SLC31_HUMAN
ID SLC31_HUMAN Reviewed; 685 AA.
AC Q07837; A8K0S1; O00658; Q15295; Q4J6B4; Q4J6B5; Q4J6B6; Q4J6B7; Q4J6B8;
AC Q4J6B9; Q52M92; Q52M94;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Neutral and basic amino acid transport protein rBAT;
DE Short=NBAT;
DE AltName: Full=D2h;
DE AltName: Full=Solute carrier family 3 member 1;
DE AltName: Full=b(0,+)-type amino acid transport protein;
GN Name=SLC3A1; Synonyms=RBAT;
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] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT ILE-618.
RC TISSUE=Kidney;
RX PubMed=8486766; DOI=10.1172/jci116415;
RA Lee W.-S., Wells R.G., Sabbag R.V., Mohandas T.K., Hediger M.A.;
RT "Cloning and chromosomal localization of a human kidney cDNA involved in
RT cystine, dibasic, and neutral amino acid transport.";
RL J. Clin. Invest. 91:1959-1963(1993).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Lee W.-S., Wells R.G., Sabbag R.V., Mohandas T.K., Hediger M.A.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney cortex;
RX PubMed=7686906; DOI=10.1016/s0021-9258(18)82410-3;
RA Bertran J., Werner A., Chillaron J., Nunes V., Biber J., Testar X.,
RA Zorzano A., Estivill X., Murer H., Palacin M.;
RT "Expression cloning of a human renal cDNA that induces high affinity
RT transport of L-cystine shared with dibasic amino acids in Xenopus
RT oocytes.";
RL J. Biol. Chem. 268:14842-14849(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ILE-618, AND FUNCTION.
RC TISSUE=Kidney cortex;
RX PubMed=8663184; DOI=10.1074/jbc.271.28.16758;
RA Miyamoto K., Segawa H., Tatsumi S., Katai K., Yamamoto H., Taketani Y.,
RA Haga H., Morita K., Takeda E.;
RT "Effects of truncation of the COOH-terminal region of a Na+-independent
RT neutral and basic amino acid transporter on amino acid transport in Xenopus
RT oocytes.";
RL J. Biol. Chem. 271:16758-16763(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-618, AND VARIANTS CSNU
RP TRP-452; HIS-461 AND THR-467.
RX PubMed=9186880; DOI=10.1038/ki.1997.258;
RA Endsley J.K., Phillips J.A. III, Hruska K.A., Denneberg T., Carlson J.,
RA George A.L. Jr.;
RT "Genomic organization of a human cystine transporter gene (SLC3A1) and
RT identification of novel mutations causing cystinuria.";
RL Kidney Int. 51:1893-1899(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND VARIANT ILE-618.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C; D; E; F AND G), ALTERNATIVE
RP SPLICING, AND VARIANT ILE-618.
RX PubMed=15913950; DOI=10.1016/j.ygeno.2005.04.001;
RA Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K.,
RA Hershkovitz E.;
RT "The 2p21 deletion syndrome: characterization of the transcription
RT content.";
RL Genomics 86:195-211(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Amygdala;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT ILE-618.
RC TISSUE=Brain, and 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 [12]
RP SUBUNIT.
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 [13]
RP DISEASE.
RX PubMed=7568194; DOI=10.1073/pnas.92.21.9667;
RA Calonge M.J., Volpini V., Bisceglia L., Rousaud F., de Sanctis L.,
RA Beccia E., Zelante L., Testar X., Zorzano A., Estivill X., Gasparini P.,
RA Nunes V., Palacin M.;
RT "Genetic heterogeneity in cystinuria: the SLC3A1 gene is linked to type I
RT but not to type III cystinuria.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9667-9671(1995).
RN [14]
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 [15]
RP INVOLVEMENT IN HCS.
RX PubMed=16385448; DOI=10.1086/498852;
RA Jaeken J., Martens K., Francois I., Eyskens F., Lecointre C., Derua R.,
RA Meulemans S., Slootstra J.W., Waelkens E., de Zegher F., Creemers J.W.M.,
RA Matthijs G.;
RT "Deletion of PREPL, a gene encoding a putative serine oligopeptidase, in
RT patients with hypotonia-cystinuria syndrome.";
RL Am. J. Hum. Genet. 78:38-51(2006).
