GENTAUR Molecular Products.

 SLC31_HUMAN             Reviewed;         685 AA.
 Q07837; A8K0S1; O00658; Q15295; Q4J6B4; Q4J6B5; Q4J6B6; Q4J6B7;
 Q4J6B8; Q4J6B9; Q52M92; Q52M94;
 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
 10-MAY-2005, sequence version 2.
 07-NOV-2018, entry version 191.
 RecName: Full=Neutral and basic amino acid transport protein rBAT;
          Short=NBAT;
 AltName: Full=D2h;
 AltName: Full=Solute carrier family 3 member 1;
 AltName: Full=b(0,+)-type amino acid transport protein;
 Name=SLC3A1; Synonyms=RBAT;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
 AND VARIANT ILE-618.
 TISSUE=Kidney;
 PubMed=8486766; DOI=10.1172/JCI116415;
 Lee W.-S., Wells R.G., Sabbag R.V., Mohandas T.K., Hediger M.A.;
 "Cloning and chromosomal localization of a human kidney cDNA involved
 in cystine, dibasic, and neutral amino acid transport.";
 J. Clin. Invest. 91:1959-1963(1993).
 [2]
 SEQUENCE REVISION TO C-TERMINUS.
 Lee W.-S., Wells R.G., Sabbag R.V., Mohandas T.K., Hediger M.A.;
 Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
 [3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE
 SPECIFICITY.
 TISSUE=Kidney cortex;
 PubMed=7686906;
 Bertran J., Werner A., Chillaron J., Nunes V., Biber J., Testar X.,
 Zorzano A., Estivill X., Murer H., Palacin M.;
 "Expression cloning of a human renal cDNA that induces high affinity
 transport of L-cystine shared with dibasic amino acids in Xenopus
 oocytes.";
 J. Biol. Chem. 268:14842-14849(1993).
 [4]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ILE-618, AND FUNCTION.
 TISSUE=Kidney cortex;
 PubMed=8663184; DOI=10.1074/jbc.271.28.16758;
 Miyamoto K., Segawa H., Tatsumi S., Katai K., Yamamoto H.,
 Taketani Y., Haga H., Morita K., Takeda E.;
 "Effects of truncation of the COOH-terminal region of a Na+-
 independent neutral and basic amino acid transporter on amino acid
 transport in Xenopus oocytes.";
 J. Biol. Chem. 271:16758-16763(1996).
 [5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-618, AND VARIANTS CSNU
 TRP-452; HIS-461 AND THR-467.
 PubMed=9186880; DOI=10.1038/ki.1997.258;
 Endsley J.K., Phillips J.A. III, Hruska K.A., Denneberg T.,
 Carlson J., George A.L. Jr.;
 "Genomic organization of a human cystine transporter gene (SLC3A1) and
 identification of novel mutations causing cystinuria.";
 Kidney Int. 51:1893-1899(1997).
 [6]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND VARIANT ILE-618.
 TISSUE=Kidney;
 PubMed=11318953; DOI=10.1046/j.1523-1755.2001.0590051821.x;
 Mizoguchi K., Cha S.H., Chairoungdua A., Kim J.Y., Shigeta Y.,
 Matsuo H., Fukushima J., Awa Y., Akakura K., Goya T., Ito H.,
 Endou H., Kanai Y.;
 "Human cystinuria-related transporter: localization and functional
 characterization.";
 Kidney Int. 59:1821-1833(2001).
 [7]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C; D; E; F AND G), ALTERNATIVE
 SPLICING, AND VARIANT ILE-618.
 PubMed=15913950; DOI=10.1016/j.ygeno.2005.04.001;
 Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K.,
 Hershkovitz E.;
 "The 2p21 deletion syndrome: characterization of the transcription
 content.";
 Genomics 86:195-211(2005).
 [8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
 TISSUE=Amygdala;
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [9]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
 TISSUE=Kidney;
 Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
 Tanaka A., Yokoyama S.;
 Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
 [10]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15815621; DOI=10.1038/nature03466;
 Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
 Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
 Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
 Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
 Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
 Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
 Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
 Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
 Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
 Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
 McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
 Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
 Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
 Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
 Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
 Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
 Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
 Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
 Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
 Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
 McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
 Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
 Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
 Waterston R.H., Wilson R.K.;
 "Generation and annotation of the DNA sequences of human chromosomes 2
 and 4.";
 Nature 434:724-731(2005).
 [11]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT
 ILE-618.
 TISSUE=Brain, and Kidney;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [12]
 SUBUNIT.
 PubMed=10588648; DOI=10.1091/mbc.10.12.4135;
 Pfeiffer R., Loffing J., Rossier G., Bauch C., Meier C., Eggermann T.,
 Loffing-Cueni D., Kuehn L.C., Verrey F.;
 "Luminal heterodimeric amino acid transporter defective in
 cystinuria.";
 Mol. Biol. Cell 10:4135-4147(1999).
 [13]
 DISEASE.
 PubMed=7568194; DOI=10.1073/pnas.92.21.9667;
 Calonge M.J., Volpini V., Bisceglia L., Rousaud F., de Sanctis L.,
 Beccia E., Zelante L., Testar X., Zorzano A., Estivill X.,
 Gasparini P., Nunes V., Palacin M.;
 "Genetic heterogeneity in cystinuria: the SLC3A1 gene is linked to
 type I but not to type III cystinuria.";
 Proc. Natl. Acad. Sci. U.S.A. 92:9667-9671(1995).
 [14]
 SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
 PubMed=12167606;
 Fernandez E., Carrascal M., Rousaud F., Abian J., Zorzano A.,
 Palacin M., Chillaron J.;
 "rBAT-b(0,+)AT heterodimer is the main apical reabsorption system for
 cystine in the kidney.";
 Am. J. Physiol. 283:F540-F548(2002).
 [15]
 INVOLVEMENT IN HCS.
 PubMed=16385448; DOI=10.1086/498852;
 Jaeken J., Martens K., Francois I., Eyskens F., Lecointre C.,
 Derua R., Meulemans S., Slootstra J.W., Waelkens E., de Zegher F.,
 Creemers J.W.M., Matthijs G.;
 "Deletion of PREPL, a gene encoding a putative serine oligopeptidase,
 in patients with hypotonia-cystinuria syndrome.";
 Am. J. Hum. Genet. 78:38-51(2006).
 [16]
 VARIANTS CSNU GLN-181; LYS-467; THR-467; THR-615; ARG-652 AND PRO-678,
 AND CHARACTERIZATION OF VARIANT THR-467.
 PubMed=8054986; DOI=10.1038/ng0494-420;
 Calonge M.J., Gasparini P., Chillaron J., Chillon M., Gallucci M.,
 Rousaud F., Zelante L., Testar X., Dallapiccola B., Di Silverio F.,
 Barcelo P., Estivill X., Zorzano A., Nunes V., Palacin M.;
 "Cystinuria caused by mutations in rBAT, a gene involved in the
 transport of cystine.";
 Nat. Genet. 6:420-425(1994).
 [17]
 VARIANT CSNU GLN-128.
 PubMed=7539209;
 Pras E., Raben N., Golomb E., Arber N., Aksentijevich I.,
 Schapiro J.M., Harel D., Katz G., Liberman U., Pras M., Kastner D.L.;
 "Mutations in the SLC3A1 transporter gene in cystinuria.";
 Am. J. Hum. Genet. 56:1297-1303(1995).
 [18]
 VARIANTS CSNU TRP-365; HIS-582 AND SER-648, AND VARIANT ILE-618.
 PubMed=7573036;
 Gasparini P., Calonge M.J., Bisceglia L., Purroy J., Dianzani I.,
 Notarangelo A., Rousaud F., Gallucci M., Testar X., Ponzone A.,
 Estivill X., Zorzano A., Palacin M., Nunes V., Zelante L.;
 "Molecular genetics of cystinuria: identification of four new
 mutations and seven polymorphisms, and evidence for genetic
 heterogeneity.";
 Am. J. Hum. Genet. 57:781-788(1995).
 [19]
 VARIANTS CSNU LYS-268 AND ALA-341, AND CHARACTERIZATION OF VARIANTS
 CSNU LYS-268 AND ALA-341.
 PubMed=7575432; DOI=10.1042/bj3100951;
 Miyamoto K., Katai K., Tatsumi S., Sone K., Segawa H., Yamamoto H.,
 Taketani Y., Takada K., Morita K., Kanayama H., Kagawa S., Takeda E.;
 "Mutations of the basic amino acid transporter gene associated with
 cystinuria.";
 Biochem. J. 310:951-955(1995).
