ID   CPT1A_HUMAN             Reviewed;         773 AA.
AC   P50416; Q8TCU0; Q9BWK0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   27-MAR-2024, entry version 212.
DE   RecName: Full=Carnitine O-palmitoyltransferase 1, liver isoform;
DE            Short=CPT1-L;
DE            EC=2.3.1.21 {ECO:0000269|PubMed:11350182, ECO:0000269|PubMed:9691089};
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 {ECO:0000312|HGNC:HGNC:2328}; Synonyms=CPT1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=7892212; DOI=10.1073/pnas.92.6.1984;
RA   Britton C.H., Schultz R.A., Zhang B., Esser V., Foster D.W., McGarry J.D.;
RT   "Human liver mitochondrial carnitine palmitoyltransferase I:
RT   characterization of its cDNA and chromosomal localization and partial
RT   analysis of the gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:1984-1988(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CPT1AD VAL-414 AND CYS-498, AND
RP   VARIANT THR-275.
RX   PubMed=12189492; DOI=10.1007/s00439-002-0752-0;
RA   Gobin S., Bonnefont J.-P., Prip-Buus C., Mugnier C., Ferrec M.,
RA   Demaugre F., Saudubray J.-M., Rostane H., Djouadi F., Wilcox W.,
RA   Cederbaum S., Haas R., Nyhan W.L., Green A., Gray G., Girard J.,
RA   Thuillier L.;
RT   "Organization of the human liver carnitine palmitoyltransferase 1 gene
RT   (CPT1A) and identification of novel mutations in hypoketotic
RT   hypoglycaemia.";
RL   Hum. Genet. 111:179-189(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-473.
RX   PubMed=16651524; DOI=10.1073/pnas.0602205103;
RA   Wolfgang M.J., Kurama T., Dai Y., Suwa A., Asaumi M., Matsumoto S.,
RA   Cha S.H., Shimokawa T., Lane M.D.;
RT   "The brain-specific carnitine palmitoyltransferase-1c regulates energy
RT   homeostasis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7282-7287(2006).
RN   [6]
RP   INDUCTION BY FATTY ACIDS.
RX   PubMed=16271724; DOI=10.1016/j.jmb.2005.09.097;
RA   Napal L., Marrero P.F., Haro D.;
RT   "An intronic peroxisome proliferator-activated receptor-binding sequence
RT   mediates fatty acid induction of the human carnitine palmitoyltransferase
RT   1A.";
RL   J. Mol. Biol. 354:751-759(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [9]
RP   3D-STRUCTURE MODELING.
RX   PubMed=14711372; DOI=10.1042/bj20031373;
RA   Morillas M., Lopez-Vinas E., Valencia A., Serra D., Gomez-Puertas P.,
RA   Hegardt F.G., Asins G.;
RT   "Structural model of carnitine palmitoyltransferase I based on the
RT   carnitine acetyltransferase crystal.";
RL   Biochem. J. 379:777-784(2004).
RN   [10]
RP   STRUCTURE BY NMR OF 1-42, AND DOMAIN.
RX   PubMed=21990363; DOI=10.1074/jbc.m111.306951;
RA   Rao J.N., Warren G.Z., Estolt-Povedano S., Zammit V.A., Ulmer T.S.;
RT   "An environment-dependent structural switch underlies the regulation of
RT   carnitine palmitoyltransferase 1A.";
RL   J. Biol. Chem. 286:42545-42554(2011).
RN   [11]
RP   VARIANT CPT1AD GLY-454, CHARACTERIZATION OF VARIANT CPT1AD GLY-454,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9691089; DOI=10.1172/jci2927;
RA   Ijlst L., Mandel H., Oostheim W., Ruiter J.P.N., Gutman A., Wanders R.J.;
RT   "Molecular basis of hepatic carnitine palmitoyltransferase I deficiency.";
RL   J. Clin. Invest. 102:527-531(1998).
