ID   CTR1_RAT                Reviewed;         624 AA.
AC   P30823;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, 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:10196347};
DE            Short=EcoR {ECO:0000303|PubMed:10196347};
DE   AltName: Full=Solute carrier family 7 member 1 {ECO:0000312|RGD:3716};
DE   AltName: Full=System Y+ basic amino acid transporter;
GN   Name=Slc7a1 {ECO:0000312|RGD:3716}; Synonyms=Atrc1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION (MICROBIAL INFECTION).
RX   PubMed=10196347; DOI=10.1128/jvi.73.5.4461-4464.1999;
RA   Takase-Yoden S., Watanabe R.;
RT   "Contribution of virus-receptor interaction to distinct viral proliferation
RT   of neuropathogenic and nonneuropathogenic murine leukemia viruses in rat
RT   glial cells.";
RL   J. Virol. 73:4461-4464(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-288.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=8473910; DOI=10.1111/j.1471-4159.1993.tb13428.x;
RA   Stoll J., Wadhwani K.C., Smith Q.R.;
RT   "Identification of the cationic amino acid transporter (system y+) of the
RT   rat blood-brain barrier.";
RL   J. Neurochem. 60:1956-1959(1993).
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:0000250|UniProtKB:Q09143}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for the ecotropic
CC       murine retroviral leukemia virus. {ECO:0000269|PubMed:10196347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:Q09143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935,
CC         ChEBI:CHEBI:32551; Evidence={ECO:0000250|UniProtKB:Q09143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199,
CC         ChEBI:CHEBI:46911; Evidence={ECO:0000250|UniProtKB:Q09143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoarginine(in) = L-homoarginine(out);
CC         Xref=Rhea:RHEA:71203, ChEBI:CHEBI:143006;
CC         Evidence={ECO:0000250|UniProtKB:Q09143};
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       (By similarity). {ECO:0000250|UniProtKB:P30825,
CC       ECO:0000250|UniProtKB:Q09143}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q09143};
CC       Multi-pass membrane protein {ECO:0000255}.
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; D67087; BAA11090.1; -; mRNA.
DR   EMBL; L10152; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P30823; -.
DR   SMR; P30823; -.
DR   STRING; 10116.ENSRNOP00000072647; -.
DR   GlyCosmos; P30823; 2 sites, No reported glycans.
DR   GlyGen; P30823; 2 sites.
DR   PhosphoSitePlus; P30823; -.
DR   SwissPalm; P30823; -.
DR   jPOST; P30823; -.
DR   PaxDb; 10116-ENSRNOP00000001234; -.
DR   UCSC; RGD:3716; rat.
DR   AGR; RGD:3716; -.
DR   RGD; 3716; Slc7a1.
DR   eggNOG; KOG1286; Eukaryota.
DR   InParanoid; P30823; -.
DR   PhylomeDB; P30823; -.
DR   Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR   PRO; PR:P30823; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0005290; F:L-histidine transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0015189; F:L-lysine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0000064; F:L-ornithine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0001618; F:virus receptor activity; ISO:RGD.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; ISO:RGD.
DR   GO; GO:0015802; P:basic amino acid transport; TAS:RGD.
DR   GO; GO:0015807; P:L-amino acid transport; ISO:RGD.
DR   GO; GO:0097638; P:L-arginine import across plasma membrane; IMP:ARUK-UCL.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; IMP:RGD.
DR   GO; GO:1903810; P:L-histidine import across plasma membrane; ISO:RGD.
DR   GO; GO:1903352; P:L-ornithine transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0015819; P:lysine transport; ISO:RGD.
DR   GO; GO:0015822; P:ornithine transport; ISO:RGD.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR   GO; GO:0032006; P:regulation of TOR signaling; IMP:RGD.
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.
PE   2: Evidence at transcript level;
KW   Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..624
FT                   /note="High affinity cationic amino acid transporter 1"
FT                   /id="PRO_0000054263"
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..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..332
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..403
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        425..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..521
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        522..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        547..554
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        576..579
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        580..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        601..624
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         618
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q09143"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        111
FT                   /note="F -> L (in Ref. 2; L10152)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   624 AA;  67267 MW;  33339B2F74E5F052 CRC64;
     MGCKNLLSLG QQMLRRKVVD CSREESRLSR CLNTYDLVAL GVGSTLGAGV YVLAGAVARE
     NAGPAIVISF LIAALASVLA GLCYGEFGAR VPKTGSAYLY SYVTVGELWA FITGWNLILS
     YIIGTSSVAR AWSATFDELI GKPIGEFSRQ HMALNAPGVL AQTPDIFAVI IIIILTGLLT
     LGVKESAMVN KIFTCINVLV LCFIMVSGFV KGSIENWQLT ENKSSPLCGN NDTNVKYGEG
     GFMPFGFSGV LSGAATCFYA FVGFDCIATT GEEVKNPQKA IPVGIVASLL ICFIAYFGVS
     AALTLMMPYF CLDTDSPLPG AFKYRGWEEA KYAVAVGSLC ALSTSPLGSM FPMPRVIYAM
     AEDGLLFKFL AKINDRTKTP IIATVTSGAI AAVMAFLFEL KDLVDLMSIG TLLAYSLVAA
     CVLVLRYQPE QPNLVYQMAR TTDELDQVDQ NEMVSASESQ TGFLPAAEKF SLKTILSPKN
     MEPSKFSGLI VNISAGLLAV LIITVCIVAV LGREALAEGT LWAVFVMTGS VLLCMLVTGI
     IWRQPESKTK LSFKVPFVPV LPVLSIFVNI YLMMQLDQGT WVRFAVWMLI AFAIYFGYGV
     WHSEEASLAA GQAKTPDSNL DQCK
//