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Protein

Enoyl-CoA delta isomerase 2, mitochondrial

Gene

Eci2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (PubMed:24344334). Has a preference for 3-trans substrates (By similarity).By similarity1 Publication

Catalytic activityi

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei90Acyl-CoABy similarity1
Binding sitei109Acyl-CoABy similarity1
Sitei277Important for catalytic activityBy similarity1

GO - Molecular functioni

GO - Biological processi

  • fatty acid beta-oxidation Source: Ensembl
  • fatty acid catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiR-MMU-390918. Peroxisomal lipid metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA delta isomerase 2, mitochondrial (EC:5.3.3.81 Publication)
Alternative name(s):
Delta(3),delta(2)-enoyl-CoA isomerase
Short name:
D3,D2-enoyl-CoA isomerase
Dodecenoyl-CoA isomerase
Peroxisomal 3,2-trans-enoyl-CoA isomerase
Short name:
pECI
Gene namesi
Name:Eci2
Synonyms:Peci
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1346064. Eci2.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: MGI
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
  • peroxisomal matrix Source: UniProtKB
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 36MitochondrionSequence analysisAdd BLAST36
ChainiPRO_000021402837 – 391Enoyl-CoA delta isomerase 2, mitochondrialAdd BLAST355

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei49N6-acetyllysine; alternateBy similarity1
Modified residuei49N6-succinyllysine; alternateCombined sources1
Modified residuei53N6-succinyllysineCombined sources1
Modified residuei60N6-acetyllysine; alternateCombined sources1
Modified residuei60N6-succinyllysine; alternateCombined sources1
Modified residuei68N6-succinyllysineCombined sources1
Modified residuei79N6-succinyllysineCombined sources1
Modified residuei88N6-succinyllysineCombined sources1
Modified residuei90N6-acetyllysine; alternateCombined sources1
Modified residuei90N6-succinyllysine; alternateCombined sources1
Modified residuei99PhosphoserineBy similarity1
Modified residuei117PhosphoserineBy similarity1
Modified residuei127N6-succinyllysineCombined sources1
Modified residuei159N6-succinyllysineCombined sources1
Modified residuei286N6-succinyllysineCombined sources1

Post-translational modificationi

Acetylation of Lys-60 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9WUR2.
PeptideAtlasiQ9WUR2.
PRIDEiQ9WUR2.

PTM databases

iPTMnetiQ9WUR2.
PhosphoSitePlusiQ9WUR2.
SwissPalmiQ9WUR2.

Expressioni

Tissue specificityi

Expressed in liver and kidney (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000021417.
ExpressionAtlasiQ9WUR2. baseline and differential.
GenevisibleiQ9WUR2. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9WUR2. 2 interactors.
STRINGi10090.ENSMUSP00000131735.

Structurei

3D structure databases

ProteinModelPortaliQ9WUR2.
SMRiQ9WUR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 122ACBPROSITE-ProRule annotationAdd BLAST86

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 68Acyl-CoA bindingBy similarity5
Regioni149 – 319ECH-likeAdd BLAST171
Regioni196 – 200Substrate bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi389 – 391Microbody targeting signalSequence analysis3

Sequence similaritiesi

In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0016. Eukaryota.
KOG0817. Eukaryota.
COG1024. LUCA.
COG4281. LUCA.
GeneTreeiENSGT00760000119100.
HOVERGENiHBG006723.
InParanoidiQ9WUR2.
KOiK13239.
OMAiSDECMNA.
OrthoDBiEOG091G0T5I.
PhylomeDBiQ9WUR2.
TreeFamiTF313375.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WUR2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAVTWSRAR CWCPSVLQVF RLQVAKLHLG RPTMRASQQD FENALNQVKL
60 70 80 90 100
LKKDPGNEVK LRLYALYKQA TEGPCNMPKP GMLDFVNKAK WDAWNALGSL
110 120 130 140 150
PKETARQNYV DLVSSLSSSS EAPSQGKRGA DEKARESKDI LVTSEDGITK
160 170 180 190 200
ITFNRPTKKN AISFQMYRDI ILALKNASTD NTVMAVFTGT GDYYCSGNDL
210 220 230 240 250
TNFTSATGGI EEAASNGAVL LRDFVNSFID FPKPLVAVVN GPAVGISVTL
260 270 280 290 300
LGLFDAVFAS DRATFHTPFS QLGQSPEACS SYTFPKMMGS AKAAEMLLFG
310 320 330 340 350
KKLTAREAWA QGLVTEVFPE STFETEVWTR LKTYAKLPPN AMRISKELIR
360 370 380 390
KNEKEKLYAV NAEECTTLQA RWLSEECMNA IMSFVSRKPK L
Length:391
Mass (Da):43,268
Last modified:September 1, 2009 - v2
Checksum:i0B93D3908DF77AF8
GO
Isoform 2 (identifier: Q9WUR2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Show »
Length:358
Mass (Da):39,503
Checksum:i2E22207290123AE5
GO

