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UniProtKB - P43155 (CACP_HUMAN)

Entry version 192 (12 Aug 2020)
Sequence version 5 (25 Nov 2008)
Previous versions | rss
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Protein

Carnitine O-acetyltransferase

Gene

CRAT

Organism
Homo sapiens (Human)
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 reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation (PubMed:15099582, PubMed:29395073). Responsible for the synthesis of short- and branched-chain acylcarnitines (PubMed:23485643). Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates (PubMed:23485643). Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates (PubMed:23485643).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 '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=240 µM for acetyl-CoA1 Publication
  2. KM=499 µM for butyryl-CoA1 Publication
  3. KM=590 µM for trans-2-butenoyl-CoA1 Publication
  1. Vmax=2.5 nmol/min/µg enzyme towards acetyl-CoA1 Publication
  2. Vmax=10.7 nmol/min/µg enzyme towards butyryl-CoA1 Publication
  3. Vmax=0.13 nmol/min/µg enzyme towards trans-2-butenoyl-CoA1 Publication
  1. KM=78 µM for acetyl-CoA1 Publication
  1. Vmax=4.4 nmol/min/µg enzyme towards acetyl-CoA1 Publication

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 sitei343Proton acceptorCurated1
<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 sitei419Coenzyme ABy similarity1
Binding sitei452Carnitine1 Publication1
Binding sitei454Carnitine1 Publication1
Binding sitei456Coenzyme A; via amide nitrogenBy similarity1
Binding sitei465Carnitine1 Publication1
Binding sitei504Coenzyme ABy similarity1
Binding sitei555Coenzyme A; via carbonyl oxygenBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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:HS01816-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.7, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P43155

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-389887, Beta-oxidation of pristanoyl-CoA
R-HSA-9033241, Peroxisomal protein import

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P43155

Protein family/group databases

Transport Classification Database

More...TCDBi		4.C.2.1.1, the carnitine o-acyl transferase (crat) family

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001053
SLP:000001057 [P43155-1]
SLP:000001058 [P43155-2]

<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-acetyltransferaseCurated (EC:2.3.1.1371 Publication, EC:2.3.1.72 Publications)
Short name:
Carnitine acetylase
Alternative name(s):
Carnitine acetyltransferase
Short name:
CAT
Short name:
CrAT1 Publication
<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:CRATImported
Synonyms:CAT1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000095321.16

Human Gene Nomenclature Database

More...HGNCi		HGNC:2342, CRAT

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600184, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P43155

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Peroxisome

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Neurodegeneration with brain iron accumulation 8 (NBIA8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder associated with iron accumulation, primarily in the basal ganglia. Disease onset is in early childhood. Clinical features include speech delay, progressive cerebellar ataxia, unbalanced gait, and loss of ambulation. NBIA8 transmission pattern is consistent with autosomal recessive inheritance.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080636321R → H in NBIA8; unknown pathological significance; loss of expression at the protein level and drastic decrease in beta-oxidation of palmitate in homozygous patient's primary fibroblasts as compared to wild-type cells; primary fibroblasts from a homozygous patient show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface. 1 PublicationCorresponds to variant dbSNP:rs138665095EnsemblClinVar.1

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>Mutagenesisi452Y → A: Increases the KM for carnitine 100-fold. 1 Publication1
Mutagenesisi452Y → F: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold. 1 Publication1
Mutagenesisi465T → A: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold. 1 Publication1
Mutagenesisi518R → Q: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold. 1 Publication1
Mutagenesisi566F → A: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold. 1 Publication1
Mutagenesisi566F → Y: No effect. 1 Publication1

Keywords - Diseasei

Neurodegeneration

Organism-specific databases

DisGeNET

More...DisGeNETi		1384

MalaCards human disease database

More...MalaCardsi		CRAT
MIMi617917, phenotype

Open Targets

More...OpenTargetsi		ENSG00000095321

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26862

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P43155, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3184

Drug and drug target database

More...DrugBanki		DB02648, (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium
DB01992, Coenzyme A
DB00583, Levocarnitine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CRAT

Domain mapping of disease mutations (DMDM)

More...DMDMi		215274265

<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 '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_00002101721 – 626Carnitine O-acetyltransferaseAdd BLAST626

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 residuei93N6-succinyllysineBy similarity1
Modified residuei261N6-acetyllysine; alternateCombined sources1
Modified residuei261N6-succinyllysine; alternateBy similarity1
Modified residuei268N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-341
CPTAC-342