 [20]
 VARIANT CSNU SER-122.
 PubMed=10738006;
 DOI=10.1002/(SICI)1098-1004(200004)15:4<390::AID-HUMU33>3.0.CO;2-K;
 Gitomer W.L., Reed B.Y., Pak C.Y.C.;
 "Identification of two novel mutations [P122S (364C>T) and 1601delAC]
 in the SLC3A1 gene in type I cystinurics.";
 Hum. Mutat. 15:390-390(2000).
 [21]
 VARIANTS CSNU CYS-151; LYS-253; HIS-362; ARG-398; HIS-461; THR-467;
 VAL-481; LYS-482; ARG-510; THR-584; SER-599 AND GLU-600, AND VARIANT
 ILE-618.
 PubMed=11748844; DOI=10.1002/humu.1228;
 Harnevik L., Fjellstedt E., Molbaek A., Tiselius H.-G., Denneberg T.,
 Soederkvist P.;
 "Identification of 12 novel mutations in the SLC3A1 gene in Swedish
 cystinuria patients.";
 Hum. Mutat. 18:516-525(2001).
 [22]
 VARIANTS CSNU MET-216; CYS-362; TRP-365; THR-467 AND ALA-508.
 PubMed=12234283; DOI=10.1046/j.1523-1755.2002.00552.x;
 Botzenhart E., Vester U., Schmidt C., Hesse A., Halber M., Wagner C.,
 Lang F., Hoyer P., Zerres K., Eggermann T.;
 "Cystinuria in children: distribution and frequencies of mutations in
 the SLC3A1 and SLC7A9 genes.";
 Kidney Int. 62:1136-1142(2002).
 [23]
 VARIANTS CSNU ARG-140; TYR-179; MET-216; PRO-365; TRP-452; THR-467 AND
 TRP-547.
 PubMed=16138908; DOI=10.1111/j.1529-8817.2005.00185.x;
 Skopkova Z., Hrabincova E., Stastna S., Kozak L., Adam T.;
 "Molecular genetic analysis of SLC3A1 and SLC7A9 genes in Czech and
 Slovak cystinuric patients.";
 Ann. Hum. Genet. 69:501-507(2005).
 [24]
 VARIANTS CSNU PRO-89; ARG-123; CYS-124; PRO-130; GLY-137; GLN-149;
 MET-189; PRO-348; LYS-410; ARG-441; LEU-455; CYS-456; HIS-456;
 LEU-507; SER-568 AND TRP-666.
 PubMed=15635077; DOI=10.1136/jmg.2004.022244;
 Font-Llitjos M., Jimenez-Vidal M., Bisceglia L., Di Perna M.,
 de Sanctis L., Rousaud F., Zelante L., Palacin M., Nunes V.;
 "New insights into cystinuria: 40 new mutations, genotype-phenotype
 correlation, and digenic inheritance causing partial phenotype.";
 J. Med. Genet. 42:58-68(2005).
 [25]
 VARIANTS CSNU ALA-183; PRO-346; THR-445 AND ARG-673.
 PubMed=16609684; DOI=10.1038/sj.ki.5000241;
 Shigeta Y., Kanai Y., Chairoungdua A., Ahmed N., Sakamoto S.,
 Matsuo H., Kim D.K., Fujimura M., Anzai N., Mizoguchi K., Ueda T.,
 Akakura K., Ichikawa T., Ito H., Endou H.;
 "A novel missense mutation of SLC7A9 frequent in Japanese cystinuria
 cases affecting the C-terminus of the transporter.";
 Kidney Int. 69:1198-1206(2006).
 [26]
 VARIANTS CSNU GLY-137; TRP-365; GLN-452; THR-467 AND TRP-547.
 PubMed=19782624; DOI=10.1016/j.ymgme.2009.09.001;
 Bisceglia L., Fischetti L., Bonis P.D., Palumbo O., Augello B.,
 Stanziale P., Carella M., Zelante L.;
 "Large rearrangements detected by MLPA, point mutations, and survey of
 the frequency of mutations within the SLC3A1 and SLC7A9 genes in a
 cohort of 172 cystinuric Italian patients.";
 Mol. Genet. Metab. 99:42-52(2010).
