MCAT_MACFA
ID MCAT_MACFA Reviewed; 301 AA.
AC Q8HXY2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Mitochondrial carnitine/acylcarnitine carrier protein {ECO:0000305};
DE AltName: Full=Carnitine/acylcarnitine translocase;
DE Short=CAC;
DE Short=CACT;
DE AltName: Full=Solute carrier family 25 member 20;
GN Name=SLC25A20; Synonyms=CACT; ORFNames=QccE-14128;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RA Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the electroneutral exchange of acylcarnitines (O-
CC acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths
CC (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-
CC carnitines) with free carnitine ((R)-carnitine or L-carnitine) across
CC the mitochondrial inner membrane, via a ping-pong mechanism. Key player
CC in the mitochondrial oxidation pathway, it translocates the fatty acids
CC in the form of acylcarnitines into the mitochondrial matrix, where the
CC carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo
CC fatty acid beta-oxidation. Catalyzes the unidirectional transport
CC (uniport) of carnitine at lower rates than the antiport (exchange).
CC {ECO:0000250|UniProtKB:O43772}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-acetyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-acetyl-(R)-carnitine(out); Xref=Rhea:RHEA:49908,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57589;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-acyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-acyl-(R)-carnitine(out); Xref=Rhea:RHEA:49924,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:75659;
CC Evidence={ECO:0000250|UniProtKB:O43772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-propanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-propanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49912,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:53210;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-hexadecanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-hexadecanoyl-(R)-carnitine(out);
CC Xref=Rhea:RHEA:49916, ChEBI:CHEBI:16347, ChEBI:CHEBI:17490;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-octanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-octanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49920,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:18102;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959,
CC ChEBI:CHEBI:16347; Evidence={ECO:0000250|UniProtKB:O43772};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AB083307; BAC20586.1; -; mRNA.
DR RefSeq; NP_001271045.1; NM_001284116.1.
DR AlphaFoldDB; Q8HXY2; -.
DR SMR; Q8HXY2; -.
DR STRING; 9541.XP_005547110.1; -.
DR GeneID; 102124681; -.
DR CTD; 788; -.
DR eggNOG; KOG0758; Eukaryota.
DR OrthoDB; 1072378at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015227; F:acyl carnitine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:1902603; P:carnitine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43772"
FT CHAIN 2..301
FT /note="Mitochondrial carnitine/acylcarnitine carrier
FT protein"
FT /id="PRO_0000090629"
FT TOPO_DOM 2..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..73
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..170
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..267
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 8..99
FT /note="Solcar 1"
FT REPEAT 108..196
FT /note="Solcar 2"
FT REPEAT 207..293
FT /note="Solcar 3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43772"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
FT MOD_RES 157
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
FT MOD_RES 170
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
FT MOD_RES 170
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
SQ SEQUENCE 301 AA; 32954 MW; F80789BBBBD82611 CRC64;
MADQPKPISP LKNLLAGGFG GVCLVFVGHP LDTVKVRLQT QPPSLPGQPP MYSGTFDCFR
KTLFREGIRG LYRGMAAPII GVTPMFAVCF FGFGLGKKLQ QKHPEDVLSY PQLFAAGMLS
GIFTTGIMTP GERIKCLLQI QASSGETKYT GTLDCAKKLY QEFGIRGIYK GTVVTLMRDV
PASGMYFMTY EWVKNIFTPE GKRVSELSVP RVLVAGGIAG IFNWAVAIPP DVLKSRFQTA
PPGKYPNGFR DVLRELIPDE GVTSLYKGFN AVMIRAFPAN AACFLGFEVA MKFLNWATPN
L
