Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 169 (02 Jun 2021)
Sequence version 2 (01 May 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Carnitine O-palmitoyltransferase 1, liver isoform

Gene

Cpt1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (PubMed:16908527, PubMed:21990363).

Plays an important role in hepatic triglyceride metabolism (PubMed:18349115).

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by malonyl-CoA.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=184.2 µM for carnitine1 Publication
  2. KM=46.5 µM for palmitoyl-CoA1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid beta-oxidation

    This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei473Proton acceptorBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei589CarnitineBy similarity1
    Binding sitei602CarnitineBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processFatty acid metabolism, Lipid metabolism, Transport

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-14439

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.1.21, 5301

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-RNO-200425, Carnitine metabolism
    R-RNO-5362517, Signaling by Retinoic Acid

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P32198

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00659

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000777

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Carnitine O-palmitoyltransferase 1, liver isoform (EC:2.3.1.213 Publications)
    Short name:
    CPT1-L
    Alternative name(s):
    Carnitine O-palmitoyltransferase I, liver isoform
    Short name:
    CPT I
    Short name:
    CPTI-L
    Carnitine palmitoyltransferase 1A
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:Cpt1a
    Synonyms:Cpt-1, Cpt1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    2396, Cpt1a

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 47CytoplasmicSequence analysisAdd BLAST46
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei48 – 73HelicalSequence analysisAdd BLAST26
    Topological domaini74 – 102Mitochondrial intermembraneSequence analysisAdd BLAST29
    Transmembranei103 – 122HelicalSequence analysisAdd BLAST20
    Topological domaini123 – 773CytoplasmicSequence analysisAdd BLAST651

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi3E → R: Decreases susceptibility to inhibition by malonyl-CoA. 1 Publication1
    Mutagenesisi9A → G: Increases susceptibility to inhibition by malonyl-CoA. 1 Publication1
    Mutagenesisi18G → A: Increases susceptibility to inhibition by malonyl-CoA. 1 Publication1
    Mutagenesisi381A → D: Reduces activity by 86%. No effect on inhibition by malonyl-coenzyme A. 1 Publication1
    Mutagenesisi473H → A: Loss of activity. 1 Publication1
    Mutagenesisi477D → A: Reduces activity by 98%. 1 Publication1
    Mutagenesisi560K → A: Reduces activity by 50%. 1 Publication1
    Mutagenesisi567D → A: Reduces activity by 97%. 1
    Mutagenesisi590E → D: Reduces activity by over 60%. 1 Publication1
    Mutagenesisi593M → A, E or S: Almost abolishes inhibition by malonyl-coenzyme A. 1 Publication1
    Mutagenesisi608C → A: Slightly lowers inhibition by malonyl-coenzyme A. 1 Publication1
    Mutagenesisi685S → A: Reduces activity by 50%. 1 Publication1
    Mutagenesisi686T → A: Loss of activity. 1 Publication1
    Mutagenesisi687S → A: Loss of activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3858

    DrugCentral

    More...
    DrugCentrali
    P32198

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002101612 – 773Carnitine O-palmitoyltransferase 1, liver isoformAdd BLAST772

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanine1 Publication1
    Modified residuei2823'-nitrotyrosine1 Publication1
    Modified residuei588Phosphothreonine1 Publication1
    Modified residuei5893'-nitrotyrosine1 Publication1
    Modified residuei604Phosphothreonine1 Publication1
    Modified residuei741Phosphoserine1 Publication1
    Modified residuei747Phosphoserine1 Publication1

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P32198

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P32198

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P32198

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P32198

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P32198

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Liver and kidney.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSRNOG00000014254, Expressed in liver and 21 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P32198, RN

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homohexamer and homotrimer (PubMed:19136561).

    Identified in a complex that contains at least CPT1A, ACSL1 and VDAC1 (PubMed:21622568). Also identified in complexes with ACSL1 and VDAC2 and VDAC3.

    2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P32198

    Protein interaction database and analysis system

    More...
    IntActi
    P32198, 2 interactors

    Molecular INTeraction database

    More...
    MINTi
    P32198

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000019652

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P32198

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P32198

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni555 – 567Coenzyme A bindingBy similarityAdd BLAST13

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    A conformation change in the N-terminal region spanning the first 42 residues plays an important role in the regulation of enzyme activity by malonyl-CoA.1 Publication

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG3716, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT01030000234593

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_013513_2_1_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P32198

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    ASHMWEN

    Database of Orthologous Groups

    More...
    OrthoDBi
    559299at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P32198

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313836

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.559.40, 1 hit
    3.30.559.70, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000542, Carn_acyl_trans
    IPR039551, Cho/carn_acyl_trans
    IPR042232, Cho/carn_acyl_trans_1
    IPR042231, Cho/carn_acyl_trans_2
    IPR032476, CPT_N

