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Reviewed, UniProtKB/Swiss-Prot P18886 (CPT2_RAT)

Last modified February 9, 2010. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

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

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General annotation (Comments)

Catalytic activity

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

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.6.

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion
Chain26 – 658633Carnitine O-palmitoyltransferase 2, mitochondrial
PRO_0000004427

Regions

Region179 – 20830Interaction with mitochondrial inner membrane
Region452 – 46413Coenzyme A binding By similarity

Sites

Active site3721Proton acceptor
Binding site4861Carnitine
Binding site4881Carnitine
Binding site4991Carnitine

Amino acid modifications

Modified residue5101N6-acetyllysine By similarity
Modified residue5441N6-acetyllysine By similarity

Experimental info

Sequence conflict1351M → V in AAB48047. Ref.2
Sequence conflict1671Q → R in AAB48047. Ref.2
Sequence conflict2451V → I in AAB48047. Ref.2
Sequence conflict2671L → S in AAB48047. Ref.2
Sequence conflict3461D → E in AAB48047. Ref.2
Sequence conflict3731S → A in AAB48047. Ref.2
Sequence conflict3941T → S in AAB48047. Ref.2

Secondary structure

1 .................................................................................................... 658
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P18886-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: E48D1429E6B2EB27

FASTA65874,110
        10         20         30         40         50         60 
MMPRLLFRAW PRCPSLVLGA PSRPLSAVSG PDDYLQHSIV PTMHYQDSLP RLPIPKLEDT 

        70         80         90        100        110        120 
MKRYLNAQKP LLDDSQFRRT EALCKNFETG VGKELHAHLL AQDKQNKHTS YISGPWFDMY 

       130        140        150        160        170        180 
LTARDSIVLN FNPFMAFNPD PKSEYNDQLT RATNLTVSAV RFLKTLQAGL LEPEVFHLNP 

       190        200        210        220        230        240 
SKSDTDAFKR LIRFVPPSLS WYGAYLVNAY PLDMSQYFRL FNSTRIPRPN RDELFTDTKA 

       250        260        270        280        290        300 
RHLLVLRKGH FYVFDVLDQD GNIVNPLEIQ AHLKYILSDS SPVPEFPVAY LTSENRDVWA 

       310        320        330        340        350        360 
ELRQKLIFDG NEETLKKVDS AVFCLCLDDF PMKDLIHLSH TMLHGDGTNR WFDKSFNLIV 

       370        380        390        400        410        420 
AEDGTAAVHF EHSWGDGVAV LRFFNEVFRD STQTPAITPQ SQPAATNSSA SVETLSFNLS 

       430        440        450        460        470        480 
GALKAGITAA KEKFDTTVKT LSIDSIQFQR GGKEFLKKKQ LSPDAVAQLA FQMAFLRQYG 

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

       550        560        570        580        590        600 
QLTKEAAMGQ GFDRHLYALR YLATARGLNL PELYLDPAYQ QMNHNILSTS TLNSPAVSLG 

       610        620        630        640        650 
GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDIFDA LEGKAIKT

« Hide

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References

[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: 2355018] [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: 9136891] [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: 1869564] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF TRANSIT PEPTIDE.
[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: 16781677] [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: 16615913] [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: 17585909] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 27-658 IN COMPLEX WITH PALMITOYL-AMINOCARNITHINE, SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05470 mRNA. Translation: AAB02339.1.
U88295 mRNA. Translation: AAB48047.1.
IPIIPI00195593.
PIRA35447.
RefSeqNP_037062.1.
UniGeneRn.11389

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP18886.

Proteomic databases

PRIDEP18886.

Genome annotation databases

EnsemblENSRNOT00000016954; ENSRNOP00000016954; ENSRNOG00000012443; Rattus norvegicus. [Genome view]
GeneID25413.
KEGGrno:25413.
UCSCNM_012930. rat.

Organism-specific databases

CTD25413.
RGD2398. Cpt2.

Phylogenomic databases

eggNOGroNOG04743.
HOVERGENP18886.
InParanoidP18886.
PhylomeDBP18886.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14441.
BRENDA2.3.1.21. 248.

Gene expression databases

ArrayExpressP18886.
GenevestigatorP18886.
GermOnlineENSRNOG00000012443. Rattus norvegicus.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. Carn_acyl_trans. 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 Resources

NextBio606547.

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Entry information

Entry nameCPT2_RAT
AccessionPrimary (citable) accession number: P18886
Secondary accession number(s): P97781
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 9, 2010
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents