ID A7YXV1_KARVE Unreviewed; 314 AA.
AC A7YXV1;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008};
DE AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008};
OS Karlodinium veneficum (Dinoflagellate) (Karlodinium micrum).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Gymnodiniales; Kareniaceae;
OC Karlodinium.
OX NCBI_TaxID=407301 {ECO:0000313|EMBL:ABV22230.1};
RN [1] {ECO:0000313|EMBL:ABV22230.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1975 {ECO:0000313|EMBL:ABV22230.1};
RX PubMed=17360573; DOI=10.1073/pnas.0700258104;
RA Zhang H., Hou Y., Miranda L., Campbell D.A., Sturm N.R., Gaasterland T.,
RA Lin S.;
RT "Spliced leader RNA trans-splicing in dinoflagellates.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4618-4623(2007).
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}.
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DR EMBL; EF134116; ABV22230.1; -; mRNA.
DR AlphaFoldDB; A7YXV1; -.
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 2: Evidence at transcript level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; 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 113..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368008"
FT TRANSMEM 174..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368008"
FT TRANSMEM 213..237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368008"
FT REPEAT 9..103
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 115..204
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 214..304
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 314 AA; 34045 MW; A0D27E5FB8C6692C CRC64;
MPKEEVSFQA WAMDFTLGGV SGAVSRTFTA PIERVKLLIQ TQDANPLIRS GEVKRYTGIV
DCFSRIHAEQ GMAAFWRGNF TNCIRYFPTQ AFNLSFKDTI KKMFPKYSPK ENFGMFFAVN
MASGGMAAAG SLCIVYPLDY ARTRLASDVG SGKKTFTGLG DCLKKTASGP LGPAGLYAGF
GVSLAGIIPY RGFQLGAFDT LVGLNPYKND TGVLGIVSTF ASAQTAIILG AGISYPFDTV
RRRLQMQAEK PVEEHIYKGT FDCLKKIAAE EGVAAGVYKG FVANAFRSVG AALVLVLYER
GKNTLDFKRC LIIL
//
