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P82251 (BAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
b(0,+)-type amino acid transporter 1

Short name=b(0,+)AT1
Alternative name(s):
Glycoprotein-associated amino acid transporter b0,+AT1
Solute carrier family 7 member 9
Gene names
Name:SLC7A9
Synonyms:BAT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1

Subunit structure

Disulfide-linked heterodimer with the amino acid transport protein SLC3A1. Interacts with CAV1 By similarity. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.7.

Tissue specificity

Expressed in the brush border membrane in the kidney (at protein level). Kidney, small intestine, liver and placenta. Ref.1 Ref.7

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.4 Ref.8 Ref.9 Ref.10

Sequence similarities

Belongs to the amino acid-polyamine-organocation (APC) superfamily.

Ontologies

Keywords
   Biological processAmino-acid transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCystinuria
Disease mutation
   DomainTransmembrane
Transmembrane helix
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-cystine transport

Traceable author statement Ref.1. Source: GOC

amino acid transport

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular amino acid metabolic process

Traceable author statement Ref.1. Source: ProtInc

ion transport

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

neutral amino acid transport

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex assembly

Traceable author statement PubMed 10799513. Source: ProtInc

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement PubMed 10799513. Source: ProtInc

   Cellular_componentbrush border membrane

Inferred from direct assay Ref.7. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionL-cystine transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

amino acid transmembrane transporter activity

Traceable author statement PubMed 10799513. Source: ProtInc

neutral amino acid transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

peptide antigen binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487b(0,+)-type amino acid transporter 1
PRO_0000054258

Regions

Topological domain1 – 2929Cytoplasmic Potential
Transmembrane30 – 5021Helical; Potential
Topological domain51 – 6010Extracellular Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 9918Cytoplasmic Potential
Transmembrane100 – 12021Helical; Potential
Topological domain121 – 14828Extracellular Potential
Transmembrane149 – 16921Helical; Potential
Topological domain170 – 1789Cytoplasmic Potential
Transmembrane179 – 19921Helical; Potential
Topological domain200 – 21011Extracellular Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 25120Cytoplasmic Potential
Transmembrane252 – 27221Helical; Potential
Topological domain273 – 29624Extracellular Potential
Transmembrane297 – 31721Helical; Potential
Topological domain318 – 34831Cytoplasmic Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 3745Extracellular Potential
Transmembrane375 – 39521Helical; Potential
Topological domain396 – 40914Cytoplasmic Potential
Transmembrane410 – 43021Helical; Potential
Topological domain431 – 4344Extracellular Potential
Transmembrane435 – 45521Helical; Potential
Topological domain456 – 48732Cytoplasmic Potential

Natural variations

Natural variant101Missing in CSNU. Ref.8
VAR_018997
Natural variant441I → T in CSNU; type I. Ref.4
VAR_014363
Natural variant521P → L in CSNU. Ref.8
VAR_018998
Natural variant631G → R in CSNU. Ref.8
VAR_018999
Natural variant691W → L in CSNU. Ref.8
VAR_019000
Natural variant701A → V in CSNU; mild loss of amino acid transport activity. Ref.8
VAR_019001
Natural variant1051G → R in CSNU; type III; frequent mutation; severe loss of amino acid transport activity. Ref.1 Ref.8 Ref.9
Corresponds to variant rs121908480 [ dbSNP | Ensembl ].
VAR_010256
Natural variant1231T → M in CSNU. Ref.8
Corresponds to variant rs79987078 [ dbSNP | Ensembl ].
VAR_019002
Natural variant1261A → T in CSNU. Ref.8
VAR_019003
Natural variant1421V → A.
Corresponds to variant rs12150889 [ dbSNP | Ensembl ].
VAR_048153
Natural variant1581A → AA in CSNU. Ref.8
VAR_019004
Natural variant1701V → M in CSNU; type III; frequent mutation; complete loss of amino acid transport activity. Ref.1 Ref.8
VAR_010257
Natural variant1821A → T in CSNU; type III; frequent mutation; mild loss of amino acid transport activity. Ref.1 Ref.8 Ref.10
Corresponds to variant rs79389353 [ dbSNP | Ensembl ].
VAR_010258
Natural variant1871I → F in CSNU. Ref.8
VAR_019005
Natural variant1931I → II in CSNU. Ref.8
VAR_019006
Natural variant1951G → R in CSNU; type III. Ref.1 Ref.8
VAR_010259
Natural variant2231L → M. Ref.4
Corresponds to variant rs1007160 [ dbSNP | Ensembl ].
VAR_019007
Natural variant2241A → V in CSNU; non-classic type I. Ref.9
VAR_022603
Natural variant2301W → R in CSNU. Ref.8
VAR_019008
Natural variant2411I → T in CSNU. Ref.8
VAR_019009
Natural variant2441Missing in CSNU. Ref.8
VAR_019010
Natural variant2591G → R in CSNU; type III. Ref.1 Ref.8
VAR_010260
Natural variant2611P → L in CSNU; types I and III. Ref.4 Ref.10
VAR_014364
Natural variant3301V → M in CSNU; type III. Ref.10
VAR_015885
Natural variant3311A → V in CSNU; non-classic type I. Ref.9
VAR_022604
Natural variant3331R → W in CSNU; frequent mutation; severe loss of amino acid transport activity. Ref.8
VAR_019011
Natural variant3541A → T in CSNU; type III; severe loss of amino acid transport activity. Ref.4 Ref.8
VAR_014365
Natural variant3791S → R in CSNU. Ref.8
VAR_019012
Natural variant3821A → T in CSNU. Ref.8
VAR_019013

