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P52825 (CPT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carnitine O-palmitoyltransferase 2, mitochondrial

EC=2.3.1.21
Alternative name(s):
Carnitine palmitoyltransferase II
Short name=CPT II
Gene names
Name:Cpt2
Synonyms:Cpt-2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion By similarity
Chain26 – 658633Carnitine O-palmitoyltransferase 2, mitochondrial
PRO_0000004426

Regions

Topological domain26 – 178153Mitochondrial matrix By similarity
Intramembrane179 – 20830Note=Mitochondrial inner membrane; By similarity
Topological domain209 – 658450Mitochondrial matrix By similarity
Region452 – 46413Coenzyme A binding By similarity

Sites

Active site3721Proton acceptor By similarity
Binding site4861Carnitine By similarity
Binding site4881Carnitine By similarity
Binding site4991Carnitine By similarity

Amino acid modifications

Modified residue691N6-succinyllysine Ref.6
Modified residue791N6-acetyllysine Ref.7
Modified residue851N6-succinyllysine Ref.6
Modified residue2391N6-acetyllysine; alternate Ref.7
Modified residue2391N6-succinyllysine; alternate Ref.6
Modified residue3051N6-acetyllysine Ref.7
Modified residue4181N6-acetyllysine; alternate Ref.7
Modified residue4181N6-succinyllysine; alternate Ref.6
Modified residue4241N6-succinyllysine Ref.6
Modified residue4391N6-succinyllysine Ref.6
Modified residue5101N6-acetyllysine; alternate Ref.7
Modified residue5101N6-succinyllysine; alternate Ref.6
Modified residue5441N6-acetyllysine; alternate Ref.7
Modified residue5441N6-succinyllysine; alternate Ref.6

Experimental info

Sequence conflict5031R → C in AAA18921. Ref.1
Sequence conflict5031R → C in AAA18922. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52825 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 3A02DA887DF1D3A1

FASTA65873,981
        10         20         30         40         50         60 
MMPRLLLRDW PRCPSLVLGA PSRPLSAVSG PAEYLQHSIV PTMHYQDSLP RLPIPKLEDT 

        70         80         90        100        110        120 
MKRYLSAQKP LLNDSQFRKT EVLCKDFENG IGKELHAHLL AQDKQNKHTS YISGPWFDMY 

       130        140        150        160        170        180 
LTARDSVVLN FNPFMAFNPD PKSEYNDQLT RATNLTVSAV RFLKTLRAGL LEPEVFHLNP 

       190        200        210        220        230        240 
ARSDTDAFKR LIRFVPSSLS WYGAYLVNAY PLDMSQYFRL FNSTRIPKPS RDELFTDTKA 

       250        260        270        280        290        300 
RHLLVLRKGH FYVFDVLDQD GNIVNPSEIQ AHLKYILSDS SPVPEFPLAY LTSENRDVWA 

       310        320        330        340        350        360 
ELRQKLIHGG NEETLRKVDS AVFCLCLDDF PMKDLVHLSH TMLHGDGTNR WFDKSFNLIV 

       370        380        390        400        410        420 
AKDGTAAVHF EHAWGDGVAV LRFFNEVFRD STQTPAIAPQ SQPAATDSSV SVQKLSFKLS 

       430        440        450        460        470        480 
SALKAGVTAA KEKFDATMKT LTIDAIQFQR GGKEFLKKKK LSPDAVAQLA FQMAFLRQYG 

       490        500        510        520        530        540 
QTVATYESCS TAAFKHGRTE TIRPASIFTK RCSEAFVREP SKHSVGELQH MMAECSKYHG 

       550        560        570        580        590        600 
QLTKEAAMGQ GFDRHLFALR YLAAARGVTL PELYQDPAYQ RINHNILSTS TLSSPAVSLG 

       610        620        630        640        650 
GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDMFDA LEGKAIKT 

« Hide

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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., 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]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-85; LYS-239; LYS-418; LYS-424; LYS-439; LYS-510 AND LYS-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[7]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-239; LYS-305; LYS-418; LYS-510 AND LYS-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01170 expand/collapse EMBL AC list , U01166, U01167, U01168, 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.
PIRA49362.
RefSeqNP_034079.2. NM_009949.2.
UniGeneMm.307620.

3D structure databases

ProteinModelPortalP52825.
SMRP52825. Positions 33-658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP52825. 2 interactions.
MINTMINT-1845154.

PTM databases

PhosphoSiteP52825.

Proteomic databases

PaxDbP52825.
PRIDEP52825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030345; ENSMUSP00000030345; ENSMUSG00000028607.
GeneID12896.
KEGGmmu:12896.
UCSCuc008uan.2. mouse.

Organism-specific databases

CTD1376.
MGIMGI:109176. Cpt2.

Phylogenomic databases

eggNOGNOG70127.
GeneTreeENSGT00550000074786.
HOGENOMHOG000007446.
HOVERGENHBG098001.
InParanoidQ3TFS0.
KOK08766.
OMAYNDQLTR.
OrthoDBEOG776SPG.
TreeFamTF315202.

Gene expression databases

ArrayExpressP52825.
BgeeP52825.
CleanExMM_CPT2.
GenevestigatorP52825.

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

NextBio282510.
PROP52825.
SOURCESearch...

Entry information

Entry nameCPT2_MOUSE
AccessionPrimary (citable) accession number: P52825
Secondary accession number(s): Q3TFS0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot