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Neutral and basic amino acid transport protein rBAT (NBAT) (D2h) (Solute carrier family 3 member 1) (b(0, )-type amino acid transport protein)

 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.
20-JUN-2018, entry version 189.
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; VDVQKTQ; -.
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; -.
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; TAS:ProtInc.
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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