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P43155 (CACP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carnitine O-acetyltransferase

Short name=Carnitine acetylase
EC=2.3.1.7
Alternative name(s):
Carnitine acetyltransferase
Short name=CAT
Short name=CrAT
Gene names
Name:CRAT
Synonyms:CAT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.

Catalytic activity

Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.

Subunit structure

Monomer. Ref.7

Subcellular location

Endoplasmic reticulum Potential. Peroxisome Potential. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Potential.

Isoform 1: Mitochondrion Potential.

Isoform 2: Peroxisome Potential.

Tissue specificity

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

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion inner membrane
Peroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarnitine metabolic process, CoA-linked

Inferred from direct assay Ref.8PubMed 2351134. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation using acyl-CoA oxidase

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 2351134. Source: UniProtKB

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisome

Inferred from direct assay PubMed 2351134. Source: UniProtKB

   Molecular_functioncarnitine O-acetyltransferase activity

Inferred from direct assay Ref.8PubMed 2351134. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43155-1)

Also known as: SM-1400;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P43155-2)

Also known as: SM-1200;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P43155-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Carnitine O-acetyltransferase
PRO_0000210172

Regions

Region423 – 4308Coenzyme A binding By similarity
Motif624 – 6263Microbody targeting signal Potential

Sites

Active site3431Proton acceptor Probable
Binding site4191Coenzyme A By similarity
Binding site4521Carnitine
Binding site4541Carnitine
Binding site4561Coenzyme A; via amide nitrogen By similarity
Binding site4651Carnitine
Binding site5041Coenzyme A By similarity
Binding site5551Coenzyme A; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue931N6-succinyllysine By similarity
Modified residue2611N6-acetyllysine; alternate Ref.6
Modified residue2611N6-succinyllysine; alternate By similarity
Modified residue2681N6-acetyllysine Ref.6

Natural variations

Alternative sequence1 – 2121Missing in isoform 2.
VSP_000792
Alternative sequence282 – 36382Missing in isoform 3.
VSP_012798
Natural variant3721L → M. Ref.1 Ref.3 Ref.5
Corresponds to variant rs3118635 [ dbSNP | Ensembl ].
VAR_047780
Natural variant6241A → P.
Corresponds to variant rs17459086 [ dbSNP | Ensembl ].
VAR_047781

Experimental info

Mutagenesis4521Y → A: Increases the KM for carnitine 100-fold. Ref.8
Mutagenesis4521Y → F: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold. Ref.8
Mutagenesis4651T → A: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold. Ref.8
Mutagenesis5181R → Q: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold. Ref.8
Mutagenesis5661F → A: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold. Ref.8
Mutagenesis5661F → Y: No effect. Ref.8
Sequence conflict881E → G in CAA55359. Ref.5
Sequence conflict3491P → F in CAA55359. Ref.5
Sequence conflict5171D → G in CAA55359. Ref.5
Sequence conflict5341M → T in CAA55359. Ref.5

Secondary structure

........................................................................................ 626
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SM-1400) [UniParc].

Last modified November 25, 2008. Version 5.
Checksum: 51B65E7C94E458D7

FASTA62670,858
        10         20         30         40         50         60 
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE 

        70         80         90        100        110        120 
EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP 

       130        140        150        160        170        180 
GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC 

       190        200        210        220        230        240 
RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS 

       250        260        270        280        290        300 
LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY 

       310        320        330        340        350        360 
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP IVTLLDYVIE 

       370        380        390        400        410        420 
YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD 

       430        440        450        460        470        480 
FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK 

       490        500        510        520        530        540 
AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD 

       550        560        570        580        590        600 
TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA 

       610        620 
ARLAHYLEKA LLDMRALLQS HPRAKL 

« Hide

Isoform 2 (SM-1200) [UniParc].

Checksum: 915540218D46D9C7
Show »

FASTA60568,569
Isoform 3 [UniParc].

