ECH1_HUMAN
ID ECH1_HUMAN Reviewed; 328 AA.
AC Q13011; A8K745; Q8WVX0; Q96EZ9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 204.
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|HGNC:HGNC:3149};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=7558027; DOI=10.1006/geno.1995.1077;
RA Fitzpatrick D.R., Germain-Lee E., Valle D.;
RT "Isolation and characterization of rat and human cDNAs encoding a novel
RT putative peroxisomal enoyl-CoA hydratase.";
RL Genomics 27:457-466(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fitzpatrick D.R., Valle D.;
RT "Genomic structure of human ECH1.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-41.
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-41.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-41.
RC TISSUE=Melanoma, and Pancreatic carcinoma;
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 [6]
RP PROTEIN SEQUENCE OF 149-158 AND 215-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 66-77; 113-131; 149-211; 215-230 AND 232-245, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, VARIANT [LARGE SCALE
RP ANALYSIS] ALA-41, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 50-322.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human peroxisomal delta3,5,delta2,4-dienoyl CoA
RT isomerase (ECH1).";
RL Submitted (FEB-2009) to the PDB data bank.
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 -!- INTERACTION:
CC Q13011; O75521: ECI2; NbExp=4; IntAct=EBI-711968, EBI-2512024;
CC Q13011; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-711968, EBI-10175124;
CC Q13011; P42858: HTT; NbExp=2; IntAct=EBI-711968, EBI-466029;
CC Q13011; P40763: STAT3; NbExp=2; IntAct=EBI-711968, EBI-518675;
CC Q13011; Q13077: TRAF1; NbExp=4; IntAct=EBI-711968, EBI-359224;
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; U16660; AAC50222.1; -; mRNA.
DR EMBL; AF030249; AAB86485.1; -; Genomic_DNA.
DR EMBL; AF030246; AAB86485.1; JOINED; Genomic_DNA.
DR EMBL; AF030247; AAB86485.1; JOINED; Genomic_DNA.
DR EMBL; AF030248; AAB86485.1; JOINED; Genomic_DNA.
DR EMBL; AK291860; BAF84549.1; -; mRNA.
DR EMBL; CH471126; EAW56824.1; -; Genomic_DNA.
DR EMBL; BC011792; AAH11792.1; -; mRNA.
DR EMBL; BC017408; AAH17408.1; -; mRNA.
DR CCDS; CCDS33014.1; -.
DR PIR; I38882; I38882.
DR RefSeq; NP_001389.2; NM_001398.2.
DR PDB; 2VRE; X-ray; 1.95 A; A/B/C=50-322.
DR PDBsum; 2VRE; -.
DR AlphaFoldDB; Q13011; -.
DR SMR; Q13011; -.
DR BioGRID; 108220; 202.
DR IntAct; Q13011; 199.
DR MINT; Q13011; -.
DR STRING; 9606.ENSP00000221418; -.
DR ChEMBL; CHEMBL4523284; -.
DR iPTMnet; Q13011; -.
DR MetOSite; Q13011; -.
DR PhosphoSitePlus; Q13011; -.
DR SwissPalm; Q13011; -.
DR BioMuta; ECH1; -.
DR DMDM; 82654933; -.
DR REPRODUCTION-2DPAGE; IPI00011416; -.
DR UCD-2DPAGE; Q13011; -.
DR EPD; Q13011; -.
DR jPOST; Q13011; -.
DR MassIVE; Q13011; -.
DR MaxQB; Q13011; -.
DR PaxDb; Q13011; -.
DR PeptideAtlas; Q13011; -.
DR PRIDE; Q13011; -.
DR ProteomicsDB; 59100; -.
DR TopDownProteomics; Q13011; -.
DR Antibodypedia; 1042; 279 antibodies from 30 providers.
DR DNASU; 1891; -.
DR Ensembl; ENST00000221418.9; ENSP00000221418.3; ENSG00000104823.9.
DR Ensembl; ENST00000634245.2; ENSP00000489530.1; ENSG00000282853.2.
DR GeneID; 1891; -.
DR KEGG; hsa:1891; -.
DR MANE-Select; ENST00000221418.9; ENSP00000221418.3; NM_001398.3; NP_001389.2.
DR UCSC; uc002oji.4; human.
DR CTD; 1891; -.
DR DisGeNET; 1891; -.
DR GeneCards; ECH1; -.
DR HGNC; HGNC:3149; ECH1.
DR HPA; ENSG00000104823; Tissue enhanced (skeletal).
DR MIM; 600696; gene.
DR neXtProt; NX_Q13011; -.
DR OpenTargets; ENSG00000104823; -.
DR PharmGKB; PA27596; -.
DR VEuPathDB; HostDB:ENSG00000104823; -.
DR eggNOG; KOG1681; Eukaryota.
DR GeneTree; ENSGT00940000159610; -.
DR InParanoid; Q13011; -.
DR OMA; QYVAHVE; -.
DR OrthoDB; 1094098at2759; -.
DR PhylomeDB; Q13011; -.
DR TreeFam; TF314317; -.
DR PathwayCommons; Q13011; -.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q13011; -.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 1891; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; ECH1; human.
DR EvolutionaryTrace; Q13011; -.
DR GeneWiki; ECH1; -.
DR GenomeRNAi; 1891; -.
DR Pharos; Q13011; Tbio.
DR PRO; PR:Q13011; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q13011; protein.
DR Bgee; ENSG00000104823; Expressed in apex of heart and 100 other tissues.
DR ExpressionAtlas; Q13011; baseline and differential.
DR Genevisible; Q13011; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; NAS:UniProtKB.
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 3D-structure; Acetylation; Direct protein sequencing;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Mitochondrion;
KW Peroxisome; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..328
FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase,
FT mitochondrial"
FT /id="PRO_0000007417"
FT MOTIF 326..328
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 116..120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 197
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 205
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q62651"
FT MOD_RES 231
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35459"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 327
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 41
FT /note="E -> A (in dbSNP:rs9419)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:24275569"
FT /id="VAR_014927"
FT VARIANT 217
FT /note="G -> R (in dbSNP:rs2229259)"
FT /id="VAR_033913"
FT CONFLICT 210
FT /note="Q -> E (in Ref. 1; AAC50222 and 2; AAB86485)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> H (in Ref. 1; AAC50222 and 2; AAB86485)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="G -> D (in Ref. 1; AAC50222 and 2; AAB86485)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="A -> P (in Ref. 1; AAC50222 and 2; AAB86485)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> P (in Ref. 1; AAC50222 and 2; AAB86485)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..271
FT /note="SPVA -> TTVL (in Ref. 1; AAC50222 and 2; AAB86485)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="A -> P (in Ref. 1; AAC50222 and 2; AAB86485)"
FT /evidence="ECO:0000305"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 135..158
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:2VRE"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 269..284
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:2VRE"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:2VRE"
SQ SEQUENCE 328 AA; 35816 MW; 211E0FF40379E6DA CRC64;
MAAGIVASRR LRDLLTRRLT GSNYPGLSIS LRLTGSSAQE EASGVALGEA PDHSYESLRV
TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA DCRAVVISGA GKMFTAGIDL
MDMASDILQP KGDDVARISW YLRDIITRYQ ETFNVIERCP KPVIAAVHGG CIGGGVDLVT
ACDIRYCAQD AFFQVKEVDV GLAADVGTLQ RLPKVIGNQS LVNELAFTAR KMMADEALGS
GLVSRVFPDK EVMLDAALAL AAEISSKSPV AVQSTKVNLL YSRDHSVAES LNYVASWNMS
MLQTQDLVKS VQATTENKEL KTVTFSKL
