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DescriptionRecName: Full=High affinity cationic amino acid transporter 1; Short=CAT-1 {ECO:0000250|UniProtKB:P30825}; Short=CAT1; AltName: Full=Ecotropic retroviral leukemia receptor; AltName: Full=Ecotropic retrovirus receptor {ECO:0000303|PubMed:2541919}; Short=ERR; AltName: Full=Solute carrier family 7 member 1 {ECO:0000312|MGI:MGI:88117}; AltName: Full=System Y+ basic amino acid transporter;
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MyHits synonymsCTR1_MOUSE , Q09143 , P30824 , 157EE960CE737B6E
match map segment
ipfam:AA_permease_C ipfam:AA_permease_2  
Legends: 1, Phosphoserine. {ECO:0000244|PubMed:21183079}; 2, N-linked (GlcNAc...) asparagine. {ECO:0000255}; 3, TOPO_DOM Cytoplasmic. {ECO:0000255}; 4, TRANSMEM Helical. {ECO:0000255}; 5, TOPO_DOM Extracellular. {ECO:0000255}; 6, ipfam:AA_permease_C [T].
ID   CTR1_MOUSE              Reviewed;         622 AA.
AC   Q09143; P30824;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   10-MAY-2017, entry version 143.
DE   RecName: Full=High affinity cationic amino acid transporter 1;
DE            Short=CAT-1 {ECO:0000250|UniProtKB:P30825};
DE            Short=CAT1;
DE   AltName: Full=Ecotropic retroviral leukemia receptor;
DE   AltName: Full=Ecotropic retrovirus receptor {ECO:0000303|PubMed:2541919};
DE            Short=ERR;
DE   AltName: Full=Solute carrier family 7 member 1 {ECO:0000312|MGI:MGI:88117};
DE   AltName: Full=System Y+ basic amino acid transporter;
GN   Name=Slc7a1 {ECO:0000312|MGI:MGI:88117}; Synonyms=Atrc1, Rec-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION (MICROBIAL INFECTION).
RC   TISSUE=Fibroblast;
RX   PubMed=2541919; DOI=10.1016/0092-8674(89)90134-7;
RA   Albritton L.M., Tseng L., Scadden D., Cunningham J.M.;
RT   "A putative murine ecotropic retrovirus receptor gene encodes a
RT   multiple membrane-spanning protein and confers susceptibility to virus
RT   infection.";
RL   Cell 57:659-666(1989).
RN   [2]
RP   FUNCTION.
RX   PubMed=1652100; DOI=10.1038/352725a0;
RA   Kim J.W., Closs E.I., Albritton L.M., Cunningham J.M.;
RT   "Transport of cationic amino acids by the mouse ecotropic retrovirus
RT   receptor.";
RL   Nature 352:725-728(1991).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:1652100}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for the
CC       ecotropic murine retroviral leukemia virus.
CC       {ECO:0000269|PubMed:2541919}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highest levels found in the testis and bone
CC       marrow. Not found in the liver.
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}.
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DR   EMBL; M26687; AAA37574.1; -; mRNA.
DR   CCDS; CCDS19882.1; -.
DR   PIR; A32742; A32742.
DR   RefSeq; NP_001288353.1; NM_001301424.1.
DR   RefSeq; NP_031539.3; NM_007513.4.
DR   RefSeq; XP_006504859.1; XM_006504796.1.
DR   UniGene; Mm.275489; -.
DR   ProteinModelPortal; Q09143; -.
DR   IntAct; Q09143; 1.
DR   STRING; 10090.ENSMUSP00000046714; -.
DR   TCDB; 2.A.3.3.1; the amino acid-polyamine-organocation (apc) family.
DR   iPTMnet; Q09143; -.
DR   PhosphoSitePlus; Q09143; -.
DR   SwissPalm; Q09143; -.
DR   EPD; Q09143; -.
DR   PaxDb; Q09143; -.
DR   PeptideAtlas; Q09143; -.
DR   PRIDE; Q09143; -.
DR   Ensembl; ENSMUST00000048116; ENSMUSP00000046714; ENSMUSG00000041313.
DR   GeneID; 11987; -.
DR   KEGG; mmu:11987; -.
DR   UCSC; uc009aos.2; mouse.
DR   CTD; 6541; -.
