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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:27
Primary Accession Number DB00138
Secondary Accession Number
  • NUTR00023
Name L-Cystine
Drug Type
  • Approved
  • Nutraceutical
  • Small Molecule
Description A covalently linked dimeric nonessential amino acid formed by the oxidation of cysteine. Two molecules of cysteine are joined together by a disulfide bridge to form cystine. [PubChem]
Synonyms
  1. (-)-Cystine
  2. Cysteine disulfide
  3. Cystine acid
  4. L-Dicysteine
  5. L-alpha-Diamino-beta-dithiolactic acid
Brand Names Not Available
Brand Mixtures Not Available
Chemical IUPAC Name (2R)-2-amino-3-[(2R)-2-amino-3-hydroxy-3-oxopropyl]disulfanylpropanoic acid
Chemical Formula C6H12N2O4S2
Chemical Structure Structure
CAS Registry Number 56-89-3
InChI Identifier InChI=1/C6H12N2O4S2/c7-3(5(9)10)1-13-14-2-4(8)6(11)12/h3-4H,1-2,7-8H2,(H,9,10)(H,11,12)/t3-,4-/m0/s1/f/h9,11H
InChI Key LEVWYRKDKASIDU-JYGOYGMTDR
KEGG Drug D03636 Link Image
KEGG Compound C00491 Link Image
PubChem Compound 67678 Link Image
PubChem Substance 3774 Link Image
ChEBI ID 16283 Link Image
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link http://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/lcy_0088.shtml Link Image
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 240.3000
Monoisotopic Molecular Weight 240.0238
State Solid
Melting Point 260-261 oC
Experimental Water Solubility Soluble Source: PhysProp
Predicted Water Solubility 1.68e+01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -5.5 Source: PhysProp
Predicted LogP -3.16 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -1.16 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1SSQ Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES N[C@@H](CSSC[C@H](N)C(O)=O)C(O)=O
Canonical SMILES NC(CSSCC(N)C(O)=O)C(O)=O
Drug Category
  • Dietary supplement
  • Micronutrient
  • Non-Essential Amino Acids
ATC Codes Not Available
AHFS Codes Not Available
Indication It has been claimed that L-cysteine has anti-inflammatory properties, that it can protect against various toxins, and that it might be helpful in osteoarthritis and rheumatoid arthritis. More research will have to be done before L-cysteine can be indicated for any of these conditions. Research to date has mostly been in animal models.
Pharmacology L-Cystine is a covalently linked dimeric nonessential amino acid formed by the oxidation of cysteine. Two molecules of cysteine are joined together by a disulfide bridge to form cystine. Cystine is a chemical substance which naturally occurs as a deposit in the urine, and can form a calculus (hard mineral formation) when deposited in the kidney. The compound produced when two cysteine molecules linked by a disulfide (S-S) bond. Cystine is required for proper vitamin B6 utilization and is also helpful in the healing of burns and wounds, breaking down mucus deposits in illnesses such as bronchitis as well as cystic fibrosis. Cysteine also assists in the supply of insulin to the pancreas, which is needed for the assimilation of sugars and starches. It increases the level of glutathione in the lungs, liver, kidneys and bone marrow, and this may have an anti-aging effect on the body by reducing age-spots etc.
Mechanism of Action Certain conditions, e.g. an acetaminophen overdose, deplete hepatic glutathione and subject the tissues to oxidative stress resulting in loss of cellular integrity. L-Cystine serves as a major precursor for synthesis of glutathione.
Absorption Not Available
Toxicity With typical doses of 1 to 1.5 grams daily, the most commonly reported side effects have been gastrointestinal, such as nausea. There are rare reports of cystine renal stone formation, Single injections of L-cysteine (0.6-1.5 g/kg) into 4-day-old pups resulted in massive damage to cortical neurons, permanent retinal dystrophy, atrophy of the brain and hyperactivity.