Encyclopedia of Proteome Dynamics

More...EPDi		P43155

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P43155

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P43155

MaxQB - The MaxQuant DataBase

More...MaxQBi		P43155

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

More...PaxDbi		P43155

PeptideAtlas

More...PeptideAtlasi		P43155

PRoteomics IDEntifications database

More...PRIDEi		P43155

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55592 [P43155-1]
55593 [P43155-2]
55594 [P43155-3]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1073, 4 N-Linked glycans (2 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P43155, 2 sites, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P43155

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

More...PhosphoSitePlusi		P43155

<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

Mostly in skeletal muscle, less in heart, liver and pancreas, only weakly detectable in brain, placenta, lung and kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000095321, Expressed in sperm and 243 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P43155, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P43155, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000095321, Tissue enhanced (skeletal muscle, testis)

<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

Monomer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107774, 10 interactors

Protein interaction database and analysis system

More...IntActi		P43155, 15 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000315013

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P43155

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P43155, protein

<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

Secondary structure

1626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P43155

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P43155

<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>Regioni423 – 430Coenzyme A bindingBy similarity8

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi624 – 626Microbody targeting signalSequence analysis3

<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

Belongs to the carnitine/choline acetyltransferase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3717, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00960000186627

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_013513_5_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P43155

Identification of Orthologs from Complete Genome Data

More...OMAi		NWIYEWW

Database of Orthologous Groups

More...OrthoDBi		559299at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P43155

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

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

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>Sequences (3+)i

<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.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P43155-1) [UniParc]FASTAAdd to basket
Also known as: SM-1400

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY 
        60         70         80         90        100
LKALQPIVSE EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE 
       110        120        130        140        150
WWLKTAYLQY RQPVVIYSSP GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK 
       160        170        180        190        200
VMIDNETLPV EYLGGKPLCM NQYYQILSSC RVPGPKQDTV SNFSKTKKPP 
       210        220        230        240        250
THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS LQTNKEPVGI 
       260        270        280        290        300
LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY 
       310        320        330        340        350
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP 
       360        370        380        390        400
IVTLLDYVIE YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL 
       410        420        430        440        450
SIMIQDLDIT VMVFHHFGKD FPKSEKLSPD AFIQMALQLA YYRIYGQACA 
       460        470        480        490        500
TYESASLRMF HLGRTDTIRS ASMDSLTFVK AMDDSSVTEH QKVELLRKAV 
       510        520        530        540        550
QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD TSYAIAMHFH 
       560        570        580        590        600
LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA 
       610        620 
ARLAHYLEKA LLDMRALLQS HPRAKL
Length:626
Mass (Da):70,858
Last modified:November 25, 2008 - v5
<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:i51B65E7C94E458D7
GO
Isoform 2 (identifier: P43155-2) [UniParc]FASTAAdd to basket
Also known as: SM-1200

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Show »
Length:605
Mass (Da):68,569
Checksum:i915540218D46D9C7
GO
Isoform 3 (identifier: P43155-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     282-363: Missing.

Show »
Length:544
Mass (Da):61,870
Checksum:i2AD5B9AA49773E5C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C0E1H7C0E1_HUMAN
Carnitine O-acetyltransferase
CRAT
31Annotation score:

Annotation score:1 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>
A6PVN3A6PVN3_HUMAN
Carnitine O-acetyltransferase
CRAT
161Annotation score:

Annotation score:1 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>
B7ZBP5B7ZBP5_HUMAN
Carnitine O-acetyltransferase
CRAT
98Annotation score:

Annotation score:1 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>
H0Y4Z7H0Y4Z7_HUMAN
Carnitine O-acetyltransferase
CRAT
201Annotation score:

Annotation score:1 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>
F2Z2C5F2Z2C5_HUMAN
Carnitine O-acetyltransferase
CRAT
40Annotation score:

Annotation score:1 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 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 conflicti88E → G in CAA55359 (PubMed:7829107).Curated1
Sequence conflicti349P → F in CAA55359 (PubMed:7829107).Curated1
Sequence conflicti517D → G in CAA55359 (PubMed:7829107).Curated1
Sequence conflicti534M → T in CAA55359 (PubMed:7829107).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_080636321R → H in NBIA8; unknown pathological significance; loss of expression at the protein level and drastic decrease in beta-oxidation of palmitate in homozygous patient's primary fibroblasts as compared to wild-type cells; primary fibroblasts from a homozygous patient show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface. 1 PublicationCorresponds to variant dbSNP:rs138665095EnsemblClinVar.1
Natural variantiVAR_047780372L → M3 PublicationsCorresponds to variant dbSNP:rs3118635Ensembl.1
Natural variantiVAR_047781624A → P. Corresponds to variant dbSNP:rs17459086Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0007921 – 21Missing in isoform 2. CuratedAdd BLAST21
Alternative sequenceiVSP_012798282 – 363Missing in isoform 3. 2 PublicationsAdd BLAST82

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
BT006801 mRNA Translation: AAP35447.1
AL158151 Genomic DNA No translation available.
BC000723 mRNA Translation: AAH00723.1
X79825 Genomic DNA No translation available.
X79827 Genomic DNA No translation available.
X78706 mRNA Translation: CAA55359.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS6919.1 [P43155-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A55720

NCBI Reference Sequences

More...RefSeqi		XP_005251765.1, XM_005251708.3 [P43155-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000318080; ENSP00000315013; ENSG00000095321 [P43155-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1384

UCSC genome browser

More...UCSCi		uc004bxh.4, human [P43155-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
BT006801 mRNA Translation: AAP35447.1
AL158151 Genomic DNA No translation available.
BC000723 mRNA Translation: AAH00723.1
X79825 Genomic DNA No translation available.
X79827 Genomic DNA No translation available.
X78706 mRNA Translation: CAA55359.1
CCDSiCCDS6919.1 [P43155-1]
PIRiA55720
RefSeqiXP_005251765.1, XM_005251708.3 [P43155-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NM8X-ray1.60A35-626[»]
1S5OX-ray1.80A35-626[»]
SMRiP43155
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107774, 10 interactors
IntActiP43155, 15 interactors
STRINGi9606.ENSP00000315013

Chemistry databases

BindingDBiP43155
ChEMBLiCHEMBL3184
DrugBankiDB02648, (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium
DB01992, Coenzyme A
DB00583, Levocarnitine
SwissLipidsiSLP:000001053
SLP:000001057 [P43155-1]
SLP:000001058 [P43155-2]

Protein family/group databases

TCDBi4.C.2.1.1, the carnitine o-acyl transferase (crat) family

PTM databases

GlyConnecti1073, 4 N-Linked glycans (2 sites)
GlyGeniP43155, 2 sites, 1 N-linked glycan (1 site)
iPTMnetiP43155
PhosphoSitePlusiP43155

Polymorphism and mutation databases

BioMutaiCRAT
DMDMi215274265

Proteomic databases

CPTACiCPTAC-341
CPTAC-342
EPDiP43155
jPOSTiP43155
MassIVEiP43155
MaxQBiP43155
PaxDbiP43155
PeptideAtlasiP43155
PRIDEiP43155
ProteomicsDBi55592 [P43155-1]
55593 [P43155-2]
55594 [P43155-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		17825, 220 antibodies

The DNASU plasmid repository

More...DNASUi		1384

Genome annotation databases

EnsembliENST00000318080; ENSP00000315013; ENSG00000095321 [P43155-1]
GeneIDi1384
UCSCiuc004bxh.4, human [P43155-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1384
DisGeNETi1384
EuPathDBiHostDB:ENSG00000095321.16

GeneCards: human genes, protein and diseases

More...GeneCardsi		CRAT
HGNCiHGNC:2342, CRAT
HPAiENSG00000095321, Tissue enhanced (skeletal muscle, testis)
MalaCardsiCRAT
MIMi600184, gene
617917, phenotype
neXtProtiNX_P43155
OpenTargetsiENSG00000095321
PharmGKBiPA26862

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3717, Eukaryota
GeneTreeiENSGT00960000186627
HOGENOMiCLU_013513_5_0_1
InParanoidiP43155
OMAiNWIYEWW
OrthoDBi559299at2759
PhylomeDBiP43155
TreeFamiTF313836

Enzyme and pathway databases

BioCyciMetaCyc:HS01816-MONOMER
BRENDAi2.3.1.7, 2681
PathwayCommonsiP43155
ReactomeiR-HSA-389887, Beta-oxidation of pristanoyl-CoA
R-HSA-9033241, Peroxisomal protein import
SABIO-RKiP43155

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		1384, 5 hits in 869 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CRAT, human
EvolutionaryTraceiP43155

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CRAT_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1384
PharosiP43155, Tbio

Protein Ontology

More...PROi		PR:P43155
RNActiP43155, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000095321, Expressed in sperm and 243 other tissues
ExpressionAtlasiP43155, baseline and differential
GenevisibleiP43155, HS

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
PANTHERiPTHR22589, PTHR22589, 1 hit
PfamiView protein in Pfam
PF00755, Carn_acyltransf, 1 hit
PROSITEiView protein in PROSITE
PS00439, ACYLTRANSF_C_1, 1 hit
PS00440, ACYLTRANSF_C_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiCACP_HUMAN
<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: P43155
Secondary accession number(s): Q5T952, Q9BW16
<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: November 1, 1995
Last sequence update: November 25, 2008
Last modified: August 12, 2020
This is version 192 of the entry and version 5 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
  6. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
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