ID S7A13_RAT Reviewed; 479 AA. AC Q5RKI7; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 24-JAN-2024, entry version 115. DE RecName: Full=Solute carrier family 7 member 13; DE AltName: Full=Sodium-independent aspartate/glutamate transporter 1; GN Name=Slc7a13; 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 [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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). CC -!- FUNCTION: Associates with SLC3A1/rBAT to form a functional CC heterodimeric complex that transports anionic and neutral amino acids CC across the apical plasma membrane of renal epithelium. Preferentially CC mediates exchange transport, but can also operate via facilitated CC diffusion. May act as a major transporter for L-cystine in late CC proximal tubules, ensuring its reabsorption from the luminal fluid in CC exchange for cytosolic L-glutamate or L-aspartate. CC {ECO:0000250|UniProtKB:Q91WN3}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-cystine(out) = L-aspartate(out) + L- CC cystine(in); Xref=Rhea:RHEA:76299, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:35491; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cystine(out) = L-cystine(in); Xref=Rhea:RHEA:76303, CC ChEBI:CHEBI:35491; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-glutamate(out) = L-aspartate(out) + L- CC glutamate(in); Xref=Rhea:RHEA:76307, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-glutamine(out) = L-aspartate(out) + L- CC glutamine(in); Xref=Rhea:RHEA:76311, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-methionine(out) = L-aspartate(out) + L- CC methionine(in); Xref=Rhea:RHEA:76315, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-leucine(out) = L-aspartate(out) + L- CC leucine(in); Xref=Rhea:RHEA:76319, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:57427; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-valine(out) = L-aspartate(out) + L- CC valine(in); Xref=Rhea:RHEA:76323, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:57762; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-phenylalanine(out) = L-aspartate(out) + L- CC phenylalanine(in); Xref=Rhea:RHEA:76327, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-tyrosine(out) = L-aspartate(out) + L- CC tyrosine(in); Xref=Rhea:RHEA:76331, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:58315; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + L-tryptophan(out) = L-aspartate(out) + L- CC tryptophan(in); Xref=Rhea:RHEA:76335, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:57912; Evidence={ECO:0000250|UniProtKB:Q91WN3}; CC -!- SUBUNIT: Disulfide-linked heterodimer composed of the catalytic light CC subunit SLC7A13 and the heavy subunit SLC3A1. CC {ECO:0000250|UniProtKB:Q91WN3}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000250|UniProtKB:Q91WN3}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) CC superfamily. {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; BC085796; AAH85796.1; -; mRNA. DR RefSeq; NP_001012100.1; NM_001012100.1. DR AlphaFoldDB; Q5RKI7; -. DR SMR; Q5RKI7; -. DR STRING; 10116.ENSRNOP00000032751; -. DR iPTMnet; Q5RKI7; -. DR PhosphoSitePlus; Q5RKI7; -. DR PaxDb; 10116-ENSRNOP00000032751; -. DR Ensembl; ENSRNOT00000035685.7; ENSRNOP00000032751.4; ENSRNOG00000024903.7. DR GeneID; 313089; -. DR KEGG; rno:313089; -. DR UCSC; RGD:1311633; rat. DR AGR; RGD:1311633; -. DR CTD; 157724; -. DR RGD; 1311633; Slc7a13. DR eggNOG; KOG1287; Eukaryota. DR GeneTree; ENSGT00940000162798; -. DR HOGENOM; CLU_007946_3_0_1; -. DR InParanoid; Q5RKI7; -. DR OrthoDB; 1103451at2759; -. DR PhylomeDB; Q5RKI7; -. DR TreeFam; TF313355; -. DR PRO; PR:Q5RKI7; -. DR Proteomes; UP000002494; Chromosome 5. DR Bgee; ENSRNOG00000024903; Expressed in kidney and 9 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central. DR GO; GO:0015810; P:aspartate transmembrane transport; ISO:RGD. DR GO; GO:0015811; P:L-cystine transport; ISO:RGD. DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISO:RGD. DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1. DR InterPro; IPR002293; AA/rel_permease1. DR PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1. DR PANTHER; PTHR11785:SF238; SOLUTE CARRIER FAMILY 7 MEMBER 13; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. DR Genevisible; Q5RKI7; RN. PE 2: Evidence at transcript level; KW Amino-acid transport; Antiport; Cell membrane; Disulfide bond; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..479 FT /note="Solute carrier family 7 member 13" FT /id="PRO_0000330727" FT TOPO_DOM 1..14 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 15..35 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 36..47 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 48..68 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 69..89 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 90..110 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 111..129 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 130..150 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 151..165 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 166..186 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 187..208 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 209..229 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 230..242 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 243..263 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 264..289 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical; Name=8" FT /evidence="ECO:0000255" FT TOPO_DOM 311..338 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 339..359 FT /note="Helical; Name=9" FT /evidence="ECO:0000255" FT TOPO_DOM 360 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 361..381 FT /note="Helical; Name=10" FT /evidence="ECO:0000255" FT TOPO_DOM 382..396 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 397..417 FT /note="Helical; Name=11" FT /evidence="ECO:0000255" FT TOPO_DOM 418..423 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 424..444 FT /note="Helical; Name=12" FT /evidence="ECO:0000255" FT TOPO_DOM 445..479 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" SQ SEQUENCE 479 AA; 53551 MW; 9EDA418E533B2B96 CRC64; MAMDIEKKIY LKRQLGYFWG TNFLIINIIG AGIFVSPKGV LQYSSMNVGV SLCVWVFCAV LSMTSTLCAA EIGITFPYTV AHYYFLKRCF GPFVAFLRLW TSLFTGPGVL ASQALLLAEY GIQPFYPSCS APAVPKKCLA LAMLWIVGIL NSRGVKELSW LQTVSMVLKM GILSFISLSG LFLLVTGRKE NVRRLQNAFD AEFPEVSRLI EAIFQGYFAF SGGGSFTYVA GELKEPSKTI PRCIFTALPL VTVVYLLANL SYLTVLSPQE LLSSDAVALT WTDRVIPQLT WSVPFAISAS LFSNLVTSVF ETSRTSYIAS RNGQLPLLCS TLNVHSSPFI AVLLDVSMGS IAIVLTNLIE LINYLFFVFS IWTVLSVIGI LKLRYQEPNL HRPYKVFSPF LFITAAISLS MVLIPLIKSP KMQYIYVFLF FLGGLLFYVP LIHFKLKLIW FQKLTCYLQL LFNICIPDVS DEHVAEEES //