OCTC_RAT
ID OCTC_RAT Reviewed; 612 AA.
AC P11466; P48033;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Peroxisomal carnitine O-octanoyltransferase;
DE Short=COT;
DE EC=2.3.1.137 {ECO:0000250|UniProtKB:Q9UKG9};
GN Name=Crot; Synonyms=Cot;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7495866; DOI=10.1016/0167-4781(95)00146-8;
RA Choi S.J., Oh D.H., Song C.S., Roy A.K., Chatterjee B.;
RT "Molecular cloning and sequence analysis of the rat liver carnitine
RT octanoyltransferase cDNA, its natural gene and the gene promoter.";
RL Biochim. Biophys. Acta 1264:215-222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-547.
RC TISSUE=Liver;
RX PubMed=3233218; DOI=10.1021/bi00425a018;
RA Chatterjee B., Song C.S., Kim J.-M., Roy A.K.;
RT "Cloning, sequencing, and regulation of rat liver carnitine
RT octanoyltransferase: transcriptional stimulation of the enzyme during
RT peroxisome proliferation.";
RL Biochemistry 27:9000-9006(1988).
RN [3]
RP MUTAGENESIS OF ALA-238 AND HIS-327, AND 3D-STRUCTURE MODELING.
RX PubMed=11553629; DOI=10.1074/jbc.m106920200;
RA Morillas M., Gomez-Puertas P., Roca R., Serra D., Asins G., Valencia A.,
RA Hegardt F.G.;
RT "Structural model of the catalytic core of carnitine palmitoyltransferase I
RT and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473
RT and alanine 381 and COT alanine 238 impairs the catalytic activity.";
RL J. Biol. Chem. 276:45001-45008(2001).
RN [4]
RP MUTAGENESIS OF GLY-553, AND 3D-STRUCTURE MODELING.
RX PubMed=15155769; DOI=10.1074/jbc.m402685200;
RA Cordente A.G., Lopez-Vinas E., Vazquez M.I., Swiegers J.H., Pretorius I.S.,
RA Gomez-Puertas P., Hegardt F.G., Asins G., Serra D.;
RT "Redesign of carnitine acetyltransferase specificity by protein
RT engineering.";
RL J. Biol. Chem. 279:33899-33908(2004).
CC -!- FUNCTION: Beta-oxidation of fatty acids. The highest activity concerns
CC the C6 to C10 chain length substrate. {ECO:0000250|UniProtKB:Q9UKG9}.
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; EC=2.3.1.137;
CC Evidence={ECO:0000250|UniProtKB:Q9UKG9};
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:Q9UKG9};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40948.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA40948.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; U26033; AAC52317.1; -; mRNA.
DR EMBL; J02844; AAA40948.1; ALT_SEQ; mRNA.
DR PIR; A31948; A31948.
DR PIR; S60025; S60025.
DR RefSeq; NP_114193.1; NM_031987.1.
DR AlphaFoldDB; P11466; -.
DR SMR; P11466; -.
DR IntAct; P11466; 4.
DR STRING; 10116.ENSRNOP00000063856; -.
DR iPTMnet; P11466; -.
DR PhosphoSitePlus; P11466; -.
DR PaxDb; P11466; -.
DR GeneID; 83842; -.
DR KEGG; rno:83842; -.
DR CTD; 54677; -.
DR RGD; 70908; Crot.
DR eggNOG; KOG3718; Eukaryota.
DR InParanoid; P11466; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P11466; -.
DR BRENDA; 2.3.1.137; 5301.
DR Reactome; R-RNO-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR PRO; PR:P11466; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005777; C:peroxisome; IDA:RGD.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IDA:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; ISS:UniProtKB.
DR GO; GO:0015936; P:coenzyme A metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; ISO:RGD.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0015909; P:long-chain fatty acid transport; TAS:RGD.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0001579; P:medium-chain fatty acid transport; TAS:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
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 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Peroxisome; Reference proteome; Transferase; Transport.
FT CHAIN 1..612
FT /note="Peroxisomal carnitine O-octanoyltransferase"
FT /id="PRO_0000210171"
FT MOTIF 610..612
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 410..417
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKG9"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MOD_RES 406
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MOD_RES 406
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MUTAGEN 238
FT /note="A->D: Reduces activity by 80%. No effect on
FT inhibition by malonyl-coenzyme A."
FT /evidence="ECO:0000269|PubMed:11553629"
FT MUTAGEN 327
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11553629"
FT MUTAGEN 553
FT /note="G->M: Lowers activity towards medium and long chain
FT fatty acids. Increases activity towards short chain fatty
FT acids."
FT /evidence="ECO:0000269|PubMed:15155769"
FT CONFLICT 334
FT /note="L -> F (in Ref. 2; AAA40948)"
FT /evidence="ECO:0000305"
FT CONFLICT 463..464
FT /note="VR -> RQ (in Ref. 2; AAA40948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 70302 MW; 41B2F3474C8838D1 CRC64;
MENQLAKSIE ERTFQYQDSL PPLPVPSLEE SLKKYLESVK PFANEDEYKK TEEIVQKFQD
GVGKTLHQKL LERAKGKRNW LEEWWLNVAY LDVRIPSQLN VNFVGPSPHF EHYWPAREGT
QLERGSILLW HNLNYWQLLR REKLPVHKSG NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF
KTESEGHCPT HIAVLCRGRA FVFDVLHDGC LITPPELLRQ LTYIYQKCWN EPVGPSIAAL
TSEERTRWAK AREYLIGLDP ENLTLLEKIQ SSLFVYSIED TSPHATPENF SQVFEMLLGG
DPAVRWGDKS YNLISFANGI FGCSCDHAPY DAMLMVNIAH YVDEKLLETE GRWKGSEKVR
DIPLPEELAF TVDEKILNDV YQAKAQHLKA ASDLQIAAST FTSFGKKLTK KEALHPDTFI
QLALQLAYYR LHGRPGCCYE TAMTRYFYHG RTETVRSCTV EAVRWCQSMQ DPSASLLERQ
QKMLDAFAKH NKMMRDCSHG KGFDRHLLGL LLIAKEEGLP VPELFEDPLF SRSGGGGNFV
LSTSLVGYLR IQGVVVPMVH NGYGFFYHIR DDRFVVTCSS WRSCLETDAE KLVEMIFHAF
HDMIHLMNTA HL
