BAT1_HUMAN
ID BAT1_HUMAN Reviewed; 487 AA.
AC P82251; B2R9A6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=b(0,+)-type amino acid transporter 1;
DE Short=b(0,+)AT1;
DE AltName: Full=Glycoprotein-associated amino acid transporter b0,+AT1;
DE AltName: Full=Solute carrier family 7 member 9;
GN Name=SLC7A9; Synonyms=BAT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CSNU ARG-105; MET-170; THR-182;
RP ARG-195 AND ARG-259, CHARACTERIZATION OF VARIANT CSNU MET-170, FUNCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10471498; DOI=10.1038/12652;
RA Feliubadalo L., Font M., Purroy J., Rousaud F., Estivill X., Nunes V.,
RA Golomb E., Centola M., Aksentijevich I., Kreiss Y., Goldman B., Pras M.,
RA Kastner D.L., Pras E., Gasparini P., Bisceglia L., Beccia E., Gallucci M.,
RA De Sanctis L., Ponzone A., Rizzoni G.F., Zelante L., Bassi M.T.,
RA George A.L. Jr., Manzoni M., De Grandi A., Riboni M., Endsley J.K.,
RA Ballabio A., Borsani G., Reig N., Fernandez E., Estevez R., Pineda M.,
RA Torrents D., Camps M., Lloberas J., Zorzano A., Palacin M.;
RT "Non-type I cystinuria caused by mutations in SLC7A9, encoding a subunit
RT (b0,+AT) of rBAT.";
RL Nat. Genet. 23:52-57(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=10588648; DOI=10.1091/mbc.10.12.4135;
RA Pfeiffer R., Loffing J., Rossier G., Bauch C., Meier C., Eggermann T.,
RA Loffing-Cueni D., Kuehn L.C., Verrey F.;
RT "Luminal heterodimeric amino acid transporter defective in cystinuria.";
RL Mol. Biol. Cell 10:4135-4147(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=11318953; DOI=10.1046/j.1523-1755.2001.0590051821.x;
RA Mizoguchi K., Cha S.H., Chairoungdua A., Kim J.Y., Shigeta Y., Matsuo H.,
RA Fukushima J., Awa Y., Akakura K., Goya T., Ito H., Endou H., Kanai Y.;
RT "Human cystinuria-related transporter: localization and functional
RT characterization.";
RL Kidney Int. 59:1821-1833(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CSNU THR-44; LEU-261 AND
RP THR-354, AND VARIANT MET-223.
RX PubMed=12371955; DOI=10.1046/j.1523-1755.2002.00602.x;
RA Leclerc D., Boutros M., Suh D., Wu Q., Palacin M., Ellis J.R., Goodyer P.,
RA Rozen R.;
RT "SLC7A9 mutations in all three cystinuria subtypes.";
RL Kidney Int. 62:1550-1559(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
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).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12167606; DOI=10.1152/ajprenal.00071.2002;
RA Fernandez E., Carrascal M., Rousaud F., Abian J., Zorzano A., Palacin M.,
RA Chillaron J.;
RT "rBAT-b(0,+)AT heterodimer is the main apical reabsorption system for
RT cystine in the kidney.";
RL Am. J. Physiol. 283:F540-F548(2002).
RN [8]
RP VARIANTS CSNU ARG-10 DEL; LEU-52; ARG-63; LEU-69; VAL-70; ARG-105; MET-123;
RP THR-126; ALA-158 INS; MET-170; THR-182; PHE-187; ILE-193 INS; ARG-195;
RP ARG-230; THR-241; GLU-244 DEL; ARG-259; TRP-333; THR-354; ARG-379 AND
RP THR-382, AND CHARACTERIZATION OF VARIANTS CSNU VAL-70; ARG-105; MET-170;
RP THR-182; TRP-333 AND THR-354.
RX PubMed=11157794; DOI=10.1093/hmg/10.4.305;
RA Font M., Feliubadalo L., Estivill X., Nunes V., Golomb E., Kreiss Y.,
RA Pras E., Bisceglia L., d'Adamo A.P., Zelante L., Gasparini P., Bassi M.T.,
RA George A.L. Jr., Manzoni M., Riboni M., Ballabio A., Borsani G., Reig N.,
RA Fernandez E., Zorzano A., Bertran J., Palacin M.;
RT "Functional analysis of mutations in SLC7A9, and genotype-phenotype
RT correlation in non-type I cystinuria.";
RL Hum. Mol. Genet. 10:305-316(2001).
