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Protein

Enoyl-CoA delta isomerase 1, mitochondrial

Gene

Eci1

Organism
Mus musculus (Mouse)
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.

Catalytic activityi

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

Pathwayi: 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 sitei140 – 1401Substrate; via amide nitrogenBy similarity
Binding sitei164 – 1641SubstrateBy similarity
Sitei165 – 1651Important for catalytic activityBy similarity

GO - Molecular functioni

  • dodecenoyl-CoA delta-isomerase activity Source: MGI

GO - Biological processi

  • fatty acid beta-oxidation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA delta isomerase 1, mitochondrial (EC:5.3.3.8)
Alternative name(s):
3,2-trans-enoyl-CoA isomerase
Delta(3),Delta(2)-enoyl-CoA isomerase
Short name:
D3,D2-enoyl-CoA isomerase
Dodecenoyl-CoA isomerase
Gene namesi
Name:Eci1
Synonyms:Dci
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:94871. Eci1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionBy similarityAdd
BLAST
Chaini29 – 289261Enoyl-CoA delta isomerase 1, mitochondrialPRO_0000007421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-acetyllysine; alternateCombined sources
Modified residuei48 – 481N6-succinyllysine; alternateCombined sources
Modified residuei71 – 711N6-succinyllysineCombined sources
Modified residuei76 – 761N6-acetyllysineCombined sources
Modified residuei222 – 2221N6-acetyllysine; alternateCombined sources
Modified residuei222 – 2221N6-succinyllysine; alternateCombined sources
Modified residuei229 – 2291N6-acetyllysine; alternateCombined sources
Modified residuei229 – 2291N6-succinyllysine; alternateCombined sources
Modified residuei255 – 2551N6-acetyllysine; alternateCombined sources
Modified residuei255 – 2551N6-succinyllysine; alternateCombined sources
Modified residuei270 – 2701N6-acetyllysine; alternateCombined sources
Modified residuei270 – 2701N6-succinyllysine; alternateCombined sources
Modified residuei275 – 2751N6-succinyllysineCombined sources
Modified residuei283 – 2831N6-acetyllysine; alternateCombined sources
Modified residuei283 – 2831N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP42125.
PaxDbiP42125.
PRIDEiP42125.

PTM databases

iPTMnetiP42125.
PhosphoSiteiP42125.
SwissPalmiP42125.

Expressioni

Gene expression databases

GenevisibleiP42125. MM.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

MINTiMINT-1860275.
STRINGi10090.ENSMUSP00000024946.

Structurei

3D structure databases

ProteinModelPortaliP42125.
SMRiP42125. Positions 29-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 975Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410ISNQ. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00390000005678.
HOVERGENiHBG001112.
InParanoidiP42125.
KOiK13238.
OMAiSCDYRIM.
OrthoDBiEOG7Z69CV.
TreeFamiTF314436.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 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.

P42125-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALAAARRLL LHAGSRLGRR EAVDGARRFA NKRVLVETEG PAGVAVMKLR
60 70 80 90 100
NPPVNSLSLE CLTEFTISLE KLENDKSIRG VILTSECPGI FSAGLDLLEM
110 120 130 140 150
YGRNPAHYAE YWKNVQELWL RLYTSNMILV SAINGASPAG GCLLALCCDY
160 170 180 190 200
RVMADNPKYT IGLNESLLGI VAPFWFKDMY VNTIGHREAE RALQLGTLFS
210 220 230 240 250
PAEALKVGVV DEVVPEDQVH SKARSVMTKW LAIPDHSRQL TKNMMRKATA
260 270 280
DNLIKQREAD IQNFTSFISK DSIQKSLHMY LEKLKQKKG
Length:289
Mass (Da):32,250
Last modified:October 3, 2012 - v2
Checksum:i950B7A39D9458B91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281R → P in CAA78417 (PubMed:8224148).Curated
Sequence conflicti28 – 281R → P in CAA78418 (PubMed:8224148).Curated
Sequence conflicti190 – 1912ER → DG in CAA78417 (PubMed:8224148).Curated
Sequence conflicti190 – 1912ER → DG in CAA78418 (PubMed:8224148).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14049 mRNA. Translation: CAA78417.1.
Z14050
, Z14051, Z14052, Z14053, Z14054 Genomic DNA. Translation: CAA78418.1.
AK029481 mRNA. Translation: BAC26469.1.
AC154237 Genomic DNA. No translation available.
CH466606 Genomic DNA. Translation: EDL22317.1.
BC022712 mRNA. Translation: AAH22712.1.
BC054444 mRNA. Translation: AAH54444.1.
CCDSiCCDS28480.1.
PIRiS38770.
RefSeqiNP_034153.2. NM_010023.4.
UniGeneiMm.291743.

Genome annotation databases

EnsembliENSMUST00000024946; ENSMUSP00000024946; ENSMUSG00000024132.
GeneIDi13177.
KEGGimmu:13177.
UCSCiuc008avv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14049 mRNA. Translation: CAA78417.1.
Z14050
, Z14051, Z14052, Z14053, Z14054 Genomic DNA. Translation: CAA78418.1.
AK029481 mRNA. Translation: BAC26469.1.
AC154237 Genomic DNA. No translation available.
CH466606 Genomic DNA. Translation: EDL22317.1.
BC022712 mRNA. Translation: AAH22712.1.
BC054444 mRNA. Translation: AAH54444.1.
CCDSiCCDS28480.1.
PIRiS38770.
RefSeqiNP_034153.2. NM_010023.4.
UniGeneiMm.291743.

3D structure databases

ProteinModelPortaliP42125.
SMRiP42125. Positions 29-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1860275.
STRINGi10090.ENSMUSP00000024946.

PTM databases

iPTMnetiP42125.
PhosphoSiteiP42125.
SwissPalmiP42125.

Proteomic databases

EPDiP42125.
PaxDbiP42125.
PRIDEiP42125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024946; ENSMUSP00000024946; ENSMUSG00000024132.
GeneIDi13177.
KEGGimmu:13177.
UCSCiuc008avv.2. mouse.

Organism-specific databases

CTDi1632.
MGIiMGI:94871. Eci1.

Phylogenomic databases

eggNOGiENOG410ISNQ. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00390000005678.
HOVERGENiHBG001112.
InParanoidiP42125.
KOiK13238.
OMAiSCDYRIM.
OrthoDBiEOG7Z69CV.
TreeFamiTF314436.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-MMU-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.

Miscellaneous databases

NextBioi283284.
PROiP42125.
SOURCEiSearch...

Gene expression databases

GenevisibleiP42125. MM.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and gene organization of the mouse mitochondrial 3,2-trans-enoyl-CoA isomerase."
    Stoffel W., Dueker M., Hofmann K.O.
    FEBS Lett. 333:119-122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: FVB/N.
    Tissue: Colon and Mammary tumor.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "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-48; LYS-71; LYS-222; LYS-229; LYS-255; LYS-270; LYS-275 AND LYS-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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-48; LYS-76; LYS-222; LYS-229; LYS-255; LYS-270 AND LYS-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiECI1_MOUSE
AccessioniPrimary (citable) accession number: P42125
Secondary accession number(s): Q8QZV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 3, 2012
Last modified: March 16, 2016
This is version 120 of the entry and version 2 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

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.