ID T1JXF2_TETUR Unreviewed; 396 AA.
AC T1JXF2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Mitochondrial coenzyme A transporter SLC25A42 {ECO:0000256|ARBA:ARBA00040682};
DE AltName: Full=Solute carrier family 25 member 42 {ECO:0000256|ARBA:ARBA00041886};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur02g11720.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur02g11720.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Mitochondrial carrier mediating the transport of coenzyme A
CC (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine
CC nucleotides and adenosine 3',5'-diphosphate.
CC {ECO:0000256|ARBA:ARBA00037333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA(in) + ADP(out) = 3'-dephospho-CoA(out) +
CC ADP(in); Xref=Rhea:RHEA:72843, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036693};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00024537};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + AMP(in) = ADP(in) + AMP(out); Xref=Rhea:RHEA:72851,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036261};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + CoA(in) = ADP(in) + CoA(out); Xref=Rhea:RHEA:72839,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out);
CC Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate(in) + ADP(out) = adenosine 3',5'-
CC bisphosphate(out) + ADP(in); Xref=Rhea:RHEA:72847, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036979};
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; CAEY01000828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JXF2; -.
DR STRING; 32264.T1JXF2; -.
DR EnsemblMetazoa; tetur02g11720.1; tetur02g11720.1; tetur02g11720.
DR eggNOG; KOG0752; Eukaryota.
DR HOGENOM; CLU_015166_10_6_1; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24089:SF736; MITOCHONDRIAL COENZYME A TRANSPORTER SLC25A42; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF00153; Mito_carr; 2.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT TRANSMEM 185..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 32..118
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 129..214
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 45250 MW; B2F6A3DA8CF76E50 CRC64;
MQERHSTVDQ LSPQTPLGAK KMSGQGEISN ASKVVTSLIA GAVAGGLAKT IIAPLDRTKI
NFQIKNIPFS FYEAYKFIVI SYKESGFTSL WRGNSATMAR VLPYAAIQYS SHEQFKRLLS
VETNEDKRKH PIRSYVAGSL AGVVSTSLTY PLDLARARMA VTHREKYNSL GAVFRKTIKR
EGPGAVYKGY LPTILGVIPY AGTSFFTYET LKRLHHVEMI FTSLTLHLLP IDILSWIHEV
CASLALLNLF IFLIHRLKYL LNTIIRDVRW SRNIIRSYKF LRYLKGLSNC ESVILCHKIN
SLREATREQL ESLDDIYPIC FQDFSELITA RITRYNHYFH ELCLRKWLYV QDVCPLCHKT
LYGPNENNPS EEPHQNTDIH ESNEQTPVAA DQREKS
//