ID A0A2K6NDL6_RHIRO Unreviewed; 468 AA.
AC A0A2K6NDL6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Solute carrier family 25 member 23 {ECO:0000313|Ensembl:ENSRROP00000002369.1};
GN Name=SLC25A23 {ECO:0000313|Ensembl:ENSRROP00000002369.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000002369.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000002369.1}
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_010365471.1; XM_010367169.1.
DR AlphaFoldDB; A0A2K6NDL6; -.
DR Ensembl; ENSRROT00000010685.1; ENSRROP00000002369.1; ENSRROG00000009609.1.
DR GeneID; 104665370; -.
DR KEGG; rro:104665370; -.
DR CTD; 79085; -.
DR GeneTree; ENSGT00940000159428; -.
DR OMA; ICAQFSI; -.
DR OrthoDB; 1330359at2759; -.
DR Proteomes; UP000233200; Unplaced.
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:UP000233200};
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 38..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 52394 MW; 4E5A7EF8809C2653 CRC64;
MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISCEGDA
DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISISLEQAEK
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
//