M2OM_RAT
ID M2OM_RAT Reviewed; 314 AA.
AC P97700;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Mitochondrial 2-oxoglutarate/malate carrier protein {ECO:0000303|PubMed:16291728, ECO:0000303|PubMed:7703504};
DE Short=OGCP;
DE Short=alpha-oxoglutarate carrier;
DE AltName: Full=Solute carrier family 25 member 11;
DE Short=SLC25A11;
GN Name=Slc25a11; Synonyms=Slc20a4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Bei D., Lehmann J.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TRANSPORT ACTIVITY.
RX PubMed=5083502; DOI=10.1111/j.1432-1033.1972.tb02003.x;
RA Palmieri F., Quagliariello E., Klingenberger M.;
RT "Kinetics and specificity of the oxoglutarate carrier in rat-liver
RT mitochondria.";
RL Eur. J. Biochem. 29:408-416(1972).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TRANSPORT ACTIVITY.
RX PubMed=3355813; DOI=10.1016/0005-2728(88)90030-8;
RA Bisaccia F., Indiveri C., Palmieri F.;
RT "Purification and reconstitution of two anion carriers from rat liver
RT mitochondria: the dicarboxylate and the 2-oxoglutarate carrier.";
RL Biochim. Biophys. Acta 933:229-240(1988).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND TRANSPORT ACTIVITY.
RX PubMed=7703504; DOI=10.3109/10425179409039711;
RA Dolce V., Messina A., Cambria A., Palmieri F.;
RT "Cloning and sequencing of the rat cDNA encoding the mitochondrial 2-
RT oxoglutarate carrier protein.";
RL DNA Seq. 5:103-109(1994).
RN [5]
RP FUNCTION.
RX PubMed=16291728; DOI=10.1124/jpet.105.094599;
RA Xu F., Putt D.A., Matherly L.H., Lash L.H.;
RT "Modulation of expression of rat mitochondrial 2-oxoglutarate carrier in
RT NRK-52E cells alters mitochondrial transport and accumulation of
RT glutathione and susceptibility to chemically induced apoptosis.";
RL J. Pharmacol. Exp. Ther. 316:1175-1186(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the transport of 2-oxoglutarate (alpha-
CC oxoglutarate) across the inner mitochondrial membrane in an
CC electroneutral exchange for malate (PubMed:5083502, PubMed:3355813,
CC PubMed:7703504). Can also exchange 2-oxoglutarate for other
CC dicarboxylic acids such as malonate, succinate, maleate and
CC oxaloacetate, although with lower affinity (PubMed:3355813,
CC PubMed:7703504). Contributes to several metabolic processes, including
CC the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in
CC gluconeogenesis from lactate, and in nitrogen metabolism
CC (PubMed:5083502, PubMed:3355813). Maintains mitochondrial fusion and
CC fission events, and the organization and morphology of cristae (By
CC similarity). Involved in the regulation of apoptosis (PubMed:16291728).
CC Helps protect from cytotoxic-induced apoptosis by modulating
CC glutathione levels in mitochondria (PubMed:16291728).
CC {ECO:0000250|UniProtKB:Q02978, ECO:0000269|PubMed:16291728,
CC ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:5083502,
CC ECO:0000269|PubMed:7703504}.
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:0000269|PubMed:3355813,
CC ECO:0000269|PubMed:5083502, ECO:0000269|PubMed:7703504};
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:0000305|PubMed:3355813};
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:0000305|PubMed:3355813};
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:0000305|PubMed:3355813};
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:0000305|PubMed:3355813};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:3355813, ECO:0000305|PubMed:5083502}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, heart and brain.
CC {ECO:0000269|PubMed:7703504}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; U84727; AAB41797.1; -; mRNA.
DR RefSeq; NP_071793.1; NM_022398.2.
DR BioGRID; 249007; 2.
DR IntAct; P97700; 3.
DR MINT; P97700; -.
DR STRING; 10116.ENSRNOP00000005144; -.
DR iPTMnet; P97700; -.
DR PhosphoSitePlus; P97700; -.
DR jPOST; P97700; -.
DR PaxDb; P97700; -.
DR PRIDE; P97700; -.
DR GeneID; 64201; -.
DR KEGG; rno:64201; -.
DR UCSC; RGD:708476; rat.
DR CTD; 8402; -.
DR RGD; 708476; Slc25a11.
DR eggNOG; KOG0759; Eukaryota.
DR InParanoid; P97700; -.
DR OrthoDB; 892773at2759; -.
DR PhylomeDB; P97700; -.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR PRO; PR:P97700; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; IMP:RGD.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Antiport; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT CHAIN 2..314
FT /note="Mitochondrial 2-oxoglutarate/malate carrier protein"
FT /id="PRO_0000090627"
FT TRANSMEM 24..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..240
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 23..108
FT /note="Solcar 1"
FT REPEAT 117..208
FT /note="Solcar 2"
FT REPEAT 217..306
FT /note="Solcar 3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR62"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT MOD_RES 102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR62"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR62"
SQ SEQUENCE 314 AA; 34244 MW; 0DD88F3865E79D04 CRC64;
MAATASPGAG RMDGKPRTSP KSVKFLFGGL AGMGATVFVQ PLDLVXNRMQ LSGEGAKTRE
YKTSFHALTS ILKAEGLRGI YTGLSAGLLR QATYTTTRLG IYTVLFERLT GADGTPPGFL
LKALIGMTAG ATGAFVGPPA EVALIRMTAD GRLPADQRRG YKNVFNALIR IAREEGVPTL
WRGCIPTMAR AVVVNAAQLA SYSQSKQFLL DSGYFSDNIL CHFCAIMISG LVTTAASMPV
DIVKTRIQNM RMIDEKPEYK NGLDVLLKVV RYEGFFSLWK GFTPYYARLG PHTVLTFIFL
EQMNKAYKRL FLSG