 -!- FUNCTION: Involved in the high-affinity, sodium-independent
     transport of cystine and neutral and dibasic amino acids (system
     B(0,+)-like activity). May function as an activator of SLC7A9 and
     be involved in the high-affinity reabsorption of cystine in the
     kidney tubule. {ECO:0000269|PubMed:11318953,
     ECO:0000269|PubMed:7686906, ECO:0000269|PubMed:8486766,
     ECO:0000269|PubMed:8663184}.
 -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
     transport protein SLC7A9. {ECO:0000269|PubMed:10588648,
     ECO:0000269|PubMed:12167606}.
 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12167606};
     Single-pass type II membrane protein
     {ECO:0000269|PubMed:12167606}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=7;
     Name=A;
       IsoId=Q07837-1; Sequence=Displayed;
     Name=B;
       IsoId=Q07837-2; Sequence=VSP_054339;
     Name=C;
       IsoId=Q07837-3; Sequence=VSP_054342, VSP_054343;
     Name=D;
       IsoId=Q07837-4; Sequence=VSP_054340, VSP_054341;
     Name=E;
       IsoId=Q07837-5; Sequence=VSP_054344, VSP_054345;
     Name=F;
       IsoId=Q07837-6; Sequence=VSP_054346, VSP_054349;
     Name=G;
       IsoId=Q07837-7; Sequence=VSP_054347, VSP_054348;
 -!- TISSUE SPECIFICITY: Expressed in the brush border membrane in the
     kidney (at protein level). Predominantly expressed in the kidney,
     small intestine and pancreas. Weakly expressed in liver.
     {ECO:0000269|PubMed:12167606, ECO:0000269|PubMed:7686906,
     ECO:0000269|PubMed:8486766}.
 -!- DISEASE: Cystinuria (CSNU) [MIM:220100]: An autosomal disorder
     characterized by impaired epithelial cell transport of cystine and
     dibasic amino acids (lysine, ornithine, and arginine) in the
     proximal renal tubule and gastrointestinal tract. The impaired
     renal reabsorption of cystine and its low solubility causes the
     formation of calculi in the urinary tract, resulting in
     obstructive uropathy, pyelonephritis, and, rarely, renal failure.
     {ECO:0000269|PubMed:10738006, ECO:0000269|PubMed:11748844,
     ECO:0000269|PubMed:12234283, ECO:0000269|PubMed:15635077,
     ECO:0000269|PubMed:16138908, ECO:0000269|PubMed:16609684,
     ECO:0000269|PubMed:19782624, ECO:0000269|PubMed:7539209,
     ECO:0000269|PubMed:7573036, ECO:0000269|PubMed:7575432,
     ECO:0000269|PubMed:8054986, ECO:0000269|PubMed:9186880}. Note=The
     disease is caused by mutations affecting the gene represented in
     this entry.
 -!- DISEASE: Hypotonia-cystinuria syndrome (HCS) [MIM:606407]:
     Characterized generalized hypotonia at birth, nephrolithiasis,
     growth hormone deficiency, minor facial dysmorphism, failure to
     thrive, followed by hyperphagia and rapid weight gain in late
     childhood. {ECO:0000269|PubMed:16385448}. Note=The disease is
     caused by mutations affecting the gene represented in this entry.
 -----------------------------------------------------------------------
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 EMBL; M95548; AAA35500.1; -; mRNA.
 EMBL; L11696; AAA81778.1; -; mRNA.
 EMBL; D82326; BAA11541.1; -; mRNA.
 EMBL; U60819; AAB39829.1; -; Genomic_DNA.
 EMBL; U60810; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; U60811; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; U60812; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; U60813; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; U60816; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; U60818; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; U60814; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; U60815; AAB39829.1; JOINED; Genomic_DNA.
 EMBL; AB033549; BAB16841.1; -; mRNA.
 EMBL; DQ023512; AAY89643.1; -; mRNA.
 EMBL; DQ023513; AAY89644.1; -; mRNA.
 EMBL; DQ023514; AAY89645.1; -; mRNA.
 EMBL; DQ023515; AAY89646.1; -; mRNA.
 EMBL; DQ023516; AAY89647.1; -; mRNA.
 EMBL; DQ023517; AAY89648.1; -; mRNA.
 EMBL; AK223146; BAD96866.1; -; mRNA.
 EMBL; AK289636; BAF82325.1; -; mRNA.
