Entry sw:CTR1_HUMAN

ID   CTR1_HUMAN              Reviewed;         629 AA.
AC   P30825; Q5JR50;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   30-NOV-2016, entry version 157.
DE   RecName: Full=High affinity cationic amino acid transporter 1;
DE            Short=CAT-1;
DE            Short=CAT1;
DE   AltName: Full=Ecotropic retroviral leukemia receptor homolog;
DE   AltName: Full=Ecotropic retrovirus receptor homolog;
DE            Short=ERR;
DE   AltName: Full=Solute carrier family 7 member 1;
DE   AltName: Full=System Y+ basic amino acid transporter;
GN   Name=SLC7A1; Synonyms=ATRC1, ERR, REC1L;
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], AND TISSUE SPECIFICITY.
RX   PubMed=1718082; DOI=10.1016/0042-6822(91)90748-Z;
RA   Yoshimoto T., Yoshimoto E., Meruelo D.;
RT   "Molecular cloning and characterization of a novel human gene
RT   homologous to the murine ecotropic retroviral receptor.";
RL   Virology 185:10-17(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Urinary bladder;
RX   PubMed=1348489; DOI=10.1016/0888-7543(92)90431-Q;
RA   Albritton L.M., Bowcock A.M., Eddy R.L., Morton C.C., Tseng L.,
RA   Farrer L.A., Cavalli-Sforza L.L., Shows T.B., Cunningham J.M.;
RT   "The human cationic amino acid transporter (ATRC1): physical and
RT   genetic mapping to 13q12-q14.";
RL   Genomics 12:430-434(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Placenta;
RX   PubMed=10485994; DOI=10.1007/s002329900558;
RA   Kamath S.G., Furesz T.C., Way B.A., Smith C.H.;
RT   "Identification of three cationic amino acid transporters in placental
RT   trophoblast: cloning, expression, and characterization of hCAT-1.";
RL   J. Membr. Biol. 171:55-62(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [6]
RP   PROTEIN SEQUENCE OF 5-15; 131-142 AND 361-373, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-216 AND ASN-226.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: High-affinity, low capacity permease involved in the
CC       transport of the cationic amino acids (arginine, lysine and
CC       ornithine) in non-hepatic tissues. May also function as an
CC       ecotropic retroviral leukemia receptor.
CC       {ECO:0000269|PubMed:10485994}.
CC   -!- INTERACTION:
CC       Q969F0:FATE1; NbExp=5; IntAct=EBI-4289564, EBI-743099;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10485994};
CC       Multi-pass membrane protein {ECO:0000303|PubMed:10485994}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1718082}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3)
CC       family. {ECO:0000305}.
DR   EMBL; X59155; CAA41869.1; -; mRNA.
DR   EMBL; X57303; CAA40560.1; -; mRNA.
DR   EMBL; AF078107; AAC27721.1; -; mRNA.
DR   EMBL; AL596114; CAI39913.1; -; Genomic_DNA.
DR   EMBL; BC063303; AAH63303.1; -; mRNA.
DR   EMBL; BC069358; AAH69358.1; -; mRNA.
DR   EMBL; BC115407; AAI15408.1; -; mRNA.
DR   CCDS; CCDS9333.1; -.
DR   PIR; S29685; S29685.
DR   RefSeq; NP_003036.1; NM_003045.4.
DR   RefSeq; XP_005266564.1; XM_005266507.3.
DR   RefSeq; XP_016876205.1; XM_017020716.1.
DR   UniGene; Hs.14846; -.
DR   ProteinModelPortal; P30825; -.
DR   BioGrid; 112432; 59.
DR   IntAct; P30825; 6.
DR   MINT; MINT-3012079; -.
DR   STRING; 9606.ENSP00000370128; -.
DR   DrugBank; DB00125; L-Arginine.
DR   DrugBank; DB00123; L-Lysine.
DR   DrugBank; DB00129; L-Ornithine.
DR   TCDB; 2.A.3.3.9; the amino acid-polyamine-organocation (apc) family.
DR   iPTMnet; P30825; -.
DR   PhosphoSitePlus; P30825; -.
DR   SwissPalm; P30825; -.
DR   BioMuta; SLC7A1; -.
DR   DMDM; 1706185; -.
DR   EPD; P30825; -.
DR   MaxQB; P30825; -.
DR   PaxDb; P30825; -.
DR   PeptideAtlas; P30825; -.
DR   PRIDE; P30825; -.
DR   Ensembl; ENST00000380752; ENSP00000370128; ENSG00000139514.
DR   GeneID; 6541; -.
DR   KEGG; hsa:6541; -.
DR   UCSC; uc001uso.4; human.
DR   CTD; 6541; -.
DR   DisGeNET; 6541; -.
DR   GeneCards; SLC7A1; -.
DR   HGNC; HGNC:11057; SLC7A1.
DR   HPA; HPA039721; -.
DR   MIM; 104615; gene.
DR   neXtProt; NX_P30825; -.
DR   OpenTargets; ENSG00000139514; -.
DR   PharmGKB; PA35917; -.
DR   eggNOG; KOG1286; Eukaryota.
DR   eggNOG; COG0531; LUCA.
DR   GeneTree; ENSGT00760000119151; -.