RN [16]
RP INVOLVEMENT IN HCS.
RX PubMed=21686663; DOI=10.1136/bcr.08.2008.0719;
RA Chabrol B., Martens K., Meulemans S., Cano A., Jaeken J., Matthijs G.,
RA Creemers J.W.;
RT "Deletion of C2orf34, PREPL and SLC3A1 causes atypical hypotonia-cystinuria
RT syndrome.";
RL BMJ Case Rep. 2009:0-0(2009).
RN [17]
RP VARIANTS CSNU GLN-181; LYS-467; THR-467; THR-615; ARG-652 AND PRO-678, AND
RP CHARACTERIZATION OF VARIANT THR-467.
RX PubMed=8054986; DOI=10.1038/ng0494-420;
RA Calonge M.J., Gasparini P., Chillaron J., Chillon M., Gallucci M.,
RA Rousaud F., Zelante L., Testar X., Dallapiccola B., Di Silverio F.,
RA Barcelo P., Estivill X., Zorzano A., Nunes V., Palacin M.;
RT "Cystinuria caused by mutations in rBAT, a gene involved in the transport
RT of cystine.";
RL Nat. Genet. 6:420-425(1994).
RN [18]
RP VARIANT CSNU GLN-128.
RX PubMed=7539209;
RA Pras E., Raben N., Golomb E., Arber N., Aksentijevich I., Schapiro J.M.,
RA Harel D., Katz G., Liberman U., Pras M., Kastner D.L.;
RT "Mutations in the SLC3A1 transporter gene in cystinuria.";
RL Am. J. Hum. Genet. 56:1297-1303(1995).
RN [19]
RP VARIANTS CSNU TRP-365; HIS-582 AND SER-648, AND VARIANT ILE-618.
RX PubMed=7573036;
RA Gasparini P., Calonge M.J., Bisceglia L., Purroy J., Dianzani I.,
RA Notarangelo A., Rousaud F., Gallucci M., Testar X., Ponzone A.,
RA Estivill X., Zorzano A., Palacin M., Nunes V., Zelante L.;
RT "Molecular genetics of cystinuria: identification of four new mutations and
RT seven polymorphisms, and evidence for genetic heterogeneity.";
RL Am. J. Hum. Genet. 57:781-788(1995).
RN [20]
RP VARIANTS CSNU LYS-268 AND ALA-341, AND CHARACTERIZATION OF VARIANTS CSNU
RP LYS-268 AND ALA-341.
RX PubMed=7575432; DOI=10.1042/bj3100951;
RA Miyamoto K., Katai K., Tatsumi S., Sone K., Segawa H., Yamamoto H.,
RA Taketani Y., Takada K., Morita K., Kanayama H., Kagawa S., Takeda E.;
RT "Mutations of the basic amino acid transporter gene associated with
RT cystinuria.";
RL Biochem. J. 310:951-955(1995).
RN [21]
RP VARIANT CSNU SER-122.
RX PubMed=10738006;
RX DOI=10.1002/(sici)1098-1004(200004)15:4<390::aid-humu33>3.0.co;2-k;
RA Gitomer W.L., Reed B.Y., Pak C.Y.C.;
RT "Identification of two novel mutations [P122S (364C>T) and 1601delAC] in
RT the SLC3A1 gene in type I cystinurics.";
RL Hum. Mutat. 15:390-390(2000).
RN [22]
RP VARIANTS CSNU CYS-151; LYS-253; HIS-362; ARG-398; HIS-461; THR-467;
RP VAL-481; LYS-482; ARG-510; THR-584; SER-599 AND GLU-600, AND VARIANT
RP ILE-618.
RX PubMed=11748844; DOI=10.1002/humu.1228;
RA Harnevik L., Fjellstedt E., Molbaek A., Tiselius H.-G., Denneberg T.,
RA Soederkvist P.;
RT "Identification of 12 novel mutations in the SLC3A1 gene in Swedish
RT cystinuria patients.";
RL Hum. Mutat. 18:516-525(2001).