Experimental info

Sequence conflict521P → S in CAB54003. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P82251 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EF2C30DDE15594F1

FASTA48753,481
        10         20         30         40         50         60 
MGDTGLRKRR EDEKSIQSQE PKTTSLQKEL GLISGISIIV GTIIGSGIFV SPKSVLSNTE 

        70         80         90        100        110        120 
AVGPCLIIWA ACGVLATLGA LCFAELGTMI TKSGGEYPYL MEAYGPIPAY LFSWASLIVI 

       130        140        150        160        170        180 
KPTSFAIICL SFSEYVCAPF YVGCKPPQIV VKCLAAAAIL FISTVNSLSV RLGSYVQNIF 

       190        200        210        220        230        240 
TAAKLVIVAI IIISGLVLLA QGNTKNFDNS FEGAQLSVGA ISLAFYNGLW AYDGWNQLNY 

       250        260        270        280        290        300 
ITEELRNPYR NLPLAIIIGI PLVTACYILM NVSYFTVMTA TELLQSQAVA VTFGDRVLYP 

       310        320        330        340        350        360 
ASWIVPLFVA FSTIGAANGT CFTAGRLIYV AGREGHMLKV LSYISVRRLT PAPAIIFYGI 

       370        380        390        400        410        420 
IATIYIIPGD INSLVNYFSF AAWLFYGLTI LGLIVMRFTR KELERPIKVP VVIPVLMTLI 

       430        440        450        460        470        480 
SVFLVLAPII SKPTWEYLYC VLFILSGLLF YFLFVHYKFG WAQKISKPIT MHLQMLMEVV 


