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P42126 (ECI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ECI1
Synonyms:DCI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.

Catalytic activity

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. Ref.6

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homotrimer. Ref.9

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42126-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P42126-2)

The sequence of this isoform differs from the canonical sequence as follows:
     172-188: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion By similarity
Chain42 – 302261Enoyl-CoA delta isomerase 1, mitochondrial
PRO_0000007420

Regions

Region106 – 1105Substrate binding

Sites

Binding site1531Substrate; via amide nitrogen
Binding site1771Substrate
Site1781Important for catalytic activity

Amino acid modifications

Modified residue611N6-acetyllysine; alternate By similarity
Modified residue611N6-succinyllysine; alternate By similarity
Modified residue841N6-succinyllysine By similarity
Modified residue891N6-acetyllysine Ref.7
Modified residue2831N6-acetyllysine; alternate By similarity
Modified residue2831N6-succinyllysine; alternate By similarity
Modified residue2881N6-succinyllysine By similarity

Natural variations

Alternative sequence172 – 18817Missing in isoform 2.
VSP_001358

Experimental info

Mutagenesis1781E → A: Loss of activity. Ref.9
Sequence conflict141L → P in AAH00762. Ref.4
Sequence conflict141L → P in AAH19316. Ref.4
Sequence conflict411R → P in CAA81065. Ref.1
Sequence conflict441S → C AA sequence Ref.6
Sequence conflict541G → A in CAA81065. Ref.1
Sequence conflict781L → F AA sequence Ref.6
Sequence conflict931G → V in AAA35485. Ref.5
Sequence conflict1141Missing AA sequence Ref.6
Sequence conflict192 – 1932TL → PY AA sequence Ref.6
Sequence conflict204 – 2074RALQ → SAPE in AAA35485. Ref.5
Sequence conflict2101L → S AA sequence Ref.6
Sequence conflict213 – 2153PPA → RRP in AAA35485. Ref.5
Sequence conflict2421Q → K AA sequence Ref.6
Sequence conflict2451A → T AA sequence Ref.6
Sequence conflict2481D → E AA sequence Ref.6
Sequence conflict2911Q → E AA sequence Ref.6

Secondary structure

............................................ 302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 6E63827DE9BE886B

FASTA30232,816
        10         20         30         40         50         60 
MALVASVRVP ARVLLRAGAR LPGAALGRTE RAAGGGDGAR RFGSQRVLVE PDAGAGVAVM 

        70         80         90        100        110        120 
KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR PGVFSAGLDL TEMCGRSPAH 

       130        140        150        160        170        180 
YAGYWKAVQE LWLRLYQSNL VLVSAINGAC PAGGCLVALT CDYRILADNP RYCIGLNETQ 

       190        200        210        220        230        240 
LGIIAPFWLK DTLENTIGHR AAERALQLGL LFPPAEALQV GIVDQVVPEE QVQSTALSAI 

       250        260        270        280        290        300 
AQWMAIPDHA RQLTKAMMRK ATASRLVTQR DADVQNFVSF ISKDSIQKSL QMYLERLKEE 


KG 

« Hide

Isoform 2 [UniParc].

Checksum: F3689BA4B6F7FC72
Show »

FASTA28530,896

References

« Hide 'large scale' references
[1]"Human mitochondrial 3,2-trans-enoyl-CoA isomerase (DCI): gene structure and localization to chromosome 16p13.3."
Janssen U., Fink T., Lichter P., Stoffel W.
Genomics 23:223-228(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Liver and Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 2).
Tissue: Lung and Placenta.
[5]"cDNA cloning and amino acid sequence of human mitochondrial delta 3 delta 2-enoyl-CoA isomerase: comparison of the human enzyme with its rat counterpart, mitochondrial short-chain isomerase."
Kilponen J.M., Haeyrinen H.M., Rehn M.V., Hiltunen K.J.
Biochem. J. 300:1-5(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-302 (ISOFORM 1).
[6]"Delta 3, delta 2-enoyl-CoA isomerase is the protein that copurifies with human glutathione S-transferases from S-hexylglutathione affinity matrices."
Takahashi Y., Hirata Y., Burstein Y., Listowsky I.
Biochem. J. 304:849-852(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 42-84; 89-116; 190-220; 242-255 AND 288-298, CATALYTIC ACTIVITY.
Tissue: Liver.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group."
Partanen S.T., Novikov D.K., Popov A.N., Mursula A.M., Hiltunen J.K., Wierenga R.K.
J. Mol. Biol. 342:1197-1208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 43-302 IN COMPLEX WITH OCTANOYL-COENZYME A, SUBUNIT, MUTAGENESIS OF GLU-178.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z25820 mRNA. Translation: CAA81065.1.
Z25821 expand/collapse EMBL AC list , Z25822, Z25823, Z25824 Genomic DNA. Translation: CAA81066.1.
AK291127 mRNA. Translation: BAF83816.1.
CH471112 Genomic DNA. Translation: EAW85524.1.
BC000762 mRNA. Translation: AAH00762.1.
BC002746 mRNA. Translation: AAH02746.1.
BC020228 mRNA. Translation: AAH20228.1.
BC019316 mRNA. Translation: AAH19316.1.
L24774 mRNA. Translation: AAA35485.1.
CCDSCCDS10464.1. [P42126-1]
CCDS58410.1. [P42126-2]
PIRA55723.
RefSeqNP_001171500.1. NM_001178029.1. [P42126-2]
NP_001910.2. NM_001919.3. [P42126-1]
UniGeneHs.403436.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SG4X-ray1.30A/B/C43-302[»]
ProteinModelPortalP42126.
SMRP42126. Positions 45-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108000. 6 interactions.
IntActP42126. 3 interactions.
MINTMINT-3015421.
STRING9606.ENSP00000301729.

PTM databases

PhosphoSiteP42126.

Polymorphism databases

DMDM1169204.

2D gel databases

OGPP42126.

Proteomic databases

MaxQBP42126.
PaxDbP42126.
PeptideAtlasP42126.
PRIDEP42126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301729; ENSP00000301729; ENSG00000167969. [P42126-1]
ENST00000562238; ENSP00000456319; ENSG00000167969. [P42126-2]
GeneID1632.
KEGGhsa:1632.
UCSCuc002cpr.3. human. [P42126-1]
uc002cps.3. human. [P42126-2]

Organism-specific databases

CTD1632.
GeneCardsGC16M002299.
HGNCHGNC:2703. ECI1.
HPAHPA041746.
HPA043227.
MIM600305. gene.
neXtProtNX_P42126.
PharmGKBPA27173.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1024.
HOVERGENHBG001112.
InParanoidP42126.
KOK13238.
OMAALTCDYR.
OrthoDBEOG7Z69CV.
PhylomeDBP42126.
TreeFamTF314436.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressP42126.
BgeeP42126.
CleanExHS_DCI.
GenevestigatorP42126.

Family and domain databases

Gene3D3.90.226.10. 1 hit.
InterProIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 1 hit.
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSECI1. human.
EvolutionaryTraceP42126.
GenomeRNAi1632.
NextBio6694.
PROP42126.
SOURCESearch...

Entry information

Entry nameECI1_HUMAN
AccessionPrimary (citable) accession number: P42126
Secondary accession number(s): A8K512 expand/collapse secondary AC list , Q13290, Q7Z2L6, Q7Z2L7, Q9BUB8, Q9BW05, Q9UDG6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM