ID A0A182RND9_ANOFN Unreviewed; 305 AA.
AC A0A182RND9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Mitochondrial 2-oxodicarboxylate carrier {ECO:0000256|ARBA:ARBA00039747};
DE AltName: Full=Solute carrier family 25 member 21 {ECO:0000256|ARBA:ARBA00041874};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN007770-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN007770-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN007770-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A182RND9; -.
DR STRING; 62324.A0A182RND9; -.
DR EnsemblMetazoa; AFUN007770-RA; AFUN007770-PA; AFUN007770.
DR VEuPathDB; VectorBase:AFUN007770; -.
DR VEuPathDB; VectorBase:AFUN2_014577; -.
DR OrthoDB; 314985at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
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 SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|RuleBase:RU000488}.
FT REPEAT 10..104
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 112..201
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 210..299
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 305 AA; 33382 MW; 4B7CED46D59D05B8 CRC64;
MPSDVKEFLR QAAMQVGAGG SAGFVEVCIM HPLDLVKTRL QLQASPVAGV AKSTTYYNGV
FDCISKMAKT EGVFSLYKGI LPPVLVETPK RAVKFLTFEQ YKRFFMFGSD KPTPLTFSLA
GLGAGITEAI LVNPFEMVKV TLQANKNKMG QVPSTWAVTK QIINESGFGL NGLNRGLTAT
IGRNGVFNMI YFGFYHSVKG IIPEYKDPVQ EFLRKVGIGF VSGTLGSIVN IPFDVAKSRI
QGPQPVPGQV KYRTTFGSMM IVAREEGFAA LYKGLTPKVM RLGPGGAIML VVYDYVYAFL
DDYFK
//