RN   [12]
RP   VARIANTS CPT1AD CYS-123; TRP-304; TRP-357; ARG-395 DEL; LEU-479 AND
RP   PRO-484, AND VARIANT THR-275.
RX   PubMed=11441142;
RA   Brown N.F., Mullur R.S., Subramanian I., Esser V., Bennett M.J.,
RA   Saudubray J.-M., Feigenbaum A.S., Kobari J.A., Macleod P.M., McGarry J.D.,
RA   Cohen J.C.;
RT   "Molecular characterization of L-CPT I deficiency in six patients: insights
RT   into function of the native enzyme.";
RL   J. Lipid Res. 42:1134-1142(2001).
RN   [13]
RP   VARIANT CPT1AD GLU-710, CHARACTERIZATION OF VARIANT CPT1AD GLU-710,
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=11350182; DOI=10.1006/mgme.2001.3176;
RA   Prip-Buus C., Thuillier L., Abadi N., Prasad C., Dilling L., Klasing J.,
RA   Demaugre F., Greenberg C.R., Haworth J.C., Droin V., Kadhom N., Gobin S.,
RA   Kamoun P., Girard J., Bonnefont J.-P.;
RT   "Molecular and enzymatic characterization of a unique carnitine
RT   palmitoyltransferase 1A mutation in the Hutterite community.";
RL   Mol. Genet. Metab. 73:46-54(2001).
RN   [14]
RP   CHARACTERIZATION OF VARIANT CPT1AD GLY-360.
RX   PubMed=12111367; DOI=10.1007/s100380200047;
RA   Ogawa E., Kanazawa M., Yamamoto S., Ohtsuka S., Ogawa A., Ohtake A.,
RA   Takayanagi M., Kohno Y.;
RT   "Expression analysis of two mutations in carnitine palmitoyltransferase IA
RT   deficiency.";
RL   J. Hum. Genet. 47:342-347(2002).
RN   [15]
RP   VARIANT CPT1AD GLU-709, CHARACTERIZATION OF VARIANTS CPT1AD THR-275;
RP   VAL-414; CYS-498; GLU-709 AND GLU-710, SUBCELLULAR LOCATION, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14517221; DOI=10.1074/jbc.m310130200;
RA   Gobin S., Thuillier L., Jogl G., Faye A., Tong L., Chi M., Bonnefont J.-P.,
RA   Girard J., Prip-Buus C.;
RT   "Functional and structural basis of carnitine palmitoyltransferase 1A
RT   deficiency.";
RL   J. Biol. Chem. 278:50428-50434(2003).
RN   [16]
RP   VARIANT CPT1AD ILE-314.
RX   PubMed=15669684; DOI=10.1023/b:boli.0000042979.42120.55;
RA   Stoler J.M., Sabry M.A., Hanley C., Hoppel C.L., Shih V.E.;
RT   "Successful long-term treatment of hepatic carnitine palmitoyltransferase I
RT   deficiency and a novel mutation.";
RL   J. Inherit. Metab. Dis. 27:679-684(2004).
RN   [17]
RP   VARIANTS CPT1AD GLY-316; VAL-343 AND TRP-465.
RX   PubMed=15110323; DOI=10.1016/j.ymgme.2004.02.004;
RA   Bennett M.J., Boriack R.L., Narayan S., Rutledge S.L., Raff M.L.;
RT   "Novel mutations in CPT 1A define molecular heterogeneity of hepatic
RT   carnitine palmitoyltransferase I deficiency.";
RL   Mol. Genet. Metab. 82:59-63(2004).
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 (PubMed:9691089, PubMed:11350182,
CC       PubMed:14517221, PubMed:16651524). Plays an important role in hepatic
CC       triglyceride metabolism (By similarity). {ECO:0000250|UniProtKB:P32198,
CC       ECO:0000269|PubMed:11350182, ECO:0000269|PubMed:14517221,
CC       ECO:0000269|PubMed:16651524, ECO:0000269|PubMed:9691089}.
