CPT1A_HORSE
ID CPT1A_HORSE Reviewed; 776 AA.
AC Q68Y62;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, liver isoform;
DE Short=CPT1-L;
DE EC=2.3.1.21 {ECO:0000250|UniProtKB:P50416};
DE AltName: Full=Carnitine O-palmitoyltransferase I, liver isoform;
DE Short=CPT I;
DE Short=CPTI-L;
DE AltName: Full=Carnitine palmitoyltransferase 1A;
GN Name=CPT1A;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hasegawa T., Sato F.;
RT "Molecular cloning of genes expressed in equine muscle.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Plays an important
CC role in hepatic triglyceride metabolism (By similarity).
CC {ECO:0000250|UniProtKB:P50416}.
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:0000250|UniProtKB:P50416};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662;
CC Evidence={ECO:0000250|UniProtKB:P50416};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Homohexamer and homotrimer (By similarity). Identified in a
CC complex that contains at least CPT1A, ACSL1 and VDAC1 (By similarity).
CC Also identified in complexes with ACSL1 and VDAC2 and VDAC3 (By
CC similarity). {ECO:0000250|UniProtKB:P32198}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P50416}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: A conformation change in the N-terminal region spanning the
CC first 42 residues plays an important role in the regulation of enzyme
CC activity by malonyl-CoA. {ECO:0000250|UniProtKB:P50416}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB188099; BAD36782.1; -; mRNA.
DR RefSeq; NP_001075277.1; NM_001081808.1.
DR AlphaFoldDB; Q68Y62; -.
DR SMR; Q68Y62; -.
DR STRING; 9796.ENSECAP00000029446; -.
DR PaxDb; Q68Y62; -.
DR PRIDE; Q68Y62; -.
DR GeneID; 100009716; -.
DR KEGG; ecb:100009716; -.
DR CTD; 1374; -.
DR InParanoid; Q68Y62; -.
DR OrthoDB; 559299at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009437; P:carnitine metabolic process; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 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; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Nitration;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P32198"
FT CHAIN 2..776
FT /note="Carnitine O-palmitoyltransferase 1, liver isoform"
FT /id="PRO_0000210158"
FT TOPO_DOM 2..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..102
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 555..567
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 602
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P32198"
FT MOD_RES 282
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P32198"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32198"
FT MOD_RES 589
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P32198"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32198"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32198"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32198"
SQ SEQUENCE 776 AA; 88545 MW; 3B10017F60AB811E CRC64;
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGV ITGVYPASPS
SWLIVVVGVM STMYAKIDPS LGIIAKINRT LDTTGYMSSQ TKNIVSGVLF GTGLWVALII
TMRYSLKVLL SYHGWMFAEH GKMSRATRIW MCMVKIFSGR KPMLYSFQTS LPRLPVPAVK
DTVNRYLESV RPLMKDEDFK RMTALAQDFA VNLGPRLQWY LKLKSWWATN YVSDWWEEYV
YLRGRGPLMV NSNYYAMDLL YVIPTHLQAA TAGNGIHAIL LYRHKLDREE IKPILFLGST
VPLCSAQWER MFNTCRIPGE ETDTIQHLRD SKHIVVFHKG RYFKVWLYHD GRLLKPREIE
QHIQRILDDP SEPHAGEAKL AALTAGERVP WAKCRQAYFG RGKNKQSLDA VEKAAFFVTL
DETEQGYREE DPDASMDSYA KSLLHGRCSD RWFDKSFTFI VFKNGKMGMN AEHSWADAPV
VGHLWEYVMS TDCFQLGYAE DGHCKGDTNP NIPYPTRLQW DIPEECQDVI ETSLNTANIL
ASDVDFHSFP FHAFGKGLIK KCRTSPDAFV QLALQLAHYK DMGKFCLTYE ASMTRLFREG
RTETVRSCSS ESCNFVLAMV DPTQTVKQKL RLFKIASEKH QHLYRLAMTG SGIDRHLFCL
YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDLE RNPEYVSSGG GFGPVADDGY
GVSYILVGEN LINFHISSKF SSPETDSHRF GKHLKQAMND IMALFGFSSN SRKEFH
