CPT1A_HUMAN
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 03-AUG-2022, entry version 203.
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; 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 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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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). Plays an important role in hepatic triglyceride
CC metabolism (By similarity). {ECO:0000250|UniProtKB:P32198,
CC ECO:0000269|PubMed:11350182, ECO:0000269|PubMed:14517221,
CC 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: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; 177.
DR IntAct; P50416; 45.
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; 1 site, 1 O-linked glycan (1 site).
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; P50416; -.
DR PeptideAtlas; P50416; -.
DR PRIDE; P50416; -.
DR ProteomicsDB; 56220; -. [P50416-1]
DR ProteomicsDB; 56221; -. [P50416-2]
DR Antibodypedia; 1640; 443 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 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; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; P50416; -.
DR OMA; MXYLESV; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P50416; -.
DR TreeFam; TF313836; -.
DR BioCyc; MetaCyc:HS03286-MON; -.
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 1086 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 197 other tissues.
DR ExpressionAtlas; P50416; baseline and differential.
DR Genevisible; P50416; HS.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
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:UniProtKB.
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: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:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; 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; 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 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"
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 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