 EMBL; AC013717; AAX88955.1; -; Genomic_DNA.
 EMBL; BC022386; AAH22386.1; -; mRNA.
 EMBL; BC093624; AAH93624.1; -; mRNA.
 EMBL; BC093626; AAH93626.1; -; mRNA.
 CCDS; CCDS1819.1; -. [Q07837-1]
 PIR; A47102; A47102.
 RefSeq; NP_000332.2; NM_000341.3. [Q07837-1]
 UniGene; Hs.112916; -.
 ProteinModelPortal; Q07837; -.
 BioGrid; 112410; 2.
 STRING; 9606.ENSP00000260649; -.
 DrugBank; DB00138; L-Cystine.
 CAZy; GH13; Glycoside Hydrolase Family 13.
 TCDB; 8.A.9.1.2; the rbat transport accessory protein (rbat) family.
 iPTMnet; Q07837; -.
 PhosphoSitePlus; Q07837; -.
 BioMuta; SLC3A1; -.
 DMDM; 67472674; -.
 PaxDb; Q07837; -.
 PeptideAtlas; Q07837; -.
 PRIDE; Q07837; -.
 ProteomicsDB; 58542; -.
 DNASU; 6519; -.
 Ensembl; ENST00000260649; ENSP00000260649; ENSG00000138079. [Q07837-1]
 Ensembl; ENST00000409229; ENSP00000386620; ENSG00000138079. [Q07837-6]
 Ensembl; ENST00000409380; ENSP00000386709; ENSG00000138079. [Q07837-2]
 Ensembl; ENST00000409740; ENSP00000386677; ENSG00000138079. [Q07837-4]
 Ensembl; ENST00000409741; ENSP00000386954; ENSG00000138079. [Q07837-5]
 Ensembl; ENST00000410056; ENSP00000387337; ENSG00000138079. [Q07837-3]
 GeneID; 6519; -.
 KEGG; hsa:6519; -.
 UCSC; uc002rty.4; human. [Q07837-1]
 CTD; 6519; -.
 DisGeNET; 6519; -.
 EuPathDB; HostDB:ENSG00000138079.13; -.
 GeneCards; SLC3A1; -.
 HGNC; HGNC:11025; SLC3A1.
 HPA; HPA038360; -.
 HPA; HPA071102; -.
 MalaCards; SLC3A1; -.
 MIM; 104614; gene.
 MIM; 220100; phenotype.
 MIM; 606407; phenotype.
 neXtProt; NX_Q07837; -.
 OpenTargets; ENSG00000138079; -.
 Orphanet; 163693; 2p21 microdeletion syndrome.
 Orphanet; 238523; Atypical hypotonia-cystinuria syndrome.
 Orphanet; 93612; Cystinuria type A.
 Orphanet; 163690; Hypotonia-cystinuria syndrome.
 PharmGKB; PA35893; -.
 eggNOG; KOG0471; Eukaryota.
 eggNOG; COG0366; LUCA.
 GeneTree; ENSGT00900000140965; -.
 HOGENOM; HOG000220640; -.
 HOVERGEN; HBG053002; -.
 InParanoid; Q07837; -.
 KO; K14210; -.
 OMA; PNGEKWA; -.
 OrthoDB; EOG091G03FE; -.
 PhylomeDB; Q07837; -.
 TreeFam; TF314498; -.
 Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
 Reactome; R-HSA-5619113; Defective SLC3A1 causes cystinuria (CSNU).
 SIGNOR; Q07837; -.
 ChiTaRS; SLC3A1; human.
 GeneWiki; SLC3A1; -.
 GenomeRNAi; 6519; -.
 PRO; PR:Q07837; -.
 Proteomes; UP000005640; Chromosome 2.
 Bgee; ENSG00000138079; Expressed in 137 organ(s), highest expression level in kidney epithelium.
 CleanEx; HS_SLC3A1; -.
 ExpressionAtlas; Q07837; baseline and differential.
 Genevisible; Q07837; HS.
 GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
 GO; GO:0016020; C:membrane; TAS:ProtInc.
 GO; GO:0005886; C:plasma membrane; TAS:Reactome.
 GO; GO:0005774; C:vacuolar membrane; IEA:Ensembl.
 GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:ProtInc.
 GO; GO:0015174; F:basic amino acid transmembrane transporter activity; TAS:ProtInc.
