ID SLC31_HUMAN Reviewed; 685 AA. AC Q07837; A8K0S1; O00658; Q15295; Q52M92; Q52M94; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 2. DT 05-APR-2011, entry version 120. DE RecName: Full=Neutral and basic amino acid transport protein rBAT; DE Short=NBAT; DE AltName: Full=B(0,+)-type amino acid transport protein; DE AltName: Full=D2h; GN Name=SLC3A1; Synonyms=RBAT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT RP ILE-618. RC TISSUE=Kidney; RX MEDLINE=93253036; 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 RT in 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], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Kidney cortex; RX MEDLINE=93315457; PubMed=7686906; 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], VARIANT ILE-618, AND FUNCTION. RC TISSUE=Kidney cortex; RX MEDLINE=96279252; PubMed=8663184; DOI=10.1074/jbc.271.28.16758; RA Miyamoto K., Segawa H., Tatsumi S., Katai K., Yamamoto H., RA Taketani Y., Haga H., Morita K., Takeda E.; RT "Effects of truncation of the COOH-terminal region of a Na+- RT independent neutral and basic amino acid transporter on amino acid RT transport in Xenopus oocytes."; RL J. Biol. Chem. 271:16758-16763(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-618, AND VARIANTS CSNU1 RP TRP-452; HIS-461 AND THR-467. RX MEDLINE=97330421; PubMed=9186880; DOI=10.1038/ki.1997.258; RA Endsley J.K., Phillips J.A. III, Hruska K.A., Denneberg T., RA Carlson J., 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], FUNCTION, AND VARIANT ILE-618. RC TISSUE=Kidney; RX MEDLINE=21219147; PubMed=11318953; RX DOI=10.1046/j.1523-1755.2001.0590051821.x; RA Mizoguchi K., Cha S.H., Chairoungdua A., Kim J.Y., Shigeta Y., RA Matsuo H., Fukushima J., Awa Y., Akakura K., Goya T., Ito H., RA 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 [LARGE SCALE MRNA]. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [9] 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP SUBUNIT. RX MEDLINE=20056095; PubMed=10588648; 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 RT cystinuria."; RL Mol. Biol. Cell 10:4135-4147(1999). RN [12] RP DISEASE. RX MEDLINE=96003840; 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., RA Gasparini P., Nunes V., Palacin M.; RT "Genetic heterogeneity in cystinuria: the SLC3A1 gene is linked to RT type I but not to type III cystinuria."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9667-9671(1995). RN [13] RP INVOLVEMENT IN HCS. RX PubMed=16385448; DOI=10.1086/498852; RA Jaeken J., Martens K., Francois I., Eyskens F., Lecointre C., RA Derua R., Meulemans S., Slootstra J.W., Waelkens E., de Zegher F., RA Creemers J.W.M., Matthijs G.; RT "Deletion of PREPL, a gene encoding a putative serine oligopeptidase, RT in patients with hypotonia-cystinuria syndrome."; RL Am. J. Hum. Genet. 78:38-51(2006). RN [14] RP VARIANTS CSNU1 GLN-181; LYS-467; THR-467; THR-615; ARG-652 AND RP PRO-678, AND CHARACTERIZATION OF VARIANT THR-467. RX MEDLINE=94332154; 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 RT transport of cystine."; RL Nat. Genet. 6:420-425(1994). RN [15] RP VARIANT CSNU1 GLN-128. RX MEDLINE=95282775; PubMed=7539209; RA Pras E., Raben N., Golomb E., Arber N., Aksentijevich I., RA Schapiro J.M., 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 [16] RP VARIANTS CSNU1 TRP-365; HIS-582 AND SER-648, AND VARIANT ILE-618. RX MEDLINE=96029269; 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 RT mutations and seven polymorphisms, and evidence for genetic RT heterogeneity."; RL Am. J. Hum. Genet. 57:781-788(1995). RN [17] RP VARIANTS CSNU1 LYS-268 AND ALA-341, AND CHARACTERIZATION OF VARIANTS RP CSNU1 LYS-268 AND ALA-341. RX MEDLINE=96013197; PubMed=7575432; 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 [18] RP VARIANT CSNU1 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] RT in the SLC3A1 gene in type I cystinurics."; RL Hum. Mutat. 15:390-390(2000). RN [19] RP VARIANTS CSNU1 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 [20] RP VARIANTS CSNU1 MET-216; CYS-362; TRP-365; THR-467 AND ALA-508. RX PubMed=12234283; DOI=10.1046/j.1523-1755.2002.00552.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 RT the SLC3A1 and SLC7A9 genes."; RL Kidney Int. 62:1136-1142(2002). CC -!- FUNCTION: Involved in the high-affinity, sodium-independent CC transport of cystine and neutral and dibasic amino acids (system CC B(0,+)-like activity). May function as an activator of SLC7A9 and CC be involved in the high-affinity reabsorption of cystine in the CC kidney tubule. CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid CC transport protein SLC7A9. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Potential). CC -!- TISSUE SPECIFICITY: Predominantly expressed in the kidney, small CC intestine and pancreas. Weakly expressed in liver. CC -!- DISEASE: Defects in SLC3A1 are a cause of cystinuria type 1 CC (CSNU1) [MIM:220100]. Cystinuria (CSNU) arises from impaired CC transport of cystine and dibasic amino acids through the CC epithelial cells of the renal tubule and gastrointestinal tract. CC -!- DISEASE: Defects in SLC3A1 are a cause of hypotonia-cystinuria CC syndrome (HCS) [MIM:606407]. HCS is characterized generalized CC hypotonia at birth, nephrolithiasis, growth hormone deficiency, CC minor facial dysmorphism, failure to thrive, followed by CC hyperphagia and rapid weight gain in late childhood. CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/SLC3A1"; CC -!- WEB RESOURCE: Name=Cysdb; Note=Cystinuria database; CC URL="http://www.cysdb.mcgill.ca/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 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 IPI; IPI00029268; -. DR PIR; A47102; A47102. DR RefSeq; NP_000332.2; NM_000341.3. DR UniGene; Hs.112916; -. DR ProteinModelPortal; Q07837; -. DR SMR; Q07837; 115-651. DR STRING; Q07837; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PhosphoSite; Q07837; -. DR PRIDE; Q07837; -. DR Ensembl; ENST00000260649; ENSP00000260649; ENSG00000138079. DR GeneID; 6519; -. DR KEGG; hsa:6519; -. DR NMPDR; fig|9606.3.peg.17810; -. DR UCSC; uc002ruc.2; human. DR CTD; 6519; -. DR GeneCards; GC02P044239; -. DR H-InvDB; HIX0002016; -. DR HGNC; HGNC:11025; SLC3A1. DR MIM; 104614; gene. DR MIM; 220100; phenotype. DR MIM; 606407; phenotype. DR neXtProt; NX_Q07837; -. DR Orphanet; 214; Cystinuria. DR Orphanet; 163690; Hypotonia - cystinuria syndrome. DR PharmGKB; PA35893; -. DR eggNOG; prNOG19137; -. DR HOGENOM; HBG669028; -. DR HOVERGEN; HBG053002; -. DR InParanoid; Q07837; -. DR OMA; DEVRKQC; -. DR OrthoDB; EOG47H5PM; -. DR PhylomeDB; Q07837; -. DR Reactome; REACT_13; Metabolism of amino acids and derivatives. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR Reactome; REACT_19419; Amino acid and oligopeptide SLC transporters. DR DrugBank; DB00138; L-Cystine. DR NextBio; 25349; -. DR ArrayExpress; Q07837; -. DR Bgee; Q07837; -. DR CleanEx; HS_SLC3A1; -. DR Genevestigator; Q07837; -. DR GermOnline; ENSG00000138079; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005624; C:membrane fraction; TAS:ProtInc. DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc. DR GO; GO:0006811; P:ion transport; TAS:Reactome. DR InterPro; IPR015902; Alpha_amylase. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR006589; Glyco_hydro_13_sub_cat_dom. DR InterPro; IPR013781; Glyco_hydro_sg_catalytic. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 2. DR PANTHER; PTHR10357; Alpha_amylase; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; Glyco_hydro_cat; 1. PE 1: Evidence at protein level; KW Amino-acid transport; Complete proteome; Cystinuria; Disease mutation; KW Disulfide bond; Glycoprotein; Membrane; Polymorphism; Signal-anchor; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 685 Neutral and basic amino acid transport FT protein rBAT. FT /FTId=PRO_0000071950. FT TOPO_DOM 1 87 Cytoplasmic (Potential). FT TRANSMEM 88 108 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 109 685 Extracellular (Potential). FT CARBOHYD 214 214 N-linked (GlcNAc...) (Potential). FT CARBOHYD 261 261 N-linked (GlcNAc...) (Potential). FT CARBOHYD 332 332 N-linked (GlcNAc...) (Potential). FT CARBOHYD 495 495 N-linked (GlcNAc...) (Potential). FT CARBOHYD 513 513 N-linked (GlcNAc...) (Potential). FT CARBOHYD 575 575 N-linked (GlcNAc...) (Potential). FT VARIANT 122 122 P -> S (in CSNU1). FT /FTId=VAR_064040. FT VARIANT 128 128 P -> Q (in CSNU1). FT /FTId=VAR_011420. FT VARIANT 151 151 Y -> C (in CSNU1). FT /FTId=VAR_038200. FT VARIANT 181 181 R -> Q (in CSNU1). FT /FTId=VAR_011421. FT VARIANT 216 216 T -> M (in CSNU1). FT /FTId=VAR_022600. FT VARIANT 253 253 N -> K (in CSNU1). FT /FTId=VAR_038201. FT VARIANT 268 268 E -> K (in CSNU1; reduction in amino acid FT transport activity). FT /FTId=VAR_011422. FT VARIANT 341 341 T -> A (in CSNU1; reduction in amino acid FT transport activity). FT /FTId=VAR_011423. FT VARIANT 362 362 R -> C (in CSNU1). FT /FTId=VAR_022601. FT VARIANT 362 362 R -> H (in CSNU1). FT /FTId=VAR_038202. FT VARIANT 365 365 R -> W (in CSNU1). FT /FTId=VAR_011424. FT VARIANT 398 398 G -> R (in CSNU1). FT /FTId=VAR_038203. FT VARIANT 452 452 R -> W (in CSNU1). FT /FTId=VAR_011425. FT VARIANT 461 461 Y -> H (in CSNU1). FT /FTId=VAR_011426. FT VARIANT 467 467 M -> K (in CSNU1). FT /FTId=VAR_011428. FT VARIANT 467 467 M -> T (in CSNU1; loss of 80% of amino FT acid transport activity). FT /FTId=VAR_011427. FT VARIANT 481 481 G -> V (in CSNU1). FT /FTId=VAR_038204. FT VARIANT 482 482 E -> K (in CSNU1). FT /FTId=VAR_038205. FT VARIANT 508 508 P -> A (in CSNU1). FT /FTId=VAR_022602. FT VARIANT 510 510 Q -> R (in CSNU1). FT /FTId=VAR_038206. FT VARIANT 582 582 Y -> H (in CSNU1). FT /FTId=VAR_011429. FT VARIANT 584 584 R -> T (in CSNU1). FT /FTId=VAR_038207. FT VARIANT 599 599 F -> S (in CSNU1). FT /FTId=VAR_038208. FT VARIANT 600 600 G -> E (in CSNU1). FT /FTId=VAR_038209. FT VARIANT 615 615 P -> T (in CSNU1). FT /FTId=VAR_011430. FT VARIANT 618 618 M -> I (in dbSNP:rs698761). FT /FTId=VAR_011431. FT VARIANT 648 648 F -> S (in CSNU1). FT /FTId=VAR_011432. FT VARIANT 652 652 T -> R (in CSNU1). FT /FTId=VAR_011433. FT VARIANT 678 678 L -> P (in CSNU1). FT /FTId=VAR_011434. 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 //