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Database: UniProt
Entry: T1JXF2_TETUR
LinkDB: T1JXF2_TETUR
Original site: T1JXF2_TETUR 
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
//
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