ID F1C704_PERFV Unreviewed; 298 AA.
AC F1C704;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
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};
DE Flags: Fragment;
GN Name=Slc25a11 {ECO:0000313|EMBL:ADX97064.1};
OS Perca flavescens (American yellow perch) (Morone flavescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8167 {ECO:0000313|EMBL:ADX97064.1};
RN [1] {ECO:0000313|EMBL:ADX97064.1}
RP NUCLEOTIDE SEQUENCE.
RA Pierron F., Normandeau E., Campbell P.G.C., Bernatchez L., Couture P.;
RT "Effects of chronic metal exposure on wild fish populations revealed by
RT high-throughput cDNA sequencing.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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; HQ206466; ADX97064.1; -; mRNA.
DR AlphaFoldDB; F1C704; -.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:InterPro.
DR GO; GO:0006839; P:mitochondrial transport; IEA:InterPro.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR002030; Mit_uncoupling_UCP-like.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45618:SF38; 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 Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 13..98
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 107..198
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 207..296
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT NON_TER 298
FT /evidence="ECO:0000313|EMBL:ADX97064.1"
SQ SEQUENCE 298 AA; 32609 MW; 3DCCE60C16119E2E CRC64;
MAETKPKTSP KAIKFLFGGL AGMGATVFVQ PLDLVKNRMQ LSGQGTKARE YKTSFHALFS
ILKNEGVGGI YTGLSAGLLR QATYTTTRLG IYTILFEKMT GADGRPPNFL LKALIGMTAG
AVGAFVGTPA EVALIRMTAD GRLPADQRRG YSNVFNALAR ITREEGVTTL WRGCIPTMAR
AVVVNAAQLA SYSQTKQALL DSGYFGDDIL CHFCASMISG LVTTAASMPV DIVKTRIQNM
KMIDGKPEYK NGVEVLMRVV RNEGFFSLWK GFTPYYARLG PHTVLTFIFL EQMNRLYK
//