ID A0A2Y9IT70_ENHLU Unreviewed; 660 AA.
AC A0A2Y9IT70;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Carnitine O-palmitoyltransferase 2, mitochondrial {ECO:0000256|ARBA:ARBA00040346};
DE EC=2.3.1.21 {ECO:0000256|ARBA:ARBA00013243};
DE AltName: Full=Carnitine palmitoyltransferase II {ECO:0000256|ARBA:ARBA00042919};
GN Name=LOC111142846 {ECO:0000313|RefSeq:XP_022351892.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022351892.1};
RN [1] {ECO:0000313|RefSeq:XP_022351892.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022351892.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00035780};
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:0000256|ARBA:ARBA00036699};
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:0000256|ARBA:ARBA00036256};
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:0000256|ARBA:ARBA00024283};
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:0000256|ARBA:ARBA00036573};
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:0000256|ARBA:ARBA00036709};
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:0000256|ARBA:ARBA00035828};
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:0000256|ARBA:ARBA00036506};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12663;
CC Evidence={ECO:0000256|ARBA:ARBA00036506};
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:0000256|ARBA:ARBA00036389};
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:0000256|ARBA:ARBA00035841};
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:0000256|ARBA:ARBA00036375};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004443}; Matrix side
CC {ECO:0000256|ARBA:ARBA00004443}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR RefSeq; XP_022351892.1; XM_022496184.1.
DR AlphaFoldDB; A0A2Y9IT70; -.
DR STRING; 391180.A0A2Y9IT70; -.
DR KEGG; elk:111142846; -.
DR OrthoDB; 1429709at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1280.180; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 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; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF51; CARNITINE O-PALMITOYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 54..644
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 660 AA; 74552 MW; D2A71A45F7BDD684 CRC64;
MVVRLLLLLR DWPRGPAIGP GSLCRSLSSG SGSREYLQRS IVPTMHFQDS LPRLPIPKLE
DTIKRYLCAQ KPLLDDDQFR KTEQHCKSFE NGIGKELHKQ LVAQDKRNRH TSYISDPWFD
MYLTARDSIV LNFNPFMAFN PDPKSEYNDQ LTRATNMTVS AVRFLKTLRA GLLEPEVFHL
NPAKSDTDTF KRLIRFVPSS LSWYGAYLVN AYPLDMSQYF RLFSSTRLPR RTRDELVTDE
KARHLLVLRK GHFYVFDVLD RDGNIVSASE IQAHLKYILS DNSPAPEFPL AYLTTEHRDV
WAELRQKLVN GGNEETLRKV DSAVFCLCLD DFPIEGLVHL SHSMLHGDGT NRWYDKSFNL
IIGKDGTAAL HFEHAWGDGV AVLRFLNEVF KDSTQAPAIS PQNQPARTDS SAAVQKLTFK
LSDALKTGIS TAKERFDAIV KTLTIDFIQF HRGGKEFLKK QRLSPDSVAQ LAFQMAFLRQ
YGQTVATYES CSTAAFKHGR TETIRPASIF TKRCSEAFVR EPSQHSIGEL QQMMAECSKY
HGQLTREAAM GQGFDRHLFA LRYLAAAKGI ALPELYLDPA YGQINHNILS TSTLSSPAVN
IGGFAPVVPD GFGIGYAVHD NWIGCNVSSY PDRNAREFLQ CVEKALEDIF DVIDGRCIKT
//
