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Database: UniProt
Entry: A0A2K6C7J6_MACNE
LinkDB: A0A2K6C7J6_MACNE
Original site: A0A2K6C7J6_MACNE 
ID   A0A2K6C7J6_MACNE        Unreviewed;       468 AA.
AC   A0A2K6C7J6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Solute carrier family 25 member 23 {ECO:0000313|Ensembl:ENSMNEP00000019624.1};
GN   Name=SLC25A23 {ECO:0000313|Ensembl:ENSMNEP00000019624.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000019624.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000019624.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-AMP(in) + ADP(out) + H(+)(out) = 3'-AMP(out) + ADP(in) +
CC         H(+)(in); Xref=Rhea:RHEA:73679, ChEBI:CHEBI:15378, ChEBI:CHEBI:60880,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036310};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-AMP(out) + phosphate(in) = 3'-AMP(in) + phosphate(out);
CC         Xref=Rhea:RHEA:73691, ChEBI:CHEBI:43474, ChEBI:CHEBI:60880;
CC         Evidence={ECO:0000256|ARBA:ARBA00036289};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + ATP(in) + H(+)(out) + Mg(2+)(in) = ADP(in) +
CC         ATP(out) + H(+)(in) + Mg(2+)(out); Xref=Rhea:RHEA:73659,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036612};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) +
CC         phosphate(out); Xref=Rhea:RHEA:65844, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036415};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out);
CC         Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + dAMP(in) + H(+)(out) = ADP(in) + dAMP(out) +
CC         H(+)(in); Xref=Rhea:RHEA:73675, ChEBI:CHEBI:15378, ChEBI:CHEBI:58245,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036316};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + diphosphate(in) = ADP(in) + diphosphate(out);
CC         Xref=Rhea:RHEA:73671, ChEBI:CHEBI:33019, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036630};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP(out) + phosphate(in) = AMP(in) + phosphate(out);
CC         Xref=Rhea:RHEA:70259, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00036908};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP(out) + 2 H(+)(out) + phosphate(in) = ATP(in) + 2 H(+)(in)
CC         + phosphate(out); Xref=Rhea:RHEA:72035, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000256|ARBA:ARBA00036970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in)
CC         + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000256|ARBA:ARBA00034993};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dADP(out) + H(+)(out) + phosphate(in) = dADP(in) + H(+)(in) +
CC         phosphate(out); Xref=Rhea:RHEA:73695, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57667;
CC         Evidence={ECO:0000256|ARBA:ARBA00036766};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dAMP(out) + phosphate(in) = dAMP(in) + phosphate(out);
CC         Xref=Rhea:RHEA:73687, ChEBI:CHEBI:43474, ChEBI:CHEBI:58245;
CC         Evidence={ECO:0000256|ARBA:ARBA00036282};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       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}.
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DR   RefSeq; XP_011744794.1; XM_011746492.1.
DR   AlphaFoldDB; A0A2K6C7J6; -.
DR   Ensembl; ENSMNET00000043865.1; ENSMNEP00000019624.1; ENSMNEG00000033667.1.
DR   GeneID; 105484653; -.
DR   CTD; 79085; -.
DR   GeneTree; ENSGT00940000159428; -.
DR   OMA; ICAQFSI; -.
DR   OrthoDB; 1330359at2759; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000033667; Expressed in temporal lobe and 10 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR24089:SF196; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-3; 1.
DR   PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Antiport {ECO:0000256|ARBA:ARBA00022449};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   DOMAIN          9..44
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          77..112
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          113..148
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          183..269
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          277..362
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          374..462
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REGION          34..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  52392 MW;  880BB72B94AD6685 CRC64;
     MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISSEGDA
     DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISITLEQAEK
     ILHSMDRDGT MTIDWQEWRD HFLLHSLENV EDVLYFWKHS TVLDIGECLT VPDEFSKQEK
     LTGMWWKQLV AGAVAGAVSR TGTAPLDRLK VFMQVHASKT NRLNILGGLR SMVLEGGIRS
     LWRGNGINVL KIAPESAIKF MAYEQIKRAI LGQQETLHVQ ERFVAGSLAG ATAQTIIYPM
     EVLKTRLTLR RTGQYKGLLD CARRILEREG PRAFYRGYLP NVLGIIPYAG IDLAVYETLK
     NWWLQQYSHD SADPGILVLL ACGTISSTCG QIASYPLALV RTRMQAQASI EGGPQLSMLG
     LLRHILSQEG MRGLYRGIAP NFMKVIPAVS ISYVVYENMK QALGVTSR
//
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