ID   CTR3_MOUSE              Reviewed;         618 AA.
AC   P70423; B1AVE2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Cationic amino acid transporter 3 {ECO:0000305};
DE            Short=CAT-3;
DE            Short=CAT3;
DE   AltName: Full=Cationic amino acid transporter y+;
DE   AltName: Full=Solute carrier family 7 member 3;
GN   Name=Slc7a3 {ECO:0000312|MGI:MGI:1100521}; Synonyms=Atrc3, Cat3;
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], FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=9334265; DOI=10.1074/jbc.272.42.26780;
RA   Ito K., Groudine M.;
RT   "A new member of the cationic amino acid transporter family is
RT   preferentially expressed in adult mouse brain.";
RL   J. Biol. Chem. 272:26780-26786(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Uniporter that mediates the uptake of cationic L-amino acids
CC       such as L-arginine, L-lysine and L-ornithine (PubMed:9334265). The
CC       transport is sodium ions- and pH-independent, moderately trans-
CC       stimulated and is mediated by passive diffusion (PubMed:9334265).
CC       {ECO:0000269|PubMed:9334265}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:9334265};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935,
CC         ChEBI:CHEBI:32551; Evidence={ECO:0000269|PubMed:9334265};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199,
CC         ChEBI:CHEBI:46911; Evidence={ECO:0000250|UniProtKB:Q8WY07};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=110 uM for L-lysine {ECO:0000269|PubMed:9334265};
CC         KM=100 uM for L-arginine {ECO:0000269|PubMed:9334265};
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in adult brain and in a wide variety of
CC       embryonic tissues. {ECO:0000269|PubMed:9334265}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8WY07}.
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; U70859; AAB09593.1; -; mRNA.
DR   EMBL; AK077593; BAC36884.1; -; mRNA.
DR   EMBL; AL672308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC050195; AAH50195.1; -; mRNA.
DR   CCDS; CCDS30309.1; -.
DR   RefSeq; NP_001288769.1; NM_001301840.1.
DR   RefSeq; NP_031541.1; NM_007515.3.
DR   RefSeq; XP_006527816.1; XM_006527753.2.
DR   RefSeq; XP_011245812.1; XM_011247510.1.
DR   RefSeq; XP_011245813.1; XM_011247511.1.
DR   RefSeq; XP_011245814.1; XM_011247512.1.
DR   RefSeq; XP_011245815.1; XM_011247513.1.
DR   RefSeq; XP_017173852.1; XM_017318363.1.
DR   RefSeq; XP_017173853.1; XM_017318364.1.
DR   AlphaFoldDB; P70423; -.
DR   SMR; P70423; -.
DR   BioGRID; 198277; 1.
DR   IntAct; P70423; 1.
DR   STRING; 10090.ENSMUSP00000109339; -.
DR   TCDB; 2.A.3.3.5; the amino acid-polyamine-organocation (apc) family.
DR   GlyCosmos; P70423; 1 site, No reported glycans.
DR   GlyGen; P70423; 1 site.
DR   iPTMnet; P70423; -.
DR   PhosphoSitePlus; P70423; -.
DR   SwissPalm; P70423; -.
DR   EPD; P70423; -.
DR   MaxQB; P70423; -.
DR   PaxDb; 10090-ENSMUSP00000098914; -.
DR   PeptideAtlas; P70423; -.
DR   ProteomicsDB; 285222; -.
DR   Antibodypedia; 586; 87 antibodies from 19 providers.
DR   DNASU; 11989; -.
DR   Ensembl; ENSMUST00000073927.5; ENSMUSP00000073582.5; ENSMUSG00000031297.15.
DR   Ensembl; ENSMUST00000101362.8; ENSMUSP00000098914.2; ENSMUSG00000031297.15.
DR   Ensembl; ENSMUST00000113710.8; ENSMUSP00000109339.2; ENSMUSG00000031297.15.
DR   GeneID; 11989; -.
DR   KEGG; mmu:11989; -.
DR   UCSC; uc009twt.2; mouse.
DR   AGR; MGI:1100521; -.
DR   CTD; 84889; -.
DR   MGI; MGI:1100521; Slc7a3.
DR   VEuPathDB; HostDB:ENSMUSG00000031297; -.
DR   eggNOG; KOG1286; Eukaryota.
DR   GeneTree; ENSGT00940000154651; -.
DR   HOGENOM; CLU_007946_15_7_1; -.
DR   InParanoid; P70423; -.
DR   OMA; TLGWPHL; -.
DR   OrthoDB; 1421713at2759; -.
DR   PhylomeDB; P70423; -.
DR   TreeFam; TF315212; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   BioGRID-ORCS; 11989; 1 hit in 77 CRISPR screens.
DR   PRO; PR:P70423; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P70423; Protein.
DR   Bgee; ENSMUSG00000031297; Expressed in epiblast (generic) and 115 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0000064; F:L-ornithine transmembrane transporter activity; 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:0097639; P:L-lysine import across plasma membrane; ISO:MGI.
DR   GO; GO:1903401; P:L-lysine transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0097640; P:L-ornithine 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:0032006; P:regulation of TOR signaling; ISO:MGI.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
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:SF20; CATIONIC AMINO ACID TRANSPORTER 3; 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; P70423; MM.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..618
FT                   /note="Cationic amino acid transporter 3"
FT                   /id="PRO_0000054267"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..61
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..191
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..335
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..380
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        402..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..474
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        475..495
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        496..506
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        507..527
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        528..539
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        540..560
FT                   /note="Helical; Name=13"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        561..568
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        569..589
FT                   /note="Helical; Name=14"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        590..618
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         605
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WY07"
FT   MOD_RES         617
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WY07"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   618 AA;  67460 MW;  605AFC255A8251DC CRC64;
     MLWQALRRFG QKLVRRRVLE LGMGETRLAR CLSTLDLVAL GVGSTLGAGV YVLAGEVAKD
     KAGPSIVICF LVAALSSVLA GLCYAEFGAR VPGSGSAYLY SYVTVGELWA FTTGWNLILS
     YVIGTASVAR AWSSAFDNLI GNHISRTLKG TILLKMPHVL AEYPDFFALA LVLLLTGLLV
     LGASKSALVT KVFTGMNLLV LSFVIISGFI KGELRNWKLT KEDYCLTMSE SNGTCSLDSM
     GSGGFMPFGL EGILRGAATC FYAFVGFDCI ATTGEEAQNP QRSIPMGIVI SMFICFLAYF
     GVSSALTLMM PYYKLHPESP LPEAFSYVGW EPARYLVAIG SLCALSTSLL GSMFPMPRVM
     YSMAEDGLLF RVLAKVHSVT HIPIVATLVS GVIAAFMAFL FELTDLVDLM SIGTLLAHSL
     VSICVLILRY QPDQEMKSVE EEMELQEETL EAEKLTVQAL FCPVNSIPTL LSGRVVYVCS
     SLLAVLLTVL CLVLTWWTTP LRSGDPVWVT VVVLILGLIL AISGVIWRQP QNRTPLHFKV
     PAVPLLPLVS IFVNVYLMMQ MTAGTWARFG IWMLIGFAIY FGYGIQHSMK EVKNHQTLPK
     TRAQTIDLDL TTSCVHSI
//