M2OM_BOVIN
ID M2OM_BOVIN Reviewed; 314 AA.
AC P22292; A5PJY2; Q5E9W4;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Mitochondrial 2-oxoglutarate/malate carrier protein {ECO:0000303|PubMed:2271695};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1457818; DOI=10.3109/10425179209034000;
RA Iacobazzi V., Palmieri F., Runswick M.J., Walker J.E.;
RT "Sequences of the human and bovine genes for the mitochondrial 2-
RT oxoglutarate carrier.";
RL DNA Seq. 3:79-88(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=2271695; DOI=10.1021/bi00502a004;
RA Runswick M.J., Walker J.E., Bisaccia F., Iacobazzi V., Palmieri F.;
RT "Sequence of the bovine 2-oxoglutarate/malate carrier protein: structural
RT relationship to other mitochondrial transport proteins.";
RL Biochemistry 29:11033-11040(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons, and Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=3814587; DOI=10.1016/0005-2728(87)90158-7;
RA Indiveri C., Palmieri F., Bisaccia F., Kraemer R.;
RT "Kinetics of the reconstituted 2-oxoglutarate carrier from bovine heart
RT mitochondria.";
RL Biochim. Biophys. Acta 890:310-318(1987).
RN [6]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=8363582; DOI=10.1042/bj2940293;
RA Fiermonte G., Walker J.E., Palmieri F.;
RT "Abundant bacterial expression and reconstitution of an intrinsic membrane-
RT transport protein from bovine mitochondria.";
RL Biochem. J. 294:293-299(1993).
RN [7]
RP FUNCTION.
RX PubMed=14598172; DOI=10.1007/s00424-003-1099-7;
RA Palmieri F.;
RT "The mitochondrial transporter family (SLC25): physiological and
RT pathological implications.";
RL Pflugers Arch. 447:689-709(2004).
RN [8]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=27479487; DOI=10.1016/j.bbapap.2016.07.009;
RA Curcio R., Muto L., Pierri C.L., Montalto A., Lauria G., Onofrio A.,
RA Fiorillo M., Fiermonte G., Lunetti P., Vozza A., Capobianco L.,
RA Cappello A.R., Dolce V.;
RT "New insights about the structural rearrangements required for substrate
RT translocation in the bovine mitochondrial oxoglutarate carrier.";
RL Biochim. Biophys. Acta 1864:1473-1480(2016).
CC -!- FUNCTION: Catalyzes the transport of 2-oxoglutarate (alpha-
CC oxoglutarate) across the inner mitochondrial membrane in an
CC electroneutral exchange for malate (PubMed:3814587, PubMed:8363582,
CC PubMed:27479487). Can also exchange 2-oxoglutarate for other
CC dicarboxylic acids such as malonate, succinate, maleate and
CC oxaloacetate, although with lower affinity (PubMed:8363582).
CC Contributes to several metabolic processes, including the malate-
CC aspartate shuttle, the oxoglutarate/isocitrate shuttle, in
CC gluconeogenesis from lactate, and in nitrogen metabolism
CC (PubMed:14598172). Maintains mitochondrial fusion and fission events,
CC and the organization and morphology of cristae (By similarity).
CC Involved in the regulation of apoptosis (By similarity). Helps protect
CC from cytotoxic-induced apoptosis by modulating glutathione levels in
CC mitochondria (By similarity). {ECO:0000250|UniProtKB:P97700,
CC ECO:0000250|UniProtKB:Q02978, ECO:0000250|UniProtKB:Q9CR62,
CC ECO:0000269|PubMed:27479487, ECO:0000269|PubMed:3814587,
CC ECO:0000269|PubMed:8363582, ECO:0000303|PubMed:14598172}.
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:8363582,
CC ECO:0000305|PubMed:14598172, ECO:0000305|PubMed:27479487,
CC ECO:0000305|PubMed:3814587};
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:0000269|PubMed:8363582};
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:0000269|PubMed:8363582};
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:0000269|PubMed:8363582};
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:0000269|PubMed:8363582};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P97700}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Heart, liver and brain.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; X66115; CAA46906.1; -; Genomic_DNA.
DR EMBL; M58703; AAA30671.1; -; mRNA.
DR EMBL; M60662; AAA30672.1; -; mRNA.
DR EMBL; BT020806; AAX08823.1; -; mRNA.
DR EMBL; BC142283; AAI42284.1; -; mRNA.
DR EMBL; BC146129; AAI46130.1; -; mRNA.
DR PIR; A36305; A36305.
DR RefSeq; NP_777096.1; NM_174671.2.
DR AlphaFoldDB; P22292; -.
DR STRING; 9913.ENSBTAP00000035103; -.
DR TCDB; 2.A.29.2.1; the mitochondrial carrier (mc) family.
DR PaxDb; P22292; -.
DR PeptideAtlas; P22292; -.
DR PRIDE; P22292; -.
DR Ensembl; ENSBTAT00000035225; ENSBTAP00000035103; ENSBTAG00000004910.
DR Ensembl; ENSBTAT00000079666; ENSBTAP00000065358; ENSBTAG00000004910.
DR GeneID; 282523; -.
DR KEGG; bta:282523; -.
DR CTD; 8402; -.
DR VEuPathDB; HostDB:ENSBTAG00000004910; -.
DR VGNC; VGNC:34742; SLC25A11.
DR eggNOG; KOG0759; Eukaryota.
DR GeneTree; ENSGT00940000158465; -.
DR HOGENOM; CLU_015166_14_1_1; -.
DR InParanoid; P22292; -.
DR OMA; FLHTPFM; -.
DR OrthoDB; 892773at2759; -.
DR TreeFam; TF354262; -.
DR Reactome; R-BTA-70263; Gluconeogenesis.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000004910; Expressed in infraspinatus muscle and 105 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
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; Direct protein sequencing; Lipid transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Repeat; 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_0000090624"
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 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; 34172 MW; 1FF22D1A0B3D36E9 CRC64;
MAATASPGAS GMDGKPRTSP KSVKFLFGGL AGMGATVFVQ PLDLVKNRMQ LSGEGAKTRE
YKTSFHALIS ILRAEGLRGI YTGLSAGLLR QATYTTTRLG IYTVLFERLT GADGTPPGFL
LKAVIGMTAG ATGAFVGTPA EVALIRMTAD GRLPVDQRRG YKNVFNALFR IVQEEGVPTL
WRGCIPTMAR AVVVNAAQLA SYSQSKQFLL DSGYFSDNIL CHFCASMISG LVTTAASMPV
DIVKTRIQNM RMIDGKPEYK NGLDVLVKVV RYEGFFSLWK GFTPYYARLG PHTVLTFIFL
EQMNKAYKRL FLSG
