ID A0A2U4BJJ2_TURTR Unreviewed; 540 AA.
AC A0A2U4BJJ2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CPT2 {ECO:0000313|RefSeq:XP_019793331.1,
GN ECO:0000313|RefSeq:XP_033722379.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019793331.1};
RN [1] {ECO:0000313|RefSeq:XP_019793331.1, ECO:0000313|RefSeq:XP_033722379.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019793331.1,
RC ECO:0000313|RefSeq:XP_033722379.1};
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 + 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. {ECO:0000256|ARBA:ARBA00005189}.
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_019793331.1; XM_019937772.2.
DR RefSeq; XP_019793332.1; XM_019937773.1.
DR RefSeq; XP_033722379.1; XM_033866488.1.
DR GeneID; 101335861; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000245320; Chromosome 1.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
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; PS00440; ACYLTRANSF_C_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801}; 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:UP000245320};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 1..524
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 540 AA; 60596 MW; 59434DBB65BB935A CRC64;
MYLTARDPVV LNFNPFMSFN PDPKSEYNDQ LTRATNMTVS AIRFLKTLRA DLLEPEVFHL
NPAKSDTDTF KRLIRFVPSS LSWYGAYLVN AYPLDMSQYF RLFNSTRLPK PSRDELFTDD
KARHLLVLRK GHFYVFDVLD QNGNIVSASE IQAHLKYILS DSSLAPEFPL SYLTSENRDI
WAELRQKLVS GGNEETLRKV DSAVFCLCLD DFPIKDLVHL SHNMLHGDGT NRWFDKSFNL
IIAKDGTAAI HFEHAWGDGV AVLRFFNEVF KDSTQAPAIT PRSQPANTDS SVAVQKLNFK
LNDALKTGIS AAKEKFDATM KTLTIDYIQF QRGGKEFLKK QKLSPDSVAQ LAFQMALLQQ
YGQTVATYES CSTAAFKHGR TETIRPASIF TKRCSEAFVR EPSKHSAGEL QQMIAKCSTY
HNQLTKEAAM GQGFDRHLFA LRYLGAAKGI DLPELYLDPA YRQINHNILS TSTLSSPAVN
IGGFAPVVPD GFGIAYAVHD NWIGCNVSAY QGRNAHEFLQ CVEKALEGMF DALEGKAIKS
//
