AT53_TOXGO
ID AT53_TOXGO Reviewed; 504 AA.
AC A0A7J6K338;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Aromatic and large neutral amino acid transporter 5-3 {ECO:0000303|PubMed:30742695};
DE AltName: Full=Apicomplexan amino acid transporter 5-3 {ECO:0000303|PubMed:30742695};
DE Short=TgApiAT5-3 {ECO:0000303|PubMed:30742695};
DE AltName: Full=Major facilitator superfamily domain-containing protein {ECO:0000305};
GN Name=ApiAT5-3 {ECO:0000303|PubMed:30742695};
GN ORFNames=TGRH88_072370 {ECO:0000312|EMBL:KAF4641427.1};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000312|EMBL:KAF4641427.1};
RN [1] {ECO:0000312|EMBL:KAF4641427.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RH-88 {ECO:0000312|EMBL:KAF4641427.1};
RA Lorenzi H.A., Venepally P., Rozenberg A., Sibley D.;
RT "Genome sequence of Toxoplasma gondii RH-88 strain.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, NOMENCLATURE,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 188-PHE--LEU-504.
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: L-tyrosine transporter that is essential for parasite
CC survival and virulence (PubMed:30742695). May also act as an aromatic
CC and large neutral amino acid transporter (PubMed:30742695). Does not
CC cotransport other charged ions (PubMed:30742695). Involved in amino
CC acid homeostasis by facilitating the net uptake of L-tyrosine and
CC maintaining intracellular pools of aromatic and large neutral amino
CC acids through exchange (PubMed:30742695).
CC {ECO:0000269|PubMed:30742695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine(in) = L-tyrosine(out); Xref=Rhea:RHEA:68572,
CC ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:30742695};
CC -!- ACTIVITY REGULATION: L-tyrosine uptake is stimulated in trans by
CC aromatic and large neutral amino acids, but not smaller or charged
CC amino acids. {ECO:0000269|PubMed:30742695}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30742695};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the tachyzoite stage.
CC {ECO:0000269|PubMed:30742695}.
CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAAUHK010000194; KAF4641427.1; -; Genomic_DNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005302; F:L-tyrosine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0080144; P:amino acid homeostasis; IMP:UniProtKB.
DR GO; GO:1903808; P:L-tyrosine import across plasma membrane; IMP:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
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..504
FT /note="Aromatic and large neutral amino acid transporter 5-
FT 3"
FT /id="PRO_0000454214"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 188..504
FT /note="Missing: Tachyzoites have severe growth defect.
FT Severe reduction in L-tyrosine and L-phenylalanine uptake.
FT Does not cause toxoplasmosis in mice."
FT /evidence="ECO:0000269|PubMed:30742695"
SQ SEQUENCE 504 AA; 54531 MW; 9BF183BBDDF6BAEB CRC64;
MESTEATMVE RKAESPSSGD RARSIELAHQ PTGAGASLSS FEVGGAKQGV NKAQDSAVNK
GAANTPPRVA FGLSRYVVLV AYCLYCLLSG PSFMNWTTIA DSLYKSGAFE WECKPGEIDT
SVLPHEPKCP EQEVSVNHLF TVASCSYFVF AMLGGIMLDF AGPKFGALTG LACLITGWTL
FGFSSESFRA YVPAMVFMGA GIDMAFFPCL CGANLFPGMV ATIIAVYGSF RSISFIVGLS
LRTIYINVEG ATFRGVMLGY VGAGLGFCLL VALFIIPRRA WPAPDEAPSA SAEQDVEAGA
DALAQKGEKN LTAIQSMKRD FLSLSFLPLF PYFVLVLITI LFFAPSAKRL IPSAYEANQI
ISIFSFVPCI ILGGIADRLG IVPVMMICNT CGLLSWILML IPGIPCFAAS QYIVSILISI
QMSFLVSQVY CYVTEIFYPE NLGKMIGFLC SVGGIISLVT DPMRKYSVDN GFYTMTVLCL
IFALINEGLL LFMYVRKRKV PKVL