RN [9]
RP VARIANTS CSNU ARG-105; VAL-224 AND VAL-331.
RX PubMed=12234283; DOI=10.1111/j.1523-1755.2002.kid552.x;
RA Botzenhart E., Vester U., Schmidt C., Hesse A., Halber M., Wagner C.,
RA Lang F., Hoyer P., Zerres K., Eggermann T.;
RT "Cystinuria in children: distribution and frequencies of mutations in the
RT SLC3A1 and SLC7A9 genes.";
RL Kidney Int. 62:1136-1142(2002).
RN [10]
RP VARIANTS CSNU THR-182; LEU-261 AND MET-330.
RX PubMed=12820697; DOI=10.1089/109065703321560886;
RA Harnevik L., Fjellstedt E., Molbaek A., Denneberg T., Soderkvist P.;
RT "Mutation analysis of SLC7A9 in cystinuria patients in Sweden.";
RL Genet. Test. 7:13-20(2003).
RN [11]
RP VARIANTS CSNU ARG-105; MET-123; ARG-319 AND TRP-333.
RX PubMed=16138908; DOI=10.1111/j.1529-8817.2005.00185.x;
RA Skopkova Z., Hrabincova E., Stastna S., Kozak L., Adam T.;
RT "Molecular genetic analysis of SLC3A1 and SLC7A9 genes in Czech and Slovak
RT cystinuric patients.";
RL Ann. Hum. Genet. 69:501-507(2005).
RN [12]
RP VARIANTS CSNU MET-62; MET-188; CYS-232; PHE-283 AND VAL-316.
RX PubMed=15635077; DOI=10.1136/jmg.2004.022244;
RA Font-Llitjos M., Jimenez-Vidal M., Bisceglia L., Di Perna M.,
RA de Sanctis L., Rousaud F., Zelante L., Palacin M., Nunes V.;
RT "New insights into cystinuria: 40 new mutations, genotype-phenotype
RT correlation, and digenic inheritance causing partial phenotype.";
RL J. Med. Genet. 42:58-68(2005).
RN [13]
RP VARIANTS CSNU ARG-195; ASP-227; GLN-333 AND LEU-482, CHARACTERIZATION OF
RP VARIANTS CSNU ARG-195; ASP-227; GLN-333 AND LEU-482, VARIANTS ALA-142 AND
RP MET-223, CHARACTERIZATION OF VARIANTS ALA-142 AND MET-223, FUNCTION,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-482.
RX PubMed=16609684; DOI=10.1038/sj.ki.5000241;
RA Shigeta Y., Kanai Y., Chairoungdua A., Ahmed N., Sakamoto S., Matsuo H.,
RA Kim D.K., Fujimura M., Anzai N., Mizoguchi K., Ueda T., Akakura K.,
RA Ichikawa T., Ito H., Endou H.;
RT "A novel missense mutation of SLC7A9 frequent in Japanese cystinuria cases
RT affecting the C-terminus of the transporter.";
RL Kidney Int. 69:1198-1206(2006).
RN [14]
RP VARIANTS CSNU MET-40; PHE-51; HIS-99; ARG-114; LEU-120; PHE-286; GLU-324;
RP GLU-401 AND PRO-426.
RX PubMed=18752446; DOI=10.1089/gte.2007.0113;
RA Di Perna M., Louizou E., Fischetti L., Dedoussis G.V., Stanziale P.,
RA Michelakakis H., Zelante L., Pras E., Bisceglia L.;
RT "Twenty-four novel mutations identified in a cohort of 85 patients by
RT direct sequencing of the SLC3A1 and SLC7A9 cystinuria genes.";
RL Genet. Test. 12:351-355(2008).
RN [15]
RP VARIANTS CSNU ARG-105; GLU-105; MET-123; THR-182 AND LYS-250.
