CRT_THEAN
ID CRT_THEAN Reviewed; 430 AA.
AC Q4UDS9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Putative chloroquine resistance transporter;
DE AltName: Full=Probable transporter cg10;
GN ORFNames=TA12005;
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara;
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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; CR940348; CAI74760.1; -; Genomic_DNA.
DR RefSeq; XP_952492.1; XM_947399.1.
DR AlphaFoldDB; Q4UDS9; -.
DR SMR; Q4UDS9; -.
DR STRING; 5874.XP_952492.1; -.
DR GeneID; 3861985; -.
DR KEGG; tan:TA12005; -.
DR VEuPathDB; PiroplasmaDB:TA12005; -.
DR eggNOG; ENOG502QR5M; Eukaryota.
DR InParanoid; Q4UDS9; -.
DR OMA; IWPALMI; -.
DR OrthoDB; 630915at2759; -.
DR Proteomes; UP000001950; Chromosome 2.
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 Pfam; PF08627; CRT-like; 1.
DR PIRSF; PIRSF037671; Transprt_Chloroquine_res; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..430
FT /note="Putative chloroquine resistance transporter"
FT /id="PRO_0000385362"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..88
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..147
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..206
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..306
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..364
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 430 AA; 48721 MW; 701B8C07228E66CC CRC64;
MLKEGSSLDL SASSSSGTLR SDNSFGNSPL DRITSLLILI YKSIRACFKW IYSKSFGIIC
ILFVILDVLT TVFFKRFIDH TKNYVMFTIQ VIIFTFWIIV CCIAILCFLF NREYMKRHFN
VRPLVFLGFL DMLSTGLSAN GSAHTSGLML VLLGQISVPL TMVSCKLILS KKYHHYQYIS
SAIILTFAVL KPILNRTDTT DNRFYNNMLY LLASVPDSIA SALREKQYTS KFFHVVKYQF
FGFLFHFFYN ILYTLLFTLP FNSVKGYFDS LYKLCVNGYK CIFFGVNTIT ENCGPTLIPT
CDNCLEAFKI YCLYILFSSA IRVAYVFIML DGSVTFTLLL GTVKVPLTSI AFSLRFIAGD
STTSFNLLDV VCFLGIVAGL LLYALGSKKI QEETDLLESP LIDDAESEHE LLSTGTEKLM
RSEICHDLFT