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR22589, PTHR22589, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00755, Carn_acyltransf, 1 hit
    PF16484, CPT_N, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00439, ACYLTRANSF_C_1, 1 hit
    PS00440, ACYLTRANSF_C_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P32198-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI
    60 70 80 90 100
    ITGVFPANPS SWLIVVVGVI SSMHAKVDPS LGMIAKISRT LDTTGRMSSQ
    110 120 130 140 150
    TKNIVSGVLF GTGLWVAVIM TMRYSLKVLL SYHGWMFAEH GKMSRSTKIW
    160 170 180 190 200
    MAMVKVLSGR KPMLYSFQTS LPRLPVPAVK DTVSRYLESV RPLMKEEDFQ
    210 220 230 240 250
    RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI YLRGRGPLMV
    260 270 280 290 300
    NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTLDREE LKPIRLLGST
    310 320 330 340 350
    IPLCSAQWER LFNTSRIPGE ETDTIQHIKD SRHIVVYHRG RYFKVWLYHD
    360 370 380 390 400
    GRLLRPRELE QQMQQILDDP SEPQPGEAKL AALTAADRVP WAKCRQTYFA
    410 420 430 440 450
    RGKNKQSLDA VEKAAFFVTL DESEQGYREE DPEASIDSYA KSLLHGRCFD
    460 470 480 490 500
    RWFDKSITFV VFKNSKIGIN AEHSWADAPV VGHLWEYVMA TDVFQLGYSE
    510 520 530 540 550
    DGHCKGDTNP NIPKPTRLQW DIPGECQEVI DASLSSASLL ANDVDLHSFP
    560 570 580 590 600
    FDSFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG
    610 620 630 640 650
    RTETVRSCTM ESCNFVQAMM DPKSTAEQRL KLFKIACEKH QHLYRLAMTG
    660 670 680 690 700
    AGIDRHLFCL YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE
    710 720 730 740 750
    KNPDYVSCGG GFGPVADDGY GVSYIIVGEN FIHFHISSKF SSPETDSHRF
    760 770
    GKHLRQAMMD IITLFGLTIN SKK
    Length:773
    Mass (Da):88,125
    Last modified:May 1, 2007 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8C15594D45430CB8
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti266H → D AA sequence (PubMed:8348957).Curated1
    Sequence conflicti374 – 375QP → NG AA sequence (PubMed:8348957).Curated2
    Sequence conflicti480V → I in AAA40876 (PubMed:8449948).Curated1
    Sequence conflicti531D → Y AA sequence (PubMed:8348957).Curated1
    Sequence conflicti708C → R AA sequence (PubMed:8348957).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    L07736 mRNA Translation: AAA40876.1
    U88294 mRNA Translation: AAB48046.1
    BC072522 mRNA Translation: AAH72522.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A46627

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_113747.2, NM_031559.2
    XP_006230757.1, XM_006230695.2
    XP_017444326.1, XM_017588837.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSRNOT00000019652; ENSRNOP00000019652; ENSRNOG00000014254

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    25757

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:25757

    UCSC genome browser

    More...
    UCSCi
    RGD:2396, rat

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L07736 mRNA Translation: AAA40876.1
    U88294 mRNA Translation: AAB48046.1
    BC072522 mRNA Translation: AAH72522.1
    PIRiA46627
    RefSeqiNP_113747.2, NM_031559.2
    XP_006230757.1, XM_006230695.2
    XP_017444326.1, XM_017588837.1

    3D structure databases

    SMRiP32198
    ModBaseiSearch...

    Protein-protein interaction databases

    CORUMiP32198
    IntActiP32198, 2 interactors
    MINTiP32198
    STRINGi10116.ENSRNOP00000019652

    Chemistry databases

    BindingDBiP32198
    ChEMBLiCHEMBL3858
    DrugCentraliP32198
    SwissLipidsiSLP:000000777

    PTM databases

    iPTMnetiP32198
    PhosphoSitePlusiP32198

    Proteomic databases

    jPOSTiP32198
    PaxDbiP32198
    PRIDEiP32198

    Genome annotation databases

    EnsembliENSRNOT00000019652; ENSRNOP00000019652; ENSRNOG00000014254
    GeneIDi25757
    KEGGirno:25757
    UCSCiRGD:2396, rat

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    1374
    RGDi2396, Cpt1a

    Phylogenomic databases

    eggNOGiKOG3716, Eukaryota
    GeneTreeiENSGT01030000234593
    HOGENOMiCLU_013513_2_1_1
    InParanoidiP32198
    OMAiASHMWEN
    OrthoDBi559299at2759
    PhylomeDBiP32198
    TreeFamiTF313836

    Enzyme and pathway databases

    UniPathwayiUPA00659
    BioCyciMetaCyc:MONOMER-14439
    BRENDAi2.3.1.21, 5301
    ReactomeiR-RNO-200425, Carnitine metabolism
    R-RNO-5362517, Signaling by Retinoic Acid
    SABIO-RKiP32198

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P32198

    Gene expression databases

    BgeeiENSRNOG00000014254, Expressed in liver and 21 other tissues
    GenevisibleiP32198, RN

    Family and domain databases

    Gene3Di3.30.559.40, 1 hit
    3.30.559.70, 1 hit
    InterProiView protein in InterPro
    IPR000542, Carn_acyl_trans
    IPR039551, Cho/carn_acyl_trans
    IPR042232, Cho/carn_acyl_trans_1
    IPR042231, Cho/carn_acyl_trans_2
    IPR032476, CPT_N
    PANTHERiPTHR22589, PTHR22589, 1 hit
    PfamiView protein in Pfam
    PF00755, Carn_acyltransf, 1 hit
    PF16484, CPT_N, 1 hit
    PROSITEiView protein in PROSITE
    PS00439, ACYLTRANSF_C_1, 1 hit
    PS00440, ACYLTRANSF_C_2, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCPT1A_RAT
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P32198
    Secondary accession number(s): P97780, Q6IMZ4
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: May 1, 2007
    Last modified: June 2, 2021
    This is version 169 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again