ECI1_MOUSE
ID ECI1_MOUSE Reviewed; 289 AA.
AC P42125; Q8QZV3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Enoyl-CoA delta isomerase 1, mitochondrial {ECO:0000305};
DE EC=5.3.3.8 {ECO:0000250|UniProtKB:P23965};
DE AltName: Full=3,2-trans-enoyl-CoA isomerase;
DE AltName: Full=Delta(3),Delta(2)-enoyl-CoA isomerase;
DE Short=D3,D2-enoyl-CoA isomerase;
DE AltName: Full=Dodecenoyl-CoA isomerase;
DE Flags: Precursor;
GN Name=Eci1 {ECO:0000312|MGI:MGI:94871}; Synonyms=Dci;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=8224148; DOI=10.1016/0014-5793(93)80387-a;
RA Stoffel W., Dueker M., Hofmann K.O.;
RT "Molecular cloning and gene organization of the mouse mitochondrial 3,2-
RT trans-enoyl-CoA isomerase.";
RL FEBS Lett. 333:119-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 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 [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-71; LYS-222; LYS-229;
RP LYS-255; LYS-270; LYS-275 AND LYS-283, AND IDENTIFICATION BY MASS
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-76; LYS-222; LYS-229;
RP LYS-255; LYS-270 AND LYS-283, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Able to isomerize both 3-cis and 3-trans double bonds into
CC the 2-trans form in a range of enoyl-CoA species.
CC {ECO:0000250|UniProtKB:P23965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC EC=5.3.3.8; Evidence={ECO:0000250|UniProtKB:P23965};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC EC=5.3.3.8; Evidence={ECO:0000250|UniProtKB:P23965};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000250|UniProtKB:P23965};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:46044,
CC ChEBI:CHEBI:62242, ChEBI:CHEBI:85640;
CC Evidence={ECO:0000250|UniProtKB:P23965};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46045;
CC Evidence={ECO:0000250|UniProtKB:P23965};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetradecenoyl-CoA = (3Z)-tetradecenoyl-CoA;
CC Xref=Rhea:RHEA:29847, ChEBI:CHEBI:61405, ChEBI:CHEBI:61968;
CC Evidence={ECO:0000250|UniProtKB:P23965};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29849;
CC Evidence={ECO:0000250|UniProtKB:P23965};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P23965}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P23965}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P23965}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; Z14049; CAA78417.1; -; mRNA.
DR EMBL; Z14050; CAA78418.1; -; Genomic_DNA.
DR EMBL; Z14051; CAA78418.1; JOINED; Genomic_DNA.
DR EMBL; Z14052; CAA78418.1; JOINED; Genomic_DNA.
DR EMBL; Z14053; CAA78418.1; JOINED; Genomic_DNA.
DR EMBL; Z14054; CAA78418.1; JOINED; Genomic_DNA.
DR EMBL; AK029481; BAC26469.1; -; mRNA.
DR EMBL; AC154237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466606; EDL22317.1; -; Genomic_DNA.
DR EMBL; BC022712; AAH22712.1; -; mRNA.
DR EMBL; BC054444; AAH54444.1; -; mRNA.
DR CCDS; CCDS28480.1; -.
DR PIR; S38770; S38770.
DR RefSeq; NP_034153.2; NM_010023.4.
DR AlphaFoldDB; P42125; -.
DR SMR; P42125; -.
DR BioGRID; 199065; 25.
DR IntAct; P42125; 2.
DR STRING; 10090.ENSMUSP00000024946; -.
DR iPTMnet; P42125; -.
DR PhosphoSitePlus; P42125; -.
DR SwissPalm; P42125; -.
DR EPD; P42125; -.
DR jPOST; P42125; -.
DR PaxDb; P42125; -.
DR PeptideAtlas; P42125; -.
DR PRIDE; P42125; -.
DR ProteomicsDB; 277436; -.
DR Antibodypedia; 23677; 286 antibodies from 31 providers.
DR DNASU; 13177; -.
DR Ensembl; ENSMUST00000234304; ENSMUSP00000157291; ENSMUSG00000024132.
DR GeneID; 13177; -.
DR KEGG; mmu:13177; -.
DR UCSC; uc008avv.2; mouse.
DR CTD; 1632; -.
DR MGI; MGI:94871; Eci1.
DR VEuPathDB; HostDB:ENSMUSG00000024132; -.
DR eggNOG; KOG1683; Eukaryota.
DR GeneTree; ENSGT00390000005678; -.
DR HOGENOM; CLU_009834_7_5_1; -.
DR InParanoid; P42125; -.
DR OMA; WFMSSFL; -.
DR OrthoDB; 974911at2759; -.
DR PhylomeDB; P42125; -.
DR TreeFam; TF314436; -.
DR Reactome; R-MMU-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 13177; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Eci1; mouse.
DR PRO; PR:P42125; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P42125; protein.
DR Bgee; ENSMUSG00000024132; Expressed in heart right ventricle and 260 other tissues.
DR ExpressionAtlas; P42125; baseline and differential.
DR Genevisible; P42125; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:MGI.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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; Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 29..289
FT /note="Enoyl-CoA delta isomerase 1, mitochondrial"
FT /id="PRO_0000007421"
FT BINDING 93..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 165
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT MOD_RES 48
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 48
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 71
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 222
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 222
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 229
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 229
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 255
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 255
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 270
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 270
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 275
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 283
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 283
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 28
FT /note="R -> P (in Ref. 1; CAA78417/CAA78418)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="ER -> DG (in Ref. 1; CAA78417/CAA78418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32250 MW; 950B7A39D9458B91 CRC64;
MALAAARRLL LHAGSRLGRR EAVDGARRFA NKRVLVETEG PAGVAVMKLR NPPVNSLSLE
CLTEFTISLE KLENDKSIRG VILTSECPGI FSAGLDLLEM YGRNPAHYAE YWKNVQELWL
RLYTSNMILV SAINGASPAG GCLLALCCDY RVMADNPKYT IGLNESLLGI VAPFWFKDMY
VNTIGHREAE RALQLGTLFS PAEALKVGVV DEVVPEDQVH SKARSVMTKW LAIPDHSRQL
TKNMMRKATA DNLIKQREAD IQNFTSFISK DSIQKSLHMY LEKLKQKKG
