P82251 (BAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
B(0,+)-type amino acid transporter 1
Short name=B(0,+)AT

Alternative name(s):
Glycoprotein-associated amino acid transporter b0,+AT1
Solute carrier family 7 member 9

Gene names

Name:	SLC7A9
Synonyms:	BAT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subcellular location	Membrane; Multi-pass membrane protein Probable.
Tissue specificity	Kidney, small intestine, liver and placenta. Ref.1
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.7 Ref.8 Ref.9
Sequence similarities	Belongs to the amino acid-polyamine-organocation (APC) superfamily.

Ontologies

Keywords
Biological process	Amino-acid transport Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Cystinuria Disease mutation
Domain	Transmembrane Transmembrane helix
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome cellular amino acid metabolic process Traceable author statement Ref.1. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome protein complex assembly Traceable author statement PubMed 10799513. Source: ProtInc
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	L-cystine transmembrane transporter activity Traceable author statement Ref.1. 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 487	487	B(0,+)-type amino acid transporter 1		PRO_0000054258
Regions
	Topological domain	1 – 29	29	Cytoplasmic Potential
	Transmembrane	30 – 50	21	Helical; Potential
	Topological domain	51 – 60	10	Extracellular Potential
	Transmembrane	61 – 81	21	Helical; Potential
	Topological domain	82 – 99	18	Cytoplasmic Potential
	Transmembrane	100 – 120	21	Helical; Potential
	Topological domain	121 – 148	28	Extracellular Potential
	Transmembrane	149 – 169	21	Helical; Potential
	Topological domain	170 – 178	9	Cytoplasmic Potential
	Transmembrane	179 – 199	21	Helical; Potential
	Topological domain	200 – 210	11	Extracellular Potential
	Transmembrane	211 – 231	21	Helical; Potential
	Topological domain	232 – 251	20	Cytoplasmic Potential
	Transmembrane	252 – 272	21	Helical; Potential
	Topological domain	273 – 296	24	Extracellular Potential
	Transmembrane	297 – 317	21	Helical; Potential
	Topological domain	318 – 348	31	Cytoplasmic Potential
	Transmembrane	349 – 369	21	Helical; Potential
	Topological domain	370 – 374	5	Extracellular Potential
	Transmembrane	375 – 395	21	Helical; Potential
	Topological domain	396 – 409	14	Cytoplasmic Potential
	Transmembrane	410 – 430	21	Helical; Potential
	Topological domain	431 – 434	4	Extracellular Potential
	Transmembrane	435 – 455	21	Helical; Potential
	Topological domain	456 – 487	32	Cytoplasmic Potential
Natural variations
	Natural variant	10	1	Missing in CSNU. Ref.7		VAR_018997
	Natural variant	44	1	I → T in CSNU; type I. Ref.4		VAR_014363
	Natural variant	52	1	P → L in CSNU. Ref.7		VAR_018998
	Natural variant	63	1	G → R in CSNU. Ref.7		VAR_018999
	Natural variant	69	1	W → L in CSNU. Ref.7		VAR_019000
	Natural variant	70	1	A → V in CSNU; mild loss of amino acid transport activity. Ref.7		VAR_019001
	Natural variant	105	1	G → R in CSNU; type III; frequent mutation; severe loss of amino acid transport activity. Ref.1 Ref.7 Ref.8		VAR_010256
	Natural variant	123	1	T → M in CSNU. Ref.7		VAR_019002
	Natural variant	126	1	A → T in CSNU. Ref.7		VAR_019003
	Natural variant	142	1	V → A. Corresponds to variant rs12150889 [ dbSNP | Ensembl ].		VAR_048153
	Natural variant	158	1	A → AA in CSNU. Ref.7		VAR_019004
	Natural variant	170	1	V → M in CSNU; type III; frequent mutation; complete loss of amino acid transport activity. Ref.1 Ref.7		VAR_010257
	Natural variant	182	1	A → T in CSNU; type III; frequent mutation; mild loss of amino acid transport activity. Ref.1 Ref.7 Ref.9		VAR_010258
