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Database: UniProt
Entry: A5KDT4_PLAVS
LinkDB: A5KDT4_PLAVS
Original site: A5KDT4_PLAVS 
ID   A5KDT4_PLAVS            Unreviewed;       301 AA.
AC   A5KDT4;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008};
DE   AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008};
GN   ORFNames=PVX_110895 {ECO:0000313|EMBL:EDL42380.1};
OS   Plasmodium vivax (strain Salvador I).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL42380.1, ECO:0000313|Proteomes:UP000008333};
RN   [1] {ECO:0000313|EMBL:EDL42380.1, ECO:0000313|Proteomes:UP000008333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Salvador I {ECO:0000313|EMBL:EDL42380.1,
RC   ECO:0000313|Proteomes:UP000008333};
RX   PubMed=18843361; DOI=10.1038/nature07327;
RA   Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA   Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.,
RA   Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V.,
RA   Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA   Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O.,
RA   Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA   Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA   Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT   "Comparative genomics of the neglected human malaria parasite Plasmodium
RT   vivax.";
RL   Nature 455:757-763(2008).
CC   -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the membrane.
CC       {ECO:0000256|RuleBase:RU368008}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00024143};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC         Evidence={ECO:0000256|ARBA:ARBA00024143};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC       ECO:0000256|RuleBase:RU368008}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU368008}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368008}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU368008}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDL42380.1}.
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DR   EMBL; AAKM01002769; EDL42380.1; -; Genomic_DNA.
DR   RefSeq; XP_001608404.1; XM_001608354.1.
DR   AlphaFoldDB; A5KDT4; -.
DR   STRING; 126793.A5KDT4; -.
DR   EnsemblProtists; EDL42380; EDL42380; PVX_110895.
DR   GeneID; 5471291; -.
DR   KEGG; pvx:PVX_110895; -.
DR   VEuPathDB; PlasmoDB:PVX_110895; -.
DR   InParanoid; A5KDT4; -.
DR   OMA; NILISWM; -.
DR   PhylomeDB; A5KDT4; -.
DR   Proteomes; UP000008333; Chromosome 6.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:InterPro.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR   GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR002113; ADT_euk_type.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45635; ADP,ATP CARRIER PROTEIN 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR45635:SF14; ADP,ATP CARRIER PROTEIN-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00927; ADPTRNSLCASE.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000008333};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|RuleBase:RU368008};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   TRANSMEM        111..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   TRANSMEM        212..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   REPEAT          7..101
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          113..202
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          210..300
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   301 AA;  33721 MW;  DF1C09E0889B4291 CRC64;
     MSGDFKTNFA ADFLMGGVSA AISKTVVAPI ERVKMLIQTQ DSIPEIKSGQ VERYSGLINC
     FKRVSQEQGV MSLWRGNTAN IIRYFPTQAF NFAFKDYFKN VFPKYDQNTD FTKFFCVNIL
     SGATAGAISL LIVYPLDFAR TRLASDIGKG KDRQFTGLFD CLKKIYKQTG FLSLYSGFGV
     SVTGIIVYRG SYFGLYDSAK ALLFNNDKNT NIVLKWAVAQ SVTILAGLIS YPFDTVRRRM
     MMMSGRKAKE EIQYKNTIDC WIKILKNEGL AGFFKGAWAN VIRGAGGALV LVFYDELQKL
     I
//
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