 GO; GO:0003824; F:catalytic activity; IEA:InterPro.
 GO; GO:0015184; F:L-cystine transmembrane transporter activity; TAS:ProtInc.
 GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
 GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
 GO; GO:0015802; P:basic amino acid transport; TAS:ProtInc.
 GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
 GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
 GO; GO:0015811; P:L-cystine transport; TAS:ProtInc.
 InterPro; IPR006047; Glyco_hydro_13_cat_dom.
 InterPro; IPR017853; Glycoside_hydrolase_SF.
 Pfam; PF00128; Alpha-amylase; 1.
 SMART; SM00642; Aamy; 1.
 SUPFAM; SSF51445; SSF51445; 1.
 1: Evidence at protein level;
 Alternative splicing; Amino-acid transport; Complete proteome;
 Cystinuria; Disease mutation; Disulfide bond; Glycoprotein; Membrane;
 Phosphoprotein; Polymorphism; Reference proteome; Signal-anchor;
 Transmembrane; Transmembrane helix; Transport.
 CHAIN         1    685       Neutral and basic amino acid transport
                              protein rBAT.
                              /FTId=PRO_0000071950.
 TOPO_DOM      1     87       Cytoplasmic. {ECO:0000255}.
 TRANSMEM     88    108       Helical; Signal-anchor for type II
                              membrane protein. {ECO:0000255}.
 TOPO_DOM    109    685       Extracellular. {ECO:0000255}.
 MOD_RES      10     10       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q64319}.
 CARBOHYD    214    214       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    261    261       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    332    332       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    495    495       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    513    513       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    575    575       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 VAR_SEQ       1    278       Missing (in isoform B).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054339.
 VAR_SEQ       1      8       MAEDKSKR -> MTLNLVNS (in isoform D).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054340.
 VAR_SEQ       9    377       Missing (in isoform D).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054341.
 VAR_SEQ     380    391       FMGTEAYAESID -> LTTAYALISSQA (in isoform
                              C). {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054342.
 VAR_SEQ     392    685       Missing (in isoform C).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054343.
 VAR_SEQ     501    502       NT -> VS (in isoform E).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054344.
 VAR_SEQ     503    685       Missing (in isoform E).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054345.
 VAR_SEQ     541    564       QKTQPRSALKLYQDLSLLHANELL -> SISENFMLILETK
                              KWVSTESTHSP (in isoform F).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054346.
 VAR_SEQ     541    551       QKTQPRSALKL -> LLRHPCSSAVA (in isoform
                              G). {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054347.
 VAR_SEQ     552    685       Missing (in isoform G).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054348.
 VAR_SEQ     565    685       Missing (in isoform F).
                              {ECO:0000303|PubMed:15913950}.
                              /FTId=VSP_054349.
 VARIANT      89     89       L -> P (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072283.
 VARIANT     122    122       P -> S (in CSNU).
                              {ECO:0000269|PubMed:10738006}.
                              /FTId=VAR_064040.
 VARIANT     123    123       M -> R (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072284.
 VARIANT     124    124       Y -> C (in CSNU; dbSNP:rs766947722).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072285.
 VARIANT     128    128       P -> Q (in CSNU).
                              {ECO:0000269|PubMed:7539209}.
                              /FTId=VAR_011420.
 VARIANT     130    130       S -> P (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072286.
 VARIANT     137    137       D -> G (in CSNU).
                              {ECO:0000269|PubMed:15635077,
                              ECO:0000269|PubMed:19782624}.
                              /FTId=VAR_072287.
 VARIANT     140    140       G -> R (in CSNU; dbSNP:rs768848958).
                              {ECO:0000269|PubMed:16138908}.
                              /FTId=VAR_072288.
 VARIANT     149    149       L -> Q (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072289.
 VARIANT     151    151       Y -> C (in CSNU; dbSNP:rs778354350).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038200.
 VARIANT     179    179       D -> Y (in CSNU; dbSNP:rs747660493).
                              {ECO:0000269|PubMed:16138908}.
                              /FTId=VAR_072290.
 VARIANT     181    181       R -> Q (in CSNU; dbSNP:rs121912694).
                              {ECO:0000269|PubMed:8054986}.
                              /FTId=VAR_011421.
 VARIANT     183    183       V -> A (in CSNU; unknown pathological
                              significance).
