ID A0A3Q0CMB6_MESAU Unreviewed; 826 AA.
AC A0A3Q0CMB6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
GN Name=Cpt1b {ECO:0000313|RefSeq:XP_021081122.1,
GN ECO:0000313|RefSeq:XP_021081123.1, ECO:0000313|RefSeq:XP_021081124.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021081124.1};
RN [1] {ECO:0000313|RefSeq:XP_021081122.1, ECO:0000313|RefSeq:XP_021081123.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
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DR RefSeq; XP_021081122.1; XM_021225463.1.
DR RefSeq; XP_021081123.1; XM_021225464.1.
DR RefSeq; XP_021081124.1; XM_021225465.1.
DR STRING; 10036.ENSMAUP00000011351; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000189706; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 176..751
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 826 AA; 94019 MW; 6EEF831A994447A1 CRC64;
MAEAHQAVAF QFTVTPDGVD FRLSREALRH IYLSGINSWK KRLIRIKNGI LRGVYPGSPT
SWLVIVMATV GSNYCKVDIS MGLVECIQRY LPGRYGPYGT PQTQELLSMV IFSTGIWATG
IFVFRQTLKL LLSYHGWMFE MHSKTSHATK IWAICVRLLS SRRPMLYSFQ TSLPKLPVPS
VPATIHRYLD SVRPLLDEEE YYRMETLAKE FQNNTAPRLQ KYLVLKSWWA TNYVSDWWEE
YVYLRGRNPI MVNSNYYAMD FVLIRNTNVQ AARLGNAVHA MIMYRRKLDR EEIKPVMALG
MVPMCSYQME RMFNTTRIPG KETDVLQHLS ESRHVAVYHK GRFFKVWLYE GSRLLKPRDL
ELQFQRILDD PSPPQPGEEK LAALTAGGRV EWAQARRTFF SSGRNRTSLD IIERAAFFVA
LDEEPHGYNP DEENSLSLYG KALLHGNCYN RWFDKSFTLI SFKNGTLGLN TEHSWADAPI
IGHLWEFVLG TDTFHLGYSE TGHCMGEPNM KLTPPQRLQW DIPEQCREAI ENSYQVAKAL
ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DKGKFCLTYE ASMTRMFREG
RTETVRSCTS ESTAFVQAMV KGSHTKEDLQ ALFRKASEKH QNMYRLAMTG AGIDRHLFCL
YIVSKYLGVS SPFLAEVLSE PWSLSTSQIP QSQIRMFDPN QYPNHLGAGG GFGPVADDGY
GVSYMIAGEN TMFFHVSSKF SSSETVSLLC SHLGWSQEEG LPGVSQKHPP SLGCGEESSC
GSIWMGAVLR MCLSSQFPQN SQRFGNHIRQ ALSDIADLFK VTKAES
//
