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P18886

- CPT2_RAT

UniProt

P18886 - CPT2_RAT

Protein

Carnitine O-palmitoyltransferase 2, mitochondrial

Gene

Cpt2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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 acceptor
    Binding sitei486 – 4861Carnitine
    Binding sitei488 – 4881Carnitine
    Binding sitei499 – 4991Carnitine

    GO - Molecular functioni

    1. carnitine O-palmitoyltransferase activity Source: RGD

    GO - Biological processi

    1. fatty acid beta-oxidation Source: RGD
    2. long-chain fatty acid transport Source: RGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14441.
    SABIO-RKP18886.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2398. Cpt2.

    Subcellular locationi

    Mitochondrion inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Matrix side 1 Publication

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB-SubCell
    2. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2525MitochondrionAdd
    BLAST
    Chaini26 – 658633Carnitine O-palmitoyltransferase 2, mitochondrialPRO_0000004427Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-succinyllysineBy similarity
    Modified residuei85 – 851N6-succinyllysineBy similarity
    Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
    Modified residuei305 – 3051N6-acetyllysineBy similarity
    Modified residuei424 – 4241N6-succinyllysineBy similarity
    Modified residuei439 – 4391N6-succinyllysineBy similarity
    Modified residuei510 – 5101N6-acetyllysine; alternateBy similarity
    Modified residuei510 – 5101N6-succinyllysine; alternateBy similarity
    Modified residuei544 – 5441N6-acetyllysine; alternateBy similarity
    Modified residuei544 – 5441N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP18886.
    PRIDEiP18886.

    Expressioni

    Gene expression databases

    GenevestigatoriP18886.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000016954.

    Structurei

    Secondary structure

    1
    658
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni42 – 454
    Helixi46 – 483
    Helixi57 – 6812
    Turni69 – 713
    Helixi74 – 8916
    Helixi91 – 10515
    Turni106 – 1083
    Helixi113 – 12210
    Turni128 – 1314
    Beta strandi134 – 1374
    Helixi143 – 1464
    Helixi148 – 16720
    Beta strandi175 – 1784
    Helixi180 – 1834
    Helixi186 – 1927
    Turni197 – 1993
    Helixi200 – 2067
    Beta strandi209 – 2113
    Helixi217 – 2204
    Beta strandi221 – 2266
    Beta strandi229 – 2313
    Beta strandi233 – 2364
    Beta strandi242 – 2476
    Beta strandi250 – 2578
    Helixi266 – 27813
    Helixi288 – 2936
    Helixi296 – 30813
    Turni309 – 3113
    Helixi312 – 3209
    Beta strandi324 – 3274
    Helixi335 – 3439
    Turni344 – 3463
    Beta strandi347 – 3493
    Beta strandi354 – 3607
    Beta strandi366 – 3705
    Beta strandi372 – 3743
    Helixi378 – 39316
    Helixi408 – 4114
    Beta strandi412 – 4143
    Helixi421 – 43818
    Beta strandi442 – 4487
    Helixi453 – 4586
    Helixi463 – 47917
    Beta strandi485 – 4906
    Beta strandi499 – 5024
    Helixi507 – 51711
    Helixi520 – 5223
    Helixi525 – 54723
    Helixi553 – 56513
    Helixi572 – 5754
    Helixi577 – 5826
    Beta strandi586 – 5916
    Beta strandi597 – 6015
    Beta strandi610 – 6167
    Beta strandi621 – 6277
    Beta strandi629 – 6313
    Helixi633 – 65119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DEBX-ray1.60A/B27-658[»]
    2FW3X-ray2.50A27-658[»]
    2FYOX-ray2.00A27-658[»]
    2H4TX-ray1.90A/B32-656[»]
    2RCUX-ray1.78A/B27-658[»]
    4EP9X-ray2.03A27-658[»]
    4EPHX-ray2.30A27-658[»]
    4EYWX-ray1.88A/B27-658[»]
    ProteinModelPortaliP18886.
    SMRiP18886. Positions 32-658.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18886.

    Topological domain

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

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei179 – 20830Note=Mitochondrial inner membraneAdd
    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.
    HOGENOMiHOG000007446.
    HOVERGENiHBG098001.
    InParanoidiP18886.
    KOiK08766.
    PhylomeDBiP18886.

    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.

    P18886-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMPRLLFRAW PRCPSLVLGA PSRPLSAVSG PDDYLQHSIV PTMHYQDSLP    50
    RLPIPKLEDT MKRYLNAQKP LLDDSQFRRT EALCKNFETG VGKELHAHLL 100
    AQDKQNKHTS YISGPWFDMY LTARDSIVLN FNPFMAFNPD PKSEYNDQLT 150
    RATNLTVSAV RFLKTLQAGL LEPEVFHLNP SKSDTDAFKR LIRFVPPSLS 200
    WYGAYLVNAY PLDMSQYFRL FNSTRIPRPN RDELFTDTKA RHLLVLRKGH 250
    FYVFDVLDQD GNIVNPLEIQ AHLKYILSDS SPVPEFPVAY LTSENRDVWA 300
    ELRQKLIFDG NEETLKKVDS AVFCLCLDDF PMKDLIHLSH TMLHGDGTNR 350
    WFDKSFNLIV AEDGTAAVHF EHSWGDGVAV LRFFNEVFRD STQTPAITPQ 400
    SQPAATNSSA SVETLSFNLS GALKAGITAA KEKFDTTVKT LSIDSIQFQR 450
    GGKEFLKKKQ LSPDAVAQLA FQMAFLRQYG QTVATYESCS TAAFKHGRTE 500
    TIRPASIFTK RCSEAFVRDP SKHSVGELQH MMAECSKYHG QLTKEAAMGQ 550
    GFDRHLYALR YLATARGLNL PELYLDPAYQ QMNHNILSTS TLNSPAVSLG 600
    GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDIFDA 650
    LEGKAIKT 658
    Length:658
    Mass (Da):74,110
    Last modified:November 1, 1990 - v1
    Checksum:iE48D1429E6B2EB27
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351M → V in AAB48047. (PubMed:9136891)Curated
    Sequence conflicti167 – 1671Q → R in AAB48047. (PubMed:9136891)Curated
    Sequence conflicti245 – 2451V → I in AAB48047. (PubMed:9136891)Curated
    Sequence conflicti267 – 2671L → S in AAB48047. (PubMed:9136891)Curated
    Sequence conflicti346 – 3461D → E in AAB48047. (PubMed:9136891)Curated
    Sequence conflicti373 – 3731S → A in AAB48047. (PubMed:9136891)Curated
    Sequence conflicti394 – 3941T → S in AAB48047. (PubMed:9136891)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05470 mRNA. Translation: AAB02339.1.
    U88295 mRNA. Translation: AAB48047.1.
    PIRiA35447.
    RefSeqiNP_037062.1. NM_012930.1.
    UniGeneiRn.11389.

    Genome annotation databases

    GeneIDi25413.
    KEGGirno:25413.
    UCSCiRGD:2398. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05470 mRNA. Translation: AAB02339.1 .
    U88295 mRNA. Translation: AAB48047.1 .
    PIRi A35447.
    RefSeqi NP_037062.1. NM_012930.1.
    UniGenei Rn.11389.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DEB X-ray 1.60 A/B 27-658 [» ]
    2FW3 X-ray 2.50 A 27-658 [» ]
    2FYO X-ray 2.00 A 27-658 [» ]
    2H4T X-ray 1.90 A/B 32-656 [» ]
    2RCU X-ray 1.78 A/B 27-658 [» ]
    4EP9 X-ray 2.03 A 27-658 [» ]
    4EPH X-ray 2.30 A 27-658 [» ]
    4EYW X-ray 1.88 A/B 27-658 [» ]
    ProteinModelPortali P18886.
    SMRi P18886. Positions 32-658.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000016954.

    Chemistry

    BindingDBi P18886.
    ChEMBLi CHEMBL4037.

    Proteomic databases

    PaxDbi P18886.
    PRIDEi P18886.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25413.
    KEGGi rno:25413.
    UCSCi RGD:2398. rat.

    Organism-specific databases

    CTDi 1376.
    RGDi 2398. Cpt2.

    Phylogenomic databases

    eggNOGi NOG70127.
    HOGENOMi HOG000007446.
    HOVERGENi HBG098001.
    InParanoidi P18886.
    KOi K08766.
    PhylomeDBi P18886.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14441.
    SABIO-RK P18886.

    Miscellaneous databases

    EvolutionaryTracei P18886.
    NextBioi 606547.
    PROi P18886.

    Gene expression databases

    Genevestigatori P18886.

    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. "Cloning, sequencing, and expression of a cDNA encoding rat liver mitochondrial carnitine palmitoyltransferase II."
      Woeltje K.F., Esser V., Weis B.C., Sen A., Cox W.F., McPhaul M.J., Slaughter C.A., Foster D.W., McGarry J.D.
      J. Biol. Chem. 265:10720-10725(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Sprague-Dawley.
      Tissue: Liver.
    2. "Functional characterization of mitochondrial carnitine palmitoyltransferases I and II expressed in the yeast Pichia pastoris."
      de Vries Y., Arvidson D.N., Waterham H.R., Cregg J.M., Woldegiorgis G.
      Biochemistry 36:5285-5292(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Liver.
    3. "Mitochondrial import and processing of rat liver carnitine palmitoyltransferase II defines the amino terminus of the mature protein. Possibility of differential modification of the rat and human isoforms."
      Brown N.F., Esser V., Gonzalez A.D., Evans C.T., Slaughter C.A., Foster D.W., McGarry J.D.
      J. Biol. Chem. 266:15446-15449(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PEPTIDE CLEAVAGE SITE.
    4. "Crystal structure of rat carnitine palmitoyltransferase II (CPT-II)."
      Hsiao Y.-S., Jogl G., Esser V., Tong L.
      Biochem. Biophys. Res. Commun. 346:974-980(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-656.
    5. "The crystal structure of carnitine palmitoyltransferase 2 and implications for diabetes treatment."
      Rufer A.C., Thoma R., Benz J., Stihle M., Gsell B., De Roo E., Banner D.W., Mueller F., Chomienne O., Hennig M.
      Structure 14:713-723(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 27-658 IN COMPLEX WITH THE SUBSTRATE ANALOG ST1326.
    6. "Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog."
      Rufer A.C., Lomize A., Benz J., Chomienne O., Thoma R., Hennig M.
      FEBS Lett. 581:3247-3252(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 27-658 IN COMPLEX WITH PALMITOYL-AMINOCARNITHINE, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiCPT2_RAT
    AccessioniPrimary (citable) accession number: P18886
    Secondary accession number(s): P97781
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3