ID A0A384DE00_URSMA Unreviewed; 304 AA.
AC A0A384DE00;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Kidney mitochondrial carrier protein 1 {ECO:0000256|ARBA:ARBA00040654};
DE AltName: Full=Solute carrier family 25 member 30 {ECO:0000256|ARBA:ARBA00041892};
GN Name=SLC25A30 {ECO:0000313|RefSeq:XP_008705054.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008705054.1};
RN [1] {ECO:0000313|RefSeq:XP_008705054.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008705054.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-tartrate(in) + sulfate(out) = (2R,3R)-tartrate(out) +
CC sulfate(in); Xref=Rhea:RHEA:73403, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:30924; Evidence={ECO:0000256|ARBA:ARBA00035985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-citramalate(in) + sulfate(out) = (3R)-citramalate(out) +
CC sulfate(in); Xref=Rhea:RHEA:73227, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:30934; Evidence={ECO:0000256|ARBA:ARBA00035807};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-citramalate(in) + sulfate(out) = (3S)-citramalate(out) +
CC sulfate(in); Xref=Rhea:RHEA:73223, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:30936; Evidence={ECO:0000256|ARBA:ARBA00036130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + sulfate(out) = (S)-malate(out) + sulfate(in);
CC Xref=Rhea:RHEA:71615, ChEBI:CHEBI:15589, ChEBI:CHEBI:16189;
CC Evidence={ECO:0000256|ARBA:ARBA00037004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(out) = (S)-malate(in); Xref=Rhea:RHEA:74555,
CC ChEBI:CHEBI:15589; Evidence={ECO:0000256|ARBA:ARBA00036759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S,S)-tartrate(in) + sulfate(out) = (S,S)-tartrate(out) +
CC sulfate(in); Xref=Rhea:RHEA:73407, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:30927; Evidence={ECO:0000256|ARBA:ARBA00036586};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate(in) + sulfate(out) = D-aspartate(out) +
CC sulfate(in); Xref=Rhea:RHEA:73399, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:29990; Evidence={ECO:0000256|ARBA:ARBA00036479};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate(in) + sulfate(out) = L-aspartate(out) +
CC sulfate(in); Xref=Rhea:RHEA:73395, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:29991; Evidence={ECO:0000256|ARBA:ARBA00036015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=maleate(in) + sulfate(out) = maleate(out) + sulfate(in);
CC Xref=Rhea:RHEA:73199, ChEBI:CHEBI:16189, ChEBI:CHEBI:30780;
CC Evidence={ECO:0000256|ARBA:ARBA00035765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=malonate(in) + sulfate(out) = malonate(out) + sulfate(in);
CC Xref=Rhea:RHEA:73195, ChEBI:CHEBI:15792, ChEBI:CHEBI:16189;
CC Evidence={ECO:0000256|ARBA:ARBA00036751};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxalate(in) + sulfate(out) = oxalate(out) + sulfate(in);
CC Xref=Rhea:RHEA:72275, ChEBI:CHEBI:16189, ChEBI:CHEBI:30623;
CC Evidence={ECO:0000256|ARBA:ARBA00036514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) + sulfate(out) = phosphate(out) + sulfate(in);
CC Xref=Rhea:RHEA:71631, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00036861};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000256|ARBA:ARBA00036616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=succinate(in) + sulfate(out) = succinate(out) + sulfate(in);
CC Xref=Rhea:RHEA:73411, ChEBI:CHEBI:16189, ChEBI:CHEBI:30031;
CC Evidence={ECO:0000256|ARBA:ARBA00036691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sulfate(in) = sulfate(out); Xref=Rhea:RHEA:34983,
CC ChEBI:CHEBI:16189; Evidence={ECO:0000256|ARBA:ARBA00035907};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sulfate(out) + sulfite(in) = sulfate(in) + sulfite(out);
CC Xref=Rhea:RHEA:73207, ChEBI:CHEBI:16189, ChEBI:CHEBI:17359;
CC Evidence={ECO:0000256|ARBA:ARBA00036232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sulfate(out) + thiosulfate(in) = sulfate(in) +
CC thiosulfate(out); Xref=Rhea:RHEA:73215, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:33542; Evidence={ECO:0000256|ARBA:ARBA00036708};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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_008705054.1; XM_008706832.2.
DR AlphaFoldDB; A0A384DE00; -.
DR GeneID; 103677585; -.
DR CTD; 253512; -.
DR OrthoDB; 1832865at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45618:SF11; KIDNEY MITOCHONDRIAL CARRIER PROTEIN 1; 1.
DR PANTHER; PTHR45618; MITOCHONDRIAL DICARBOXYLATE CARRIER-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00784; MTUNCOUPLING.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000261680};
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 REPEAT 28..117
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 125..210
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 304 AA; 32971 MW; E91BBFB6CD272EBE CRC64;
MCKKSPVVGY VSLIKEGTAG KMAALNWKPF VYGGLASITA ECGTFPIDLT KTRLQIQGQT
NDANFKEIRY RGMLHALVRI GREEGLKALY SGIAPAMLRQ ASYGTIKIGT YQSLKRLFVE
HPEDETLLVN VVCGILSGVV SSTIANPTDV LKIRMQAQSS TIQGGMIGNF INIYQQEGAR
GLWKGVSLTA QRAAIVVGVE LPVYDLTKKH LILSGLMGDT VYTHFLSSFT CGLAGALASN
PVDVVRTRMM NQRVLRDGRC SGYTGTLDCL LQLPIACLGV GRFNTEPSSS PMQKPLKTKR
GRGH
//
