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P18886

- CPT2_RAT

UniProt

P18886 - CPT2_RAT

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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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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

        10         20         30         40         50
MMPRLLFRAW PRCPSLVLGA PSRPLSAVSG PDDYLQHSIV PTMHYQDSLP
60 70 80 90 100
RLPIPKLEDT MKRYLNAQKP LLDDSQFRRT EALCKNFETG VGKELHAHLL
110 120 130 140 150
AQDKQNKHTS YISGPWFDMY LTARDSIVLN FNPFMAFNPD PKSEYNDQLT
160 170 180 190 200
RATNLTVSAV RFLKTLQAGL LEPEVFHLNP SKSDTDAFKR LIRFVPPSLS
210 220 230 240 250
WYGAYLVNAY PLDMSQYFRL FNSTRIPRPN RDELFTDTKA RHLLVLRKGH
260 270 280 290 300
FYVFDVLDQD GNIVNPLEIQ AHLKYILSDS SPVPEFPVAY LTSENRDVWA
310 320 330 340 350
ELRQKLIFDG NEETLKKVDS AVFCLCLDDF PMKDLIHLSH TMLHGDGTNR
360 370 380 390 400
WFDKSFNLIV AEDGTAAVHF EHSWGDGVAV LRFFNEVFRD STQTPAITPQ
410 420 430 440 450
SQPAATNSSA SVETLSFNLS GALKAGITAA KEKFDTTVKT LSIDSIQFQR
460 470 480 490 500
GGKEFLKKKQ LSPDAVAQLA FQMAFLRQYG QTVATYESCS TAAFKHGRTE
510 520 530 540 550
TIRPASIFTK RCSEAFVRDP SKHSVGELQH MMAECSKYHG QLTKEAAMGQ
560 570 580 590 600
GFDRHLYALR YLATARGLNL PELYLDPAYQ QMNHNILSTS TLNSPAVSLG
610 620 630 640 650
GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDIFDA

LEGKAIKT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 122 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