	Natural variant	187	1	I → F in CSNU. Ref.7		VAR_019005
	Natural variant	193	1	I → II in CSNU. Ref.7		VAR_019006
	Natural variant	195	1	G → R in CSNU; type III. Ref.1 Ref.7		VAR_010259
	Natural variant	223	1	L → M. Ref.4 Corresponds to variant rs1007160 [ dbSNP | Ensembl ].		VAR_019007
	Natural variant	224	1	A → V in CSNU; non-classic type I. Ref.8		VAR_022603
	Natural variant	230	1	W → R in CSNU. Ref.7		VAR_019008
	Natural variant	241	1	I → T in CSNU. Ref.7		VAR_019009
	Natural variant	244	1	Missing in CSNU. Ref.7		VAR_019010
	Natural variant	259	1	G → R in CSNU; type III. Ref.1 Ref.7		VAR_010260
	Natural variant	261	1	P → L in CSNU; types I and III. Ref.4 Ref.9		VAR_014364
	Natural variant	330	1	V → M in CSNU; type III. Ref.9		VAR_015885
	Natural variant	331	1	A → V in CSNU; non-classic type I. Ref.8		VAR_022604
	Natural variant	333	1	R → W in CSNU; frequent mutation; severe loss of amino acid transport activity. Ref.7		VAR_019011
	Natural variant	354	1	A → T in CSNU; type III; severe loss of amino acid transport activity. Ref.4 Ref.7		VAR_014365
	Natural variant	379	1	S → R in CSNU. Ref.7		VAR_019012
	Natural variant	382	1	A → T in CSNU. Ref.7		VAR_019013
Experimental info
	Sequence conflict	52	1	P → S in CAB54003. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P82251 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: EF2C30DDE15594F1	FASTA	487	53,481
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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. , 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.
[8]	"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.
[9]	"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.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF141289 mRNA. Translation: AAD55898.1. AJ249199 mRNA. Translation: CAB54003.1. AB033548 mRNA. Translation: BAB16840.1. AF421181 , 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.
IPI	IPI00011357.
RefSeq	NP_001119807.1. NM_001126335.1. NP_001229965.1. NM_001243036.1. NP_055085.1. NM_014270.4.
UniGene	Hs.408567.
3D structure databases
ProteinModelPortal	P82251.
ModBase	Search...
Protein-protein interaction databases
IntAct	P82251. 1 interaction.
STRING	9606.ENSP00000023064.
PTM databases
PhosphoSite	P82251.
Polymorphism databases
DMDM	12585187.
Proteomic databases
PRIDE	P82251.
Protocols and materials databases
DNASU	11136.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000023064; ENSP00000023064; ENSG00000021488. ENST00000587772; ENSP00000468439; ENSG00000021488. ENST00000590341; ENSP00000464822; ENSG00000021488.
GeneID	11136.
KEGG	hsa:11136.
UCSC	uc002ntu.4. human.
Organism-specific databases
CTD	11136.
GeneCards	GC19M033321.
HGNC	HGNC:11067. SLC7A9.
HPA	HPA042591.
MIM	220100. phenotype. 604144. gene.
neXtProt	NX_P82251.
Orphanet	93613. Cystinuria type B.
PharmGKB	PA35927.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0531.
HOGENOM	HOG000098892.
HOVERGEN	HBG000476.
InParanoid	P82251.
KO	K13868.
OMA	ERNGSTQ.
OrthoDB	EOG4P8FJ2.
PhylomeDB	P82251.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules. REACT_19419. Amino acid and oligopeptide SLC transporters. REACT_604. Hemostasis.
Gene expression databases
Bgee	P82251.
CleanEx	HS_BAT1. HS_SLC7A9.
Genevestigator	P82251.
GermOnline	ENSG00000021488. Homo sapiens.
Family and domain databases
InterPro	IPR002293. AA/rel_permease1. [Graphical view]
PANTHER	PTHR11785. PTHR11785. 1 hit.
PIRSF	PIRSF006060. AA_transporter. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00138. L-Cystine.
GenomeRNAi	11136.
NextBio	42332.
SOURCE	Search...

Entry information

Entry name

BAT1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.