DR   MGI; MGI:88117; Slc7a1.
DR   eggNOG; KOG1286; Eukaryota.
DR   eggNOG; COG0531; LUCA.
DR   GeneTree; ENSGT00760000119151; -.
DR   HOGENOM; HOG000250623; -.
DR   HOVERGEN; HBG000280; -.
DR   InParanoid; Q09143; -.
DR   KO; K13863; -.
DR   OMA; GVNGMFA; -.
DR   OrthoDB; EOG091G05NM; -.
DR   PhylomeDB; Q09143; -.
DR   TreeFam; TF315212; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   ChiTaRS; Slc7a1; mouse.
DR   PRO; PR:Q09143; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000041313; -.
DR   ExpressionAtlas; Q09143; baseline and differential.
DR   Genevisible; Q09143; MM.
DR   GO; GO:0016021; C:integral component of membrane; IC:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0015181; F:arginine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015809; P:arginine transport; IDA:MGI.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004755; Cat_AA_permease.
DR   InterPro; IPR029485; CAT_C.
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; Complete proteome; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    622       High affinity cationic amino acid
FT                                transporter 1.
FT                                /FTId=PRO_0000054262.
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    239       Extracellular. {ECO:0000255}.
FT   TRANSMEM    240    260       Helical. {ECO:0000255}.
FT   TOPO_DOM    261    280       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    281    300       Helical. {ECO:0000255}.
FT   TOPO_DOM    301    330       Extracellular. {ECO:0000255}.
FT   TRANSMEM    331    351       Helical. {ECO:0000255}.
FT   TOPO_DOM    352    377       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    378    398       Helical. {ECO:0000255}.
FT   TOPO_DOM    399    401       Extracellular. {ECO:0000255}.
FT   TRANSMEM    402    422       Helical. {ECO:0000255}.
FT   TOPO_DOM    423    485       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    486    506       Helical. {ECO:0000255}.
FT   TOPO_DOM    507    519       Extracellular. {ECO:0000255}.
FT   TRANSMEM    520    544       Helical. {ECO:0000255}.
FT   TOPO_DOM    545    552       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    553    573       Helical. {ECO:0000255}.
FT   TOPO_DOM    574    577       Extracellular. {ECO:0000255}.
FT   TRANSMEM    578    598       Helical. {ECO:0000255}.
FT   TOPO_DOM    599    622       Cytoplasmic. {ECO:0000255}.
FT   MOD_RES     616    616       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    223    223       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    229    229       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       551    601       ipfam:AA_permease_C [T]
FT   MYHIT        33    429       ipfam:AA_permease_2 [T]
SQ   SEQUENCE   622 AA;  67092 MW;  157EE960CE737B6E CRC64;
     MGCKNLLGLG QQMLRRKVVD CSREESRLSR CLNTYDLVAL GVGSTLGAGV YVLAGAVARE
     NAGPAIVISF LIAALASVLA GLCYGEFGAR VPKTGSAYLY SYVTVGELWA FITGWNLILS
     YIIGTSSVAR AWSATFDELI GKPIGEFSRQ HMALNAPGVL AQTPDIFAVI IIIILTGLLT
     LGVKESAMVN KIFTCINVLV LCFIVVSGFV KGSIKNWQLT EKNFSCNNND TNVKYGEGGF
     MPFGFSGVLS GAATCFYAFV GFDCIATTGE EVKNPQKAIP VGIVASLLIC FIAYFGVSAA
     LTLMMPYFCL DIDSPLPGAF KHQGWEEAKY AVAIGSLCAL STSLLGSMFP MPRVIYAMAE
     DGLLFKFLAK INNRTKTPVI ATVTSGAIAA VMAFLFELKD LVDLMSIGTL LAYSLVAACV
     LVLRYQPEQP NLVYQMARTT EELDRVDQNE LVSASESQTG FLPVAEKFSL KSILSPKNVE
     PSKFSGLIVN ISAGLLAALI ITVCIVAVLG REALAEGTLW AVFVMTGSVL LCMLVTGIIW
     RQPESKTKLS FKVPFVPVLP VLSIFVNIYL MMQLDQGTWV RFAVWMLIGF TIYFGYGIWH
     SEEASLAAGQ AKTPDSNLDQ CK
//