ID A0A3B5A3U0_9TELE Unreviewed; 681 AA.
AC A0A3B5A3U0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform {ECO:0000256|ARBA:ARBA00040569};
DE EC=2.3.1.21 {ECO:0000256|ARBA:ARBA00013243};
DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform {ECO:0000256|ARBA:ARBA00041685};
DE AltName: Full=Carnitine palmitoyltransferase 1B {ECO:0000256|ARBA:ARBA00042959};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000015918.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000015918.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty
CC acid-CoA conjugates onto carnitine, an essential step for the
CC mitochondrial uptake of long-chain fatty acids and their subsequent
CC beta-oxidation in the mitochondrion. {ECO:0000256|ARBA:ARBA00043926}.
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:ARBA00043805};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662;
CC Evidence={ECO:0000256|ARBA:ARBA00043805};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004374}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR AlphaFoldDB; A0A3B5A3U0; -.
DR Ensembl; ENSSPAT00000016175.1; ENSSPAP00000015918.1; ENSSPAG00000011942.1.
DR GeneTree; ENSGT01060000248595; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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; 6.10.250.1760; -; 1.
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 InterPro; IPR032476; CPT_N.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF69; CARNITINE O-PALMITOYLTRANSFERASE 1, MUSCLE ISOFORM; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 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:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..47
FT /note="Carnitine O-palmitoyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16484"
FT DOMAIN 70..650
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 681 AA; 77924 MW; 32BCCFE1710423E8 CRC64;
MAEAHQAVGF QFTVRPDGVD LKLSQEVIKN IYLSGVTAWK KRAIQFKSLV KMFSGRRPLL
YSFQASLPRL PVPSVDDTIH RYLESVRPLL DTEQYRQMEV LANEFNESMA TRLQRYLILK
SWWATNYVSD WWEEYIYLRG RTPIMVNSNF YIMDLLYVTP THRQAARAGN VVHAMLQYRR
KLERGEHAPL RALGTVPMCS TQMERMFNTT RIPGIETDIV QHLTDRKHLV VYHKGRFFHL
WLYTGGRHLL PSELETQFQR ILNDTSEPQP GELKLAALTA GNRVPWARAR IKYFSQGVNK
VSLDAIESAA FFLTLDDEPQ GYDPAKTNSL DSYAKSLLHG KCYDRWFDKS FTLISYPNGK
MGVNAEHSWA DAPIVGHMWE YVLATDCFHL GYTEEGHCKG DVNKGLPHPT RLQWQIPEEC
QSIIETSYLS AKQIADDVDF HGYLFNDFGK GMIKKCRTSP DAFIQLALQL AQFRDQRVFC
LTYESSMTRM FRDGRTETVR SCTSEAVAFV RAMEDAGATT AQRLALFRKA ADKHQNMYRL
AMTGSGIDRH LFCLYLVSKY LGVDSPFLKK VLSEPWKLST SQTPQQQLNL VDINKFPKYV
GAGGGFGPVA DDGYGVSYII VGENLITFHI SSKFSSPDTD SYRFGQHIQK AMLDIQALYK
PENDKKTVEK HVPLENGKKH I
//