RN [23]
RP VARIANTS CSNU MET-216; CYS-362; TRP-365; THR-467 AND ALA-508.
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 [24]
RP VARIANTS CSNU ARG-140; TYR-179; MET-216; PRO-365; TRP-452; THR-467 AND
RP TRP-547.
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 [25]
RP VARIANTS CSNU PRO-89; ARG-123; CYS-124; PRO-130; GLY-137; GLN-149; MET-189;
RP PRO-348; LYS-410; ARG-441; LEU-455; CYS-456; HIS-456; LEU-507; SER-568 AND
RP TRP-666.
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 [26]
RP VARIANTS CSNU ALA-183; PRO-346; THR-445 AND ARG-673.
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 [27]
RP VARIANTS CSNU GLY-137; TRP-365; GLN-452; THR-467 AND TRP-547.
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). May function as an activator of SLC7A9 and be involved in
CC the high-affinity reabsorption of cystine in the kidney tubule.
CC {ECO:0000269|PubMed:11318953, ECO:0000269|PubMed:7686906,
CC ECO:0000269|PubMed:8486766, ECO:0000269|PubMed:8663184}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC7A9. {ECO:0000269|PubMed:10588648,
CC ECO:0000269|PubMed:12167606}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12167606}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:12167606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=A;
CC IsoId=Q07837-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q07837-2; Sequence=VSP_054339;
CC Name=C;
CC IsoId=Q07837-3; Sequence=VSP_054342, VSP_054343;
CC Name=D;
CC IsoId=Q07837-4; Sequence=VSP_054340, VSP_054341;
CC Name=E;
CC IsoId=Q07837-5; Sequence=VSP_054344, VSP_054345;
CC Name=F;
CC IsoId=Q07837-6; Sequence=VSP_054346, VSP_054349;
CC Name=G;
CC IsoId=Q07837-7; Sequence=VSP_054347, VSP_054348;
CC -!- TISSUE SPECIFICITY: Expressed in the brush border membrane in the
CC kidney (at protein level). Predominantly expressed in the kidney, small
CC intestine and pancreas. Weakly expressed in liver.
CC {ECO:0000269|PubMed:12167606, ECO:0000269|PubMed:7686906,
CC ECO:0000269|PubMed:8486766}.
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:10738006, ECO:0000269|PubMed:11748844,
CC ECO:0000269|PubMed:12234283, ECO:0000269|PubMed:15635077,
CC ECO:0000269|PubMed:16138908, ECO:0000269|PubMed:16609684,
CC ECO:0000269|PubMed:19782624, ECO:0000269|PubMed:7539209,
CC ECO:0000269|PubMed:7573036, ECO:0000269|PubMed:7575432,
CC ECO:0000269|PubMed:8054986, ECO:0000269|PubMed:9186880}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Hypotonia-cystinuria syndrome (HCS) [MIM:606407]:
CC Characterized generalized hypotonia at birth, nephrolithiasis, growth
CC hormone deficiency, minor facial dysmorphism, failure to thrive,
CC followed by hyperphagia and rapid weight gain in late childhood.
CC {ECO:0000269|PubMed:16385448, ECO:0000269|PubMed:21686663}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Hypotonia-cystinuria syndrome is a contiguous gene syndrome
CC caused by a homozygous deletion on chromosome 2p21 that disrupts the
CC gene represented in this entry and PREPL (PubMed:16385448,
CC PubMed:21686663). A homozygous 77.4-kb deletion that disrupts the gene
CC represented in this entry, PREPL, and CAMKMT, causes atypical
CC hypotonia-cystinuria syndrome, characterized by mild to moderate
CC intellectual disability and respiratory chain complex IV deficiency
CC (PubMed:21686663). {ECO:0000269|PubMed:16385448,
CC ECO:0000269|PubMed:21686663}.
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DR EMBL; M95548; AAA35500.1; -; mRNA.
DR EMBL; L11696; AAA81778.1; -; mRNA.
DR EMBL; D82326; BAA11541.1; -; mRNA.
DR EMBL; U60819; AAB39829.1; -; Genomic_DNA.
DR EMBL; U60810; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; U60811; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; U60812; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; U60813; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; U60816; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; U60818; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; U60814; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; U60815; AAB39829.1; JOINED; Genomic_DNA.
DR EMBL; AB033549; BAB16841.1; -; mRNA.
DR EMBL; DQ023512; AAY89643.1; -; mRNA.
DR EMBL; DQ023513; AAY89644.1; -; mRNA.
DR EMBL; DQ023514; AAY89645.1; -; mRNA.
DR EMBL; DQ023515; AAY89646.1; -; mRNA.
DR EMBL; DQ023516; AAY89647.1; -; mRNA.
DR EMBL; DQ023517; AAY89648.1; -; mRNA.
DR EMBL; AK223146; BAD96866.1; -; mRNA.
DR EMBL; AK289636; BAF82325.1; -; mRNA.
DR EMBL; AC013717; AAX88955.1; -; Genomic_DNA.
DR EMBL; BC022386; AAH22386.1; -; mRNA.
DR EMBL; BC093624; AAH93624.1; -; mRNA.
DR EMBL; BC093626; AAH93626.1; -; mRNA.
DR CCDS; CCDS1819.1; -. [Q07837-1]
DR PIR; A47102; A47102.
DR RefSeq; NP_000332.2; NM_000341.3. [Q07837-1]
DR PDB; 6LI9; EM; 2.30 A; A/C=2-685.
DR PDB; 6LID; EM; 2.70 A; A/C=2-685.
DR PDB; 6YUP; EM; 2.90 A; A/C=1-685.
DR PDB; 6YUZ; EM; 2.80 A; A/C=1-685.
DR PDBsum; 6LI9; -.
DR PDBsum; 6LID; -.
DR PDBsum; 6YUP; -.
DR PDBsum; 6YUZ; -.
DR AlphaFoldDB; Q07837; -.
DR SMR; Q07837; -.
DR BioGRID; 112410; 2.
DR STRING; 9606.ENSP00000260649; -.
DR DrugBank; DB00138; Cystine.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR TCDB; 8.A.9.1.2; the rbat transport accessory protein (rbat) family.
DR GlyGen; Q07837; 6 sites.
DR iPTMnet; Q07837; -.
DR PhosphoSitePlus; Q07837; -.
DR BioMuta; SLC3A1; -.
DR DMDM; 67472674; -.
DR jPOST; Q07837; -.
DR MassIVE; Q07837; -.
DR PaxDb; Q07837; -.
DR PeptideAtlas; Q07837; -.
DR PRIDE; Q07837; -.
DR ProteomicsDB; 58542; -. [Q07837-1]
DR ProteomicsDB; 62166; -.
DR ProteomicsDB; 62167; -.
DR ProteomicsDB; 62168; -.
DR ProteomicsDB; 62169; -.
DR Antibodypedia; 29895; 235 antibodies from 28 providers.
DR DNASU; 6519; -.
DR Ensembl; ENST00000260649.11; ENSP00000260649.6; ENSG00000138079.14. [Q07837-1]
DR Ensembl; ENST00000409229.7; ENSP00000386620.3; ENSG00000138079.14. [Q07837-6]
DR Ensembl; ENST00000409380.5; ENSP00000386709.1; ENSG00000138079.14. [Q07837-2]
DR Ensembl; ENST00000409740.3; ENSP00000386677.3; ENSG00000138079.14. [Q07837-4]
DR Ensembl; ENST00000409741.5; ENSP00000386954.1; ENSG00000138079.14. [Q07837-5]
DR Ensembl; ENST00000410056.7; ENSP00000387337.3; ENSG00000138079.14. [Q07837-3]
DR GeneID; 6519; -.
DR KEGG; hsa:6519; -.
DR MANE-Select; ENST00000260649.11; ENSP00000260649.6; NM_000341.4; NP_000332.2.
DR UCSC; uc002rty.4; human. [Q07837-1]
DR CTD; 6519; -.
DR DisGeNET; 6519; -.
DR GeneCards; SLC3A1; -.
DR HGNC; HGNC:11025; SLC3A1.
