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P42126

- ECI1_HUMAN

UniProt

P42126 - ECI1_HUMAN

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Protein

Enoyl-CoA delta isomerase 1, mitochondrial

Gene

ECI1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei153 – 1531Substrate; via amide nitrogen
Binding sitei177 – 1771Substrate
Sitei178 – 1781Important for catalytic activity

GO - Molecular functioni

  1. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB
  2. intramolecular oxidoreductase activity Source: Reactome

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. fatty acid beta-oxidation Source: UniProtKB
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_160. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:2703. ECI1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: UniProtKB
  4. mitochondrion Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi178 – 1781E → A: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA27173.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionBy similarityAdd
BLAST
Chaini42 – 302261Enoyl-CoA delta isomerase 1, mitochondrialPRO_0000007420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611N6-acetyllysine; alternateBy similarity
Modified residuei61 – 611N6-succinyllysine; alternateBy similarity
Modified residuei84 – 841N6-succinyllysineBy similarity
Modified residuei89 – 891N6-acetyllysine1 Publication
Modified residuei283 – 2831N6-acetyllysine; alternateBy similarity
Modified residuei283 – 2831N6-succinyllysine; alternateBy similarity
Modified residuei288 – 2881N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP42126.
PaxDbiP42126.
PeptideAtlasiP42126.
PRIDEiP42126.

2D gel databases

OGPiP42126.

PTM databases

PhosphoSiteiP42126.

Expressioni

Gene expression databases

BgeeiP42126.
CleanExiHS_DCI.
ExpressionAtlasiP42126. baseline and differential.
GenevestigatoriP42126.

Organism-specific databases

HPAiHPA041746.
HPA043227.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi108000. 6 interactions.
IntActiP42126. 3 interactions.
MINTiMINT-3015421.
STRINGi9606.ENSP00000301729.

Structurei

Secondary structure

1
302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 527Combined sources
Turni53 – 564Combined sources
Beta strandi57 – 626Combined sources
Turni65 – 673Combined sources
Helixi72 – 8716Combined sources
Beta strandi93 – 1008Combined sources
Beta strandi102 – 1043Combined sources
Helixi110 – 1134Combined sources
Helixi118 – 13619Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi148 – 1503Combined sources
Helixi152 – 1587Combined sources
Beta strandi161 – 1677Combined sources
Helixi178 – 1814Combined sources
Helixi187 – 19711Combined sources
Helixi199 – 20810Combined sources
Helixi214 – 2196Combined sources
Beta strandi222 – 2276Combined sources
Helixi229 – 2313Combined sources
Helixi232 – 24413Combined sources
Helixi248 – 26720Combined sources
Helixi270 – 28112Combined sources
Helixi284 – 2907Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SG4X-ray1.30A/B/C43-302[»]
ProteinModelPortaliP42126.
SMRiP42126. Positions 45-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42126.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1105Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00390000005678.
HOVERGENiHBG001112.
InParanoidiP42126.
KOiK13238.
OMAiALTCDYR.
OrthoDBiEOG7Z69CV.
PhylomeDBiP42126.
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 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P42126-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MALVASVRVP ARVLLRAGAR LPGAALGRTE RAAGGGDGAR RFGSQRVLVE
60 70 80 90 100
PDAGAGVAVM KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR
110 120 130 140 150
PGVFSAGLDL TEMCGRSPAH YAGYWKAVQE LWLRLYQSNL VLVSAINGAC
160 170 180 190 200
PAGGCLVALT CDYRILADNP RYCIGLNETQ LGIIAPFWLK DTLENTIGHR
210 220 230 240 250
AAERALQLGL LFPPAEALQV GIVDQVVPEE QVQSTALSAI AQWMAIPDHA
260 270 280 290 300
RQLTKAMMRK ATASRLVTQR DADVQNFVSF ISKDSIQKSL QMYLERLKEE

KG
Length:302
Mass (Da):32,816
Last modified:November 1, 1995 - v1
Checksum:i6E63827DE9BE886B
GO
Isoform 2 (identifier: P42126-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     172-188: Missing.

Note: No experimental confirmation available.

