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Reviewed, UniProtKB/Swiss-Prot P43155 (CACP_HUMAN)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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=CrAT
      Short name=CAT
Gene names
Name: CRAT
Synonyms: CAT1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.6

Subcellular location

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

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.
Note: May be mitochondrial.
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: May be peroxisomal. 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

Region418 – 43013Coenzyme A binding By similarity
Motif624 – 6263Microbody targeting signal Potential

Sites

Active site3431Proton acceptor Probable
Binding site4521Carnitine
Binding site4541Carnitine
Binding site4651Carnitine

Natural variations

Alternative sequence1 – 2121Missing in isoform 2.
VSP_000792
Alternative sequence282 – 36382Missing in isoform 3.
VSP_012798
Natural variant3721L → M: dbSNP rs3118635. Ref.1 Ref.3 Ref.5
VAR_047780
Natural variant6241A → P: dbSNP rs17459086.
VAR_047781

Experimental info

Mutagenesis4521Y → A: Increases the KM for carnitine 100-fold. Ref.7
Mutagenesis4521Y → F: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold. Ref.7
Mutagenesis4651T → A: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold. Ref.7
Mutagenesis5181R → Q: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold. Ref.7
Mutagenesis5661F → A: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold. Ref.7
Mutagenesis5661F → Y: No effect. Ref.7
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).

Checksum: 915540218D46D9C7
Show »

FASTA60568,569
Isoform 3.

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: 15164053] [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: 15489334] [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: 7945262] [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: 7829107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-626 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT MET-372.
[6]"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: 12562770] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 35-626, SUBUNIT.
[7]"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: 15099582] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00016457.
IPI00029140.
IPI00514595.
PIRA55720.
RefSeqNP_000746.2.
NP_003994.2.
UniGeneHs.12068

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1NM8X-ray1.60A35-626[»]
1S5OX-ray1.80A35-626[»]
DisProtDP00305.
ModBaseSearch...

Protein family/group databases

TCDB4.C.2.1.1. carnitine O-acyl transferase (CrAT) family.

Proteomic databases

PRIDEP43155.

Genome annotation databases

EnsemblENSG00000095321. Homo sapiens. [Contig view]
GeneID1384.
KEGGhsa:1384.

Organism-specific databases

GeneCardsGC09M130896.
H-InvDBHIX0008446.
HGNCHGNC:2342. CRAT.
MIM600184. gene.
PharmGKBPA26862.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP43155.
HOVERGENP43155.
OMAP43155. FFELDVY.

Enzyme and pathway databases

BRENDA2.3.1.7. 247.

Gene expression databases

ArrayExpressP43155.
BgeeP43155.
CleanExHS_CRAT.
GermOnlineENSG00000095321. Homo sapiens.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. Carn_acyl_trans. 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 Resources

DrugBankDB00583. L-Carnitine.
NextBio5619.
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: June 16, 2009
This is version 89 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 9

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents