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P52825

- CPT2_MOUSE

UniProt

P52825 - CPT2_MOUSE

Protein

Carnitine O-palmitoyltransferase 2, mitochondrial

Gene

Cpt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei372 – 3721Proton acceptorBy similarity
    Binding sitei486 – 4861CarnitineBy similarity
    Binding sitei488 – 4881CarnitineBy similarity
    Binding sitei499 – 4991CarnitineBy similarity

    GO - Molecular functioni

    1. carnitine O-palmitoyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid metabolic process Source: UniProtKB-KW
    2. transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Transport

    Enzyme and pathway databases

    ReactomeiREACT_198602. PPARA activates gene expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carnitine O-palmitoyltransferase 2, mitochondrial (EC:2.3.1.21)
    Alternative name(s):
    Carnitine palmitoyltransferase II
    Short name:
    CPT II
    Gene namesi
    Name:Cpt2
    Synonyms:Cpt-2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:109176. Cpt2.

    Subcellular locationi

    Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Matrix side By similarity

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI
    3. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2525MitochondrionBy similarityAdd
    BLAST
    Chaini26 – 658633Carnitine O-palmitoyltransferase 2, mitochondrialPRO_0000004426Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-succinyllysine1 Publication
    Modified residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei85 – 851N6-succinyllysine1 Publication
    Modified residuei239 – 2391N6-acetyllysine; alternate1 Publication
    Modified residuei239 – 2391N6-succinyllysine; alternate1 Publication
    Modified residuei305 – 3051N6-acetyllysine1 Publication
    Modified residuei418 – 4181N6-acetyllysine; alternate1 Publication
    Modified residuei418 – 4181N6-succinyllysine; alternate1 Publication
    Modified residuei424 – 4241N6-succinyllysine1 Publication
    Modified residuei439 – 4391N6-succinyllysine1 Publication
    Modified residuei510 – 5101N6-acetyllysine; alternate1 Publication
    Modified residuei510 – 5101N6-succinyllysine; alternate1 Publication
    Modified residuei544 – 5441N6-acetyllysine; alternate1 Publication
    Modified residuei544 – 5441N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP52825.
    PaxDbiP52825.
    PRIDEiP52825.

    PTM databases

    PhosphoSiteiP52825.

    Expressioni

    Gene expression databases

    ArrayExpressiP52825.
    BgeeiP52825.
    CleanExiMM_CPT2.
    GenevestigatoriP52825.

    Interactioni

    Protein-protein interaction databases

    IntActiP52825. 2 interactions.
    MINTiMINT-1845154.

    Structurei

    3D structure databases

    ProteinModelPortaliP52825.
    SMRiP52825. Positions 33-658.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 178153Mitochondrial matrixBy similarityAdd
    BLAST
    Topological domaini209 – 658450Mitochondrial matrixBy similarityAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei179 – 20830Note=Mitochondrial inner membraneBy similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni452 – 46413Coenzyme A bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG70127.
    GeneTreeiENSGT00550000074786.
    HOGENOMiHOG000007446.
    HOVERGENiHBG098001.
    InParanoidiQ3TFS0.
    KOiK08766.
    OMAiRCSEAFV.
    OrthoDBiEOG776SPG.
    TreeFamiTF315202.

    Family and domain databases

    InterProiIPR000542. Carn_acyl_trans.
    [Graphical view]
    PANTHERiPTHR22589. PTHR22589. 1 hit.
    PfamiPF00755. Carn_acyltransf. 1 hit.
    [Graphical view]
    PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P52825-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMPRLLLRDW PRCPSLVLGA PSRPLSAVSG PAEYLQHSIV PTMHYQDSLP    50
    RLPIPKLEDT MKRYLSAQKP LLNDSQFRKT EVLCKDFENG IGKELHAHLL 100
    AQDKQNKHTS YISGPWFDMY LTARDSVVLN FNPFMAFNPD PKSEYNDQLT 150
    RATNLTVSAV RFLKTLRAGL LEPEVFHLNP ARSDTDAFKR LIRFVPSSLS 200
    WYGAYLVNAY PLDMSQYFRL FNSTRIPKPS RDELFTDTKA RHLLVLRKGH 250
    FYVFDVLDQD GNIVNPSEIQ AHLKYILSDS SPVPEFPLAY LTSENRDVWA 300
    ELRQKLIHGG NEETLRKVDS AVFCLCLDDF PMKDLVHLSH TMLHGDGTNR 350
    WFDKSFNLIV AKDGTAAVHF EHAWGDGVAV LRFFNEVFRD STQTPAIAPQ 400
    SQPAATDSSV SVQKLSFKLS SALKAGVTAA KEKFDATMKT LTIDAIQFQR 450
    GGKEFLKKKK LSPDAVAQLA FQMAFLRQYG QTVATYESCS TAAFKHGRTE 500
    TIRPASIFTK RCSEAFVREP SKHSVGELQH MMAECSKYHG QLTKEAAMGQ 550
    GFDRHLFALR YLAAARGVTL PELYQDPAYQ RINHNILSTS TLSSPAVSLG 600
    GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDMFDA 650
    LEGKAIKT 658
    Length:658
    Mass (Da):73,981
    Last modified:July 27, 2011 - v2
    Checksum:i3A02DA887DF1D3A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti503 – 5031R → C in AAA18921. (PubMed:8307575)Curated
    Sequence conflicti503 – 5031R → C in AAA18922. (PubMed:8307575)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01170
    , 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.
    CCDSiCCDS18443.1.
    PIRiA49362.
    RefSeqiNP_034079.2. NM_009949.2.
    UniGeneiMm.307620.

    Genome annotation databases

    EnsembliENSMUST00000030345; ENSMUSP00000030345; ENSMUSG00000028607.
    GeneIDi12896.
    KEGGimmu:12896.
    UCSCiuc008uan.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01170
    , 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 .
    CCDSi CCDS18443.1.
    PIRi A49362.
    RefSeqi NP_034079.2. NM_009949.2.
    UniGenei Mm.307620.

    3D structure databases

    ProteinModelPortali P52825.
    SMRi P52825. Positions 33-658.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P52825. 2 interactions.
    MINTi MINT-1845154.

    PTM databases

    PhosphoSitei P52825.

    Proteomic databases

    MaxQBi P52825.
    PaxDbi P52825.
    PRIDEi P52825.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030345 ; ENSMUSP00000030345 ; ENSMUSG00000028607 .
    GeneIDi 12896.
    KEGGi mmu:12896.
    UCSCi uc008uan.2. mouse.

    Organism-specific databases

    CTDi 1376.
    MGIi MGI:109176. Cpt2.

    Phylogenomic databases

    eggNOGi NOG70127.
    GeneTreei ENSGT00550000074786.
    HOGENOMi HOG000007446.
    HOVERGENi HBG098001.
    InParanoidi Q3TFS0.
    KOi K08766.
    OMAi RCSEAFV.
    OrthoDBi EOG776SPG.
    TreeFami TF315202.

    Enzyme and pathway databases

    Reactomei REACT_198602. PPARA activates gene expression.

    Miscellaneous databases

    NextBioi 282510.
    PROi P52825.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52825.
    Bgeei P52825.
    CleanExi MM_CPT2.
    Genevestigatori P52825.

    Family and domain databases

    InterProi IPR000542. Carn_acyl_trans.
    [Graphical view ]
    PANTHERi PTHR22589. PTHR22589. 1 hit.
    Pfami PF00755. Carn_acyltransf. 1 hit.
    [Graphical view ]
    PROSITEi PS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiCPT2_MOUSE
    AccessioniPrimary (citable) accession number: P52825
    Secondary accession number(s): Q3TFS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3