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:0000269|PubMed:11350182, ECO:0000269|PubMed:14517221,
CC         ECO:0000269|PubMed:16651524, ECO:0000269|PubMed:9691089};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662;
CC         Evidence={ECO:0000305|PubMed:11350182};
CC   -!- ACTIVITY REGULATION: Inhibited by malonyl-CoA.
CC       {ECO:0000269|PubMed:14517221}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=89 uM for carnitine {ECO:0000269|PubMed:11350182};
CC         KM=106.5 uM for carnitine {ECO:0000269|PubMed:14517221};
CC         KM=43 uM for palmitoyl-CoA {ECO:0000269|PubMed:11350182};
CC         KM=82.8 uM for palmitoyl-CoA {ECO:0000269|PubMed:14517221};
CC         Vmax=15 nmol/min/mg enzyme toward carnitine
CC         {ECO:0000269|PubMed:11350182};
CC         Vmax=147.8 nmol/min/mg enzyme toward carnitine
CC         {ECO:0000269|PubMed:14517221};
CC         Vmax=40 nmol/min/mg enzyme toward palmitoyl-CoA
CC         {ECO:0000269|PubMed:11350182};
CC         Vmax=88.6 nmol/min/mg enzyme toward palmitoyl-CoA
CC         {ECO:0000269|PubMed:14517221};
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:0000269|PubMed:11350182, ECO:0000269|PubMed:14517221}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P50416-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P50416-2; Sequence=VSP_012167;
CC   -!- TISSUE SPECIFICITY: Strong expression in kidney and heart, and lower in
CC       liver and skeletal muscle.
CC   -!- INDUCTION: Up-regulated by fatty acids. {ECO:0000269|PubMed:16271724}.
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:0000269|PubMed:21990363}.
CC   -!- DISEASE: Carnitine palmitoyltransferase 1A deficiency (CPT1AD)
CC       [MIM:255120]: Rare autosomal recessive metabolic disorder of long-chain
CC       fatty acid oxidation characterized by severe episodes of hypoketotic
CC       hypoglycemia usually occurring after fasting or illness. Onset is in
CC       infancy or early childhood. {ECO:0000269|PubMed:11350182,
CC       ECO:0000269|PubMed:11441142, ECO:0000269|PubMed:12111367,
CC       ECO:0000269|PubMed:12189492, ECO:0000269|PubMed:14517221,
CC       ECO:0000269|PubMed:15110323, ECO:0000269|PubMed:15669684,
CC       ECO:0000269|PubMed:9691089}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; L39211; AAC41748.1; -; mRNA.
DR   EMBL; AJ420747; CAD12625.1; -; Genomic_DNA.
DR   EMBL; AJ420748; CAD59673.1; -; Genomic_DNA.
DR   EMBL; BT009791; AAP88793.1; -; mRNA.
DR   EMBL; BC000185; AAH00185.1; -; mRNA.
DR   CCDS; CCDS31624.1; -. [P50416-2]
DR   CCDS; CCDS8185.1; -. [P50416-1]
DR   PIR; I59351; I59351.
DR   RefSeq; NP_001027017.1; NM_001031847.2. [P50416-2]
DR   RefSeq; NP_001867.2; NM_001876.3. [P50416-1]
DR   RefSeq; XP_016872709.1; XM_017017220.1. [P50416-1]
DR   PDB; 2LE3; NMR; -; A=1-42.
DR   PDBsum; 2LE3; -.
DR   AlphaFoldDB; P50416; -.
DR   BMRB; P50416; -.
DR   SMR; P50416; -.
DR   BioGRID; 107765; 191.
DR   IntAct; P50416; 50.
DR   MINT; P50416; -.
DR   STRING; 9606.ENSP00000265641; -.
DR   BindingDB; P50416; -.
DR   ChEMBL; CHEMBL1293194; -.
DR   DrugBank; DB01016; Glyburide.
DR   DrugBank; DB00583; Levocarnitine.
