ID A0A2K6KBY6_RHIBE Unreviewed; 552 AA.
AC A0A2K6KBY6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform {ECO:0000256|ARBA:ARBA00040569};
DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform {ECO:0000256|ARBA:ARBA00041685};
DE AltName: Full=Carnitine palmitoyltransferase 1B {ECO:0000256|ARBA:ARBA00042959};
GN Name=CPT1B {ECO:0000313|Ensembl:ENSRBIP00000008805.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000008805.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000008805.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000008805.1}
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 -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC {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; A0A2K6KBY6; -.
DR STRING; 61621.ENSRBIP00000008805; -.
DR Ensembl; ENSRBIT00000032413.1; ENSRBIP00000008805.1; ENSRBIG00000028289.1.
DR GeneTree; ENSGT01060000248595; -.
DR OMA; CVELECT; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:Ensembl.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
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:SF69; CARNITINE O-PALMITOYLTRANSFERASE 1, MUSCLE ISOFORM; 1.
DR Pfam; PF00755; Carn_acyltransf; 2.
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:ARBA00022787};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 66..379
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT DOMAIN 406..536
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 552 AA; 62277 MW; 854D19A150B1E631 CRC64;
LTLKNKEFKK QPRLKLEQRV TVTSYAFLEA HPDSMCRMYR RRETEHLRPP NGLVLGSDLV
LIKNTDVQAA RLGNTIHAMI MYRRKLDREE IKPVMALGIV PMCSYQMERM FNTTRVPGKE
TDVLQHLSDS RHVAVYHKGR FFKLWLYEGS RLLKPQDLEM QFQRILDDPS PPQPGEEKLA
ALTAGGRVEW AQARQAFFSS GKNKAALEAI ERAAFFVALD EESYHYDPED EASLSLYGKA
LLHGNCYNRW FDKSFTLISF KNGQLGLNAE HAWADAPIMG HLWEFVLGTD SFHLGYTETG
HCLGKPNPAL PPPMRLQWDI PKQAVIESSY QVAKALADDV ELYCFQFLPF GKGLIKKCRT
SPDAFVQIAL QLAHFRRAGW CQGPPARFTP LYIPGQGLCA GNGGEKADLR DLFQKAAKKH
QNMYRLAMTG AGIDRHLFCL YLVSKYLGVS SPFLAEVLSE PWRLSTSQIP QSQIRMFDPE
QHPNHLGAGG GFGPVADDGY GVSYMIAGEN TIFFHVSSKF SSSETNAQRF GNHIRQALLD
LADLFQVPKT DS
//
