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Protein

Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial

Gene

Ech1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.By similarity

Pathway: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei173 – 1731Substrate; via amide nitrogenBy similarity
Sitei196 – 1961Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (EC:5.3.3.-)
Gene namesi
Name:Ech1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1858208. Ech1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 327294Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrialPRO_0000007418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471N6-acetyllysine1 Publication
Modified residuei230 – 2301N6-succinyllysine1 Publication
Modified residuei267 – 2671PhosphoserineBy similarity
Modified residuei316 – 3161N6-succinyllysine1 Publication
Modified residuei326 – 3261N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO35459.
PaxDbiO35459.
PRIDEiO35459.

2D gel databases

REPRODUCTION-2DPAGEO35459.

PTM databases

PhosphoSiteiO35459.

Expressioni

Gene expression databases

BgeeiO35459.
CleanExiMM_ECH1.
ExpressionAtlasiO35459. baseline and differential.
GenevisibleiO35459. MM.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

IntActiO35459. 4 interactions.
MINTiMINT-1859888.
STRINGi10090.ENSMUSP00000066092.

Structurei

3D structure databases

ProteinModelPortaliO35459.
SMRiO35459. Positions 54-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi325 – 3273Microbody targeting signalSequence Analysis

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG005556.
InParanoidiO35459.
KOiK12663.
OMAiEIDMGMA.
OrthoDBiEOG7JHM64.
PhylomeDBiO35459.
TreeFamiTF314317.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O35459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATAMTVSSK LRGLLMQQLR GTSQLYFNIS LRSLSSSAQE ASKRAPEEVS
60 70 80 90 100
DHNYESIQVT SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD
110 120 130 140 150
CRAVVVSGAG KMFTSGIDLM DMASELMQPS GDDAARIAWY LRDLISKYQK
160 170 180 190 200
TFTVIEKCPK PVIAAIHGGC IGGGVDLVSA CDIRYCTQDA FFQIKEVDMG
210 220 230 240 250
LAADVGTLQR LPKVIGNQSL VNELTFSARK MMADEALDSG LVSRVFQDKD
260 270 280 290 300
AMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM
310 320
LQTQDIIKSV QAAMEKRDTK SITFSKL
Length:327
Mass (Da):36,118
Last modified:January 1, 1998 - v1
Checksum:iCC0E612C74FBEE2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030343 mRNA. Translation: AAB84224.1.
BC068112 mRNA. Translation: AAH68112.1.
BC087924 mRNA. Translation: AAH87924.1.
CCDSiCCDS21057.1.
RefSeqiNP_058052.1. NM_016772.1.
UniGeneiMm.291776.

Genome annotation databases

EnsembliENSMUST00000066264; ENSMUSP00000066092; ENSMUSG00000053898.
GeneIDi51798.
KEGGimmu:51798.
UCSCiuc009gab.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030343 mRNA. Translation: AAB84224.1.
BC068112 mRNA. Translation: AAH68112.1.
BC087924 mRNA. Translation: AAH87924.1.
CCDSiCCDS21057.1.
RefSeqiNP_058052.1. NM_016772.1.
UniGeneiMm.291776.

3D structure databases

ProteinModelPortaliO35459.
SMRiO35459. Positions 54-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35459. 4 interactions.
MINTiMINT-1859888.
STRINGi10090.ENSMUSP00000066092.

PTM databases

PhosphoSiteiO35459.

2D gel databases

REPRODUCTION-2DPAGEO35459.

Proteomic databases

MaxQBiO35459.
PaxDbiO35459.
PRIDEiO35459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066264; ENSMUSP00000066092; ENSMUSG00000053898.
GeneIDi51798.
KEGGimmu:51798.
UCSCiuc009gab.1. mouse.

Organism-specific databases

CTDi1891.
MGIiMGI:1858208. Ech1.

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG005556.
InParanoidiO35459.
KOiK12663.
OMAiEIDMGMA.
OrthoDBiEOG7JHM64.
PhylomeDBiO35459.
TreeFamiTF314317.

Enzyme and pathway databases

UniPathwayiUPA00659.

Miscellaneous databases

NextBioi308044.
PROiO35459.
SOURCEiSearch...

Gene expression databases

BgeeiO35459.
CleanExiMM_ECH1.
ExpressionAtlasiO35459. baseline and differential.
GenevisibleiO35459. MM.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterisation of mouse ECH1."
    Fitzpatrick D.R.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Testis.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-230 AND LYS-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiECH1_MOUSE
AccessioniPrimary (citable) accession number: O35459
Secondary accession number(s): Q5M8P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 24, 2015
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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.