CPT2_DANRE
ID CPT2_DANRE Reviewed; 669 AA.
AC Q5U3U3; B0S7W9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=si:ch211-216k22.1, zgc:101627;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) 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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH85392.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX927144; CAQ13312.1; -; Genomic_DNA.
DR EMBL; BC085392; AAH85392.1; ALT_INIT; mRNA.
DR RefSeq; NP_001007448.1; NM_001007447.1.
DR AlphaFoldDB; Q5U3U3; -.
DR SMR; Q5U3U3; -.
DR STRING; 7955.ENSDARP00000122226; -.
DR PaxDb; Q5U3U3; -.
DR PeptideAtlas; Q5U3U3; -.
DR PRIDE; Q5U3U3; -.
DR Ensembl; ENSDART00000135938; ENSDARP00000122226; ENSDARG00000038618.
DR GeneID; 100005717; -.
DR KEGG; dre:100005717; -.
DR CTD; 1376; -.
DR ZFIN; ZDB-GENE-030131-6719; cpt2.
DR eggNOG; KOG3719; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR HOGENOM; CLU_013513_4_2_1; -.
DR InParanoid; Q5U3U3; -.
DR OMA; HILVMRR; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; Q5U3U3; -.
DR TreeFam; TF315202; -.
DR Reactome; R-DRE-200425; Carnitine metabolism.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q5U3U3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000038618; Expressed in intestine and 20 other tissues.
DR ExpressionAtlas; Q5U3U3; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:RHEA.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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 Acyltransferase; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..669
FT /note="Carnitine O-palmitoyltransferase 2, mitochondrial"
FT /id="PRO_0000351546"
FT TOPO_DOM 37..190
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT INTRAMEM 191..220
FT /note="Note=Mitochondrial inner membrane"
FT /evidence="ECO:0000250"
FT TOPO_DOM 221..669
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 464..476
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
SQ SEQUENCE 669 AA; 74916 MW; B784EE6BEE30419F CRC64;
MMAGLLSTQC NSTLSKLKHL SNNPALSVLT STHRKYSSKD GAGSEYLHKS IVPSMHYQKS
LPRLPVPKLE DTIRRYLAAQ RPLLNDEQYS NTEKLAQEFQ SGAGKQLHEE LVALDKKNKH
TSYISAPWFD MYLSARESIV LNFNPFMSFN PDPKPEYNDQ LVRATNMVCS AVRFMKTLRA
GLLEPEVFHL NPAKSDTDSF KKLIRWVPPS ISWFGAYMVN AYPLDMSQYF RLFNSTRIPK
YKRDELLTDD RGRHLLVMKR GNLYVFDALD RDGNLIKPAE VQAHLKYILE DPTQASAFPL
GVLTSENRDT WTGLRQKLLD AGNGEALQLV DTALFCLCLD EEVLRDHIHI SHNMLHGDGC
NRWYDKSFSV ILAKDGQAAI NFEHSWGDGV AVLRFQNEVF KDTTEKPLVG PGSQPASVDS
SSAVRRLEFK LNDELKAGIT KAKENFQAAV SKLTIDAMEF KKGGKEQLKK KKLSPDAIAQ
LAFQMGFLRQ YGQTVATYES CSTAAFKHGR TETIRPASIH TKQCAKAFVQ QPGQHSVEQL
LGLLNECSKY HGQLTREAAM GQGFDRHLFA MRYLANSKGM ALPSLYQDPA YAAINHNILS
TSTLTSPAVS LGGFAPVVPD GFGVGYGVHD EWIGCNVSSY PARDVHEFLR CVHKSLEDIF
TVLDGNPIH
