Cystine/glutamate transporter - Homo sapiens (Human)

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Q9UPY5 (XCT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cystine/glutamate transporter

Alternative name(s):
Amino acid transport system xc-
Calcium channel blocker resistance protein CCBR1
Solute carrier family 7 member 11
xCT

Gene names

Name:

SLC7A11

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate. Ref.6
Subunit structure	Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc By similarity.
Subcellular location	Membrane; Multi-pass membrane protein Ref.6.
Sequence similarities	Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family. [View classification]

Ontologies

Keywords
Biological process	Amino-acid transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome leukocyte migration Traceable author statement. Source: Reactome response to toxin Inferred from direct assay. Source: UniProtKB
Cellular component	integral to membrane Traceable author statement. Source: ProtInc plasma membrane Traceable author statement. Source: Reactome
Molecular function	cystine:glutamate antiporter activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CD44	P16070	4	EBI-3843348,EBI-490245

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 501

501

Cystine/glutamate transporter

PRO_0000054279

Regions

Topological domain

1 – 43

Cytoplasmic Potential

Transmembrane

44 – 64

Helical; Potential

Topological domain

65 – 74

Extracellular Potential

Transmembrane

75 – 95

Helical; Potential

Topological domain

96 – 113

Cytoplasmic Potential

Transmembrane

114 – 134

Helical; Potential

Topological domain

135 – 158

Extracellular Potential

Transmembrane

159 – 179

Helical; Potential

Topological domain

180 – 189

Cytoplasmic Potential

Transmembrane

190 – 210

Helical; Potential

Topological domain

211 – 234

Extracellular Potential

Transmembrane

235 – 255

Helical; Potential

Topological domain

256 – 265

Cytoplasmic Potential

Transmembrane

266 – 286

Helical; Potential

Topological domain

287 – 317

Extracellular Potential

Transmembrane

318 – 338

Helical; Potential

Topological domain

339 – 364

Cytoplasmic Potential

Transmembrane

365 – 385

Helical; Potential

Topological domain

386 – 387

Extracellular Potential

Transmembrane

388 – 408

Helical; Potential

Topological domain

409 – 422

Cytoplasmic Potential

Transmembrane

423 – 443

Helical; Potential

Topological domain

444 – 449

Extracellular Potential

Transmembrane

450 – 470

Helical; Potential

Topological domain

471 – 501

Cytoplasmic Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.7 Ref.8 Ref.9

Glycosylation

314

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9UPY5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3EF2648B94A9F59E
Show »

FASTA

501

55,423

        10         20         30         40         50         60 
MVRKPVVSTI SKGGYLQGNV NGRLPSLGNK EPPGQEKVQL KRKVTLLRGV SIIIGTIIGA 

        70         80         90        100        110        120 
GIFISPKGVL QNTGSVGMSL TIWTVCGVLS LFGALSYAEL GTTIKKSGGH YTYILEVFGP 

       130        140        150        160        170        180 
LPAFVRVWVE LLIIRPAATA VISLAFGRYI LEPFFIQCEI PELAIKLITA VGITVVMVLN 

       190        200        210        220        230        240 
SMSVSWSARI QIFLTFCKLT AILIIIVPGV MQLIKGQTQN FKDAFSGRDS SITRLPLAFY 

       250        260        270        280        290        300 
YGMYAYAGWF YLNFVTEEVE NPEKTIPLAI CISMAIVTIG YVLTNVAYFT TINAEELLLS 

       310        320        330        340        350        360 
NAVAVTFSER LLGNFSLAVP IFVALSCFGS MNGGVFAVSR LFYVASREGH LPEILSMIHV 

       370        380        390        400        410        420 
RKHTPLPAVI VLHPLTMIML FSGDLDSLLN FLSFARWLFI GLAVAGLIYL RYKCPDMHRP 

       430        440        450        460        470        480 
FKVPLFIPAL FSFTCLFMVA LSLYSDPFST GIGFVITLTG VPAYYLFIIW DKKPRWFRIM 

       490        500 
SEKITRTLQI ILEVVPEEDK L

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of human xCT, the light chain of amino acid transport system xc-." Sato H., Tamba M., Kuriyama-Matsumura K., Okuno S., Bannai S. Antioxid. Redox Signal. 2:665-671(2000) [PubMed: 11213471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"CCBR1, novel CD98 light chain implicated in redox control and calcium signaling." Conklin D.S., Beach D.H. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure, function, and regulation of human cystine/glutamate transporter in retinal pigment epithelial cells." Bridges C.C., Kekuda R., Wang H., Prasad P.D., Mehta P., Huang W., Smith S.B., Ganapathy V. Invest. Ophthalmol. Vis. Sci. 42:47-54(2001) [PubMed: 11133847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[4]	Borsani G., Manzoni M., Palacin M., Pineda M., Gasol E. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[6]	"Membrane topology of system xc- light subunit reveals a re-entrant loop with substrate-restricted accessibility." Gasol E., Jimenez-Vidal M., Chillaron J., Zorzano A., Palacin M. J. Biol. Chem. 279:31228-31236(2004) [PubMed: 15151999] [Abstract] Cited for: FUNCTION, MEMBRANE TOPOLOGY, SUBCELLULAR LOCATION.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB026891 mRNA. Translation: BAA82628.1. AF200708 mRNA. Translation: AAG35592.1. AF252872 mRNA. Translation: AAK49111.1. AJ277882 mRNA. Translation: CAC81905.1. BC012087 mRNA. Translation: AAH12087.1.
IPI	IPI00010474.
RefSeq	NP_055146.1. NM_014331.3.
UniGene	Hs.390594.
3D structure databases
ProteinModelPortal	Q9UPY5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UPY5. 1 interaction.
STRING	Q9UPY5.
PTM databases
PhosphoSite	Q9UPY5.
Polymorphism databases
DMDM	12585385.
Proteomic databases
PRIDE	Q9UPY5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000280612; ENSP00000280612; ENSG00000151012.
GeneID	23657.
KEGG	hsa:23657.
UCSC	uc010iof.1. human.
Organism-specific databases
CTD	23657.
GeneCards	GC04M139085.
H-InvDB	HIX0004502.
HGNC	HGNC:11059. SLC7A11.
MIM	607933. gene.
neXtProt	NX_Q9UPY5.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00600000084369.
HOGENOM	HBG714539.
HOVERGEN	HBG000476.
InParanoid	Q9UPY5.
OMA	GQTQHFK.
OrthoDB	EOG4F1X35.
PhylomeDB	Q9UPY5.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15187.
Reactome	REACT_15518. Transmembrane transport of small molecules. REACT_19419. Amino acid and oligopeptide SLC transporters. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q9UPY5.
Bgee	Q9UPY5.
CleanEx	HS_SLC7A11.
Genevestigator	Q9UPY5.
GermOnline	ENSG00000151012. Homo sapiens.
Family and domain databases
InterPro	IPR004841. AA-permease_dom. IPR002293. AA/rel_permease1. IPR004760. L_AA_transporter. [Graphical view]
KO	K13869.
PANTHER	PTHR11785. AA/rel_permease1. 1 hit.
Pfam	PF00324. AA_permease. 1 hit. [Graphical view]
PIRSF	PIRSF006060. AA_transporter. 1 hit.
TIGRFAMs	TIGR00911. 2A0308. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00138. L-Cystine. DB00142. L-Glutamic Acid. DB00795. Sulfasalazine.
NextBio	46497.
SOURCE	Search...

Entry information

Entry name

XCT_HUMAN

Accession

Primary (citable) accession number: Q9UPY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 101 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.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents