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Reviewed, UniProtKB/Swiss-Prot Q704S8 (CACP_RAT)

Last modified October 13, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 By similarity.

Catalytic activity

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

Subunit structure

Monomer By similarity.

Subcellular location

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

Tissue specificity

Expressed in flagella of epididymal sperm. Ref.3

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Carnitine O-acetyltransferase
PRO_0000210174

Regions

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

Sites

Active site3431Proton acceptor
Binding site4521Carnitine By similarity
Binding site4541Carnitine By similarity
Binding site4551Coenzyme A By similarity
Binding site4651Carnitine By similarity

Amino acid modifications

Modified residue2611N6-acetyllysine By similarity
Modified residue2681N6-acetyllysine By similarity

Experimental info

Mutagenesis3431H → A: Loss of enzyme activity. Ref.1
Mutagenesis3471E → A: Loss of enzyme activity. Ref.1
Mutagenesis5641M → A: Increases activity towards medium chain fatty acids. Ref.1
Mutagenesis5641M → G: Increases activity towards medium and long chain fatty acids. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q704S8-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 85B0D5DEF7EB0FF1

FASTA62670,801
        10         20         30         40         50         60 
MLAFAARTVV KPLGLLKPSS LMKVSGRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE 

        70         80         90        100        110        120 
EEWAHTKQLV DEFQTSGGVG ERLQKGLERR AKKMENWLSE WWLKTAYLQF RQPVVIYSSP 

       130        140        150        160        170        180 
GVLLPKQDFM DLQGQLRFAA KLIEGVLDFK SMIDNETLPV EFLGGQPLCM NQYYQILSSC 

       190        200        210        220        230        240 
RVPGLKQDSV VNFLKSKKPP THITVVHNYQ FFELDVYHSD GTPLTSDQIF VQLEKIWNSS 

       250        260        270        280        290        300 
LQSNKEPVGI LTSNHRNSWA KAYSSLIKDK VNRESVNSIQ KSIFTVCLDK QVPRVSDDVY 

       310        320        330        340        350        360 
RSHVAGQMLH GGGSKFNSGN RWFDKTLQFI VAEDGSCGMV YEHAAAEGPP IVALVDHVME 

       370        380        390        400        410        420 
YTKKPELVRS PMVPLPMPKK LRFNITPEIK NDIEKAKQNI SIMIQDLDIM MLVFHHFGKD 

       430        440        450        460        470        480 
FPKSQKLSPD AFIQIALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASTDSLAFVK 

       490        500        510        520        530        540 
GMDDPKVPEQ QRVELLRKAV QAHRAYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD 

       550        560        570        580        590        600 
TSYAIAMHFN LSTSQVPAKT DCVMSFGPVV PDGYGICYNP MEAHINFSVS AYNSCAETNA 

       610        620 
ARMAHYLEKA LLDMRTLLQN HPRAKL 

« Hide

References

« Hide 'large scale' references
[1]"Redesign of carnitine acetyltransferase specificity by protein engineering."
Cordente A.G., Lopez-Vinas E., Vazquez M.I., Swiegers J.H., Pretorius I.S., Gomez-Puertas P., Hegardt F.G., Asins G., Serra D.
J. Biol. Chem. 279:33899-33908(2004) [PubMed: 15155769] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF HIS-343; GLU-347 AND MET-564, 3D-STRUCTURE MODELING.
Strain: Sprague-Dawley.
Tissue: Testis.
[2]"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].
Tissue: Testis.
[3]"Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
Reproduction 138:81-93(2009) [PubMed: 19423663] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ620886 mRNA. Translation: CAF06525.1.
BC083616 mRNA. Translation: AAH83616.1.
IPIIPI00360158.
RefSeqNP_001004085.1.
UniGeneRn.6249

3D structure databases

SMRQ704S8. Positions 31-620.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ704S8.

Genome annotation databases

EnsemblENSRNOT00000024774; ENSRNOP00000024774; ENSRNOG00000018145; Rattus norvegicus. [Genome view]
GeneID311849.
KEGGrno:311849.
UCSCNM_001004085. rat.

Organism-specific databases

CTD311849.
RGD1303031. Crat.

Phylogenomic databases

HOVERGENQ704S8.

Enzyme and pathway databases

BRENDA2.3.1.7. 248.

Gene expression databases

ArrayExpressQ704S8.
GenevestigatorQ704S8.
GermOnlineENSRNOG00000018145. Rattus norvegicus.

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

NextBio664307.

Entry information

Entry nameCACP_RAT
AccessionPrimary (citable) accession number: Q704S8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: October 13, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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