ODC_RAT
ID ODC_RAT Reviewed; 298 AA.
AC Q99JD3;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Mitochondrial 2-oxodicarboxylate carrier;
DE AltName: Full=Solute carrier family 25 member 21;
GN Name=Slc25a21; Synonyms=Odc;
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], AND TISSUE SPECIFICITY.
RX PubMed=11083877; DOI=10.1074/jbc.m009607200;
RA Fiermonte G., Dolce V., Palmieri L., Ventura M., Runswick M.J.,
RA Palmieri F., Walker J.E.;
RT "Identification of the human mitochondrial oxodicarboxylate carrier.
RT Bacterial expression, reconstitution, functional characterization, tissue
RT distribution and chromosomal location.";
RL J. Biol. Chem. 276:8225-8230(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Transports dicarboxylates across the inner membranes of
CC mitochondria by a counter-exchange mechanism. Can transport 2-
CC oxoadipate (2-oxohexanedioate), 2-oxoglutarate, adipate (hexanedioate),
CC glutarate, and to a lesser extent, pimelate (heptanedioate), 2-
CC oxopimelate (2-oxoheptanedioate), 2-aminoadipate (2-aminohexanedioate),
CC oxaloacetate, and citrate. Plays a central role in catabolism of
CC lysine, hydroxylysine, and tryptophan, by transporting common
CC metabolite intermediates (such as 2-oxoadipate) into the mitochondria,
CC where it is converted into acetyl-CoA and can enter the citric acid
CC (TCA) cycle. {ECO:0000250|UniProtKB:Q9BQT8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoadipate(in) + 2-oxoglutarate(out) = 2-oxoadipate(out) +
CC 2-oxoglutarate(in); Xref=Rhea:RHEA:71739, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:57499; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + hexanedioate(in) = 2-oxoglutarate(in) +
CC hexanedioate(out); Xref=Rhea:RHEA:71743, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17128; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + L-2-aminoadipate(in) = 2-
CC oxoglutarate(in) + L-2-aminoadipate(out); Xref=Rhea:RHEA:71747,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:58672;
CC Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + glutarate(in) = 2-oxoglutarate(in) +
CC glutarate(out); Xref=Rhea:RHEA:71751, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30921; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + 2-oxoheptanedioate(in) = 2-
CC oxoglutarate(in) + 2-oxoheptanedioate(out); Xref=Rhea:RHEA:71755,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:72701;
CC Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + heptanedioate(in) = 2-oxoglutarate(in) +
CC heptanedioate(out); Xref=Rhea:RHEA:71759, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:36165; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + citrate(in) = 2-oxoglutarate(in) +
CC citrate(out); Xref=Rhea:RHEA:71763, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11083877}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AJ289714; CAC27796.1; -; mRNA.
DR EMBL; BC089099; AAH89099.1; -; mRNA.
DR RefSeq; NP_598298.1; NM_133614.2.
DR RefSeq; XP_006240176.1; XM_006240114.3.
DR AlphaFoldDB; Q99JD3; -.
DR SMR; Q99JD3; -.
DR STRING; 10116.ENSRNOP00000037607; -.
DR iPTMnet; Q99JD3; -.
DR PhosphoSitePlus; Q99JD3; -.
DR PaxDb; Q99JD3; -.
DR Ensembl; ENSRNOT00000119506; ENSRNOP00000084175; ENSRNOG00000008931.
DR GeneID; 171151; -.
DR KEGG; rno:171151; -.
DR UCSC; RGD:621444; rat.
DR CTD; 89874; -.
DR RGD; 621444; Slc25a21.
DR eggNOG; KOG0754; Eukaryota.
DR GeneTree; ENSGT00730000111119; -.
DR HOGENOM; CLU_015166_5_2_1; -.
DR InParanoid; Q99JD3; -.
DR OrthoDB; 1236425at2759; -.
DR PhylomeDB; Q99JD3; -.
DR Reactome; R-RNO-71064; Lysine catabolism.
DR PRO; PR:Q99JD3; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Genevisible; Q99JD3; RN.
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:0015139; F:alpha-ketoglutarate transmembrane transporter activity; ISO:RGD.
DR GO; GO:1990550; P:mitochondrial alpha-ketoglutarate transmembrane transport; ISO:RGD.
DR Gene3D; 1.50.40.10; -; 2.
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 2: Evidence at transcript level;
KW Antiport; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Mitochondrial 2-oxodicarboxylate carrier"
FT /id="PRO_0000090647"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 10..99
FT /note="Solcar 1"
FT REPEAT 106..195
FT /note="Solcar 2"
FT REPEAT 204..293
FT /note="Solcar 3"
SQ SEQUENCE 298 AA; 33279 MW; AD8CEE88165D18CD CRC64;
MSASNVSLLH ETCRQVAAGG CAGLVEICLM HPLDVVKTRF QVQRSVTDPQ SYKSLRDSFQ
VIFRTEGLFG FYKGIIPPIL AETPKRAVKF STFELYKKFL GYMSLSPGLT FPIAGLGSGL
TEAVVVNPFE VVKVGLQVNR NMFTEQPSTF AYARQIIKKE GWGFQGLNKG FTATLGRHGI
FNMTYFGFYY NVKDNIPSSK DPTLEFLRKF GIGFVSGTVG SVFNIPFDVA KSRIQGPQPV
PGEIKYRGCF KTMETVYREE GILALYKGLL PKVMRLGPGG GVMLLVYEYT YAWLQENW
