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P18886

- CPT2_RAT

UniProt

P18886 - CPT2_RAT

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Protein

Carnitine O-palmitoyltransferase 2, mitochondrial

Gene
Cpt2, Cpt-2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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; Peripheral membrane protein; Matrix side 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 178153Mitochondrial matrixAdd
BLAST
Intramembranei179 – 20830Note=Mitochondrial inner membraneAdd
BLAST
Topological domaini209 – 658450Mitochondrial matrixAdd
BLAST

GO - Cellular componenti

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

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-succinyllysine By similarity
Modified residuei85 – 851N6-succinyllysine By similarity
Modified residuei239 – 2391N6-acetyllysine; alternate By similarity
Modified residuei239 – 2391N6-succinyllysine; alternate By similarity
Modified residuei305 – 3051N6-acetyllysine By similarity
Modified residuei424 – 4241N6-succinyllysine By similarity
Modified residuei439 – 4391N6-succinyllysine By similarity
Modified residuei510 – 5101N6-acetyllysine; alternate By similarity
Modified residuei510 – 5101N6-succinyllysine; alternate By similarity
Modified residuei544 – 5441N6-acetyllysine; alternate By similarity
Modified residuei544 – 5441N6-succinyllysine; alternate By 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.

Miscellaneous databases

EvolutionaryTraceiP18886.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni452 – 46413Coenzyme A binding By 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

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351M → V in AAB48047. 1 Publication
Sequence conflicti167 – 1671Q → R in AAB48047. 1 Publication
Sequence conflicti245 – 2451V → I in AAB48047. 1 Publication
Sequence conflicti267 – 2671L → S in AAB48047. 1 Publication
Sequence conflicti346 – 3461D → E in AAB48047. 1 Publication
Sequence conflicti373 – 3731S → A in AAB48047. 1 Publication
Sequence conflicti394 – 3941T → S in AAB48047. 1 Publication

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: April 16, 2014
This is version 119 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

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