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Protein

Enoyl-CoA delta isomerase 2, mitochondrial

Gene

Eci2

Organism
Rattus norvegicus (Rat)
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. Has a preference for 3-trans substrates.1 Publication

Catalytic activityi

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

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: RGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiR-RNO-390918. Peroxisomal lipid metabolism.
SABIO-RKQ5XIC0.

Chemistry databases

SwissLipidsiSLP:000001588.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA delta isomerase 2, mitochondrial (EC:5.3.3.8)
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1359427. Eci2.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: Ensembl
  • mitochondrion Source: RGD
  • nucleoplasm Source: Ensembl
  • peroxisomal matrix Source: UniProtKB-SubCell
  • peroxisome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 36MitochondrionSequence analysisAdd BLAST36
ChainiPRO_000038194337 – 391Enoyl-CoA delta isomerase 2, mitochondrialAdd BLAST355

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5XIC0.
PRIDEiQ5XIC0.

PTM databases

iPTMnetiQ5XIC0.
PhosphoSitePlusiQ5XIC0.

Expressioni

Tissue specificityi

Liver (at protein level).1 Publication

Gene expression databases

BgeeiENSRNOG00000016369.
ExpressionAtlasiQ5XIC0. baseline and differential.
GenevisibleiQ5XIC0. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022022.

Structurei

3D structure databases

ProteinModelPortaliQ5XIC0.
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.
InParanoidiQ5XIC0.
KOiK13239.
OrthoDBiEOG091G0T5I.
PhylomeDBiQ5XIC0.
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]

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms may exist.
Isoform 1 (identifier: Q5XIC0-1) [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 CWCPSLLQVL RLPVTKLHLG RPAMRATQQD FENAMNQVKL
60 70 80 90 100
LKKDPGNEVK LRLYALYKQA TEGPCTMPKP GVFDFVNKAK WDAWNALGSL
110 120 130 140 150
PKETARQNYV DLVSSLSSSS EASSQGKGGA DGKAQESKGI LVTSEGGITK
160 170 180 190 200
ITFNRPSKKN AITFQMYQDI ILALKNASTD DTVITVFTGA GDYYSSGNDL
210 220 230 240 250
TNFTSASGGM EEAANKGAIV LREFVNTFID FPKPLVAVVN GPAVGISVTL
260 270 280 290 300
LGLFDAVYAS DRATFHTPFS HLGQSPEACS SYTFPKMMGS AKAAEMLLFG
310 320 330 340 350
KKLTAREAWA QGLVTEVFPE STFETEVWTR LKTYAKLPPN SMRISKELIR
360 370 380 390
KNEKEKLHAV NEEECTTLRA RWLSEECINA IMSFVTRKPK L
Length:391
Mass (Da):43,021
Last modified:November 23, 2004 - v1
Checksum:iA8BFC0E900967C32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083764 mRNA. Translation: AAH83764.1.
RefSeqiNP_001006967.1. NM_001006966.1. [Q5XIC0-1]
UniGeneiRn.108029.

Genome annotation databases

EnsembliENSRNOT00000022022; ENSRNOP00000022022; ENSRNOG00000029549. [Q5XIC0-1]
GeneIDi291075.
KEGGirno:291075.
UCSCiRGD:1359427. rat. [Q5XIC0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083764 mRNA. Translation: AAH83764.1.
RefSeqiNP_001006967.1. NM_001006966.1. [Q5XIC0-1]
UniGeneiRn.108029.

3D structure databases

ProteinModelPortaliQ5XIC0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022022.

Chemistry databases

SwissLipidsiSLP:000001588.

PTM databases

iPTMnetiQ5XIC0.
PhosphoSitePlusiQ5XIC0.

Proteomic databases

PaxDbiQ5XIC0.
PRIDEiQ5XIC0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022022; ENSRNOP00000022022; ENSRNOG00000029549. [Q5XIC0-1]
GeneIDi291075.
KEGGirno:291075.
UCSCiRGD:1359427. rat. [Q5XIC0-1]

Organism-specific databases

CTDi10455.
RGDi1359427. Eci2.

Phylogenomic databases

eggNOGiKOG0016. Eukaryota.
KOG0817. Eukaryota.
COG1024. LUCA.
COG4281. LUCA.
GeneTreeiENSGT00760000119100.
InParanoidiQ5XIC0.
KOiK13239.
OrthoDBiEOG091G0T5I.
PhylomeDBiQ5XIC0.
TreeFamiTF313375.

Enzyme and pathway databases

ReactomeiR-RNO-390918. Peroxisomal lipid metabolism.
SABIO-RKQ5XIC0.

Miscellaneous databases

PROiQ5XIC0.

Gene expression databases

BgeeiENSRNOG00000016369.
ExpressionAtlasiQ5XIC0. baseline and differential.
GenevisibleiQ5XIC0. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q5XIC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: November 23, 2004
Last modified: November 2, 2016
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. 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.