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Database: UniProt
Entry: A0A0D9S0P5_CHLSB
LinkDB: A0A0D9S0P5_CHLSB
Original site: A0A0D9S0P5_CHLSB 
ID   A0A0D9S0P5_CHLSB        Unreviewed;       315 AA.
AC   A0A0D9S0P5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008};
DE   AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008};
GN   Name=SLC25A31 {ECO:0000313|Ensembl:ENSCSAP00000014434.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014434.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000014434.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000014434.1}
RP   IDENTIFICATION.
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|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       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
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; AQIB01017179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01017180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007997947.1; XM_007999756.1.
DR   AlphaFoldDB; A0A0D9S0P5; -.
DR   STRING; 60711.ENSCSAP00000014434; -.
DR   Ensembl; ENSCSAT00000001651.1; ENSCSAP00000014434.1; ENSCSAG00000003617.1.
DR   GeneID; 103236238; -.
DR   KEGG; csab:103236238; -.
DR   CTD; 83447; -.
DR   eggNOG; KOG0749; Eukaryota.
DR   GeneTree; ENSGT00940000160648; -.
DR   OMA; FRGIHHF; -.
DR   OrthoDB; 1330359at2759; -.
DR   BioGRID-ORCS; 103236238; 2 hits in 16 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 7.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005757; C:mitochondrial permeability transition pore complex; IEA:Ensembl.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR   GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR   GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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:SF40; ADP_ATP TRANSLOCASE 4; 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}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368008};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   TRANSMEM        121..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   TRANSMEM        222..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   REPEAT          18..110
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          123..213
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          220..307
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   315 AA;  35065 MW;  67EB8A49F59DE674 CRC64;
     MHREPPKKKA EKRLFDASSF GKDLLAGGVA AAVSKTAVAP IERVKLLLQV QASSKQISPE
     ARYKGMVDCL VRIPREQGFF SFWRGNLANV IRYFPTQALN FAFKDKYKQL FMSGVNKEKQ
     FWRWFLANLA SGGAAGATSL CVVYPLDFAR TRLGVDIGKG PEERQFKGLG DCIMKIAKSD
     GIAGLYQGFG VSVQGIIVYR ASYFGAYDTV KGLLPKSKKT PFLVSFFIAQ VVTTCSGILS
     YPFDTVRRRM MMQSGEAKRQ YKGTLDCFVK IYQHEGINSF FRGAFSNVLR GTGGALVLVL
     YDKIKEFFHI DIGGR
//
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