ID H2Q873_PANTR Unreviewed; 299 AA.
AC H2Q873; A0A2J8MI65;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Mitochondrial 2-oxodicarboxylate carrier {ECO:0000256|ARBA:ARBA00039747};
DE AltName: Full=Solute carrier family 25 member 21 {ECO:0000256|ARBA:ARBA00041874};
GN Name=SLC25A21 {ECO:0000313|EMBL:JAA02241.1,
GN ECO:0000313|Ensembl:ENSPTRP00000010658.3,
GN ECO:0000313|VGNC:VGNC:12533};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000010658.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000010658.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA02241.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02241.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA37236.1}, Skin {ECO:0000313|EMBL:JAA26623.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA18556.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000010658.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036018};
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:0000256|ARBA:ARBA00036835};
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:0000256|ARBA:ARBA00036155};
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:0000256|ARBA:ARBA00036610};
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:0000256|ARBA:ARBA00036317};
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:0000256|ARBA:ARBA00036103};
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:0000256|ARBA:ARBA00036872};
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; AACZ04059499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04059500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01009097; JAA02241.1; -; mRNA.
DR EMBL; GABF01003589; JAA18556.1; -; mRNA.
DR EMBL; GABD01006477; JAA26623.1; -; mRNA.
DR EMBL; GABE01007503; JAA37236.1; -; mRNA.
DR RefSeq; XP_522830.2; XM_522830.6.
DR STRING; 9598.ENSPTRP00000010658; -.
DR PaxDb; 9598-ENSPTRP00000010658; -.
DR Ensembl; ENSPTRT00000011515.4; ENSPTRP00000010658.3; ENSPTRG00000006283.4.
DR GeneID; 467433; -.
DR CTD; 89874; -.
DR VGNC; VGNC:12533; SLC25A21.
DR eggNOG; KOG0754; Eukaryota.
DR GeneTree; ENSGT00730000111119; -.
DR HOGENOM; CLU_015166_5_2_1; -.
DR OMA; LPFQYQF; -.
DR OrthoDB; 314985at2759; -.
DR TreeFam; TF314035; -.
DR Proteomes; UP000002277; Chromosome 14.
DR Bgee; ENSPTRG00000006283; Expressed in bone marrow and 21 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:1990550; P:mitochondrial alpha-ketoglutarate transmembrane transport; IEA:Ensembl.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR46356; MITOCHONDRIAL 2-OXODICARBOXYLATE CARRIER; 1.
DR PANTHER; PTHR46356:SF1; MITOCHONDRIAL 2-OXODICARBOXYLATE CARRIER; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT REPEAT 11..100
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 107..196
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 205..294
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 299 AA; 33200 MW; 1B3D7B9DC328A97E CRC64;
MSAKPEVGLV REASRQIVAG GSAGLVEICL MHPLDVVKTR FQIQRCATDP NSYKSLVDSF
RMIFQMEGLF GFYKGILPPI LAETPKRAVK FFTFEQYKKL LGYVSLSPAL TFAIAGLGSG
LTEAIVVNPF EVVKVGLQAN RNTFAEQPST VGYARQIIKK EGWGLQGLNK GLTATLGRHG
VFNMVYFGFY YNVKNMIPVN KDPILEFLRK FGIGLLSGTI ASVINIPFDV AKSRIQGPQP
VPGEIKYRTC FKTMATVYQE EGILALYKGL LPKIMRLGPG GAVMLLVYEY TYSWLQENW
//
