CPT2_MACFA
ID CPT2_MACFA Reviewed; 658 AA.
AC Q60HG9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Carnitine O-palmitoyltransferase 2, mitochondrial;
DE EC=2.3.1.21;
DE AltName: Full=Carnitine palmitoyltransferase II;
DE Short=CPT II;
DE Flags: Precursor;
GN Name=CPT2; ORFNames=QorA-10180;
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=Occipital cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the intramitochondrial synthesis of
CC acylcarnitines from accumulated acyl-CoA metabolites. Reconverts
CC acylcarnitines back into the respective acyl-CoA esters that can then
CC undergo beta-oxidation, an essential step for the mitochondrial uptake
CC of long-chain fatty acids and their subsequent beta-oxidation in the
CC mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18)
CC acyl-CoA esters. {ECO:0000250|UniProtKB:P23786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12663;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + decanoyl-CoA = CoA + O-decanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44828, ChEBI:CHEBI:16347, ChEBI:CHEBI:28717,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + dodecanoyl-CoA = CoA + O-dodecanoyl-R-
CC carnitine; Xref=Rhea:RHEA:40279, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:77086;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + tetradecanoyl-CoA = CoA + O-tetradecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44832, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:84634;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + octadecanoyl-CoA = CoA + O-octadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44840, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:84644;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + eicosanoyl-CoA = CoA + O-eicosanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44844, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:84645;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-
CC tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44848, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:65060, ChEBI:CHEBI:84647;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(5Z)-
CC tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44852, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:84649, ChEBI:CHEBI:84650;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-
CC octadecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44856, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:84651;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC ChEBI:CHEBI:84654; Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P23786}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB125158; BAD51946.1; -; mRNA.
DR RefSeq; XP_005543388.1; XM_005543331.2.
DR AlphaFoldDB; Q60HG9; -.
DR SMR; Q60HG9; -.
DR STRING; 9541.XP_005543388.1; -.
DR GeneID; 102137160; -.
DR KEGG; mcf:102137160; -.
DR CTD; 1376; -.
DR VEuPathDB; HostDB:ENSMFAG00000040882; -.
DR eggNOG; KOG3719; Eukaryota.
DR OMA; HILVMRR; -.
DR OrthoDB; 559299at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000233100; Chromosome 1.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:RHEA.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009437; P:carnitine metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.275.20; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR042572; Carn_acyl_trans_N.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR PANTHER; PTHR22589; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..658
FT /note="Carnitine O-palmitoyltransferase 2, mitochondrial"
FT /id="PRO_0000004425"
FT TOPO_DOM 26..178
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT INTRAMEM 179..208
FT /note="Note=Mitochondrial inner membrane"
FT /evidence="ECO:0000250"
FT TOPO_DOM 209..658
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 452..464
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 85
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 418
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 418
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 424
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 439
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 510
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 510
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
SQ SEQUENCE 658 AA; 73773 MW; F6DB87AF3A141E2A CRC64;
MVPRLLLRAW PRGPAVGPGA PSRPLSAGSG PGQYLQRSIV PTMHYQDSLP RLPIPKLEDT
IRRYLSAQKP LLDDGQFRKT EQFCKNFENG IGKELHEQLV AQDKQNKHTS YISGPWFDMY
LSARDSVVLN FNPFMAFNPD PKSEYNDQLT RATNMTVSAI RFLKTLRDGL LEPEVFHLNP
AKSDTDTFKR LIRFVPSSLS WYGAYLVNAY PLDMSQYFRL FNSTRLPKPS RDELFTDDKA
RHLLVLRKGN FYIFDVLDQD GNIVSPSEIQ AHLKYILSDS SPAPEFPLAY LTSENRDIWA
ELRQKLMSSG NEESLRKVDS AVFCLCLDDF PIKDLVHLSH NMLHGDGTNR WFDKSFNLII
AKDGSAAVHF EHSWGDGVAV LRFFNEVFKD STQIPAITPQ SQPATADSTV TVQKLNFKLT
DALKTGITAA KEKFDATMKT LTIDCLQFQR GGKEFLKKQK LSPDAVAQLA FQMAFLRQYG
QTVATYESCS TAAFKHGRTE TIRPASIYTK RCSEAFVREP SRHSAGELQQ MMAECSKYHG
QLTKEAAMGQ GFDRHLFALR HLAAAKGIIL PELYLDPAYG QINHNVLSTS TLSSPAVNLG
GFAPVVSDGF GVGYAVHGNW IGCNVSSYPG RNAREFLQCV EKALEDMFDA LEGKSIKS
