ECH1_MOUSE
ID ECH1_MOUSE Reviewed; 327 AA.
AC O35459; Q5M8P6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial {ECO:0000305};
DE EC=5.3.3.- {ECO:0000250|UniProtKB:Q62651};
DE Flags: Precursor;
GN Name=Ech1 {ECO:0000312|MGI:MGI:1858208};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fitzpatrick D.R.;
RT "Identification and characterisation of mouse ECH1.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-230 AND LYS-316, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-
CC trans-dienoyl-CoA. {ECO:0000250|UniProtKB:Q62651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z)-octadienoyl-CoA = (2E,4E)-octadienoyl-CoA;
CC Xref=Rhea:RHEA:45244, ChEBI:CHEBI:62243, ChEBI:CHEBI:85108;
CC Evidence={ECO:0000250|UniProtKB:Q62651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z,8Z,11Z,14Z)-eicosapentaenoyl-CoA = (2E,4E,8Z,11Z,14Z)-
CC eicosapentaenoyl-CoA; Xref=Rhea:RHEA:45224, ChEBI:CHEBI:85090,
CC ChEBI:CHEBI:85091; Evidence={ECO:0000250|UniProtKB:Q62651};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:Q62651}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q62651}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q62651}.
CC Peroxisome {ECO:0000250|UniProtKB:Q62651}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AF030343; AAB84224.1; -; mRNA.
DR EMBL; BC068112; AAH68112.1; -; mRNA.
DR EMBL; BC087924; AAH87924.1; -; mRNA.
DR CCDS; CCDS21057.1; -.
DR RefSeq; NP_058052.1; NM_016772.1.
DR AlphaFoldDB; O35459; -.
DR SMR; O35459; -.
DR BioGRID; 206181; 34.
DR IntAct; O35459; 3.
DR MINT; O35459; -.
DR STRING; 10090.ENSMUSP00000066092; -.
DR iPTMnet; O35459; -.
DR PhosphoSitePlus; O35459; -.
DR SwissPalm; O35459; -.
DR REPRODUCTION-2DPAGE; O35459; -.
DR EPD; O35459; -.
DR jPOST; O35459; -.
DR MaxQB; O35459; -.
DR PaxDb; O35459; -.
DR PeptideAtlas; O35459; -.
DR PRIDE; O35459; -.
DR ProteomicsDB; 275430; -.
DR Antibodypedia; 1042; 279 antibodies from 30 providers.
DR DNASU; 51798; -.
DR Ensembl; ENSMUST00000066264; ENSMUSP00000066092; ENSMUSG00000053898.
DR GeneID; 51798; -.
DR KEGG; mmu:51798; -.
DR UCSC; uc009gab.1; mouse.
DR CTD; 1891; -.
DR MGI; MGI:1858208; Ech1.
DR VEuPathDB; HostDB:ENSMUSG00000053898; -.
DR eggNOG; KOG1681; Eukaryota.
DR GeneTree; ENSGT00940000159610; -.
DR InParanoid; O35459; -.
DR OMA; QYVAHVE; -.
DR OrthoDB; 1094098at2759; -.
DR PhylomeDB; O35459; -.
DR TreeFam; TF314317; -.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 51798; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ech1; mouse.
DR PRO; PR:O35459; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35459; protein.
DR Bgee; ENSMUSG00000053898; Expressed in heart right ventricle and 259 other tissues.
DR ExpressionAtlas; O35459; baseline and differential.
DR Genevisible; O35459; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0051750; F:delta(3,5)-delta(2,4)-dienoyl-CoA isomerase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045002; Ech1-like.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR PANTHER; PTHR43149; PTHR43149; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism;
KW Mitochondrion; Peroxisome; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..327
FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase,
FT mitochondrial"
FT /id="PRO_0000007418"
FT MOTIF 325..327
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 115..119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 196
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 204
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q62651"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 230
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13011"
FT MOD_RES 316
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13011"
SQ SEQUENCE 327 AA; 36118 MW; CC0E612C74FBEE2E CRC64;
MATAMTVSSK LRGLLMQQLR GTSQLYFNIS LRSLSSSAQE ASKRAPEEVS DHNYESIQVT
SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD CRAVVVSGAG KMFTSGIDLM
DMASELMQPS GDDAARIAWY LRDLISKYQK TFTVIEKCPK PVIAAIHGGC IGGGVDLVSA
CDIRYCTQDA FFQIKEVDMG LAADVGTLQR LPKVIGNQSL VNELTFSARK MMADEALDSG
LVSRVFQDKD AMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM
LQTQDIIKSV QAAMEKRDTK SITFSKL
