MCAT_RAT
ID MCAT_RAT Reviewed; 301 AA.
AC P97521;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Mitochondrial carnitine/acylcarnitine carrier protein {ECO:0000305};
DE AltName: Full=Carnitine/acylcarnitine translocase;
DE Short=CAC {ECO:0000303|PubMed:9032458};
DE Short=CACT;
DE AltName: Full=Solute carrier family 25 member 20;
GN Name=Slc25a20 {ECO:0000312|RGD:621443}; Synonyms=Cact;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 86-101; 108-132;
RP 180-197; 207-216 AND 256-263.
RC TISSUE=Liver;
RX PubMed=9032458; DOI=10.1042/bj3210713;
RA Indiveri C., Iacobazzi V., Giangregorio N., Palmieri F.;
RT "The mitochondrial carnitine carrier protein: cDNA cloning, primary
RT structure and comparison with other mitochondrial transport proteins.";
RL Biochem. J. 321:713-719(1997).
RN [2]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=8305461; DOI=10.1016/0005-2736(94)90281-x;
RA Indiveri C., Tonazzi A., Palmieri F.;
RT "The reconstituted carnitine carrier from rat liver mitochondria: evidence
RT for a transport mechanism different from that of the other mitochondrial
RT translocators.";
RL Biochim. Biophys. Acta 1189:65-73(1994).
RN [3]
RP FUNCTION, TRANSPORT ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9731180; DOI=10.1006/bbrc.1998.9197;
RA Indiveri C., Iacobazzi V., Giangregorio N., Palmieri F.;
RT "Bacterial overexpression, purification, and reconstitution of the
RT carnitine/acylcarnitine carrier from rat liver mitochondria.";
RL Biochem. Biophys. Res. Commun. 249:589-594(1998).
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
CC (PubMed:9731180). Key player in the mitochondrial oxidation pathway, it
CC translocates the fatty acids in the form of acylcarnitines into the
CC mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-
CC 2) activates them to undergo fatty acid beta-oxidation (Probable).
CC Catalyzes the unidirectional transport (uniport) of carnitine at lower
CC rates than the antiport (exchange) (PubMed:8305461).
CC {ECO:0000269|PubMed:8305461, ECO:0000269|PubMed:9731180,
CC ECO:0000305|PubMed:8305461}.
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:0000269|PubMed:9731180, ECO:0000305|PubMed:8305461};
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:0000269|PubMed:9731180, ECO:0000305|PubMed:8305461};
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:0000269|PubMed:9731180, ECO:0000305|PubMed:8305461};
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:0000269|PubMed:9731180};
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:0000269|PubMed:9731180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959,
CC ChEBI:CHEBI:16347; Evidence={ECO:0000269|PubMed:8305461};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 mM for carnitine (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:9731180};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; X97831; CAA66410.1; -; mRNA.
DR AlphaFoldDB; P97521; -.
DR SMR; P97521; -.
DR STRING; 10116.ENSRNOP00000027520; -.
DR ChEMBL; CHEMBL2173; -.
DR SwissLipids; SLP:000001592; -.
DR TCDB; 2.A.29.8.1; the mitochondrial carrier (mc) family.
DR CarbonylDB; P97521; -.
DR iPTMnet; P97521; -.
DR PhosphoSitePlus; P97521; -.
DR jPOST; P97521; -.
DR PaxDb; P97521; -.
DR PRIDE; P97521; -.
DR UCSC; RGD:621443; rat.
DR RGD; 621443; Slc25a20.
DR eggNOG; KOG0758; Eukaryota.
DR InParanoid; P97521; -.
DR PhylomeDB; P97521; -.
DR BioCyc; MetaCyc:MON-14443; -.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR PRO; PR:P97521; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:RGD.
DR GO; GO:0015227; F:acyl carnitine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1902603; P:carnitine transmembrane transport; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Lipid transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome; Repeat;
KW Transmembrane; 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_0000090631"
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; 33154 MW; 4A4284B4FF9D7439 CRC64;
MAEEPKPISP LKNLLAGGFG GVCLVFVGHP LDTVKVRLQT QPPSLPGQPP MYSGTIDCFR
KTLFREGITG LYRGMAAPII GVTPMFAVCF FGFGLGKRLQ QKSPEDELTY PQLFTAGMLS
GVFTTGIMTP GERIKCLLQI QASSGKNKYS GTLDCAKKLY QEFGIRGFYK GTALTLMRDV
PASGMYFMTY EWLKNLFTPQ GKSVHDLSVP RVLVAGGFRG IFNWVVAIPP DVLKSRFQTA
PPGKYPNGFR DVLRELIREE GVTSLYKGFN AVMIRAFPAN AACFLGFEIP MKILNWIAPN
L