                              {ECO:0000269|PubMed:16609684}.
                              /FTId=VAR_072291.
 VARIANT     189    189       T -> M (in CSNU; dbSNP:rs140317484).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072292.
 VARIANT     216    216       T -> M (in CSNU; dbSNP:rs369641941).
                              {ECO:0000269|PubMed:12234283,
                              ECO:0000269|PubMed:16138908}.
                              /FTId=VAR_022600.
 VARIANT     253    253       N -> K (in CSNU).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038201.
 VARIANT     268    268       E -> K (in CSNU; reduction in amino acid
                              transport activity; dbSNP:rs757239030).
                              {ECO:0000269|PubMed:7575432}.
                              /FTId=VAR_011422.
 VARIANT     341    341       T -> A (in CSNU; reduction in amino acid
                              transport activity; dbSNP:rs200287661).
                              {ECO:0000269|PubMed:7575432}.
                              /FTId=VAR_011423.
 VARIANT     346    346       L -> P (in CSNU; unknown pathological
                              significance).
                              {ECO:0000269|PubMed:16609684}.
                              /FTId=VAR_072293.
 VARIANT     348    348       H -> P (in CSNU; dbSNP:rs756887216).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072294.
 VARIANT     362    362       R -> C (in CSNU; dbSNP:rs375399468).
                              {ECO:0000269|PubMed:12234283}.
                              /FTId=VAR_022601.
 VARIANT     362    362       R -> H (in CSNU; dbSNP:rs121912697).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038202.
 VARIANT     365    365       R -> P (in CSNU; dbSNP:rs567478582).
                              {ECO:0000269|PubMed:16138908}.
                              /FTId=VAR_072295.
 VARIANT     365    365       R -> W (in CSNU; dbSNP:rs765828196).
                              {ECO:0000269|PubMed:12234283,
                              ECO:0000269|PubMed:19782624,
                              ECO:0000269|PubMed:7573036}.
                              /FTId=VAR_011424.
 VARIANT     398    398       G -> R (in CSNU).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038203.
 VARIANT     410    410       N -> K (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072296.
 VARIANT     441    441       P -> R (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072297.
 VARIANT     445    445       I -> T (in CSNU; unknown pathological
                              significance; dbSNP:rs187962930).
                              {ECO:0000269|PubMed:16609684}.
                              /FTId=VAR_072298.
 VARIANT     452    452       R -> Q (in CSNU; dbSNP:rs750912461).
                              {ECO:0000269|PubMed:19782624}.
                              /FTId=VAR_072299.
 VARIANT     452    452       R -> W (in CSNU; dbSNP:rs201502095).
                              {ECO:0000269|PubMed:16138908,
                              ECO:0000269|PubMed:9186880}.
                              /FTId=VAR_011425.
 VARIANT     455    455       S -> L (in CSNU; dbSNP:rs949704245).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072300.
 VARIANT     456    456       R -> C (in CSNU; dbSNP:rs139251285).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072301.
 VARIANT     456    456       R -> H (in CSNU; dbSNP:rs373852467).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072302.
 VARIANT     461    461       Y -> H (in CSNU; dbSNP:rs144162964).
                              {ECO:0000269|PubMed:11748844,
                              ECO:0000269|PubMed:9186880}.
                              /FTId=VAR_011426.
 VARIANT     467    467       M -> K (in CSNU; dbSNP:rs121912691).
                              {ECO:0000269|PubMed:8054986}.
                              /FTId=VAR_011428.
 VARIANT     467    467       M -> T (in CSNU; loss of 80% of amino
                              acid transport activity;
                              dbSNP:rs121912691).
                              {ECO:0000269|PubMed:11748844,
                              ECO:0000269|PubMed:12234283,
                              ECO:0000269|PubMed:16138908,
                              ECO:0000269|PubMed:19782624,
                              ECO:0000269|PubMed:8054986,
                              ECO:0000269|PubMed:9186880}.
                              /FTId=VAR_011427.
 VARIANT     481    481       G -> V (in CSNU).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038204.
 VARIANT     482    482       E -> K (in CSNU).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038205.
 VARIANT     507    507       S -> L (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072303.
 VARIANT     508    508       P -> A (in CSNU; dbSNP:rs1032513393).
                              {ECO:0000269|PubMed:12234283}.
                              /FTId=VAR_022602.
