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AT1_TOXGM
ID   AT1_TOXGM               Reviewed;         534 AA.
AC   S8EZA7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Arginine transporter 1 {ECO:0000305};
DE   AltName: Full=Amino acid transporter 1 {ECO:0000303|PubMed:30742695};
DE   AltName: Full=Apicomplexan amino acid transporter 1 {ECO:0000303|PubMed:30742695};
DE            Short=TgApiAT1 {ECO:0000303|PubMed:30742695};
DE   AltName: Full=Major facilitator superfamily domain-containing protein {ECO:0000305|PubMed:28205520};
DE   AltName: Full=Novel putative transporter 1 {ECO:0000303|PubMed:28205520};
DE            Short=TgNPT1 {ECO:0000303|PubMed:28205520};
GN   Name=ApiAT1 {ECO:0000303|PubMed:30742695};
GN   Synonyms=NPT1 {ECO:0000303|PubMed:28205520};
GN   ORFNames=TGME49_215490 {ECO:0000312|EMBL:EPT26443.1};
OS   Toxoplasma gondii (strain ATCC 50611 / Me49).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=508771 {ECO:0000312|Proteomes:UP000001529};
RN   [1] {ECO:0000312|Proteomes:UP000001529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50611 / Me49 {ECO:0000312|Proteomes:UP000001529};
RA   Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA   Roos D., Caler E., Lorenzi H.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=RH {ECO:0000269|PubMed:28205520};
RX   PubMed=28205520; DOI=10.1038/ncomms14455;
RA   Rajendran E., Hapuarachchi S.V., Miller C.M., Fairweather S.J., Cai Y.,
RA   Smith N.C., Cockburn I.A., Broeer S., Kirk K., van Dooren G.G.;
RT   "Cationic amino acid transporters play key roles in the survival and
RT   transmission of apicomplexan parasites.";
RL   Nat. Commun. 8:14455-14455(2017).
RN   [3] {ECO:0000305}
RP   FUNCTION, NOMENCLATURE, AND MUTAGENESIS OF 54-GLY--ALA-534.
RX   PubMed=30742695; DOI=10.1371/journal.ppat.1007577;
RA   Parker K.E.R., Fairweather S.J., Rajendran E., Blume M., McConville M.J.,
RA   Broeer S., Kirk K., van Dooren G.G.;
RT   "The tyrosine transporter of Toxoplasma gondii is a member of the newly
RT   defined apicomplexan amino acid transporter (ApiAT) family.";
RL   PLoS Pathog. 15:e1007577-e1007577(2019).
CC   -!- FUNCTION: Selective L-arginine transporter that is essential for
CC       parasite survival and virulence (PubMed:28205520, PubMed:30742695).
CC       Does not require other inorganic ions such as sodium, chloride,
CC       potassium or calcium (PubMed:28205520). {ECO:0000269|PubMed:28205520,
CC       ECO:0000269|PubMed:30742695}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:28205520};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32145;
CC         Evidence={ECO:0000269|PubMed:28205520};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=88 uM for arginine {ECO:0000269|PubMed:28205520};
CC       pH dependence:
CC         Optimum pH is 5-8. {ECO:0000269|PubMed:28205520};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28205520};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Impaired parasite growth under conditions of
CC       restricted arginine availability (PubMed:28205520). Does not cause
CC       toxoplasmosis in mice (PubMed:28205520). {ECO:0000269|PubMed:28205520}.
CC   -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC       {ECO:0000305}.
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DR   EMBL; KE138836; EPT26443.1; -; Genomic_DNA.
DR   RefSeq; XP_002370868.1; XM_002370827.2.
DR   EnsemblProtists; TGME49_215490-t26_1; TGME49_215490-t26_1; TGME49_215490.
DR   GeneID; 7897047; -.
DR   KEGG; tgo:TGME49_215490; -.
DR   VEuPathDB; ToxoDB:TGME49_215490; -.
DR   HOGENOM; CLU_021456_0_0_1; -.
DR   PhylomeDB; S8EZA7; -.
DR   Proteomes; UP000001529; Chromosome X.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0097638; P:L-arginine import across plasma membrane; IMP:UniProtKB.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..534
FT                   /note="Arginine transporter 1"
FT                   /id="PRO_0000454212"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          261..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   MUTAGEN         54..534
FT                   /note="Missing: Impaired parasite growth under conditions
FT                   of restricted arginine availability."
FT                   /evidence="ECO:0000269|PubMed:30742695"
SQ   SEQUENCE   534 AA;  58123 MW;  D9FF572736398B51 CRC64;
     MAGLLSSCCG RVYALLPDSA HPSAQQKTPF GVNRYVLLVI YMIYALLTSS VYFGWRSMSA
     MLFKSGQFSW VCTGESADTS PEEGETDYLC ALQDTKVQSL FTIAMACHFT CSAVAGYLLD
     TVGPKAVALL GQTFNALAWI LLAFSGPNFR SVYPAFVFMG AGADVSVYPT LLIVNLFPGS
     TALIMATLGA CISLSFFVPL VLRTMWESTG ISFEAVCIGY AVAGPILCAV VAFFFIPFKA
     FKGVDNFSAC VEAEKLANSP TAQSSPKAVD SPPCDEGASS RGRLAVSHNT ERTAPDDEQE
     KDNTERISLS DLACDPRFKK QKVSFSSQAF TFLYFGICLY FTVCGWVMAY YQEAAGRFLC
     NDAEYTLEIL TPLSTIPCLL FGVVINRIGI MPVILMLNTI GLLTYVCVVA AESVVAQYFS
     VIFFFMYISI FTTQMYVFVE STFDSAHFGK LIGVASLIGG LLSLISNVLY GDVTVGMLNG
     DTRPVVIALL AVIILMYPIL LAMRTKRNRK KQMEQEDIRS RVLELKAAHA ADAA
 
 
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