DR   DrugBank; DB01074; Perhexiline.
DR   DrugCentral; P50416; -.
DR   SwissLipids; SLP:000001056; -.
DR   TCDB; 4.C.2.1.3; the carnitine o-acyl transferase (carat) family.
DR   GlyGen; P50416; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P50416; -.
DR   MetOSite; P50416; -.
DR   PhosphoSitePlus; P50416; -.
DR   SwissPalm; P50416; -.
DR   BioMuta; CPT1A; -.
DR   DMDM; 56405343; -.
DR   EPD; P50416; -.
DR   jPOST; P50416; -.
DR   MassIVE; P50416; -.
DR   MaxQB; P50416; -.
DR   PaxDb; 9606-ENSP00000265641; -.
DR   PeptideAtlas; P50416; -.
DR   ProteomicsDB; 56220; -. [P50416-1]
DR   ProteomicsDB; 56221; -. [P50416-2]
DR   Pumba; P50416; -.
DR   Antibodypedia; 1640; 484 antibodies from 37 providers.
DR   DNASU; 1374; -.
DR   Ensembl; ENST00000265641.10; ENSP00000265641.4; ENSG00000110090.13. [P50416-1]
DR   Ensembl; ENST00000376618.6; ENSP00000365803.2; ENSG00000110090.13. [P50416-2]
DR   Ensembl; ENST00000539743.5; ENSP00000446108.1; ENSG00000110090.13. [P50416-1]
DR   Ensembl; ENST00000540367.5; ENSP00000439084.1; ENSG00000110090.13. [P50416-2]
DR   GeneID; 1374; -.
DR   KEGG; hsa:1374; -.
DR   MANE-Select; ENST00000265641.10; ENSP00000265641.4; NM_001876.4; NP_001867.2.
DR   UCSC; uc001oof.5; human. [P50416-1]
DR   AGR; HGNC:2328; -.
DR   CTD; 1374; -.
DR   DisGeNET; 1374; -.
DR   GeneCards; CPT1A; -.
DR   GeneReviews; CPT1A; -.
DR   HGNC; HGNC:2328; CPT1A.
DR   HPA; ENSG00000110090; Low tissue specificity.
DR   MalaCards; CPT1A; -.
DR   MIM; 255120; phenotype.
DR   MIM; 600528; gene.
DR   neXtProt; NX_P50416; -.
DR   OpenTargets; ENSG00000110090; -.
DR   Orphanet; 156; Carnitine palmitoyl transferase 1A deficiency.
DR   PharmGKB; PA26847; -.
DR   VEuPathDB; HostDB:ENSG00000110090; -.
DR   eggNOG; KOG3716; Eukaryota.
DR   GeneTree; ENSGT01060000248595; -.
DR   HOGENOM; CLU_013513_2_1_1; -.
DR   InParanoid; P50416; -.
DR   OMA; NTEHSWG; -.
DR   OrthoDB; 1429709at2759; -.
DR   PhylomeDB; P50416; -.
DR   TreeFam; TF313836; -.
DR   BioCyc; MetaCyc:HS03286-MONOMER; -.
DR   BRENDA; 2.3.1.21; 2681.
DR   PathwayCommons; P50416; -.
DR   Reactome; R-HSA-1368082; RORA activates gene expression.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-200425; Carnitine metabolism.
DR   Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR   SABIO-RK; P50416; -.
DR   SignaLink; P50416; -.
DR   SIGNOR; P50416; -.
DR   UniPathway; UPA00659; -.
DR   BioGRID-ORCS; 1374; 14 hits in 1172 CRISPR screens.
DR   ChiTaRS; CPT1A; human.
DR   GenomeRNAi; 1374; -.
DR   Pharos; P50416; Tchem.
DR   PRO; PR:P50416; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P50416; Protein.
DR   Bgee; ENSG00000110090; Expressed in jejunal mucosa and 199 other cell types or tissues.