DR HPA; ENSG00000138079; Tissue enhanced (intestine, kidney, pancreas).
DR MalaCards; SLC3A1; -.
DR MIM; 104614; gene.
DR MIM; 220100; phenotype.
DR MIM; 606407; phenotype.
DR neXtProt; NX_Q07837; -.
DR OpenTargets; ENSG00000138079; -.
DR Orphanet; 163693; 2p21 microdeletion syndrome.
DR Orphanet; 238523; Atypical hypotonia-cystinuria syndrome.
DR Orphanet; 93612; Cystinuria type A.
DR Orphanet; 163690; Hypotonia-cystinuria syndrome.
DR PharmGKB; PA35893; -.
DR VEuPathDB; HostDB:ENSG00000138079; -.
DR eggNOG; KOG0471; Eukaryota.
DR GeneTree; ENSGT00940000158103; -.
DR HOGENOM; CLU_006462_8_0_1; -.
DR InParanoid; Q07837; -.
DR OMA; PNGEKWA; -.
DR PhylomeDB; Q07837; -.
DR TreeFam; TF314498; -.
DR PathwayCommons; Q07837; -.
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; Q07837; -.
DR SIGNOR; Q07837; -.
DR BioGRID-ORCS; 6519; 7 hits in 1069 CRISPR screens.
DR ChiTaRS; SLC3A1; human.
DR GeneWiki; SLC3A1; -.
DR GenomeRNAi; 6519; -.
DR Pharos; Q07837; Tbio.
DR PRO; PR:Q07837; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q07837; protein.
DR Bgee; ENSG00000138079; Expressed in body of pancreas and 102 other tissues.
DR ExpressionAtlas; Q07837; baseline and differential.
DR Genevisible; Q07837; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005774; C:vacuolar membrane; IEA:Ensembl.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0015810; P:aspartate transmembrane transport; IEA:Ensembl.
DR GO; GO:0015802; P:basic amino acid transport; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0015811; P:L-cystine transport; TAS:ProtInc.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IEA:Ensembl.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid transport; Cystinuria;
KW Disease variant; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..685
FT /note="Neutral and basic amino acid transport protein rBAT"
FT /id="PRO_0000071950"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64319"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..278
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054339"
FT VAR_SEQ 1..8
FT /note="MAEDKSKR -> MTLNLVNS (in isoform D)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054340"
FT VAR_SEQ 9..377
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054341"
FT VAR_SEQ 380..391
FT /note="FMGTEAYAESID -> LTTAYALISSQA (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054342"
FT VAR_SEQ 392..685
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054343"
FT VAR_SEQ 501..502
FT /note="NT -> VS (in isoform E)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054344"
FT VAR_SEQ 503..685
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054345"
FT VAR_SEQ 541..564
FT /note="QKTQPRSALKLYQDLSLLHANELL -> SISENFMLILETKKWVSTESTHSP
FT (in isoform F)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054346"
FT VAR_SEQ 541..551
FT /note="QKTQPRSALKL -> LLRHPCSSAVA (in isoform G)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054347"
FT VAR_SEQ 552..685
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054348"
FT VAR_SEQ 565..685
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_054349"
FT VARIANT 89
FT /note="L -> P (in CSNU; dbSNP:rs1453871309)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072283"
FT VARIANT 122
FT /note="P -> S (in CSNU)"
FT /evidence="ECO:0000269|PubMed:10738006"
FT /id="VAR_064040"
FT VARIANT 123
FT /note="M -> R (in CSNU; dbSNP:rs1269139353)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072284"
FT VARIANT 124
FT /note="Y -> C (in CSNU; dbSNP:rs766947722)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072285"
FT VARIANT 128
FT /note="P -> Q (in CSNU; dbSNP:rs576810133)"
FT /evidence="ECO:0000269|PubMed:7539209"
FT /id="VAR_011420"
FT VARIANT 130
FT /note="S -> P (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072286"
