SL7A1_RAT
ID SL7A1_RAT Reviewed; 624 AA.
AC P30823;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 -!- 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.ENSRNOP00000001234; -.
DR GlyGen; P30823; 2 sites.
DR PhosphoSitePlus; P30823; -.
DR SwissPalm; P30823; -.
DR jPOST; P30823; -.
DR PaxDb; P30823; -.
DR PRIDE; P30823; -.
DR UCSC; RGD:3716; rat.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA: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; IBA:GO_Central.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:RGD.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:1990822; P:basic amino acid transmembrane transport; 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; IBA:GO_Central.
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 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 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
