CRT_PLABE
ID CRT_PLABE Reviewed; 425 AA.
AC Q9GSD8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Putative chloroquine resistance transporter;
DE AltName: Full=Probable transporter cg10;
DE Short=pbcg10;
DE AltName: Full=pfcrt homolog;
GN Name=CG10;
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11343215; DOI=10.1086/320707;
RA Nomura T., Carlton J.M.-R., Baird J.K., del Portillo H.A., Fryauff D.J.,
RA Rathore D., Fidock D.A., Su X.-Z., Collins W.E., McCutchan T.F.,
RA Wootton J.C., Wellems T.E.;
RT "Evidence for different mechanisms of chloroquine resistance in 2
RT Plasmodium species that cause human malaria.";
RL J. Infect. Dis. 183:1653-1661(2001).
CC -!- FUNCTION: May regulate endogenous transporter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC Note=Localizes to the parasite digestive vacuole, the site of
CC chloroquine action. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CRT-like transporter family. {ECO:0000305}.
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DR EMBL; AF314645; AAG27734.1; -; mRNA.
DR AlphaFoldDB; Q9GSD8; -.
DR SMR; Q9GSD8; -.
DR VEuPathDB; PlasmoDB:PBANKA_1219500; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR013936; CRT-like.
DR InterPro; IPR017258; Transprt_Chloroquine.
DR PANTHER; PTHR31326; PTHR31326; 1.
DR Pfam; PF08627; CRT-like; 1.
DR PIRSF; PIRSF037671; Transprt_Chloroquine_res; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..425
FT /note="Putative chloroquine resistance transporter"
FT /id="PRO_0000385356"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..88
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..157
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..210
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..318
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 425 AA; 48937 MW; 0C6973B42B033CDE CRC64;
MTGIKKGKNK KKNMKNDDRY KELDSLITNG SEIGNNSGRS CVKRFFKIIG NEMKNNVYVY
LLSILYLCVC VMNKVFAKRT LNKMGNYSFV TSETHNIICI IVFQLLYFIY RKTSSSSVYK
NESQKNFGWQ FFLISLLDAS TVIISMIGLT RTTGNIQSFI MQLIIPVNMY FWFMFLGYRY
HLFNYLGAFI ILITIAVVET FLSFETQGEN SIIFNLIMIS AFNTLSFSNM TREVVFKKHK
INILRLNAMV VLFQFFTSLL VLPVYNIPFL KEIYMPFSEM STNINNGLRC LFYGENTIVE
NCGVGMVKMC DNCEGAWKTF ITFSFFNICD NLLACYIIDK FSTMTYTIVS CIQGPAITIA
YYFKFLAGDA VRKPRILDFL TLFGYLFGTI IYRIGNIILE KKQVIKSQNS NDSEAELTSI
ETSRA