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms Not Available
Patient Information Not Available
Contraindications Show Link Image
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. PDRhealth Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Cystine/glutamate transporter
  2. Cystinosin
  3. Neutral and basic amino acid transport protein rBAT
  4. B(0,+)-type amino acid transporter 1
Drug Target 1 [top]
Target 1 ID 33
Target 1 Name Cystine/glutamate transporter
Target 1 Synonyms
  1. Amino acid transport system xc-
  2. Calcium channel blocker resistance protein CCBR1
  3. xCT
Target 1 Gene Name SLC7A11
Target 1 Protein Sequence >Cystine/glutamate transporter 
MVRKPVVSTISKGGYLQGNVNGRLPSLGNKEPPGQEKVQLKRKVTLLRGVSIIIGTIIGA
GIFISPKGVLQNTGSVGMSLTIWTVCGVLSLFGALSYAELGTTIKKSGGHYTYILEVFGP
LPAFVRVWVELLIIRPAATAVISLAFGRYILEPFFIQCEIPELAIKLITAVGITVVMVLN
SMSVSWSARIQIFLTFCKLTAILIIIVPGVMQLIKGQTQNFKDAFSGRDSSITRLPLAFY
YGMYAYAGWFYLNFVTEEVENPEKTIPLAICISMAIVTIGYVLTNVAYFTTINAEELLLS
NAVAVTFSERLLGNFSLAVPIFVALSCFGSMNGGVFAVSRLFYVASREGHLPEILSMIHV
RKHTPLPAVIVLHPLTMIMLFSGDLDSLLNFLSFARWLFIGLAVAGLIYLRYKCPDMHRP
FKVPLFIPALFSFTCLFMVALSLYSDPFSTGIGFVITLTGVPAYYLFIIWDKKPRWFRIM
SEKITRTLQIILEVVPEEDKL
Target 1 Number of Residues 509
Target 1 Molecular Weight 55424
Target 1 Theoretical pI 9.51
Target 1 GO Classification
Function
amino acid permease activity
transporter activity
amine transporter activity
amino acid transporter activity
amino acid-polyamine transporter activity
Process
physiological process
cellular physiological process
transport
amine transport
amino acid transport
Component
intrinsic to membrane
integral to membrane
cell
membrane
Target 1 General Function Amino acid transport and metabolism
Target 1 Specific Function Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 44-64
  • 76-96
  • 136-156
  • 159-179
  • 190-210
  • 235-255
  • 266-286
  • 318-338
  • 365-385
  • 388-408
  • 423-443
  • 450-470
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 5668545 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q9UPY5 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name XCT_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein (Probable)
Target 1 Gene Sequence >1506 bp 
ATGGTCAGAAAGCCTGTTGTGTCCACCATCTCCAAAGGAGGTTACCTGCAGGGAAATGTT
AACGGGAGGCTGCCTTCCCTGGGCAACAAGGAGCCACCTGGGCAGGAGAAAGTGCAGCTG
AAGAGGAAAGTCACTTTACTGAGGGGAGTCTCCATTATCATTGGCACCATCATTGGAGCA
GGAATCTTCATCTCTCCTAAGGGCGTGCTCCAGAACACGGGCAGCGTGGGCATGTCTCTG
ACCATCTGGACGGTGTGTGGGGTCCTGTCACTATTTGGAGCTTTGTCTTATGCTGAATTG
GGAACAACTATAAAGAAATCTGGAGGTCATTACACATATATTTTGGAAGTCTTTGGTCCA
TTACCAGCTTTTGTACGAGTCTGGGTGGAACTCCTCATAATACGCCCTGCAGCTACTGCT
GTGATATCCCTGGCATTTGGACGCTACATTCTGGAACCATTTTTTATTCAATGTGAAATC
CCTGAACTTGCGATCAAGCTCATTACAGCTGTGGGCATAACTGTAGTGATGGTCCTAAAT
AGCATGAGTGTCAGCTGGAGCGCCCGGATCCAGATTTTCTTAACCTTTTGCAAGCTCACA
GCAATTCTGATAATTATAGTCCCTGGAGTTATGCAGCTAATTAAAGGTCAAACGCAGAAC
TTTAAAGACGCGTTTTCAGGAAGAGATTCAAGTATTACGCGGTTGCCACTGGCTTTTTAT
TATGGAATGTATGCATATGCTGGCTGGTTTTACCTCAACTTTGTTACTGAAGAAGTAGAA
AACCCTGAAAAAACCATTCCCCTTGCAATATGTATATCCATGGCCATTGTCACCATTGGC
TATGTGCTGACAAATGTGGCCTACTTTACGACCATTAATGCTGAGGAGCTGCTGCTTTCA
AATGCAGTGGCAGTGACCTTTTCTGAGCGGCTACTGGGAAATTTCTCATTAGCAGTTCCG
ATCTTTGTTGCCCTCTCCTGCTTTGGCTCCATGAACGGTGGTGTGTTTGCTGTCTCCAGG
TTATTCTATGTTGCGTCTCGAGAGGGTCACCTTCCAGAAATCCTCTCCATGATTCATGTC
CGCAAGCACACTCCTCTACCAGCTGTTATTGTTTTGCACCCTTTGACAATGATAATGCTC
TTCTCTGGAGACCTCGACAGTCTTTTGAATTTCCTCAGTTTTGCCAGGTGGCTTTTTATT
GGGCTGGCAGTTGCTGGGCTGATTTATCTTCGATACAAATGCCCAGATATGCATCGTCCT
TTCAAGGTGCCACTGTTCATCCCAGCTTTGTTTTCCTTCACATGCCTCTTCATGGTTGCC
CTTTCCCTCTATTCGGACCCATTTAGTACAGGGATTGGCTTCGTCATCACTCTGACTGGA
GTCCCTGCGTATTATCTCTTTATTATATGGGACAAGAAACCCAGGTGGTTTAGAATAATG
TCAGAGAAAATAACCAGAACATTACAAATAATACTGGAAGTTGTACCAGAAGAAGATAAG
TTATGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID SLC7A11 Link Image
Target 1 GenAtlas ID SLC7A11 Link Image
Target 1 HGNC ID HGNC:11059 Link Image
Target 1 Chromosome Location 4
Target 1 Locus 4q28-q32
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Sato H, Tamba M, Kuriyama-Matsumura K, Okuno S, Bannai S: Molecular cloning and expression of human xCT, the light chain of amino acid transport system xc-. Antioxid Redox Signal. 2000 Winter;2(4):665-71. [PubMed Link Image]
Target 1 Drug References
  1. Tomi M, Hosoya K, Takanaga H, Ohtsuki S, Terasaki T: Induction of xCT gene expression and L-cystine transport activity by diethyl maleate at the inner blood-retinal barrier. Invest Ophthalmol Vis Sci. 2002 Mar;43(3):774-9. [PubMed Link Image]
  2. Hosoya K, Tomi M, Ohtsuki S, Takanaga H, Saeki S, Kanai Y, Endou H, Naito M, Tsuruo T, Terasaki T: Enhancement of L-cystine transport activity and its relation to xCT gene induction at the blood-brain barrier by diethyl maleate treatment. J Pharmacol Exp Ther. 2002 Jul;302(1):225-31. [PubMed Link Image]
  3. Ruiz E, Siow RC, Bartlett SR, Jenner AM, Sato H, Bannai S, Mann GE: Vitamin C inhibits diethylmaleate-induced L-cystine transport in human vascular smooth muscle cells. Free Radic Biol Med. 2003 Jan 1;34(1):103-10. [PubMed Link Image]
  4. Tomi M, Funaki T, Abukawa H, Katayama K, Kondo T, Ohtsuki S, Ueda M, Obinata M, Terasaki T, Hosoya K: Expression and regulation of L-cystine transporter, system xc-, in the newly developed rat retinal Muller cell line (TR-MUL). Glia. 2003 Sep;43(3):208-17. [PubMed Link Image]
  5. Bridges CC, Zalups RK: Cystine and glutamate transport in renal epithelial cells transfected with human system x(-) (c). Kidney Int. 2005 Aug;68(2):653-64. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 38
Target 2 Name Cystinosin
Target 2 Synonyms Not Available
Target 2 Gene Name CTNS
Target 2 Protein Sequence >Cystinosin 
MIRNWLTIFILFPLKLVEKCESSVSLTVPPVVKLENGSSTNVSLTLRPPLNATLVITFEI
TFRSKNITILELPDEVVVPPGVTNSSFQVTSQNVGQLTVYLHGNHSNQTGPRIRFLVIRS
SAISIINQVIGWIYFVAWSISFYPQVIMNWRRKSVIGLSFDFVALNLTGFVAYSVFNIGL
LWVPYIKEQFLLKYPNGVNPVNSNDVFFSLHAVVLTLIIIVQCCLYERGGQRVSWPAIGF
LVLAWLFAFVTMIVAAVGVITWLQFLFCFSYIKLAVTLVKYFPQAYMNFYYKSTEGWSIG
NVLLDFTGGSFSLLQMFLQSYNNDQWTLIFGDPTKFGLGVFSIVFDVVFFIQHFCLYRKR
PGYDQLN
Target 2 Number of Residues 373
Target 2 Molecular Weight 41750
Target 2 Theoretical pI 9.21
Target 2 GO Classification Not Available
Target 2 General Function Involved in L-cystine transmembrane transporter activity
Target 2 Specific Function Thought to transport cystine out of lysosomes
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 122-142
  • 162-182
  • 206-226
  • 238-258
  • 262-282
  • 298-318
  • 336-356
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 3036851 Link Image
Target 2 UniProtKB/Swiss-Prot ID O60931 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CTNS_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Lysosome
  • lysosomal membrane
  • multi-pass membrane protein
Target 2 Gene Sequence >1104 bp 
ATGATAAGGAATTGGCTGACTATTTTTATCCTTTTTCCCCTGAAGCTCGTAGAGAAATGT
GAGTCAAGCGTCAGCCTCACTGTTCCTCCTGTCGTAAAGCTGGAGAACGGCAGCTCGACC
AACGTCAGCCTCACCCTGCGGCCACCATTAAATGCAACCCTGGTGATCACTTTTGAAATC
ACATTTCGTTCCAAAAATATTACTATCCTTGAGCTCCCCGATGAAGTTGTGGTGCCTCCT
GGAGTGACAAACTCCTCTTTTCAAGTGACATCTCAAAATGTTGGACAACTTACTGTTTAT
CTACATGGAAATCACTCCAATCAGACCGGCCCGAGGATACGCTTTCTTGTGATCCGCAGC
AGCGCCATTAGCATCATAAACCAGGTGATTGGCTGGATCTACTTTGTGGCCTGGTCCATC
TCCTTCTACCCTCAGGTGATCATGAATTGGAGGCGGAAAAGTGTCATTGGTCTGAGCTTC
GACTTCGTGGCTCTGAACCTGACAGGCTTCGTGGCCTACAGTGTATTCAACATCGGCCTC
CTCTGGGTGCCCTACATCAAGGAGCAGTTTCTCCTCAAATACCCCAACGGAGTGAACCCC
GTGAACAGCAACGACGTCTTCTTCAGCCTGCACGCGGTTGTCCTCACGCTGATCATCATC
GTGCAGTGCTGCCTGTATGAGCGCGGTGGCCAGCGCGTGTCCTGGCCTGCCATCGGCTTC
CTGGTGCTCGCGTGGCTCTTCGCATTTGTCACCATGATCGTGGCTGCAGTGGGAGTGATC
ACGTGGCTGCAGTTTCTCTTCTGCTTCTCCTACATCAAGCTCGCAGTCACGCTGGTCAAG
TATTTTCCACAGGCCTACATGAACTTTTACTACAAAAGCACTGAGGGCTGGAGCATTGGC
AACGTGCTCCTGGACTTCACCGGGGGCAGCTTCAGCCTCCTGCAGATGTTCCTCCAGTCC
TACAACAACGACCAGTGGACGCTGATCTTCGGAGACCCAACCAAGTTTGGACTCGGGGTC
TTCTCCATCGTCTTCGACGTCGTCTTCTTCATCCAGCACTTCTGTTTGTACAGAAAGAGA
CCGGGGTATGACCAGCTGAACTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID CTNS Link Image
Target 2 GenAtlas ID CTNS Link Image
Target 2 HGNC ID HGNC:2518 Link Image
Target 2 Chromosome Location 17
Target 2 Locus 17p13
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Anikster Y, Lucero C, Touchman JW, Huizing M, McDowell G, Shotelersuk V, Green ED, Gahl WA: Identification and detection of the common 65-kb deletion breakpoint in the nephropathic cystinosis gene (CTNS). Mol Genet Metab. 1999 Feb;66(2):111-6. [PubMed Link Image]
  2. Thoene J, Lemons R, Anikster Y, Mullet J, Paelicke K, Lucero C, Gahl W, Schneider J, Shu SG, Campbell HT: Mutations of CTNS causing intermediate cystinosis. Mol Genet Metab. 1999 Aug;67(4):283-93. [PubMed Link Image]
  3. McGowan-Jordan J, Stoddard K, Podolsky L, Orrbine E, McLaine P, Town M, Goodyer P, MacKenzie A, Heick H: Molecular analysis of cystinosis: probable Irish origin of the most common French Canadian mutation. Eur J Hum Genet. 1999 Sep;7(6):671-8. [PubMed Link Image]
  4. Attard M, Jean G, Forestier L, Cherqui S, van't Hoff W, Broyer M, Antignac C, Town M: Severity of phenotype in cystinosis varies with mutations in the CTNS gene: predicted effect on the model of cystinosin. Hum Mol Genet. 1999 Dec;8(13):2507-14. [PubMed Link Image]
  5. Anikster Y, Shotelersuk V, Gahl WA: CTNS mutations in patients with cystinosis. Hum Mutat. 1999;14(6):454-8. [PubMed Link Image]
  6. Touchman JW, Anikster Y, Dietrich NL, Maduro VV, McDowell G, Shotelersuk V, Bouffard GG, Beckstrom-Sternberg SM, Gahl WA, Green ED: The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion. Genome Res. 2000 Feb;10(2):165-73. [PubMed Link Image]
  7. Town M, Jean G, Cherqui S, Attard M, Forestier L, Whitmore SA, Callen DF, Gribouval O, Broyer M, Bates GP, van't Hoff W, Antignac C: A novel gene encoding an integral membrane protein is mutated in nephropathic cystinosis. Nat Genet. 1998 Apr;18(4):319-24. [PubMed Link Image]
  8. Shotelersuk V, Larson D, Anikster Y, McDowell G, Lemons R, Bernardini I, Guo J, Thoene J, Gahl WA: CTNS mutations in an American-based population of cystinosis patients. Am J Hum Genet. 1998 Nov;63(5):1352-62. [PubMed Link Image]
