CRT_PLACH
ID CRT_PLACH Reviewed; 424 AA.
AC Q7Z0V9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Putative chloroquine resistance transporter;
DE AltName: Full=Probable transporter cg10;
DE Short=pccg10;
DE AltName: Full=pfcrt homolog;
GN Name=CG10;
OS Plasmodium chabaudi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5825;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14668009; DOI=10.1016/j.molbiopara.2003.08.010;
RA Hunt P., Cravo P.V., Donleavy P., Carlton J.M.-R., Walliker D.;
RT "Chloroquine resistance in Plasmodium chabaudi: are chloroquine-resistance
RT transporter (crt) and multi-drug resistance (mdr1) orthologues involved?";
RL Mol. Biochem. Parasitol. 133:27-35(2004).
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; AY304549; AAP68830.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7Z0V9; -.
DR SMR; Q7Z0V9; -.
DR VEuPathDB; PlasmoDB:PCHAS_1220200; -.
DR eggNOG; ENOG502QR5M; Eukaryota.
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 3: Inferred from homology;
KW Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..424
FT /note="Putative chloroquine resistance transporter"
FT /id="PRO_0000385357"
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..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..156
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..209
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..317
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..377
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 424 AA; 48579 MW; 412D844286A1F0B3 CRC64;
MTGMKKGKNK KKNVKNDERY KELDSLISND SEIGNNSRWG GAKRICKLIG NEMRNNIYVY
LLSILYLCVS VMNKVFSKRT LNKIGNYSFV TSEVHNMICT IVFQLLYFIY RKTSNPASRN
ESQKNFGWQF FLISLLDAST VIITMIGLTR TTGNIQSFIM QLIIPVNMYF CFIFLGYRYH
LFNYLGAFII LITIAAVETV LSYETQSDNS IIFNLIMIFA LIPLSFSNMT REVVFKKHKI
NIIRLNAMVA LFQFFTSLLV LPVYNISFLK EIYMPFSEMG TNINDGLRCL FYGQSTIVEN
CGVGMVKMCD QCEGAWKTFI TYSFFNICDN LLVCYIIDKF STMTYTIVSC IQGPAITIAY
YFKFLAGDVV RQPRLLDFLT LFGYLLGTII YRIGNIILEK KKMLKALNTD GSEAELTSIE
TSTA