ID A0A3B4THD8_SERDU Unreviewed; 319 AA.
AC A0A3B4THD8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000005360.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000005360.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 AlphaFoldDB; A0A3B4THD8; -.
DR Ensembl; ENSSDUT00000005462.1; ENSSDUP00000005360.1; ENSSDUG00000003942.1.
DR GeneTree; ENSGT00940000158163; -.
DR OMA; YRGWILN; -.
DR Proteomes; UP000261420; Unplaced.
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 InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR24089:SF736; MITOCHONDRIAL COENZYME A TRANSPORTER SLC25A42; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT REPEAT 26..112
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 124..209
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 219..307
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 319 AA; 35423 MW; FF8FAE5DDE07AE8C CRC64;
MGSYLKTSAV RCFRCCGLQS SPSPLWTALD SLLCGAFAGA VAKTVIAPLD RTKIIFQVSS
KRFSAKEAFR LIYCTYMKHG LLSLWRGNSA TMVRVMPYAA IQFCSHEQYK KLLGSYFGYQ
GKALPPFPRF LAGSLAGTTA AMLTYPLDMV RARMAVTARE MYSNIMHVFV RISQEEGVKT
LYRGFTPTIL GVIPYAGITF FTYETLKKLH TEKTKRSQPY PHERLAFGAC AGLIGQSASY
PLDVVRRRMQ TAGVTGSSYG TILGTMREII TQEGVVRGLY KGLSMNWLKG PVAVGISFTT
FDITHSLLLK LHQMGYFTH
//