DR   ExpressionAtlas; P50416; baseline and differential.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IMP:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:1990698; F:palmitoleoyltransferase activity; IEA:Ensembl.
DR   GO; GO:0046222; P:aflatoxin metabolic process; IEA:Ensembl.
DR   GO; GO:0009437; P:carnitine metabolic process; IDA:UniProtKB.
DR   GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR   GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR   GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; TAS:ProtInc.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR   GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR   GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0010883; P:regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:1904772; P:response to tetrachloromethane; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
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:SF74; CARNITINE O-PALMITOYLTRANSFERASE 1, LIVER 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.
DR   Genevisible; P50416; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW   Disease variant; Fatty acid metabolism; Lipid metabolism; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Nitration; Phosphoprotein;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P32198"
FT   CHAIN           2..773
FT                   /note="Carnitine O-palmitoyltransferase 1, liver isoform"
FT                   /id="PRO_0000210159"
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..773
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|UniProtKB:P18886"
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"
FT   VAR_SEQ         746..773
FT                   /note="DSHRFGRHLKEAMTDIITLFGLSSNSKK -> GIISQGPSSDT (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT                   /id="VSP_012167"
FT   VARIANT         123
FT                   /note="R -> C (in CPT1AD; dbSNP:rs80356775)"
FT                   /evidence="ECO:0000269|PubMed:11441142"
FT                   /id="VAR_020546"
FT   VARIANT         275
FT                   /note="A -> T (in dbSNP:rs2229738)"
FT                   /evidence="ECO:0000269|PubMed:11441142,
FT                   ECO:0000269|PubMed:12189492, ECO:0000269|PubMed:14517221"
FT                   /id="VAR_020547"
FT   VARIANT         304
FT                   /note="C -> W (in CPT1AD; dbSNP:rs80356789)"
FT                   /evidence="ECO:0000269|PubMed:11441142"
FT                   /id="VAR_020548"
FT   VARIANT         314
FT                   /note="T -> I (in CPT1AD; dbSNP:rs80356776)"
FT                   /evidence="ECO:0000269|PubMed:15669684"
FT                   /id="VAR_020549"
FT   VARIANT         316
FT                   /note="R -> G (in CPT1AD; dbSNP:rs80356796)"
FT                   /evidence="ECO:0000269|PubMed:15110323"
FT                   /id="VAR_046767"
FT   VARIANT         343
FT                   /note="F -> V (in CPT1AD; dbSNP:rs80356783)"
FT                   /evidence="ECO:0000269|PubMed:15110323"
FT                   /id="VAR_046768"
FT   VARIANT         357
FT                   /note="R -> W (in CPT1AD; decreased stability;
FT                   dbSNP:rs80356777)"
FT                   /evidence="ECO:0000269|PubMed:11441142"
FT                   /id="VAR_020550"
FT   VARIANT         360
FT                   /note="E -> G (in CPT1AD; reduced protein levels;
FT                   dbSNP:rs80356787)"
FT                   /evidence="ECO:0000269|PubMed:12111367"
FT                   /id="VAR_020551"
FT   VARIANT         395
FT                   /note="Missing (in CPT1AD; loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:11441142"
FT                   /id="VAR_020552"
FT   VARIANT         414
FT                   /note="A -> V (in CPT1AD; decreased activity;
FT                   dbSNP:rs80356790)"
FT                   /evidence="ECO:0000269|PubMed:12189492,
FT                   ECO:0000269|PubMed:14517221"
FT                   /id="VAR_020553"
FT   VARIANT         454
FT                   /note="D -> G (in CPT1AD; loss of activity;
FT                   dbSNP:rs80356778)"
FT                   /evidence="ECO:0000269|PubMed:9691089"
FT                   /id="VAR_020554"
FT   VARIANT         465
FT                   /note="G -> W (in CPT1AD; dbSNP:rs80356784)"
FT                   /evidence="ECO:0000269|PubMed:15110323"
FT                   /id="VAR_046769"
FT   VARIANT         479
FT                   /note="P -> L (in CPT1AD; decreased activity;
FT                   dbSNP:rs80356779)"
FT                   /evidence="ECO:0000269|PubMed:11441142"
FT                   /id="VAR_020555"
FT   VARIANT         484
FT                   /note="L -> P (in CPT1AD; dbSNP:rs80356793)"
FT                   /evidence="ECO:0000269|PubMed:11441142"
FT                   /id="VAR_020556"
FT   VARIANT         498
FT                   /note="Y -> C (in CPT1AD; decreased activity;
FT                   dbSNP:rs80356791)"
FT                   /evidence="ECO:0000269|PubMed:12189492,
FT                   ECO:0000269|PubMed:14517221"
FT                   /id="VAR_020557"
FT   VARIANT         709
FT                   /note="G -> E (in CPT1AD; loss of activity;
FT                   dbSNP:rs28936374)"
FT                   /evidence="ECO:0000269|PubMed:14517221"
FT                   /id="VAR_020558"
FT   VARIANT         710
FT                   /note="G -> E (in CPT1AD; loss of activity;
FT                   dbSNP:rs80356780)"
FT                   /evidence="ECO:0000269|PubMed:11350182,
FT                   ECO:0000269|PubMed:14517221"
FT                   /id="VAR_020559"
FT   MUTAGEN         473
FT                   /note="H->A: Loss of carnitine O-palmitoyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:16651524"
FT   CONFLICT        479
FT                   /note="P -> Q (in Ref. 1; AAC41748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="A -> T (in Ref. 1; AAC41748)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..7
FT                   /evidence="ECO:0007829|PDB:2LE3"
FT   STRAND          9..15
FT                   /evidence="ECO:0007829|PDB:2LE3"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:2LE3"
FT   HELIX           25..39
FT                   /evidence="ECO:0007829|PDB:2LE3"
SQ   SEQUENCE   773 AA;  88368 MW;  E5DC9141B6301947 CRC64;
     MAEAHQAVAF QFTVTPDGID LRLSHEALRQ IYLSGLHSWK KKFIRFKNGI ITGVYPASPS
     SWLIVVVGVM TTMYAKIDPS LGIIAKINRT LETANCMSSQ TKNVVSGVLF GTGLWVALIV
     TMRYSLKVLL SYHGWMFTEH GKMSRATKIW MGMVKIFSGR KPMLYSFQTS LPRLPVPAVK
     DTVNRYLQSV RPLMKEEDFK RMTALAQDFA VGLGPRLQWY LKLKSWWATN YVSDWWEEYI
     YLRGRGPLMV NSNYYAMDLL YILPTHIQAA RAGNAIHAIL LYRRKLDREE IKPIRLLGST
     IPLCSAQWER MFNTSRIPGE ETDTIQHMRD SKHIVVYHRG RYFKVWLYHD GRLLKPREME
     QQMQRILDNT SEPQPGEARL AALTAGDRVP WARCRQAYFG RGKNKQSLDA VEKAAFFVTL
     DETEEGYRSE DPDTSMDSYA KSLLHGRCYD RWFDKSFTFV VFKNGKMGLN AEHSWADAPI
     VAHLWEYVMS IDSLQLGYAE DGHCKGDINP NIPYPTRLQW DIPGECQEVI ETSLNTANLL
     ANDVDFHSFP FVAFGKGIIK KCRTSPDAFV QLALQLAHYK DMGKFCLTYE ASMTRLFREG
     RTETVRSCTT ESCDFVRAMV DPAQTVEQRL KLFKLASEKH QHMYRLAMTG SGIDRHLFCL
     YVVSKYLAVE SPFLKEVLSE PWRLSTSQTP QQQVELFDLE NNPEYVSSGG GFGPVADDGY
     GVSYILVGEN LINFHISSKF SCPETDSHRF GRHLKEAMTD IITLFGLSSN SKK
//