AT8_PLABA
ID AT8_PLABA Reviewed; 506 AA.
AC A0A509AE54;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Cationic amino acid transporter 8 {ECO:0000303|PubMed:30742695};
DE AltName: Full=Apicomplexan amino acid transporter 8 {ECO:0000303|PubMed:30742695};
DE Short=PbApiAT8 {ECO:0000303|PubMed:30742695};
DE AltName: Full=Novel putative transporter 1 {ECO:0000303|PubMed:21752110};
DE Short=PbNPT1 {ECO:0000303|PubMed:21752110};
GN Name=ApiAT8 {ECO:0000303|PubMed:30742695};
GN Synonyms=NTP1 {ECO:0000303|PubMed:21752110};
GN ORFNames=PBANKA_0208300 {ECO:0000312|EMBL:VUC53957.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=NK65 {ECO:0000269|PubMed:21752110};
RX PubMed=21752110; DOI=10.1111/j.1365-2958.2011.07767.x;
RA Boisson B., Lacroix C., Bischoff E., Gueirard P., Bargieri D.Y.,
RA Franke-Fayard B., Janse C.J., Menard R., Baldacci P.;
RT "The novel putative transporter NPT1 plays a critical role in early stages
RT of Plasmodium berghei sexual development.";
RL Mol. Microbiol. 81:1343-1357(2011).
RN [3] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
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 [4] {ECO:0000305}
RP NOMENCLATURE.
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: Cationic amino acid transporter which transports L-arginine,
CC L-lysine and, to a lesser extent, L-histidine and ornithine
CC (PubMed:28205520). Plays an essential role in gametogenesis
CC (PubMed:21752110). {ECO:0000269|PubMed:21752110,
CC ECO:0000269|PubMed:28205520}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41 uM for arginine {ECO:0000269|PubMed:28205520};
CC KM=130 uM for lysine {ECO:0000269|PubMed:28205520};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21752110,
CC ECO:0000269|PubMed:28205520}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage including
CC in trophozoites, schizonts and free merozoites (PubMed:21752110).
CC Expressed in gametocytes (PubMed:21752110). Expressed during the liver
CC stage (PubMed:21752110). {ECO:0000269|PubMed:21752110}.
CC -!- DISRUPTION PHENOTYPE: Growth is normal in asexual blood stages, however
CC uptake of arginine and lysine is decreased (PubMed:21752110,
CC PubMed:28205520). Impaired production of male gametocytes and fertile
CC female gametocytes (PubMed:21752110, PubMed:28205520). Rare gametocytes
CC that are produced have unusual membrane structures (whorls) and large
CC vacuoles in their cytoplasm (PubMed:21752110).
CC {ECO:0000269|PubMed:21752110, 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; LK023117; VUC53957.1; -; Genomic_DNA.
DR STRING; 5823.A0A509AE54; -.
DR VEuPathDB; PlasmoDB:PBANKA_0208300; -.
DR OMA; TILACWF; -.
DR Proteomes; UP000074855; Chromosome 2.
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:0015189; F:L-lysine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0097639; P:L-lysine import across plasma membrane; IMP:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..506
FT /note="Cationic amino acid transporter 8"
FT /id="PRO_0000454213"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 506 AA; 57227 MW; D1A809B4FF740D05 CRC64;
MNESNCTKIV NFLKGMRLKT NPNLPGAKQK TPLNIHRFYL LLIIIIYTAT SACIYFDWTS
IRNLLLNVGK YEHLNISKYA DITLSPQYKK INNLYPMTLA IHFTMSVFCG FLYDHIGPKF
TAIIGQGFNI LSWIFLSIDT TKIDTTLIGF IFLGLGADTA FIPILTVSNL FPDISTFIMT
VIGAAASLSY AVPATLNFVY KKYPHFPFYY ICYGYIFIIL IPCLLVATFL LPMKPFKGLD
YYLENDQESD SKNKEQISYT DNDVEMQPSL IQNGNTNVSN NVNKNKATKN IIEGENFHKQ
SILLFFKVLL SYPSICIIVY FILFNISTVF YGMVTDIYFS YNKSIINIIN ILMPISFIPC
IIFGRFINKY GAAIIIIIMN AFSALMHLTA LIKHQAAGLI SAFLYMCAAS IYTSQIYCFL
LNAFPSVVFG KLLGITSLFG GMFSLFCEKL YDNISNSSGN KNDPTTISIL LAISFIIMFL
PLSILYTRNY EKNIESVNSE KNQIQA
