CTR3_MOUSE
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 03-AUG-2022, entry version 169.
DE RecName: Full=Cationic amino acid transporter 3;
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; 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, 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 129/SvCp; 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: Mediates the uptake of the cationic amino acids arginine,
CC lysine and ornithine in a sodium-independent manner.
CC {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 -!- 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.ENSMUSP00000098914; -.
DR TCDB; 2.A.3.3.5; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; P70423; 1 site.
DR iPTMnet; P70423; -.
DR PhosphoSitePlus; P70423; -.
DR SwissPalm; P70423; -.
DR EPD; P70423; -.
DR MaxQB; P70423; -.
DR PaxDb; P70423; -.
DR PeptideAtlas; P70423; -.
DR PRIDE; P70423; -.
DR ProteomicsDB; 285222; -.
DR Antibodypedia; 586; 75 antibodies from 19 providers.
DR DNASU; 11989; -.
DR Ensembl; ENSMUST00000073927; ENSMUSP00000073582; ENSMUSG00000031297.
DR Ensembl; ENSMUST00000101362; ENSMUSP00000098914; ENSMUSG00000031297.
DR Ensembl; ENSMUST00000113710; ENSMUSP00000109339; ENSMUSG00000031297.
DR GeneID; 11989; -.
DR KEGG; mmu:11989; -.
DR UCSC; uc009twt.2; mouse.
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; IAIEMSG; -.
DR OrthoDB; 439017at2759; -.
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 72 CRISPR screens.
DR PRO; PR:P70423; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70423; protein.
DR Bgee; ENSMUSG00000031297; Expressed in epiblast (generic) and 113 other tissues.
DR Genevisible; P70423; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
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:0006865; P:amino acid transport; IBA:GO_Central.
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: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 InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR015606; CAT3.
DR InterPro; IPR004755; Cat_AA_permease.
DR InterPro; IPR029485; CAT_C.
DR PANTHER; PTHR43243:SF20; PTHR43243:SF20; 1.
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; 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