SL7A1_MOUSE
ID SL7A1_MOUSE Reviewed; 622 AA.
AC Q09143; P30824;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
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; 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.
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 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 [5]
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 [6]
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 [7]
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 -!- FUNCTION: (Microbial infection) Acts as a receptor for the ecotropic
CC murine retroviral leukemia virus. {ECO:0000269|PubMed:2541919}.
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.
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 IntAct; Q09143; 1.
DR STRING; 10090.ENSMUSP00000046714; -.
DR TCDB; 2.A.3.3.1; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; Q09143; 2 sites.
DR iPTMnet; Q09143; -.
DR PhosphoSitePlus; Q09143; -.
DR SwissPalm; Q09143; -.
DR EPD; Q09143; -.
DR PaxDb; Q09143; -.
DR PeptideAtlas; Q09143; -.
DR PRIDE; Q09143; -.
DR ProteomicsDB; 285415; -.
DR Antibodypedia; 22734; 215 antibodies from 27 providers.
DR DNASU; 11987; -.
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 VEuPathDB; HostDB:ENSMUSG00000041313; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000155349; -.
DR InParanoid; Q09143; -.
DR OMA; WQLTMIS; -.
DR OrthoDB; 439017at2759; -.
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 71 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 241 other tissues.
DR ExpressionAtlas; Q09143; baseline and differential.
DR Genevisible; Q09143; MM.
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:0016021; C:integral component of 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:MGI.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; ISO:MGI.
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:MGI.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
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:MGI.
DR GO; GO:1903810; P:L-histidine import across plasma membrane; ISO:MGI.
DR GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
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 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; 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