Show »
Length:285
Mass (Da):30,896
Checksum:iF3689BA4B6F7FC72
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141L → P in AAH00762. (PubMed:15489334)Curated
Sequence conflicti14 – 141L → P in AAH19316. (PubMed:15489334)Curated
Sequence conflicti41 – 411R → P in CAA81065. (PubMed:7829074)Curated
Sequence conflicti44 – 441S → C AA sequence (PubMed:7818490)Curated
Sequence conflicti54 – 541G → A in CAA81065. (PubMed:7829074)Curated
Sequence conflicti78 – 781L → F AA sequence (PubMed:7818490)Curated
Sequence conflicti93 – 931G → V in AAA35485. (PubMed:8198519)Curated
Sequence conflicti114 – 1141Missing AA sequence (PubMed:7818490)Curated
Sequence conflicti192 – 1932TL → PY AA sequence (PubMed:7818490)Curated
Sequence conflicti204 – 2074RALQ → SAPE in AAA35485. (PubMed:8198519)Curated
Sequence conflicti210 – 2101L → S AA sequence (PubMed:7818490)Curated
Sequence conflicti213 – 2153PPA → RRP in AAA35485. (PubMed:8198519)Curated
Sequence conflicti242 – 2421Q → K AA sequence (PubMed:7818490)Curated
Sequence conflicti245 – 2451A → T AA sequence (PubMed:7818490)Curated
Sequence conflicti248 – 2481D → E AA sequence (PubMed:7818490)Curated
Sequence conflicti291 – 2911Q → E AA sequence (PubMed:7818490)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei172 – 18817Missing in isoform 2. 1 PublicationVSP_001358Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25820 mRNA. Translation: CAA81065.1.
Z25821
, 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.
CCDSiCCDS10464.1. [P42126-1]
CCDS58410.1. [P42126-2]
PIRiA55723.
RefSeqiNP_001171500.1. NM_001178029.1. [P42126-2]
NP_001910.2. NM_001919.3. [P42126-1]
UniGeneiHs.403436.

Genome annotation databases

EnsembliENST00000301729; ENSP00000301729; ENSG00000167969. [P42126-1]
ENST00000562238; ENSP00000456319; ENSG00000167969. [P42126-2]
GeneIDi1632.
KEGGihsa:1632.
UCSCiuc002cpr.3. human. [P42126-1]
uc002cps.3. human. [P42126-2]

Polymorphism databases

DMDMi1169204.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25820 mRNA. Translation: CAA81065.1 .
Z25821
, 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 .
CCDSi CCDS10464.1. [P42126-1 ]
CCDS58410.1. [P42126-2 ]
PIRi A55723.
RefSeqi NP_001171500.1. NM_001178029.1. [P42126-2 ]
NP_001910.2. NM_001919.3. [P42126-1 ]
UniGenei Hs.403436.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SG4 X-ray 1.30 A/B/C 43-302 [» ]
ProteinModelPortali P42126.
SMRi P42126. Positions 45-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108000. 6 interactions.
IntActi P42126. 3 interactions.
MINTi MINT-3015421.
STRINGi 9606.ENSP00000301729.

PTM databases

PhosphoSitei P42126.

Polymorphism databases

DMDMi 1169204.

2D gel databases

OGPi P42126.

Proteomic databases

MaxQBi P42126.
PaxDbi P42126.
PeptideAtlasi P42126.
PRIDEi P42126.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301729 ; ENSP00000301729 ; ENSG00000167969 . [P42126-1 ]
ENST00000562238 ; ENSP00000456319 ; ENSG00000167969 . [P42126-2 ]
GeneIDi 1632.
KEGGi hsa:1632.
UCSCi uc002cpr.3. human. [P42126-1 ]
uc002cps.3. human. [P42126-2 ]

Organism-specific databases

CTDi 1632.
GeneCardsi GC16M002301.
HGNCi HGNC:2703. ECI1.
HPAi HPA041746.
HPA043227.
MIMi 600305. gene.
neXtProti NX_P42126.
PharmGKBi PA27173.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1024.
GeneTreei ENSGT00390000005678.
HOVERGENi HBG001112.
InParanoidi P42126.
KOi K13238.
OMAi ALTCDYR.
OrthoDBi EOG7Z69CV.
PhylomeDBi P42126.
TreeFami TF314436.

Enzyme and pathway databases

UniPathwayi UPA00659 .
Reactomei REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.

Miscellaneous databases

ChiTaRSi ECI1. human.
EvolutionaryTracei P42126.
GenomeRNAii 1632.
NextBioi 6694.
PROi P42126.
SOURCEi Search...

Gene expression databases

Bgeei P42126.
CleanExi HS_DCI.
ExpressionAtlasi P42126. baseline and differential.
Genevestigatori P42126.

Family and domain databases

Gene3Di 3.90.226.10. 1 hit.
InterProi IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view ]
Pfami PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF52096. SSF52096. 1 hit.
PROSITEi PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiECI1_HUMAN
AccessioniPrimary (citable) accession number: P42126
Secondary accession number(s): A8K512
, Q13290, Q7Z2L6, Q7Z2L7, Q9BUB8, Q9BW05, Q9UDG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3