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   27-MAR-2024, entry version 178.
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:1652100, ECO:0000303|PubMed:2541919};
DE            Short=ERR;
DE            Short=EcoR {ECO:0000303|PubMed:1908564};
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 multiple
RT   membrane-spanning protein and confers susceptibility to virus infection.";
RL   Cell 57:659-666(1989).
RN   [2]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY.
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   FUNCTION (MICROBIAL INFECTION), FUNCTION, TRANSPORTER ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=1908564; DOI=10.1038/352729a0;
RA   Wang H., Kavanaugh M.P., North R.A., Kabat D.;
RT   "Cell-surface receptor for ecotropic murine retroviruses is a basic amino-
RT   acid transporter.";
RL   Nature 352:729-731(1991).
RN   [4]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Liver;
RX   PubMed=9174363; DOI=10.1021/bi962829p;
RA   Closs E.I., Graef P., Habermeier A., Cunningham J.M., Foerstermann U.;
RT   "Human cationic amino acid transporters hCAT-1, hCAT-2A, and hCAT-2B: three
RT   related carriers with distinct transport properties.";
RL   Biochemistry 36:6462-6468(1997).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY
RP   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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   INTERACTION WITH ASL; ASS1; NOS1 AND NOS3.
RX   PubMed=22081021; DOI=10.1038/nm.2544;
RA   Erez A., Nagamani S.C., Shchelochkov O.A., Premkumar M.H., Campeau P.M.,
RA   Chen Y., Garg H.K., Li L., Mian A., Bertin T.K., Black J.O., Zeng H.,
RA   Tang Y., Reddy A.K., Summar M., O'Brien W.E., Harrison D.G., Mitch W.E.,
RA   Marini J.C., Aschner J.L., Bryan N.S., Lee B.;
RT   "Requirement of argininosuccinate lyase for systemic nitric oxide
RT   production.";
RL   Nat. Med. 17:1619-1626(2011).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25683716; DOI=10.1016/j.celrep.2015.01.019;
RA   Hlynialuk C.J., Ling B., Baker Z.N., Cobine P.A., Yu L.D., Boulet A.,
RA   Wai T., Hossain A., El Zawily A.M., McFie P.J., Stone S.J., Diaz F.,
RA   Moraes C.T., Viswanathan D., Petris M.J., Leary S.C.;
RT   "The mitochondrial metallochaperone SCO1 is required to sustain expression
RT   of the high-affinity copper transporter CTR1 and preserve copper
RT   homeostasis.";
RL   Cell Rep. 10:933-943(2015).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=28973536; DOI=10.1093/hmg/ddx344;
RA   Baker Z.N., Jett K., Boulet A., Hossain A., Cobine P.A., Kim B.E.,
RA   El Zawily A.M., Lee L., Tibbits G.F., Petris M.J., Leary S.C.;
RT   "The mitochondrial metallochaperone SCO1 maintains CTR1 at the plasma
RT   membrane to preserve copper homeostasis in the murine heart.";
RL   Hum. Mol. Genet. 26:4617-4628(2017).
CC   -!- FUNCTION: High-affinity, low capacity permease involved in the
CC       transport of the cationic amino acids (arginine, lysine and ornithine)
CC       in non-hepatic tissues. {ECO:0000269|PubMed:1652100,
CC       ECO:0000269|PubMed:1908564, ECO:0000269|PubMed:9174363}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for the ecotropic
CC       murine retroviral leukemia virus. {ECO:0000269|PubMed:1908564,
CC       ECO:0000269|PubMed:2541919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:1652100,
CC         ECO:0000269|PubMed:1908564, ECO:0000269|PubMed:9174363};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935,
CC         ChEBI:CHEBI:32551; Evidence={ECO:0000269|PubMed:1652100,
CC         ECO:0000269|PubMed:1908564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199,
CC         ChEBI:CHEBI:46911; Evidence={ECO:0000269|PubMed:1652100,
CC         ECO:0000269|PubMed:1908564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoarginine(in) = L-homoarginine(out);
CC         Xref=Rhea:RHEA:71203, ChEBI:CHEBI:143006;
CC         Evidence={ECO:0000269|PubMed:1652100};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.14 mM for L-arginine {ECO:0000269|PubMed:9174363};
CC         KM=0.077 mM for L-arginine {ECO:0000269|PubMed:1908564};
CC         KM=0.105 mM for L-ornithine {ECO:0000269|PubMed:1908564};
CC         KM=0.073 mM for L-lysine {ECO:0000269|PubMed:1908564};
CC   -!- SUBUNIT: Interacts with TM4SF5; the interaction is negatively regulated
CC       by arginine (By similarity). Forms tissue-specific complexes with ASL,
CC       ASS1 and nitric oxide synthase NOS1 or NOS3; the complex regulates
CC       cell-autonomous L-arginine synthesis and citrulline recycling while
CC       channeling extracellular L-arginine to nitric oxide synthesis pathway
CC       (PubMed:22081021). {ECO:0000250|UniProtKB:P30825,
CC       ECO:0000269|PubMed:22081021}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25683716,
CC       ECO:0000269|PubMed:28973536}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=In the absence of SCO1 in cardiomyocytes a
CC       mislocalization to the cytoplasm is seen.