PPEEDPE 

« Hide

References

« Hide 'large scale' references
[1]"Non-type I cystinuria caused by mutations in SLC7A9, encoding a subunit (b0,+AT) of rBAT."
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 D.L., Pras E., Gasparini P., Bisceglia L., Beccia E., Gallucci M. expand/collapse author list , De Sanctis L., Ponzone A., Rizzoni G.F., Zelante L., Bassi M.T., George A.L. Jr., Manzoni M., De Grandi A., Riboni M., Endsley J.K., Ballabio A., Borsani G., Reig N., Fernandez E., Estevez R., Pineda M., Torrents D., Camps M., Lloberas J., Zorzano A., Palacin M.
Nat. Genet. 23:52-57(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CSNU ARG-105; MET-170; THR-182; ARG-195 AND ARG-259, CHARACTERIZATION OF VARIANT CSNU MET-170, FUNCTION, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"Luminal heterodimeric amino acid transporter defective in cystinuria."
Pfeiffer R., Loffing J., Rossier G., Bauch C., Meier C., Eggermann T., Loffing-Cueni D., Kuehn L.C., Verrey F.
Mol. Biol. Cell 10:4135-4147(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"Human cystinuria-related transporter: localization and functional characterization."
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.
Kidney Int. 59:1821-1833(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[4]"SLC7A9 mutations in all three cystinuria subtypes."
Leclerc D., Boutros M., Suh D., Wu Q., Palacin M., Ellis J.R., Goodyer P., Rozen R.
Kidney Int. 62:1550-1559(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CSNU THR-44; LEU-261 AND THR-354, VARIANT MET-223.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[7]"rBAT-b(0,+)AT heterodimer is the main apical reabsorption system for cystine in the kidney."
Fernandez E., Carrascal M., Rousaud F., Abian J., Zorzano A., Palacin M., Chillaron J.
Am. J. Physiol. 283:F540-F548(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Functional analysis of mutations in SLC7A9, and genotype-phenotype correlation in non-type I cystinuria."
Font M., Feliubadalo L., Estivill X., Nunes V., Golomb E., Kreiss Y., Pras E., Bisceglia L., d'Adamo A.P., Zelante L., Gasparini P., Bassi M.T., George A.L. Jr., Manzoni M., Riboni M., Ballabio A., Borsani G., Reig N. expand/collapse author list , Fernandez E., Zorzano A., Bertran J., Palacin M.
Hum. Mol. Genet. 10:305-316(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CSNU ARG-10 DEL; LEU-52; ARG-63; LEU-69; VAL-70; ARG-105; MET-123; THR-126; ALA-158 INS; MET-170; THR-182; PHE-187; ILE-193 INS; ARG-195; ARG-230; THR-241; GLU-244 DEL; ARG-259; TRP-333; THR-354; ARG-379 AND THR-382, CHARACTERIZATION OF VARIANTS CSNU VAL-70; ARG-105; MET-170; THR-182; TRP-333 AND THR-354.
[9]"Cystinuria in children: distribution and frequencies of mutations in the SLC3A1 and SLC7A9 genes."
Botzenhart E., Vester U., Schmidt C., Hesse A., Halber M., Wagner C., Lang F., Hoyer P., Zerres K., Eggermann T.
Kidney Int. 62:1136-1142(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CSNU ARG-105; VAL-224 AND VAL-331.
[10]"Mutation analysis of SLC7A9 in cystinuria patients in Sweden."
Harnevik L., Fjellstedt E., Molbaek A., Denneberg T., Soderkvist P.
Genet. Test. 7:13-20(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CSNU THR-182; LEU-261 AND MET-330.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF141289 mRNA. Translation: AAD55898.1.
AJ249199 mRNA. Translation: CAB54003.1.
AB033548 mRNA. Translation: BAB16840.1.
AF421181 expand/collapse EMBL AC list , AF421170, AF421171, AF421172, AF421173, AF421174, AF421175, AF421176, AF421177, AF421178, AF421179, AF421180 Genomic DNA. Translation: AAN40878.1.
AK313708 mRNA. Translation: BAG36453.1.
BC017962 mRNA. Translation: AAH17962.1.
CCDSCCDS12425.1.
RefSeqNP_001119807.1. NM_001126335.1.
NP_001229965.1. NM_001243036.1.
NP_055085.1. NM_014270.4.
UniGeneHs.743345.

3D structure databases

ProteinModelPortalP82251.
SMRP82251. Positions 30-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116309. 2 interactions.
IntActP82251. 2 interactions.
MINTMINT-3023541.
STRING9606.ENSP00000023064.

Chemistry

DrugBankDB00138. L-Cystine.

Protein family/group databases

TCDB2.A.3.8.19. the amino acid-polyamine-organocation (apc) family.

PTM databases

PhosphoSiteP82251.

Polymorphism databases

DMDM12585187.

Proteomic databases

PRIDEP82251.

Protocols and materials databases

DNASU11136.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000023064; ENSP00000023064; ENSG00000021488.
ENST00000587772; ENSP00000468439; ENSG00000021488.
ENST00000590341; ENSP00000464822; ENSG00000021488.
GeneID11136.
KEGGhsa:11136.
UCSCuc002ntu.4. human.

Organism-specific databases

CTD11136.
GeneCardsGC19M033321.
HGNCHGNC:11067. SLC7A9.
HPAHPA042591.
MIM220100. phenotype.
604144. gene.
neXtProtNX_P82251.
Orphanet93613. Cystinuria type B.
PharmGKBPA35927.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0531.
HOGENOMHOG000098892.
HOVERGENHBG000476.
InParanoidP82251.
KOK13868.
OMASFSEYVC.
OrthoDBEOG73BVCR.
PhylomeDBP82251.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_19419. Amino acid and oligopeptide SLC transporters.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP82251.
BgeeP82251.
CleanExHS_BAT1.
HS_SLC7A9.
GenevestigatorP82251.

Family and domain databases

InterProIPR002293. AA/rel_permease1.
[Graphical view]
PANTHERPTHR11785. PTHR11785. 1 hit.
PfamPF13520. AA_permease_2. 1 hit.
[Graphical view]
PIRSFPIRSF006060. AA_transporter. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi11136.
NextBio42332.
PROP82251.
SOURCESearch...

Entry information

Entry nameBAT1_HUMAN
AccessionPrimary (citable) accession number: P82251
Secondary accession number(s): B2R9A6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM