ID Q0IH35_XENLA Unreviewed; 305 AA.
AC Q0IH35;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Mitochondrial 2-oxoglutarate/malate carrier protein {ECO:0000256|ARBA:ARBA00040264};
DE AltName: Full=Solute carrier family 25 member 11 {ECO:0000256|ARBA:ARBA00041881};
GN Name=slc25a11.L {ECO:0000313|RefSeq:NP_001090497.1,
GN ECO:0000313|Xenbase:XB-GENE-979678};
GN Synonyms=MGC154791 {ECO:0000313|EMBL:AAI23334.1}, slc25a11
GN {ECO:0000313|RefSeq:NP_001090497.1,
GN ECO:0000313|Xenbase:XB-GENE-979678};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI23334.1};
RN [1] {ECO:0000313|RefSeq:NP_001090497.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI23334.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000313|EMBL:AAI23334.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001090497.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-
CC oxoglutarate(in); Xref=Rhea:RHEA:71587, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036491};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + maleate(in) = 2-oxoglutarate(in) +
CC maleate(out); Xref=Rhea:RHEA:71599, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30780; Evidence={ECO:0000256|ARBA:ARBA00036076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + malonate(in) = 2-oxoglutarate(in) +
CC malonate(out); Xref=Rhea:RHEA:71591, ChEBI:CHEBI:15792,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036366};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + oxaloacetate(in) = 2-oxoglutarate(in) +
CC oxaloacetate(out); Xref=Rhea:RHEA:71603, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + succinate(in) = 2-oxoglutarate(in) +
CC succinate(out); Xref=Rhea:RHEA:71595, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031; Evidence={ECO:0000256|ARBA:ARBA00036084};
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 EMBL; BC123333; AAI23334.1; -; mRNA.
DR RefSeq; NP_001090497.1; NM_001097028.1.
DR STRING; 8355.Q0IH35; -.
DR PaxDb; 8355-Q0IH35; -.
DR DNASU; 779410; -.
DR GeneID; 779410; -.
DR KEGG; xla:779410; -.
DR AGR; Xenbase:XB-GENE-979678; -.
DR CTD; 779410; -.
DR Xenbase; XB-GENE-979678; slc25a11.L.
DR OMA; TLWRGAI; -.
DR OrthoDB; 2086232at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 779410; Expressed in muscle tissue and 19 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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:SF9; MITOCHONDRIAL 2-OXOGLUTARATE_MALATE CARRIER PROTEIN; 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; 3.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000186698};
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|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT TRANSMEM 16..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 14..99
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 108..199
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 208..297
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 305 AA; 33596 MW; D6A98C1E2696BEF1 CRC64;
MAEAGKQRTS PKSVKFLFGG LAGMGATVFV QPLDLVKNRM QLSGEGAKTK EYKTSFHAVG
SILRNEGLRG IYTGLSAGLL RQATYTTTRL GIYTILFEKF TKADGTPPNF FMKAAIGMTA
GATGAFVGTP AEVALIRMTA DGRMPVDQRR GYTNVFNALV RMTREEGITT LWRGCIPTMA
RAVVVNAAQL ASYSQSKQFL LDSGYFGDDI LCHFCASMIS GLVTTAASMP VDIAKTRIQN
MRMIDGKPEY KNGLDVLMKV VRHEGFFSLW KGFTPYYARL GPHTVLTFIF LEQMNKYYKK
LFLSG
//