RX PubMed=19782624; DOI=10.1016/j.ymgme.2009.09.001;
RA Bisceglia L., Fischetti L., Bonis P.D., Palumbo O., Augello B.,
RA Stanziale P., Carella M., Zelante L.;
RT "Large rearrangements detected by MLPA, point mutations, and survey of the
RT frequency of mutations within the SLC3A1 and SLC7A9 genes in a cohort of
RT 172 cystinuric Italian patients.";
RL Mol. Genet. Metab. 99:42-52(2010).
CC -!- FUNCTION: Involved in the high-affinity, sodium-independent transport
CC of cystine and neutral and dibasic amino acids (system b(0,+)-like
CC activity). Thought to be responsible for the high-affinity reabsorption
CC of cystine in the kidney tubule. {ECO:0000269|PubMed:10471498,
CC ECO:0000269|PubMed:10588648, ECO:0000269|PubMed:16609684}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A1. Interacts with CAV1. {ECO:0000250|UniProtKB:P82252}.
CC -!- INTERACTION:
CC P82251; O43889-2: CREB3; NbExp=3; IntAct=EBI-3936589, EBI-625022;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12167606, ECO:0000269|PubMed:16609684}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16609684,
CC ECO:0000305|PubMed:12167606}.
CC -!- TISSUE SPECIFICITY: Expressed in the brush border membrane in the
CC kidney (at protein level). Kidney, small intestine, liver and placenta.
CC {ECO:0000269|PubMed:10471498, ECO:0000269|PubMed:12167606}.
CC -!- DISEASE: Cystinuria (CSNU) [MIM:220100]: An autosomal disorder
CC characterized by impaired epithelial cell transport of cystine and
CC dibasic amino acids (lysine, ornithine, and arginine) in the proximal
CC renal tubule and gastrointestinal tract. The impaired renal
CC reabsorption of cystine and its low solubility causes the formation of
CC calculi in the urinary tract, resulting in obstructive uropathy,
CC pyelonephritis, and, rarely, renal failure.
CC {ECO:0000269|PubMed:10471498, ECO:0000269|PubMed:11157794,
CC ECO:0000269|PubMed:12234283, ECO:0000269|PubMed:12371955,
CC ECO:0000269|PubMed:12820697, ECO:0000269|PubMed:15635077,
CC ECO:0000269|PubMed:16138908, ECO:0000269|PubMed:16609684,
CC ECO:0000269|PubMed:18752446, ECO:0000269|PubMed:19782624}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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; AF141289; AAD55898.1; -; mRNA.
DR EMBL; AJ249199; CAB54003.1; -; mRNA.
DR EMBL; AB033548; BAB16840.1; -; mRNA.
DR EMBL; AF421181; AAN40878.1; -; Genomic_DNA.
DR EMBL; AF421170; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421171; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421172; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421173; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421174; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421175; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421176; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421177; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421178; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421179; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AF421180; AAN40878.1; JOINED; Genomic_DNA.
DR EMBL; AK313708; BAG36453.1; -; mRNA.
DR EMBL; BC017962; AAH17962.1; -; mRNA.
DR CCDS; CCDS12425.1; -.
DR RefSeq; NP_001119807.1; NM_001126335.1.
DR RefSeq; NP_001229965.1; NM_001243036.1.
DR RefSeq; NP_055085.1; NM_014270.4.
DR RefSeq; XP_011524704.1; XM_011526402.2.
DR PDB; 6LI9; EM; 2.30 A; B/D=2-487.
DR PDB; 6LID; EM; 2.70 A; B/D=2-487.
DR PDB; 6YUP; EM; 2.90 A; D/E=1-487.
DR PDB; 6YV1; EM; 3.40 A; A=1-487.
DR PDBsum; 6LI9; -.
DR PDBsum; 6LID; -.
DR PDBsum; 6YUP; -.
DR PDBsum; 6YV1; -.
DR AlphaFoldDB; P82251; -.
DR SMR; P82251; -.
DR BioGRID; 116309; 4.
DR IntAct; P82251; 4.
DR MINT; P82251; -.
DR STRING; 9606.ENSP00000023064; -.
DR DrugBank; DB00138; Cystine.
DR DrugBank; DB00130; L-Glutamine.
DR TCDB; 2.A.3.8.19; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P82251; -.
DR PhosphoSitePlus; P82251; -.
