P52825 (CPT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 90.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Carnitine O-palmitoyltransferase 2, mitochondrial EC=2.3.1.21 Alternative name(s): Carnitine palmitoyltransferase II Short name=CPT II | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 658 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine. |
| Subcellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity. |
| Sequence similarities | Belongs to the carnitine/choline acetyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism Transport |
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Domain | Transit peptide |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrionInferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI nucleolusInferred from electronic annotation. Source: Compara |
| Molecular_function | carnitine O-palmitoyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 25 | 25 | Mitochondrion By similarity | ||||||
| Chain | 26 – 658 | 633 | Carnitine O-palmitoyltransferase 2, mitochondrial | PRO_0000004426 | |||||
Regions | |||||||||
| Topological domain | 26 – 178 | 153 | Mitochondrial matrix By similarity | ||||||
| Intramembrane | 179 – 208 | 30 | Note=Mitochondrial inner membrane; By similarity | ||||||
| Topological domain | 209 – 658 | 450 | Mitochondrial matrix By similarity | ||||||
| Region | 452 – 464 | 13 | Coenzyme A binding By similarity | ||||||
Sites | |||||||||
| Active site | 372 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 486 | 1 | Carnitine By similarity | ||||||
| Binding site | 488 | 1 | Carnitine By similarity | ||||||
| Binding site | 499 | 1 | Carnitine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 544 | 1 | N6-acetyllysine Ref.6 | ||||||
Experimental info | |||||||||
| Sequence conflict | 503 | 1 | R → C in AAA18921. Ref.1 | ||||||
| Sequence conflict | 503 | 1 | R → C in AAA18922. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genomic structure of and a cardiac promoter for the mouse carnitine palmitoyltransferase II gene." Gelb B.D. Genomics 18:651-655(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: 129/Sv. |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Stomach. |
| [3] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [4] | Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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]. |
| [6] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-544, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U01170 U01169 Unassigned DNA. Translation: AAA18922.1.U01163 mRNA. Translation: AAA18921.1. AK169038 mRNA. Translation: BAE40828.1. AL611936 Genomic DNA. Translation: CAM23589.1. CH466527 Genomic DNA. Translation: EDL30761.1. BC138514 mRNA. Translation: AAI38515.1. BC145859 mRNA. Translation: AAI45860.1. |
| IPI | IPI00131424. |
| PIR | A49362. |
| RefSeq | NP_034079.2. NM_009949.2. |
| UniGene | Mm.307620. |
3D structure databases | |
| ProteinModelPortal | P52825. |
| SMR | P52825. Positions 33-658. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P52825. |
Proteomic databases | |
| PaxDb | P52825. |
| PRIDE | P52825. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000030345; ENSMUSP00000030345; ENSMUSG00000028607. |
| GeneID | 12896. |
| KEGG | mmu:12896. |
Organism-specific databases | |
| CTD | 1376. |
| MGI | MGI:109176. Cpt2. |
Phylogenomic databases | |
| eggNOG | NOG70127. |
| GeneTree | ENSGT00550000074786. |
| HOGENOM | HOG000007446. |
| HOVERGEN | HBG098001. |
| InParanoid | Q3TFS0. |
| KO | K08766. |
| OMA | YNDQLTR. |
| OrthoDB | EOG4WM4TB. |
Gene expression databases | |
| ArrayExpress | P52825. |
| Bgee | P52825. |
| CleanEx | MM_CPT2. |
| Genevestigator | P52825. |
| GermOnline | ENSMUSG00000028607. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000542. Carn_acyl_trans. [Graphical view] |
| PANTHER | PTHR22589. PTHR22589. 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 | |
| NextBio | 282510. |
| SOURCE | Search... |
Entry information
| Entry name | CPT2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P52825 Secondary accession number(s): Q3TFS0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