Target 2 Drug References
  1. Kalatzis V, Cherqui S, Antignac C, Gasnier B: Cystinosin, the protein defective in cystinosis, is a H(+)-driven lysosomal cystine transporter. EMBO J. 2001 Nov 1;20(21):5940-9. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1963
Target 3 Name Neutral and basic amino acid transport protein rBAT
Target 3 Synonyms
  1. B(0,+)-type amino acid transport protein
  2. D2H
  3. NBAT
Target 3 Gene Name SLC3A1
Target 3 Protein Sequence >Neutral and basic amino acid transport protein rBAT 
MAEDKSKRDSIEMSMKGCQTNNGFVHNEDILEQTPDPGSSTDNLKHSTRGILGSQEPDFK
GVQPYAGMPKEVLFQFSGQARYRIPREILFWLTVASVLVLIAATIAIIALSPKCLDWWQE
GPMYQIYPRSFKDSNKDGNGDLKGIQDKLDYITALNIKTVWITSFYKSSLKDFRYGVEDF
REVDPIFGTMEDFENLVAAIHDKGLKLIIDFIPNHTSDKHIWFQLSRTRTGKYTDYYIWH
DCTHENGKTIPPNNWLSVYGNSSWHFDEVRNQCYFHQFMKEQPDLNFRNPDVQEEIKEIL
RFWLTKGVDGFSLDAVKFLLEAKHLRDEIQVNKTQIPDTVTQYSELYHDFTTTQVGMHDI
VRSFRQTMDQYSTEPGRYRFMGTEAYAESIDRTVMYYGLPFIQEADFPFNNYLSMLDTVS
GNSVYEVITSWMENMPEGKWPNWMIGGPDSSRLTSRLGNQYVNVMNMLLFTLPGTPITYY
GEEIGMGNIVAANLNESYDINTLRSKSPMQWDNSSNAGFSEASNTWLPTNSDYHTVNVDV
QKTQPRSALKLYQDLSLLHANELLLNRGWFCHLRNDSHYVVYTRELDGIDRIFIVVLNFG
ESTLLNLHNMISGLPAKMRIRLSTNSADKGSKVDTSGIFLDKGEGLIFEHNTKNLLHRQT
AFRDRCFVSNRACYSSVLNILYTSC
Target 3 Number of Residues 696
Target 3 Molecular Weight 78853
Target 3 Theoretical pI 5.81
Target 3 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
amylase activity
alpha-amylase activity
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 3 General Function Carbohydrate transport and metabolism
Target 3 Specific 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
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 88-108
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 306442 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q07837 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name SLC31_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • single-pass type II membrane protein (Potential)
Target 3 Gene Sequence >2058 bp 
ATGGCTGAAGATAAAAGCAAGAGAGACTCCATCGAGATGAGTATGAAGGGATGCCAGACA
AACAACGGGTTTGTCCATAATGAAGACATTCTGGAGCAGACCCCGGATCCAGGCAGCTCA
ACAGACAACCTGAAGCACAGCACCAGGGGCATCCTTGGCTCCCAGGAGCCCGACTTCAAG
GGCGTCCAGCCCTATGCGGGGATGCCCAAGGAGGTGCTGTTCCAGTTCTCTGGCCAGGCC
CGCTACCGCATACCTCGGGAGATCCTCTTCTGGCTCACAGTGGCTTCTGTGCTGGTGCTC
ATCGCGGCCACCATAGCCATCATTGCCCTCTCTCCAAAGTGCCTAGACTGGTGGCAGGAG
GGGCCCATGTACCAGATCTACCCAAGGTCTTTCAAGGACAGTAACAAGGATGGGAACGGA
GATCTGAAAGGTATTCAAGATAAACTGGACTACATCACAGCTTTAAATATAAAAACTGTT
TGGATTACTTCATTTTATAAATCGTCCCTTAAAGATTTCAGATATGGTGTTGAAGATTTC
CGGGAAGTTGATCCCATTTTTGGAACGATGGAAGATTTTGAGAATCTGGTTGCAGCCATA
CATGATAAAGGTTTAAAATTAATCATCGATTTCATACCAAACCACACGAGTGATAAACAT
ATTTGGTTTCAATTGAGTCGGACACGGACAGGAAAATATACTGATTATTATATCTGGCAT
GACTGTACCCATGAAAATGGCAAAACCATTCCACCCAACAACTGGTTAAGTGTGTATGGA
AACTCCAGTTGGCACTTTGACGAAGTGCGAAACCAATGTTATTTTCATCAGTTTATGAAA
GAGCAACCTGATTTAAATTTCCGCAATCCTGATGTTCAAGAAGAAATAAAAGAAATTTTA
CGGTTCTGGCTCACAAAGGGTGTTGATGGTTTTAGTTTGGATGCTGTTAAATTCCTCCTA
GAAGCAAAGCACCTGAGAGATGAGATCCAAGTAAATAAGACCCAAATCCCGGACACGGTC
ACACAATACTCGGAGCTGTACCATGACTTCACCACCACGCAGGTGGGAATGCACGACATT
GTCCGCAGCTTCCGGCAGACCATGGACCAATACAGCACGGAGCCCGGCAGATACAGGTTC
ATGGGGACTGAAGCCTATGCAGAGAGTATTGACAGGACCGTGATGTACTATGGATTGCCA
TTTATCCAAGAAGCTGATTTTCCCTTCAACAATTACCTCAGCATGCTAGACACTGTTTCT
GGGAACAGCGTGTATGAGGTTATCACATCCTGGATGGAAAACATGCCAGAAGGAAAATGG