DR SwissPalm; P82251; -.
DR BioMuta; SLC7A9; -.
DR DMDM; 12585187; -.
DR CPTAC; CPTAC-1190; -.
DR CPTAC; CPTAC-1191; -.
DR MassIVE; P82251; -.
DR PaxDb; P82251; -.
DR PeptideAtlas; P82251; -.
DR PRIDE; P82251; -.
DR ProteomicsDB; 57704; -.
DR Antibodypedia; 28931; 92 antibodies from 18 providers.
DR DNASU; 11136; -.
DR Ensembl; ENST00000023064.9; ENSP00000023064.3; ENSG00000021488.13.
DR Ensembl; ENST00000587772.1; ENSP00000468439.1; ENSG00000021488.13.
DR Ensembl; ENST00000590341.5; ENSP00000464822.1; ENSG00000021488.13.
DR GeneID; 11136; -.
DR KEGG; hsa:11136; -.
DR MANE-Select; ENST00000023064.9; ENSP00000023064.3; NM_014270.5; NP_055085.1.
DR UCSC; uc002ntu.6; human.
DR CTD; 11136; -.
DR DisGeNET; 11136; -.
DR GeneCards; SLC7A9; -.
DR HGNC; HGNC:11067; SLC7A9.
DR HPA; ENSG00000021488; Group enriched (intestine, kidney).
DR MalaCards; SLC7A9; -.
DR MIM; 220100; phenotype.
DR MIM; 604144; gene.
DR neXtProt; NX_P82251; -.
DR OpenTargets; ENSG00000021488; -.
DR Orphanet; 93613; Cystinuria type B.
DR PharmGKB; PA35927; -.
DR VEuPathDB; HostDB:ENSG00000021488; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000156370; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; P82251; -.
DR OMA; HKAFGIH; -.
DR OrthoDB; 621852at2759; -.
DR PhylomeDB; P82251; -.
DR PathwayCommons; P82251; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-5619113; Defective SLC3A1 causes cystinuria (CSNU).
DR Reactome; R-HSA-5660883; Defective SLC7A9 causes cystinuria (CSNU).
DR SignaLink; P82251; -.
DR BioGRID-ORCS; 11136; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; SLC7A9; human.
DR GenomeRNAi; 11136; -.
DR Pharos; P82251; Tbio.
DR PRO; PR:P82251; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P82251; protein.
DR Bgee; ENSG00000021488; Expressed in ileal mucosa and 106 other tissues.
DR ExpressionAtlas; P82251; baseline and differential.
DR Genevisible; P82251; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
DR GO; GO:0015811; P:L-cystine transport; IMP:UniProtKB.
DR GO; GO:0015804; P:neutral amino acid transport; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell membrane; Cystinuria;
KW Disease variant; Disulfide bond; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..487
FT /note="b(0,+)-type amino acid transporter 1"
FT /id="PRO_0000054258"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82252"
FT VARIANT 10
FT /note="Missing (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_018997"
FT VARIANT 40
FT /note="V -> M (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072308"
FT VARIANT 44
FT /note="I -> T (in CSNU; type I; dbSNP:rs121908485)"
FT /evidence="ECO:0000269|PubMed:12371955"
FT /id="VAR_014363"
FT VARIANT 51
FT /note="S -> F (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072309"
FT VARIANT 52
FT /note="P -> L (in CSNU; dbSNP:rs1198613438)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_018998"
FT VARIANT 62
FT /note="V -> M (in CSNU; dbSNP:rs964489627)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072310"
FT VARIANT 63
FT /note="G -> R (in CSNU; dbSNP:rs1395997436)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_018999"
FT VARIANT 69
FT /note="W -> L (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019000"
FT VARIANT 70
FT /note="A -> V (in CSNU; mild loss of amino acid transport
FT activity; dbSNP:rs769448665)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019001"
FT VARIANT 99
FT /note="Y -> H (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072311"
FT VARIANT 105
FT /note="G -> E (in CSNU)"
FT /evidence="ECO:0000269|PubMed:19782624"
FT /id="VAR_072312"
FT VARIANT 105
FT /note="G -> R (in CSNU; type III; severe loss of amino acid
FT transport activity; dbSNP:rs121908480)"
FT /evidence="ECO:0000269|PubMed:10471498,
FT ECO:0000269|PubMed:11157794, ECO:0000269|PubMed:12234283,
FT ECO:0000269|PubMed:16138908, ECO:0000269|PubMed:19782624"
FT /id="VAR_010256"
FT VARIANT 114
FT /note="W -> R (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072313"
FT VARIANT 120
FT /note="I -> L (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072314"
FT VARIANT 123
FT /note="T -> M (in CSNU; dbSNP:rs79987078)"
FT /evidence="ECO:0000269|PubMed:11157794,
FT ECO:0000269|PubMed:16138908, ECO:0000269|PubMed:19782624"
FT /id="VAR_019002"
FT VARIANT 126
FT /note="A -> T (in CSNU; dbSNP:rs372306844)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019003"
FT VARIANT 142
FT /note="V -> A (no effect on amino acid transport activity;
FT dbSNP:rs12150889)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_048153"
FT VARIANT 158
FT /note="A -> AA (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019004"
FT VARIANT 170
FT /note="V -> M (in CSNU; type III; complete loss of amino
FT acid transport activity; dbSNP:rs121908479)"
FT /evidence="ECO:0000269|PubMed:10471498,
FT ECO:0000269|PubMed:11157794"
FT /id="VAR_010257"
FT VARIANT 182
FT /note="A -> T (in CSNU; type III; mild loss of amino acid
FT transport activity; dbSNP:rs79389353)"
FT /evidence="ECO:0000269|PubMed:10471498,
FT ECO:0000269|PubMed:11157794, ECO:0000269|PubMed:12820697,
FT ECO:0000269|PubMed:19782624"
FT /id="VAR_010258"
FT VARIANT 187
FT /note="I -> F (in CSNU; dbSNP:rs368441237)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019005"
FT VARIANT 188
FT /note="V -> M (in CSNU; dbSNP:rs531029519)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072315"
FT VARIANT 193
FT /note="I -> II (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019006"
FT VARIANT 195
FT /note="G -> R (in CSNU; type III; decreased amino acid
FT transport activity; dbSNP:rs121908482)"
FT /evidence="ECO:0000269|PubMed:10471498,
FT ECO:0000269|PubMed:11157794, ECO:0000269|PubMed:16609684"
FT /id="VAR_010259"
FT VARIANT 223
FT /note="L -> M (slightly decreased amino acid transport
FT activity; dbSNP:rs1007160)"
FT /evidence="ECO:0000269|PubMed:12371955,
FT ECO:0000269|PubMed:16609684"
FT /id="VAR_019007"
FT VARIANT 224
FT /note="A -> V (in CSNU; non-classic type I;
FT dbSNP:rs140873167)"
FT /evidence="ECO:0000269|PubMed:12234283"
FT /id="VAR_022603"
FT VARIANT 227
FT /note="N -> D (in CSNU; decreased amino acid transport
FT activity)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_072316"
FT VARIANT 230
FT /note="W -> R (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019008"
FT VARIANT 232
FT /note="Y -> C (in CSNU; dbSNP:rs121908487)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072317"
FT VARIANT 241
FT /note="I -> T (in CSNU; dbSNP:rs777371504)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019009"
FT VARIANT 244
FT /note="Missing (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019010"
FT VARIANT 250
FT /note="R -> K (in CSNU; dbSNP:rs766529640)"
FT /evidence="ECO:0000269|PubMed:19782624"
FT /id="VAR_072318"
FT VARIANT 259
FT /note="G -> R (in CSNU; type III; dbSNP:rs121908483)"
FT /evidence="ECO:0000269|PubMed:10471498,
FT ECO:0000269|PubMed:11157794"
FT /id="VAR_010260"
FT VARIANT 261
FT /note="P -> L (in CSNU; types I and III;
FT dbSNP:rs121908486)"
FT /evidence="ECO:0000269|PubMed:12371955,
FT ECO:0000269|PubMed:12820697"
FT /id="VAR_014364"
FT VARIANT 283
FT /note="L -> F (in CSNU; dbSNP:rs1357600282)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072319"
FT VARIANT 286
FT /note="S -> F (in CSNU; unknown pathological significance;
