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Database: UniProt
Entry: M4AEP2_XIPMA
LinkDB: M4AEP2_XIPMA
Original site: M4AEP2_XIPMA 
ID   M4AEP2_XIPMA            Unreviewed;       299 AA.
AC   M4AEP2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
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   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000012936.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000012936.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000012936.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the membrane.
CC       {ECO:0000256|RuleBase:RU368008}.
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}.
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DR   AlphaFoldDB; M4AEP2; -.
DR   STRING; 8083.ENSXMAP00000012936; -.
DR   Ensembl; ENSXMAT00000012952.2; ENSXMAP00000012936.2; ENSXMAG00000028921.1.
DR   eggNOG; KOG0749; Eukaryota.
DR   GeneTree; ENSGT00940000162883; -.
DR   HOGENOM; CLU_015166_12_0_1; -.
DR   InParanoid; M4AEP2; -.
DR   OMA; GYAMWMV; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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:SF13; ADP_ATP TRANSLOCASE 3; 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:UP000002852};
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        211..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   REPEAT          7..99
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          112..202
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          213..298
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   299 AA;  33126 MW;  4B75A97BC7447C68 CRC64;
     MMTDTAISFA KDFLAGGIAA AISKTAVAPI ERVKLLLQVQ HASKQITADK QYKGIVDCVV
     RIPKEQGFLS FWRGNLANVI RYFPTQALNF AFKDKYKKIF LDGVDKRTQF WRYFAGNLAS
     GGAAGATSLC FVYPLDFART RLAADVGKAG QEREFKGLGD CLMKIFKSDG LKGLYQGFNV
     SVQGIIIYRA AYFGVYDTAK GMLPDPKNTH IVVSWMIAQS VTAVAGLVSY PFDTVRRRMM
     MQSGRKGADI MYTGTLDCWR KIARDEGSKA FFKGAWSNVL RGMGGAFVLV LYDELKKVI
//
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