DR   HOGENOM; HOG000250623; -.
DR   HOVERGEN; HBG000280; -.
DR   InParanoid; P30825; -.
DR   KO; K13863; -.
DR   OMA; LAMIICP; -.
DR   OrthoDB; EOG091G05NM; -.
DR   PhylomeDB; P30825; -.
DR   TreeFam; TF315212; -.
DR   BioCyc; ZFISH:ENSG00000139514-MONOMER; -.
DR   Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR   ChiTaRS; SLC7A1; human.
DR   GeneWiki; SLC7A1; -.
DR   GenomeRNAi; 6541; -.
DR   PRO; PR:P30825; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000139514; -.
DR   CleanEx; HS_SLC7A1; -.
DR   ExpressionAtlas; P30825; baseline and differential.
DR   Genevisible; P30825; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR   GO; GO:0015181; F:arginine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015189; F:L-lysine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR   GO; GO:0015809; P:arginine transport; IEA:Ensembl.
DR   GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006810; P:transport; NAS:ProtInc.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004755; Cat_AA_permease.
DR   InterPro; IPR029485; CAT_C.
DR   PANTHER; PTHR11785; PTHR11785; 3.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   Pfam; PF13906; AA_permease_C; 1.
DR   TIGRFAMs; TIGR00906; 2A0303; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    629       High affinity cationic amino acid
FT                                transporter 1.
FT                                /FTId=PRO_0000054261.
FT   TOPO_DOM      1     35       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     36     57       Helical. {ECO:0000255}.
FT   TOPO_DOM     58     61       Extracellular. {ECO:0000255}.
FT   TRANSMEM     62     82       Helical. {ECO:0000255}.
FT   TOPO_DOM     83    102       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    103    123       Helical. {ECO:0000255}.
FT   TOPO_DOM    124    162       Extracellular. {ECO:0000255}.
FT   TRANSMEM    163    183       Helical. {ECO:0000255}.
FT   TOPO_DOM    184    191       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    192    212       Helical. {ECO:0000255}.
FT   TOPO_DOM    213    246       Extracellular. {ECO:0000255}.
FT   TRANSMEM    247    267       Helical. {ECO:0000255}.
FT   TOPO_DOM    268    287       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    288    307       Helical. {ECO:0000255}.
FT   TOPO_DOM    308    337       Extracellular. {ECO:0000255}.
FT   TRANSMEM    338    358       Helical. {ECO:0000255}.
FT   TOPO_DOM    359    384       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    385    405       Helical. {ECO:0000255}.
FT   TOPO_DOM    406    408       Extracellular. {ECO:0000255}.
FT   TRANSMEM    409    429       Helical. {ECO:0000255}.
FT   TOPO_DOM    430    492       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    493    513       Helical. {ECO:0000255}.
FT   TOPO_DOM    514    526       Extracellular. {ECO:0000255}.
FT   TRANSMEM    527    551       Helical. {ECO:0000255}.
FT   TOPO_DOM    552    559       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    560    580       Helical. {ECO:0000255}.
FT   TOPO_DOM    581    584       Extracellular. {ECO:0000255}.
FT   TRANSMEM    585    605       Helical. {ECO:0000255}.
FT   TOPO_DOM    606    629       Cytoplasmic. {ECO:0000255}.
FT   CARBOHYD    216    216       N-linked (GlcNAc...); atypical.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD    235    235       N-linked (GlcNAc...). {ECO:0000255}.
FT   CONFLICT     23     23       R -> P (in Ref. 2; CAA40560).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        32    437       ipfam:AA_permease_2 [T]
FT   MYHIT       558    608       ipfam:AA_permease_C [T]
SQ   SEQUENCE   629 AA;  67638 MW;  717734D4793647C5 CRC64;
     MGCKVLLNIG QQMLRRKVVD CSREETRLSR CLNTFDLVAL GVGSTLGAGV YVLAGAVARE
     NAGPAIVISF LIAALASVLA GLCYGEFGAR VPKTGSAYLY SYVTVGELWA FITGWNLILS
     YIIGTSSVAR AWSATFDELI GRPIGEFSRT HMTLNAPGVL AENPDIFAVI IILILTGLLT
     LGVKESAMVN KIFTCINVLV LGFIMVSGFV KGSVKNWQLT EEDFGNTSGR LCLNNDTKEG
     KPGVGGFMPF GFSGVLSGAA TCFYAFVGFD CIATTGEEVK NPQKAIPVGI VASLLICFIA
     YFGVSAALTL MMPYFCLDNN SPLPDAFKHV GWEGAKYAVA VGSLCALSAS LLGSMFPMPR
     VIYAMAEDGL LFKFLANVND RTKTPIIATL ASGAVAAVMA FLFDLKDLVD LMSIGTLLAY
     SLVAACVLVL RYQPEQPNLV YQMASTSDEL DPADQNELAS TNDSQLGFLP EAEMFSLKTI
     LSPKNMEPSK ISGLIVNIST SLIAVLIITF CIVTVLGREA LTKGALWAVF LLAGSALLCA
     VVTGVIWRQP ESKTKLSFKV PFLPVLPILS IFVNVYLMMQ LDQGTWVRFA VWMLIGFIIY
     FGYGLWHSEE ASLDADQART PDGNLDQCK
//