FT dbSNP:rs755135545)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072320"
FT VARIANT 316
FT /note="A -> V (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072321"
FT VARIANT 319
FT /note="G -> R (in CSNU)"
FT /evidence="ECO:0000269|PubMed:16138908"
FT /id="VAR_072322"
FT VARIANT 324
FT /note="A -> E (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072323"
FT VARIANT 330
FT /note="V -> M (in CSNU; type III; dbSNP:rs201618022)"
FT /evidence="ECO:0000269|PubMed:12820697"
FT /id="VAR_015885"
FT VARIANT 331
FT /note="A -> V (in CSNU; non-classic type I;
FT dbSNP:rs768466784)"
FT /evidence="ECO:0000269|PubMed:12234283"
FT /id="VAR_022604"
FT VARIANT 333
FT /note="R -> Q (in CSNU; decreased amino acid transport
FT activity; dbSNP:rs769576205)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_072324"
FT VARIANT 333
FT /note="R -> W (in CSNU; severe loss of amino acid transport
FT activity; dbSNP:rs121908484)"
FT /evidence="ECO:0000269|PubMed:11157794,
FT ECO:0000269|PubMed:16138908"
FT /id="VAR_019011"
FT VARIANT 354
FT /note="A -> T (in CSNU; type III; severe loss of amino acid
FT transport activity; dbSNP:rs939028046)"
FT /evidence="ECO:0000269|PubMed:11157794,
FT ECO:0000269|PubMed:12371955"
FT /id="VAR_014365"
FT VARIANT 379
FT /note="S -> R (in CSNU; dbSNP:rs142270619)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019012"
FT VARIANT 382
FT /note="A -> T (in CSNU; dbSNP:rs774878350)"
FT /evidence="ECO:0000269|PubMed:11157794"
FT /id="VAR_019013"
FT VARIANT 401
FT /note="K -> E (in CSNU; unknown pathological significance;
FT dbSNP:rs760264924)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072325"
FT VARIANT 426
FT /note="L -> P (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18752446"
FT /id="VAR_072326"
FT VARIANT 482
FT /note="P -> L (in CSNU; decreased amino acid transport
FT activity; no effect on localization to the apical membrane;
FT dbSNP:rs146815072)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_072327"
FT MUTAGEN 482
FT /note="P->A,G,S,V: No effect on amino acid transport
FT activity."
FT /evidence="ECO:0000269|PubMed:16609684"
FT MUTAGEN 482
FT /note="P->F,I,M,W: Decreased amino acid transport
FT activity."
FT /evidence="ECO:0000269|PubMed:16609684"
FT CONFLICT 52
FT /note="P -> S (in Ref. 2; CAB54003)"
FT /evidence="ECO:0000305"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 62..89
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:6YUP"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 177..200
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:6LID"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6LID"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 251..274
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 326..333
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 374..395
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 412..431
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 436..454
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:6LID"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 463..477
FT /evidence="ECO:0007829|PDB:6LI9"
SQ SEQUENCE 487 AA; 53481 MW; EF2C30DDE15594F1 CRC64;
MGDTGLRKRR EDEKSIQSQE PKTTSLQKEL GLISGISIIV GTIIGSGIFV SPKSVLSNTE
AVGPCLIIWA ACGVLATLGA LCFAELGTMI TKSGGEYPYL MEAYGPIPAY LFSWASLIVI
KPTSFAIICL SFSEYVCAPF YVGCKPPQIV VKCLAAAAIL FISTVNSLSV RLGSYVQNIF
TAAKLVIVAI IIISGLVLLA QGNTKNFDNS FEGAQLSVGA ISLAFYNGLW AYDGWNQLNY
ITEELRNPYR NLPLAIIIGI PLVTACYILM NVSYFTVMTA TELLQSQAVA VTFGDRVLYP
ASWIVPLFVA FSTIGAANGT CFTAGRLIYV AGREGHMLKV LSYISVRRLT PAPAIIFYGI
IATIYIIPGD INSLVNYFSF AAWLFYGLTI LGLIVMRFTR KELERPIKVP VVIPVLMTLI
SVFLVLAPII SKPTWEYLYC VLFILSGLLF YFLFVHYKFG WAQKISKPIT MHLQMLMEVV
PPEEDPE
