CPT2_XENLA
ID CPT2_XENLA Reviewed; 659 AA.
AC Q7ZXE1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-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; BC045036; AAH45036.1; -; mRNA.
DR RefSeq; NP_001080201.1; NM_001086732.1.
DR RefSeq; XP_018114871.1; XM_018259382.1.
DR RefSeq; XP_018114872.1; XM_018259383.1.
DR RefSeq; XP_018114874.1; XM_018259385.1.
DR AlphaFoldDB; Q7ZXE1; -.
DR SMR; Q7ZXE1; -.
DR MaxQB; Q7ZXE1; -.
DR DNASU; 379893; -.
DR GeneID; 379893; -.
DR KEGG; xla:379893; -.
DR CTD; 379893; -.
DR Xenbase; XB-GENE-963406; cpt2.S.
DR OMA; HILVMRR; -.
DR OrthoDB; 559299at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 379893; Expressed in blastula and 19 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:RHEA.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
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; PS00440; ACYLTRANSF_C_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..659
FT /note="Carnitine O-palmitoyltransferase 2, mitochondrial"
FT /id="PRO_0000351547"
FT TOPO_DOM 28..180
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT INTRAMEM 181..210
FT /note="Note=Mitochondrial inner membrane"
FT /evidence="ECO:0000250"
FT TOPO_DOM 211..659
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT ACT_SITE 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 454..466
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
SQ SEQUENCE 659 AA; 74557 MW; E91F6D7A497553DF CRC64;
MARLLTSSSA LRWRTITSSQ PVLLRAYSSG SSDTEYLQRS IVPTMHFQKS LPRLPIPKFE
DTIKRYLNAQ RPLLDDVQFK KTEQLALNFQ NGVGKQLHEE LVQQDKQNKH TSYISGPWFD
MYLCARDSIV LNSNPFMSFT PDPRPEYNSQ LIRATNMTVS AMRFLKTMRA GYLEPEIFHL
NPAKSDTLTF RKLIRFVPSS LSWYGAYMVN AYPLDMSQYF RLFNCTRIPK PNRDELLTDE
KGRHLLVLRK GNFYVFDVID KDGNIVKASE IQAHLQHILS DNTPTPEFPL GYLTSEERNK
WAVLRQKLLD NENEEALAKV DSAVFCLCLD DFPIKDRVHL SHNMLHGSGL NRWFDKSFSI
IMTEDGTAAI NFEHSWGDGV AVLRFQNEVF KDSTQRPAIS PESCSAPVDS SKAVQRLHFN
LDDSLKAAIT DAKTKFDTSV NALSIATMEF KKGGKEFLKT QKLSPDAISQ LSFQMAFLRQ
YGKTTATYES CSTAAFKHGR TETIRPASIY TKKCSEALVM NPSKHSPAEL RSMLHECSKY
HGQLTKEAAM GQGFDRHLFA LRHLASSKGL PIPEIYQDIP YAQINHNVLS TSTLTSPAVQ
LGGFAPVVPD GFGVGYGVHD DWIGCNVSSY PARDVRQFVQ CVHQSLDDIF SVLQDKPLK
