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Protein

Carnitine O-palmitoyltransferase 2, mitochondrial

Gene

Cpt2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei372Proton acceptor1
Binding sitei486Carnitine1
Binding sitei488Carnitine1
Binding sitei499Carnitine1

GO - Molecular functioni

  • carnitine O-palmitoyltransferase activity Source: RGD

GO - Biological processi

  • fatty acid beta-oxidation Source: RGD
  • 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.
BRENDAi2.3.1.21. 5301.
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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2398. Cpt2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 178Mitochondrial matrixAdd BLAST153
Intramembranei179 – 208Note=Mitochondrial inner membraneAdd BLAST30
Topological domaini209 – 658Mitochondrial matrixAdd BLAST450

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4037.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionAdd BLAST25
ChainiPRO_000000442726 – 658Carnitine O-palmitoyltransferase 2, mitochondrialAdd BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei69N6-succinyllysineBy similarity1
Modified residuei85N6-succinyllysineBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
Modified residuei239N6-succinyllysine; alternateBy similarity1
Modified residuei305N6-acetyllysineBy similarity1
Modified residuei424N6-succinyllysineBy similarity1
Modified residuei439N6-succinyllysineBy similarity1
Modified residuei510N6-acetyllysine; alternateBy similarity1
Modified residuei510N6-succinyllysine; alternateBy similarity1
Modified residuei544N6-acetyllysine; alternateBy similarity1
Modified residuei544N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP18886.
PRIDEiP18886.

PTM databases

iPTMnetiP18886.
PhosphoSitePlusiP18886.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016954.

Chemistry databases

BindingDBiP18886.

Structurei

Secondary structure

1658
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni42 – 45Combined sources4
Helixi46 – 48Combined sources3
Helixi57 – 68Combined sources12
Turni69 – 71Combined sources3
Helixi74 – 89Combined sources16
Helixi91 – 105Combined sources15
Turni106 – 108Combined sources3
Helixi113 – 122Combined sources10
Turni128 – 131Combined sources4
Beta strandi134 – 137Combined sources4
Helixi143 – 146Combined sources4
Helixi148 – 167Combined sources20
Beta strandi175 – 178Combined sources4
Helixi180 – 183Combined sources4
Helixi186 – 192Combined sources7
Turni197 – 199Combined sources3
Helixi200 – 206Combined sources7
Beta strandi209 – 211Combined sources3
Helixi217 – 220Combined sources4
Beta strandi221 – 226Combined sources6
Beta strandi229 – 231Combined sources3
Beta strandi233 – 236Combined sources4
Beta strandi242 – 247Combined sources6
Beta strandi250 – 257Combined sources8
Helixi266 – 278Combined sources13
Helixi288 – 293Combined sources6
Helixi296 – 308Combined sources13
Turni309 – 311Combined sources3
Helixi312 – 320Combined sources9
Beta strandi324 – 327Combined sources4
Helixi335 – 343Combined sources9
Turni344 – 346Combined sources3
Beta strandi347 – 349Combined sources3
Beta strandi354 – 360Combined sources7
Beta strandi366 – 370Combined sources5
Beta strandi372 – 374Combined sources3
Helixi378 – 393Combined sources16
Helixi408 – 411Combined sources4
Beta strandi412 – 414Combined sources3
Helixi421 – 438Combined sources18
Beta strandi442 – 448Combined sources7
Helixi453 – 458Combined sources6
Helixi463 – 479Combined sources17
Beta strandi485 – 490Combined sources6
Beta strandi499 – 502Combined sources4
Helixi507 – 517Combined sources11
Helixi520 – 522Combined sources3
Helixi525 – 547Combined sources23
Helixi553 – 565Combined sources13
Helixi572 – 575Combined sources4
Helixi577 – 582Combined sources6
Beta strandi586 – 591Combined sources6
Beta strandi597 – 601Combined sources5
Beta strandi610 – 616Combined sources7
Beta strandi621 – 627Combined sources7
Beta strandi629 – 631Combined sources3
Helixi633 – 651Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18886.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni452 – 464Coenzyme A bindingBy similarityAdd BLAST13

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3719. Eukaryota.
ENOG410XNZ9. LUCA.
HOGENOMiHOG000007446.
HOVERGENiHBG098001.
InParanoidiP18886.
KOiK08766.
PhylomeDBiP18886.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti135M → V in AAB48047 (PubMed:9136891).Curated1
Sequence conflicti167Q → R in AAB48047 (PubMed:9136891).Curated1
Sequence conflicti245V → I in AAB48047 (PubMed:9136891).Curated1
Sequence conflicti267L → S in AAB48047 (PubMed:9136891).Curated1
Sequence conflicti346D → E in AAB48047 (PubMed:9136891).Curated1
Sequence conflicti373S → A in AAB48047 (PubMed:9136891).Curated1
Sequence conflicti394T → S in AAB48047 (PubMed:9136891).Curated1

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.
PIRiA35447.
RefSeqiNP_037062.1. NM_012930.1.
UniGeneiRn.11389.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016954.

Chemistry databases

BindingDBiP18886.
ChEMBLiCHEMBL4037.

PTM databases

iPTMnetiP18886.
PhosphoSitePlusiP18886.

Proteomic databases

PaxDbiP18886.
PRIDEiP18886.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1376.
RGDi2398. Cpt2.

Phylogenomic databases

eggNOGiKOG3719. Eukaryota.
ENOG410XNZ9. LUCA.
HOGENOMiHOG000007446.
HOVERGENiHBG098001.
InParanoidiP18886.
KOiK08766.
PhylomeDBiP18886.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14441.
BRENDAi2.3.1.21. 5301.
SABIO-RKP18886.

Miscellaneous databases

EvolutionaryTraceiP18886.
PROiP18886.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 2 hits.
PfamiPF00755. Carn_acyltransf. 1 hit.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 134 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.