CCTAACTGGATGATTGGTGGACCAGACAGTTCACGGCTGACTTCGCGTTTGGGGAATCAG
TATGTCAACGTGATGAACATGCTTCTTTTCACACTCCCTGGAACTCCTATAACTTACTAT
GGAGAAGAAATTGGAATGGGAAATATTGTAGCCGCAAATCTCAATGAAAGCTATGATATT
AATACCCTTCGCTCAAAGTCACCAATGCAGTGGGACAATAGTTCAAATGCTGGTTTTTCT
GAAGCTAGTAACACCTGGTTACCTACCAATTCAGATTACCACACTGTGAATGTTGATGTC
CAAAAGACTCAGCCCAGATCGGCTTTGAAGTTATATCAAGATTTAAGTCTACTTCATGCC
AATGAGCTACTCCTCAACAGGGGCTGGTTTTGCCATTTGAGGAATGACAGCCACTATGTT
GTGTACACAAGAGAGCTGGATGGCATCGACAGAATCTTTATCGTGGTTCTGAATTTTGGA
GAATCAACACTGTTAAATCTACATAATATGATTTCGGGCCTTCCCGCTAAAATAAGAATA
AGGTTAAGTACCAATTCTGCCGACAAAGGCAGTAAAGTTGATACAAGTGGCATTTTTCTG
GACAAGGGAGAGGGACTCATCTTTGAACACAACACGAAGAATCTCCTTCATCGCCAAACA
GCTTTCAGAGATAGATGCTTTGTTTCCAATCGAGCATGCTATTCCAGTGTACTGAACATA
CTGTATACCTCGTGTTAG
Target 3 GenBank Gene ID
Target 3 GeneCard ID SLC3A1 Link Image
Target 3 GenAtlas ID SLC3A1 Link Image
Target 3 HGNC ID HGNC:11025 Link Image
Target 3 Chromosome Location 2
Target 3 Locus 2p16.3
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Pfeiffer R, Loffing J, Rossier G, Bauch C, Meier C, Eggermann T, Loffing-Cueni D, Kuhn LC, Verrey F: Luminal heterodimeric amino acid transporter defective in cystinuria. Mol Biol Cell. 1999 Dec;10(12):4135-47. [PubMed Link Image]
  2. Mizoguchi K, Cha SH, Chairoungdua A, Kim DK, 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. 2001 May;59(5):1821-33. [PubMed Link Image]
  3. Pras E, Raben N, Golomb E, Arber N, Aksentijevich I, Schapiro JM, Harel D, Katz G, Liberman U, Pras M, et al.: Mutations in the SLC3A1 transporter gene in cystinuria. Am J Hum Genet. 1995 Jun;56(6):1297-303. [PubMed Link Image]
  4. Calonge MJ, Volpini V, Bisceglia L, Rousaud F, de Sanctis L, Beccia E, Zelante L, Testar X, Zorzano A, Estivill X, et al.: 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. 1995 Oct 10;92(21):9667-71. [PubMed Link Image]
  5. Gasparini P, Calonge MJ, Bisceglia L, Purroy J, Dianzani I, Notarangelo A, Rousaud F, Gallucci M, Testar X, Ponzone A, et al.: Molecular genetics of cystinuria: identification of four new mutations and seven polymorphisms, and evidence for genetic heterogeneity. Am J Hum Genet. 1995 Oct;57(4):781-8. [PubMed Link Image]
  6. Miyamoto K, Katai K, Tatsumi S, Sone K, Segawa H, Yamamoto H, Taketani Y, Takada K, Morita K, Kanayama H, et al.: Mutations of the basic amino acid transporter gene associated with cystinuria. Biochem J. 1995 Sep 15;310 ( Pt 3):951-5. [PubMed Link Image]
  7. 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. 1993 Jul 15;268(20):14842-9. [PubMed Link Image]
  8. Calonge MJ, Gasparini P, Chillaron J, Chillon M, Gallucci M, Rousaud F, Zelante L, Testar X, Dallapiccola B, Di Silverio F, et al.: Cystinuria caused by mutations in rBAT, a gene involved in the transport of cystine. Nat Genet. 1994 Apr;6(4):420-5. [PubMed Link Image]
  9. Lee WS, Wells RG, Sabbag RV, Mohandas TK, Hediger MA: Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport. J Clin Invest. 1993 May;91(5):1959-63. [PubMed Link Image]
  10. 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. 1996 Jul 12;271(28):16758-63. [PubMed Link Image]
  11. 9186880 Endsley JK, Phillips JA 3rd, Hruska KA, Denneberg T, Carlson J, George AL Jr: Genomic organization of a human cystine transporter gene (SLC3A1) and identification of novel mutations causing cystinuria. Kidney Int. 1997 Jun;51(6):1893-9.
Target 3 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 3998
Target 4 Name B(0,+)-type amino acid transporter 1
Target 4 Synonyms
  1. 0,+)-type amino acid transporter 1 (B(0,+)AT
  2. Glycoprotein- associated amino acid transporter b0,+AT1
Target 4 Gene Name SLC7A9
Target 4 Protein Sequence >B(0,+)-type amino acid transporter 1 
MGDTGLRKRREDEKSIQSQEPKTTSLQKELGLISGISIIVGTIIGSGIFVSPKSVLSNTE
AVGPCLIIWAACGVLATLGALCFAELGTMITKSGGEYPYLMEAYGPIPAYLFSWASLIVI
KPTSFAIICLSFSEYVCAPFYVGCKPPQIVVKCLAAAAILFISTVNSLSVRLGSYVQNIF
TAAKLVIVAIIIISGLVLLAQGNTKNFDNSFEGAQLSVGAISLAFYNGLWAYDGWNQLNY
ITEELRNPYRNLPLAIIIGIPLVTACYILMNVSYFTVMTATELLQSQAVAVTFGDRVLYP
ASWIVPLFVAFSTIGAANGTCFTAGRLIYVAGREGHMLKVLSYISVRRLTPAPAIIFYGI
IATIYIIPGDINSLVNYFSFAAWLFYGLTILGLIVMRFTRKELERPIKVPVVIPVLMTLI
SVFLVLAPIISKPTWEYLYCVLFILSGLLFYFLFVHYKFGWAQKISKPITMHLQMLMEVV
PPEEDPE
Target 4 Number of Residues 495
Target 4 Molecular Weight 53482
Target 4 Theoretical pI 8.21
Target 4 GO Classification
Function
transporter activity
amine transporter activity
amino acid transporter activity
amino acid-polyamine transporter activity
Process
physiological process
cellular physiological process
transport
amine transport
amino acid transport
Component
cell
membrane
Target 4 General Function Amino acid transport and metabolism
Target 4 Specific Function Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system b(0,+)-like activity). Thought to be responsible for the high- affinity reabsorption of cystine in the kidney tubule
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • 30-50
  • 61-81
  • 100-120
  • 149-169
  • 179-199
  • 211-231
  • 252-272
  • 297-317
  • 349-369
  • 375-395
  • 410-430
  • 435-455
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 5916108 Link Image
Target 4 UniProtKB/Swiss-Prot ID P82251 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name BAT1_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Membrane
Target 4 Gene Sequence >1464 bp 
ATGGGGGATACTGGCCTGAGAAAGCGGAGAGAGGATGAGAAGTCGATCCAGAGCCAAGAG
CCTAAGACCACCAGTCTCCAAAAGGAGCTGGGCCTCATCAGTGGCATCTCCATCATCGTG
GGCACCATCATTGGCTCTGGGATCTTCGTTTCCCCCAAGTCTGTGCTCAGCAACACGGAA
GCTGTGGGGCCCTGCCTCATCATATGGGCGGCTTGCGGGGTCCTCGCGACGCTGGGTGCC
CTGTGCTTTGCGGAGCTTGGCACAATGATCACCAAGTCAGGGGGAGAGTATCCCTACCTG
ATGGAGGCCTACGGGCCCATCCCCGCCTACCTCTTCTCCTGGGCCAGCCTGATCGTCATT
AAGCCCACGTCCTTCGCCATCATCTGCCTCAGCTTCTCCGAGTATGTGTGTGCGCCCTTC
TATGTGGGCTGCAAGCCTCCTCAAATCGTTGTGAAATGCCTGGCCGCCGCCGCCATCTTG
TTCATCTCGACAGTGAACTCACTGAGCGTGCGGCTGGGAAGCTACGTCCAGAACATCTTC
ACCGCGGCCAAGCTGGTGATCGTGGCCATCATCATCATCAGCGGGCTGGTGCTCCTGGCC
CAAGGAAACACAAAGAATTTTGATAATTCTTTCGAGGGCGCCCAGCTGTCTGTGGGAGCC
ATCAGCCTGGCGTTTTACAATGGACTCTGGGCCTATGATGGATGGAATCAACTCAATTAC
ATCACAGAAGAACTTAGAAACCCTTACAGAAACCTGCCTTTGGCCATTATCATCGGGATC
CCCCTGGTGACGGCGTGCTACATCCTCATGAACGTGTCCTACTTCACCGTGATGACTGCC
ACCGAACTCCTGCAGTCCCAGGCGGTGGCTGTGACATTTGGTGACCGTGTTCTCTATCCT
GCTTCTTGGATCGTTCCACTTTTTGTGGCATTTTCAACCATCGGTGCTGCTAACGGGACC
TGCTTCACAGCGGGCAGACTCATTTACGTGGCGGGCCGGGAGGGTCACATGCTCAAAGTG
CTTTCTTACATCAGCGTCAGGCGCCTCACTCCAGCCCCCGCCATCATCTTTTATGGTATC
ATAGCAACGATTTATATCATCCCTGGTGACATAAACTCGTTAGTCAATTATTTCAGCTTT
GCTGCATGGCTGTTTTATGGCCTGACGATTCTAGGACTCATCGTGATGAGATTTACAAGG
AAAGAGCTGGAAAGGCCTATCAAGGTGCCCGTAGTCATTCCCGTCTTGATGACACTCATC
TCTGTGTTTTTGGTTCTGGCTCCAATCATCAGCAAGCCCACCTGGGAGTACCTCTACTGT
GTGCTGTTTATATTAAGCGGCCTTTTATTTTACTTCCTGTTTGTCCACTACAAGTTTGGA
TGGGCTCAGAAAATCTCAAAGCCGATTACCATGCACCTTCAGATGCTAATGGAAGTGGTC
CCACCGGAGGAAGACCCTGAGTAA
Target 4 GenBank Gene ID
Target 4 GeneCard ID SLC7A9 Link Image
Target 4 GenAtlas ID SLC7A9 Link Image
Target 4 HGNC ID HGNC:11067 Link Image
Target 4 Chromosome Location 19
Target 4 Locus 19q13.1
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Feliubadalo L, Font M, Purroy J, Rousaud F, Estivill X, Nunes V, Golomb E, Centola M, Aksentijevich I, Kreiss Y, Goldman B, Pras M, Kastner DL, Pras E, Gasparini P, Bisceglia L, Beccia E, Gallucci M, de Sanctis L, Ponzone A, Rizzoni GF, Zelante L, Bassi MT, George AL Jr, Manzoni M, De Grandi A, Riboni M, Endsley JK, Ballabio A, Borsani G, Reig N, Fernandez E, Estevez R, Pineda M, Torrents D, Camps M, Lloberas J, Zorzano A, Palacin M: Non-type I cystinuria caused by mutations in SLC7A9, encoding a subunit (bo,+AT) of rBAT. Nat Genet. 1999 Sep;23(1):52-7. [PubMed Link Image]
  2. Pfeiffer R, Loffing J, Rossier G, Bauch C, Meier C, Eggermann T, Loffing-Cueni D, Kuhn LC, Verrey F: Luminal heterodimeric amino acid transporter defective in cystinuria. Mol Biol Cell. 1999 Dec;10(12):4135-47. [PubMed Link Image]
  3. Mizoguchi K, Cha SH, Chairoungdua A, Kim DK, 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. 2001 May;59(5):1821-33. [PubMed Link Image]
  4. Leclerc D, Boutros M, Suh D, Wu Q, Palacin M, Ellis JR, Goodyer P, Rozen R: SLC7A9 mutations in all three cystinuria subtypes. Kidney Int. 2002 Nov;62(5):1550-9. [PubMed Link Image]
  5. Harnevik L, Fjellstedt E, Molbaek A, Denneberg T, Soderkvist P: Mutation analysis of SLC7A9 in cystinuria patients in Sweden. Genet Test. 2003 Spring;7(1):13-20. [PubMed Link Image]
Target 4 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.