Reviewed,
UniProtKB/Swiss-Prot Q704S8 (CACP_RAT)
Last modified
February 9, 2010.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 626 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. Ref.1 |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism Transport |
| Cellular component | Endoplasmic reticulum Membrane Mitochondrion Mitochondrion inner membrane Peroxisome |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological process | fatty acid metabolic process Ref.1 Inferred from direct assay. Source: RGD transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Ref.1 Traceable author statement. Source: RGD extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membraneInferred from electronic annotation. Source: UniProtKB-KW peroxisome Ref.1Traceable author statement. Source: RGD |
| Molecular function | carnitine O-acetyltransferase activity Ref.1 Inferred from direct assay. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 626 | 626 | Carnitine O-acetyltransferase | PRO_0000210174 | |||||
Regions | |||||||||
| Region | 418 – 430 | 13 | Coenzyme A binding By similarity | ||||||
| Motif | 624 – 626 | 3 | Microbody targeting signal Potential | ||||||
Sites | |||||||||
| Active site | 343 | 1 | Proton acceptor | ||||||
| Binding site | 452 | 1 | Carnitine By similarity | ||||||
| Binding site | 454 | 1 | Carnitine By similarity | ||||||
| Binding site | 455 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 465 | 1 | Carnitine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 261 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 268 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 343 | 1 | H → A: Loss of enzyme activity. Ref.1 | ||||||
| Mutagenesis | 347 | 1 | E → A: Loss of enzyme activity. Ref.1 | ||||||
| Mutagenesis | 564 | 1 | M → A: Increases activity towards medium chain fatty acids. Ref.1 | ||||||
| Mutagenesis | 564 | 1 | M → G: Increases activity towards medium and long chain fatty acids. Ref.1 | ||||||
Sequences
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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 | |
|---|---|
| EMBL GenBank DDBJ | AJ620886 mRNA. Translation: CAF06525.1. BC083616 mRNA. Translation: AAH83616.1. |
| IPI | IPI00949645. |
| RefSeq | NP_001004085.1. |
| UniGene | Rn.6249 |
3D structure databases | |
| SMR | Q704S8. Positions 30-625. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q704S8. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000065128; ENSRNOP00000063089; ENSRNOG00000018145; Rattus norvegicus. [Genome view] |
| GeneID | 311849. |
| KEGG | rno:311849. |
| UCSC | NM_001004085. rat. |
Organism-specific databases | |
| CTD | 311849. |
| RGD | 1303031. Crat. |
Phylogenomic databases | |
| eggNOG | roNOG07896. |
| HOVERGEN | Q704S8. |
| InParanoid | Q704S8. |
| PhylomeDB | Q704S8. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-14440. |
| BRENDA | 2.3.1.7. 248. |
Gene expression databases | |
| ArrayExpress | Q704S8. |
| Genevestigator | Q704S8. |
| GermOnline | ENSRNOG00000018145. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000542. Carn_acyl_trans. [Graphical view] |
| PANTHER | PTHR22589. Carn_acyl_trans. 1 hit. |
| Pfam | PF00755. Carn_acyltransf. 1 hit. [Graphical view] |
| PROSITE | PS00439. ACYLTRANSF_C_1. 1 hit. PS00440. ACYLTRANSF_C_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 664307. |
Entry information
| Entry name | CACP_RAT | ||||||||
| Accession | Primary (citable) accession number: Q704S8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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