ID A0A2D1QAC2_9SAUR Unreviewed; 400 AA. AC A0A2D1QAC2; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 14-DEC-2022, entry version 14. DE RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008}; DE AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008}; GN Name=slc25a5 {ECO:0000313|EMBL:ATP07232.1}; OS Emydura macquarii (Murray river turtle). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudinata; Testudines; Pleurodira; Chelidae; Emydura. OX NCBI_TaxID=90392 {ECO:0000313|EMBL:ATP07232.1}; RN [1] {ECO:0000313|EMBL:ATP07232.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29036698; RA Radhakrishnan S., Valenzuela N.; RT "Chromosomal Context Affects the Molecular Evolution of Sex-linked Genes RT and Their Autosomal Counterparts in Turtles and Other Vertebrates."; RL J. Hered. 108:720-730(2017). 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:ARBA00024537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; CC Evidence={ECO:0000256|ARBA:ARBA00024169}; CC -!- SUBUNIT: Monomer. {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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MF686771; ATP07232.1; -; Genomic_DNA. 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; -; 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; 4. 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|RuleBase:RU368008}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000488}; KW Transmembrane helix {ECO:0000256|RuleBase:RU368008}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}. FT TRANSMEM 279..299 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU368008" SQ SEQUENCE 400 AA; 44244 MW; FE71D84DE566EC03 CRC64; MADAALSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXQHASKQIT ADMQYKGIID CVVRIPKEQG FLSFWRGNLA NVIRYFPTQA LNFAFKDKYK QVFLGGVDKR TQFWRYFAGN LASGGAAGAT SLCFVYPLDF ARTRLAADVG KAGADREFKG LGDCLVKIFK SDGLKGLYQG FNVSVQGIII YRAAYFGIYD TAKXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXGML PDPKNTHIIV SWMIAQTVTA VAGLTSYPFD TVRRRMMMQS GRKAXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXTD IMYSGTIDCW RKIARDEGSK AFFKGAWSNV LRGMGGAFVL VLYDEIKKYT //