Sequence cautioni

The sequence AAH01983 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35R → K in BAB26315 (PubMed:16141072).Curated1
Sequence conflicti128R → C in AAH01983 (PubMed:15489334).Curated1
Sequence conflicti135R → Q in AAH01983 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0378551 – 33Missing in isoform 2. 1 PublicationAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF153613 mRNA. Translation: AAD34174.1.
AK009478 mRNA. Translation: BAB26315.2.
BC001983 mRNA. Translation: AAH01983.1. Different initiation.
CCDSiCCDS26450.1. [Q9WUR2-2]
CCDS49234.1. [Q9WUR2-1]
RefSeqiNP_001103801.1. NM_001110331.1. [Q9WUR2-1]
NP_035998.2. NM_011868.3. [Q9WUR2-2]
XP_006516736.1. XM_006516673.2. [Q9WUR2-2]
XP_006516737.1. XM_006516674.2. [Q9WUR2-2]
XP_006516738.1. XM_006516675.2. [Q9WUR2-2]
XP_006516739.1. XM_006516676.3. [Q9WUR2-2]
XP_006516740.1. XM_006516677.1. [Q9WUR2-2]
UniGeneiMm.491141.

Genome annotation databases

EnsembliENSMUST00000021854; ENSMUSP00000021854; ENSMUSG00000021417. [Q9WUR2-2]
ENSMUST00000171229; ENSMUSP00000131735; ENSMUSG00000021417. [Q9WUR2-1]
ENSMUST00000178421; ENSMUSP00000137411; ENSMUSG00000021417. [Q9WUR2-2]
GeneIDi23986.
KEGGimmu:23986.
UCSCiuc007qbx.3. mouse. [Q9WUR2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF153613 mRNA. Translation: AAD34174.1.
AK009478 mRNA. Translation: BAB26315.2.
BC001983 mRNA. Translation: AAH01983.1. Different initiation.
CCDSiCCDS26450.1. [Q9WUR2-2]
CCDS49234.1. [Q9WUR2-1]
RefSeqiNP_001103801.1. NM_001110331.1. [Q9WUR2-1]
NP_035998.2. NM_011868.3. [Q9WUR2-2]
XP_006516736.1. XM_006516673.2. [Q9WUR2-2]
XP_006516737.1. XM_006516674.2. [Q9WUR2-2]
XP_006516738.1. XM_006516675.2. [Q9WUR2-2]
XP_006516739.1. XM_006516676.3. [Q9WUR2-2]
XP_006516740.1. XM_006516677.1. [Q9WUR2-2]
UniGeneiMm.491141.

3D structure databases

ProteinModelPortaliQ9WUR2.
SMRiQ9WUR2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WUR2. 2 interactors.
STRINGi10090.ENSMUSP00000131735.

PTM databases

iPTMnetiQ9WUR2.
PhosphoSitePlusiQ9WUR2.
SwissPalmiQ9WUR2.

Proteomic databases

PaxDbiQ9WUR2.
PeptideAtlasiQ9WUR2.
PRIDEiQ9WUR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021854; ENSMUSP00000021854; ENSMUSG00000021417. [Q9WUR2-2]
ENSMUST00000171229; ENSMUSP00000131735; ENSMUSG00000021417. [Q9WUR2-1]
ENSMUST00000178421; ENSMUSP00000137411; ENSMUSG00000021417. [Q9WUR2-2]
GeneIDi23986.
KEGGimmu:23986.
UCSCiuc007qbx.3. mouse. [Q9WUR2-1]

Organism-specific databases

CTDi10455.
MGIiMGI:1346064. Eci2.

Phylogenomic databases

eggNOGiKOG0016. Eukaryota.
KOG0817. Eukaryota.
COG1024. LUCA.
COG4281. LUCA.
GeneTreeiENSGT00760000119100.
HOVERGENiHBG006723.
InParanoidiQ9WUR2.
KOiK13239.
OMAiSDECMNA.
OrthoDBiEOG091G0T5I.
PhylomeDBiQ9WUR2.
TreeFamiTF313375.

Enzyme and pathway databases

ReactomeiR-MMU-390918. Peroxisomal lipid metabolism.

Miscellaneous databases

PROiQ9WUR2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021417.
ExpressionAtlasiQ9WUR2. baseline and differential.
GenevisibleiQ9WUR2. MM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiECI2_MOUSE
AccessioniPrimary (citable) accession number: Q9WUR2
Secondary accession number(s): Q99M61, Q9D785
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: September 1, 2009
Last modified: November 30, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.