Checksum: 2AD5B9AA49773E5C
Show »

FASTA54461,870

References

« Hide 'large scale' references
[1]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT MET-372.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT MET-372.
Tissue: Placenta.
[4]"Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations."
Corti O., DiDonato S., Finocchiaro G.
Biochem. J. 303:37-41(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
[5]"Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1."
Corti O., Finocchiaro G., Rossi E., Zuffardi O., Didonato S.
Genomics 23:94-99(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-626 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT MET-372.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261 AND LYS-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer."
Wu D., Govindasamy L., Lian W., Gu Y., Kukar T., Agbandje-McKenna M., McKenna R.
J. Biol. Chem. 278:13159-13165(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 35-626, SUBUNIT.
[8]"Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase."
Govindasamy L., Kukar T., Lian W., Pedersen B., Gu Y., Agbandje-McKenna M., Jin S., McKenna R., Wu D.
J. Struct. Biol. 146:416-424(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 35-626 IN COMPLEX WITH CARNITINE, MUTAGENESIS OF TYR-452; THR-465; ARG-518 AND PHE-566.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT006801 mRNA. Translation: AAP35447.1.
AL158151 Genomic DNA. Translation: CAI12869.1.
BC000723 mRNA. Translation: AAH00723.1.
X79825 Genomic DNA. No translation available.
X79827 Genomic DNA. No translation available.
X78706 mRNA. Translation: CAA55359.1.
CCDSCCDS6919.1. [P43155-1]
PIRA55720.
RefSeqNP_000746.2. NM_000755.3.
NP_001244292.1. NM_001257363.1.
XP_005251765.1. XM_005251708.1. [P43155-2]
XP_005251766.1. XM_005251709.2. [P43155-2]
UniGeneHs.12068.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NM8X-ray1.60A35-626[»]
1S5OX-ray1.80A35-626[»]
DisProtDP00305.
ProteinModelPortalP43155.
SMRP43155. Positions 31-620.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107774. 1 interaction.
IntActP43155. 3 interactions.
STRING9606.ENSP00000315013.

Chemistry

BindingDBP43155.
ChEMBLCHEMBL3184.
DrugBankDB00583. L-Carnitine.

Protein family/group databases

TCDB4.C.2.1.1. the carnitine o-acyl transferase (crat) family.

PTM databases

PhosphoSiteP43155.

Polymorphism databases

DMDM215274265.

Proteomic databases

MaxQBP43155.
PaxDbP43155.
PRIDEP43155.

Protocols and materials databases

DNASU1384.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318080; ENSP00000315013; ENSG00000095321. [P43155-1]
GeneID1384.
KEGGhsa:1384.
UCSCuc004bxh.3. human. [P43155-1]

Organism-specific databases

CTD1384.
GeneCardsGC09M131857.
H-InvDBHIX0169130.
HGNCHGNC:2342. CRAT.
HPAHPA019230.
HPA020260.
HPA022815.
MIM600184. gene.
neXtProtNX_P43155.
PharmGKBPA26862.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70127.
HOGENOMHOG000233845.
HOVERGENHBG107717.
InParanoidP43155.
KOK00624.
OMAYLERALL.
OrthoDBEOG7WHH90.
PhylomeDBP43155.
TreeFamTF313836.

Enzyme and pathway databases

BioCycMetaCyc:HS01816-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP43155.

Gene expression databases

ArrayExpressP43155.
BgeeP43155.
CleanExHS_CRAT.
GenevestigatorP43155.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. PTHR22589. 1 hit.
PfamPF00755. Carn_acyltransf. 1 hit.
[Graphical view]
PROSITEPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43155.
GeneWikiCRAT_(gene).
GenomeRNAi1384.
NextBio5619.
PROP43155.
SOURCESearch...

Entry information

Entry nameCACP_HUMAN
AccessionPrimary (citable) accession number: P43155
Secondary accession number(s): Q5T952, Q9BW16
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 143 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM