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P42126

- ECI1_HUMAN

UniProt

P42126 - ECI1_HUMAN

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
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiP42126.
    BgeeiP42126.
    CleanExiHS_DCI.
    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 – 527
    Turni53 – 564
    Beta strandi57 – 626
    Turni65 – 673
    Helixi72 – 8716
    Beta strandi93 – 1008
    Beta strandi102 – 1043
    Helixi110 – 1134
    Helixi118 – 13619
    Beta strandi139 – 1468
    Beta strandi148 – 1503
    Helixi152 – 1587
    Beta strandi161 – 1677
    Helixi178 – 1814
    Helixi187 – 19711
    Helixi199 – 20810
    Helixi214 – 2196
    Beta strandi222 – 2276
    Helixi229 – 2313
    Helixi232 – 24413
    Helixi248 – 26720
    Helixi270 – 28112
    Helixi284 – 2907

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MALVASVRVP ARVLLRAGAR LPGAALGRTE RAAGGGDGAR RFGSQRVLVE    50
    PDAGAGVAVM KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR 100
    PGVFSAGLDL TEMCGRSPAH YAGYWKAVQE LWLRLYQSNL VLVSAINGAC 150
    PAGGCLVALT CDYRILADNP RYCIGLNETQ LGIIAPFWLK DTLENTIGHR 200
    AAERALQLGL LFPPAEALQV GIVDQVVPEE QVQSTALSAI AQWMAIPDHA 250
    RQLTKAMMRK ATASRLVTQR DADVQNFVSF ISKDSIQKSL QMYLERLKEE 300
    KG 302
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 GC16M002299.
    HGNCi HGNC:2703. ECI1.
    HPAi HPA041746.
    HPA043227.
    MIMi 600305. gene.
    neXtProti NX_P42126.
    PharmGKBi PA27173.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1024.
    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

    ArrayExpressi P42126.
    Bgeei P42126.
    CleanExi HS_DCI.
    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

    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: October 1, 2014
    This is version 146 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