CC       {ECO:0000269|PubMed:28973536}.
CC   -!- TISSUE SPECIFICITY: Highest levels found in the testis and bone marrow.
CC       Not found in the liver. {ECO:0000269|PubMed:1652100}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.
CC       {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   AlphaFoldDB; Q09143; -.
DR   SMR; Q09143; -.
DR   BioGRID; 198275; 1.
DR   IntAct; Q09143; 1.
DR   STRING; 10090.ENSMUSP00000046714; -.
DR   TCDB; 2.A.3.3.1; the amino acid-polyamine-organocation (apc) family.
DR   GlyCosmos; Q09143; 2 sites, No reported glycans.
DR   GlyGen; Q09143; 2 sites.
DR   iPTMnet; Q09143; -.
DR   PhosphoSitePlus; Q09143; -.
DR   SwissPalm; Q09143; -.
DR   EPD; Q09143; -.
DR   PaxDb; 10090-ENSMUSP00000046714; -.
DR   PeptideAtlas; Q09143; -.
DR   ProteomicsDB; 285415; -.
DR   Pumba; Q09143; -.
DR   Antibodypedia; 22734; 240 antibodies from 27 providers.
DR   DNASU; 11987; -.
DR   Ensembl; ENSMUST00000048116.15; ENSMUSP00000046714.9; ENSMUSG00000041313.15.
DR   GeneID; 11987; -.
DR   KEGG; mmu:11987; -.
DR   UCSC; uc009aos.2; mouse.
DR   AGR; MGI:88117; -.
DR   CTD; 6541; -.
DR   MGI; MGI:88117; Slc7a1.
DR   VEuPathDB; HostDB:ENSMUSG00000041313; -.
DR   eggNOG; KOG1286; Eukaryota.
DR   GeneTree; ENSGT00940000155349; -.
DR   InParanoid; Q09143; -.
DR   OMA; LMFGWAP; -.
DR   OrthoDB; 1421713at2759; -.
DR   PhylomeDB; Q09143; -.
DR   TreeFam; TF315212; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   BioGRID-ORCS; 11987; 13 hits in 76 CRISPR screens.
DR   ChiTaRS; Slc7a1; mouse.
DR   PRO; PR:Q09143; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q09143; Protein.
DR   Bgee; ENSMUSG00000041313; Expressed in brain blood vessel and 243 other cell types or tissues.
DR   ExpressionAtlas; Q09143; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IC:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005290; F:L-histidine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0001618; F:virus receptor activity; IDA:UniProtKB.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR   GO; GO:0015807; P:L-amino acid transport; ISO:MGI.
DR   GO; GO:0097638; P:L-arginine import across plasma membrane; ISO:MGI.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; IDA:UniProtKB.
DR   GO; GO:1903810; P:L-histidine import across plasma membrane; ISO:MGI.
DR   GO; GO:1903352; P:L-ornithine transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0015819; P:lysine transport; ISO:MGI.
DR   GO; GO:0015822; P:ornithine transport; ISO:MGI.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR   GO; GO:0032006; P:regulation of TOR signaling; ISO:MGI.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 2.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004755; Cat_AA_permease.
DR   InterPro; IPR029485; CAT_C.
DR   NCBIfam; TIGR00906; 2A0303; 1.
DR   PANTHER; PTHR43243:SF28; HIGH AFFINITY CATIONIC AMINO ACID TRANSPORTER 1; 1.
DR   PANTHER; PTHR43243; INNER MEMBRANE TRANSPORTER YGJI-RELATED; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   Pfam; PF13906; AA_permease_C; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   Genevisible; Q09143; MM.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..622
FT                   /note="High affinity cationic amino acid transporter 1"
FT                   /id="PRO_0000054262"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..61
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..191
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..330
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..401
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        423..485
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..519
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        520..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..552
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        574..577
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        578..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        599..622
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         616
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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
//