DOM 1..45 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 46..66 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 67..74 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 75..96 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 97..117 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 118..150 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 151..158 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 159..179 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 180..182 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 183..211 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 212..231 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 232..253 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 254..266 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 267..288 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 289..313 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 314..339 FT /note="Helical; Name=8" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 340..365 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 366..383 FT /note="Helical; Name=9" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 384..387 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 388..409 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 410..424 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 425..447 FT /note="Helical; Name=11" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TRANSMEM 448..467 FT /note="Helical; Name=12" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT TOPO_DOM 468..533 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 500..533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 54 FT /ligand="L-leucine" FT /ligand_id="ChEBI:CHEBI:57427" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT BINDING 135 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT BINDING 247 FT /ligand="L-leucine" FT /ligand_id="ChEBI:CHEBI:57427" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT BINDING 396 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT SITE 135 FT /note="Important for substrate specificity" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT SITE 247 FT /note="Important for substrate specificity" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QXW9" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 29 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 529 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT DISULFID 155 FT /note="Interchain (with C-103 in SLC3A2)" FT /evidence="ECO:0000250|UniProtKB:Q9UHI5" SQ SEQUENCE 533 AA; 58190 MW; 99479DB60DA69DF0 CRC64; MEKGTRQRNN TAKNHPDRGS DTSPEAEASS GGGGVALKKE IGLVSACGII VGNIIGSGIF VSPKGVLENA GSVGLALIVW IVTGVITAVG ALCYAELGVT IPKSGGDYSY VKDIFGGLAG FLRLWIAVLV IYPTNQAVIA LTFSNYVLQP LFPTCFPPES GLRLLAAICL LLLTWVNCSS VRWATRVQDI FTAGKLLALA LIIIMGVVQI CKGEFFWLEP KNAFENFQEP DIGLVALAFL QGSFAYGGWN FLNYVTEELV DPYKNLPRAI FISIPLVTFV YVFANIAYVT AMSPQELLAS NAVAVTFGEK LLGVMAWIMP ISVALSTFGG VNGSLFTSSR LFFAGAREGH LPSVLAMIHV KRCTPIPALL FTCLSTLLML VTSDMYTLIN YVGFINYLFY GVTVAGQIVL RWKKPDIPRP IKISLLFPII YLLFWAFLLI FSLWSEPVVC GIGLAIMLTG VPVYFLGVYW QHKPKCFNDF IESLTLVSQK MCVVVYPQEG DSGTEETIDD VEEQHKPIFQ PTPVKDPDSE EQP //