 VARIANT     510    510       Q -> R (in CSNU; dbSNP:rs778925791).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038206.
 VARIANT     547    547       S -> W (in CSNU; dbSNP:rs368796166).
                              {ECO:0000269|PubMed:16138908,
                              ECO:0000269|PubMed:19782624}.
                              /FTId=VAR_072304.
 VARIANT     568    568       G -> S (in CSNU; dbSNP:rs376639206).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072305.
 VARIANT     582    582       Y -> H (in CSNU; dbSNP:rs776729515).
                              {ECO:0000269|PubMed:7573036}.
                              /FTId=VAR_011429.
 VARIANT     584    584       R -> T (in CSNU; dbSNP:rs759696513).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038207.
 VARIANT     599    599       F -> S (in CSNU; dbSNP:rs146963107).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038208.
 VARIANT     600    600       G -> E (in CSNU; dbSNP:rs141944551).
                              {ECO:0000269|PubMed:11748844}.
                              /FTId=VAR_038209.
 VARIANT     615    615       P -> T (in CSNU; dbSNP:rs121912696).
                              {ECO:0000269|PubMed:8054986}.
                              /FTId=VAR_011430.
 VARIANT     618    618       M -> I (in dbSNP:rs698761).
                              {ECO:0000269|PubMed:11318953,
                              ECO:0000269|PubMed:11748844,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:15913950,
                              ECO:0000269|PubMed:7573036,
                              ECO:0000269|PubMed:8486766,
                              ECO:0000269|PubMed:8663184,
                              ECO:0000269|PubMed:9186880}.
                              /FTId=VAR_011431.
 VARIANT     648    648       F -> S (in CSNU).
                              {ECO:0000269|PubMed:7573036}.
                              /FTId=VAR_011432.
 VARIANT     652    652       T -> R (in CSNU; dbSNP:rs121912695).
                              {ECO:0000269|PubMed:8054986}.
                              /FTId=VAR_011433.
 VARIANT     666    666       C -> W (in CSNU).
                              {ECO:0000269|PubMed:15635077}.
                              /FTId=VAR_072306.
 VARIANT     673    673       C -> R (in CSNU; unknown pathological
                              significance; dbSNP:rs756823144).
                              {ECO:0000269|PubMed:16609684}.
                              /FTId=VAR_072307.
 VARIANT     678    678       L -> P (in CSNU; dbSNP:rs121912693).
                              {ECO:0000269|PubMed:8054986}.
                              /FTId=VAR_011434.
 SEQUENCE   685 AA;  78852 MW;  F9D6DFD548283899 CRC64;
 MAEDKSKRDS IEMSMKGCQT NNGFVHNEDI LEQTPDPGSS TDNLKHSTRG ILGSQEPDFK
 GVQPYAGMPK EVLFQFSGQA RYRIPREILF WLTVASVLVL IAATIAIIAL SPKCLDWWQE
 GPMYQIYPRS FKDSNKDGNG DLKGIQDKLD YITALNIKTV WITSFYKSSL KDFRYGVEDF
 REVDPIFGTM EDFENLVAAI HDKGLKLIID FIPNHTSDKH IWFQLSRTRT GKYTDYYIWH
 DCTHENGKTI PPNNWLSVYG NSSWHFDEVR NQCYFHQFMK EQPDLNFRNP DVQEEIKEIL
 RFWLTKGVDG FSLDAVKFLL EAKHLRDEIQ VNKTQIPDTV TQYSELYHDF TTTQVGMHDI
 VRSFRQTMDQ YSTEPGRYRF MGTEAYAESI DRTVMYYGLP FIQEADFPFN NYLSMLDTVS
 GNSVYEVITS WMENMPEGKW PNWMIGGPDS SRLTSRLGNQ YVNVMNMLLF TLPGTPITYY
 GEEIGMGNIV AANLNESYDI NTLRSKSPMQ WDNSSNAGFS EASNTWLPTN SDYHTVNVDV
 QKTQPRSALK LYQDLSLLHA NELLLNRGWF CHLRNDSHYV VYTRELDGID RIFIVVLNFG
 ESTLLNLHNM ISGLPAKMRI RLSTNSADKG SKVDTSGIFL DKGEGLIFEH NTKNLLHRQT
 AFRDRCFVSN RACYSSVLNI LYTSC

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