FT VARIANT 137
FT /note="D -> G (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077,
FT ECO:0000269|PubMed:19782624"
FT /id="VAR_072287"
FT VARIANT 140
FT /note="G -> R (in CSNU; dbSNP:rs768848958)"
FT /evidence="ECO:0000269|PubMed:16138908"
FT /id="VAR_072288"
FT VARIANT 149
FT /note="L -> Q (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072289"
FT VARIANT 151
FT /note="Y -> C (in CSNU; dbSNP:rs778354350)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038200"
FT VARIANT 179
FT /note="D -> Y (in CSNU; dbSNP:rs747660493)"
FT /evidence="ECO:0000269|PubMed:16138908"
FT /id="VAR_072290"
FT VARIANT 181
FT /note="R -> Q (in CSNU; dbSNP:rs121912694)"
FT /evidence="ECO:0000269|PubMed:8054986"
FT /id="VAR_011421"
FT VARIANT 183
FT /note="V -> A (in CSNU; unknown pathological significance;
FT dbSNP:rs1233216697)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_072291"
FT VARIANT 189
FT /note="T -> M (in CSNU; dbSNP:rs140317484)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072292"
FT VARIANT 216
FT /note="T -> M (in CSNU; dbSNP:rs369641941)"
FT /evidence="ECO:0000269|PubMed:12234283,
FT ECO:0000269|PubMed:16138908"
FT /id="VAR_022600"
FT VARIANT 253
FT /note="N -> K (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038201"
FT VARIANT 268
FT /note="E -> K (in CSNU; reduction in amino acid transport
FT activity; dbSNP:rs757239030)"
FT /evidence="ECO:0000269|PubMed:7575432"
FT /id="VAR_011422"
FT VARIANT 341
FT /note="T -> A (in CSNU; reduction in amino acid transport
FT activity; dbSNP:rs200287661)"
FT /evidence="ECO:0000269|PubMed:7575432"
FT /id="VAR_011423"
FT VARIANT 346
FT /note="L -> P (in CSNU; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_072293"
FT VARIANT 348
FT /note="H -> P (in CSNU; dbSNP:rs756887216)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072294"
FT VARIANT 362
FT /note="R -> C (in CSNU; dbSNP:rs375399468)"
FT /evidence="ECO:0000269|PubMed:12234283"
FT /id="VAR_022601"
FT VARIANT 362
FT /note="R -> H (in CSNU; dbSNP:rs121912697)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038202"
FT VARIANT 365
FT /note="R -> P (in CSNU; dbSNP:rs567478582)"
FT /evidence="ECO:0000269|PubMed:16138908"
FT /id="VAR_072295"
FT VARIANT 365
FT /note="R -> W (in CSNU; dbSNP:rs765828196)"
FT /evidence="ECO:0000269|PubMed:12234283,
FT ECO:0000269|PubMed:19782624, ECO:0000269|PubMed:7573036"
FT /id="VAR_011424"
FT VARIANT 398
FT /note="G -> R (in CSNU; dbSNP:rs1297802490)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038203"
FT VARIANT 410
FT /note="N -> K (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072296"
FT VARIANT 441
FT /note="P -> R (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072297"
FT VARIANT 445
FT /note="I -> T (in CSNU; unknown pathological significance;
FT dbSNP:rs187962930)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_072298"
FT VARIANT 452
FT /note="R -> Q (in CSNU; dbSNP:rs750912461)"
FT /evidence="ECO:0000269|PubMed:19782624"
FT /id="VAR_072299"
FT VARIANT 452
FT /note="R -> W (in CSNU; dbSNP:rs201502095)"
FT /evidence="ECO:0000269|PubMed:16138908,
FT ECO:0000269|PubMed:9186880"
FT /id="VAR_011425"
FT VARIANT 455
FT /note="S -> L (in CSNU; dbSNP:rs949704245)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072300"
FT VARIANT 456
FT /note="R -> C (in CSNU; dbSNP:rs139251285)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072301"
FT VARIANT 456
FT /note="R -> H (in CSNU; dbSNP:rs373852467)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072302"
FT VARIANT 461
FT /note="Y -> H (in CSNU; dbSNP:rs144162964)"
FT /evidence="ECO:0000269|PubMed:11748844,
FT ECO:0000269|PubMed:9186880"
FT /id="VAR_011426"
FT VARIANT 467
FT /note="M -> K (in CSNU; dbSNP:rs121912691)"
FT /evidence="ECO:0000269|PubMed:8054986"
FT /id="VAR_011428"
FT VARIANT 467
FT /note="M -> T (in CSNU; loss of 80% of amino acid transport
FT activity; dbSNP:rs121912691)"
FT /evidence="ECO:0000269|PubMed:11748844,
FT ECO:0000269|PubMed:12234283, ECO:0000269|PubMed:16138908,
FT ECO:0000269|PubMed:19782624, ECO:0000269|PubMed:8054986,
FT ECO:0000269|PubMed:9186880"
FT /id="VAR_011427"
FT VARIANT 481
FT /note="G -> V (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038204"
FT VARIANT 482
FT /note="E -> K (in CSNU)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038205"
FT VARIANT 507
FT /note="S -> L (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072303"
FT VARIANT 508
FT /note="P -> A (in CSNU; dbSNP:rs1032513393)"
FT /evidence="ECO:0000269|PubMed:12234283"
FT /id="VAR_022602"
FT VARIANT 510
FT /note="Q -> R (in CSNU; dbSNP:rs778925791)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038206"
FT VARIANT 547
FT /note="S -> W (in CSNU; dbSNP:rs368796166)"
FT /evidence="ECO:0000269|PubMed:16138908,
FT ECO:0000269|PubMed:19782624"
FT /id="VAR_072304"
FT VARIANT 568
FT /note="G -> S (in CSNU; dbSNP:rs376639206)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072305"
FT VARIANT 582
FT /note="Y -> H (in CSNU; dbSNP:rs776729515)"
FT /evidence="ECO:0000269|PubMed:7573036"
FT /id="VAR_011429"
FT VARIANT 584
FT /note="R -> T (in CSNU; dbSNP:rs759696513)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038207"
FT VARIANT 599
FT /note="F -> S (in CSNU; dbSNP:rs146963107)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038208"
FT VARIANT 600
FT /note="G -> E (in CSNU; dbSNP:rs141944551)"
FT /evidence="ECO:0000269|PubMed:11748844"
FT /id="VAR_038209"
FT VARIANT 615
FT /note="P -> T (in CSNU; dbSNP:rs121912696)"
FT /evidence="ECO:0000269|PubMed:8054986"
FT /id="VAR_011430"
FT VARIANT 618
FT /note="M -> I (in dbSNP:rs698761)"
FT /evidence="ECO:0000269|PubMed:11318953,
FT ECO:0000269|PubMed:11748844, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15913950, ECO:0000269|PubMed:7573036,
FT ECO:0000269|PubMed:8486766, ECO:0000269|PubMed:8663184,
FT ECO:0000269|PubMed:9186880"
FT /id="VAR_011431"
FT VARIANT 648
FT /note="F -> S (in CSNU; dbSNP:rs1279289214)"
FT /evidence="ECO:0000269|PubMed:7573036"
FT /id="VAR_011432"
FT VARIANT 652
FT /note="T -> R (in CSNU; dbSNP:rs121912695)"
FT /evidence="ECO:0000269|PubMed:8054986"
FT /id="VAR_011433"
FT VARIANT 666
FT /note="C -> W (in CSNU)"
FT /evidence="ECO:0000269|PubMed:15635077"
FT /id="VAR_072306"
FT VARIANT 673
FT /note="C -> R (in CSNU; unknown pathological significance;
FT dbSNP:rs756823144)"
FT /evidence="ECO:0000269|PubMed:16609684"
FT /id="VAR_072307"
FT VARIANT 678
FT /note="L -> P (in CSNU; dbSNP:rs121912693)"
FT /evidence="ECO:0000269|PubMed:8054986"
FT /id="VAR_011434"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 80..110
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6YUZ"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:6LID"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 412..415
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 462..471
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 480..485
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:6YUZ"
FT HELIX 548..561
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 577..585
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 591..598
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 600..605
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 616..625
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 660..662
FT /evidence="ECO:0007829|PDB:6LI9"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:6LI9"
FT TURN 676..679
FT /evidence="ECO:0007829|PDB:6LI9"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:6LI9"
SQ 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
