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P30084

- ECHM_HUMAN

UniProt

P30084 - ECHM_HUMAN

Protein

Enoyl-CoA hydratase, mitochondrial

Gene

ECHS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.

    Catalytic activityi

    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei141 – 1411Substrate; via amide nitrogen
    Sitei164 – 1641Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. enoyl-CoA hydratase activity Source: Reactome
    2. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05132-MONOMER.
    ReactomeiREACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
    SABIO-RKP30084.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-CoA hydratase, mitochondrial (EC:4.2.1.17)
    Alternative name(s):
    Enoyl-CoA hydratase 1
    Short-chain enoyl-CoA hydratase
    Short name:
    SCEH
    Gene namesi
    Name:ECHS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:3151. ECHS1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27597.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727Mitochondrion1 PublicationAdd
    BLAST
    Chaini28 – 290263Enoyl-CoA hydratase, mitochondrialPRO_0000007411Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011N6-acetyllysine; alternateBy similarity
    Modified residuei101 – 1011N6-succinyllysine; alternateBy similarity
    Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
    Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
    Modified residuei118 – 1181N6-acetyllysine1 Publication
    Modified residuei204 – 2041N6-succinyllysineBy similarity
    Modified residuei211 – 2111N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30084.
    PaxDbiP30084.
    PeptideAtlasiP30084.
    PRIDEiP30084.

    2D gel databases

    DOSAC-COBS-2DPAGEP30084.
    REPRODUCTION-2DPAGEIPI00024993.
    P30084.
    SWISS-2DPAGEP30084.
    UCD-2DPAGEP30084.

    PTM databases

    PhosphoSiteiP30084.

    Expressioni

    Tissue specificityi

    Liver, fibroblast, muscle. Barely detectable in spleen and kidney.

    Gene expression databases

    BgeeiP30084.
    CleanExiHS_ECHS1.
    GenevestigatoriP30084.

    Organism-specific databases

    HPAiCAB003783.
    HPA021995.
    HPA022476.

    Interactioni

    Subunit structurei

    Homohexamer; dimer of trimers.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-719602,EBI-5323863
    STAT3P407633EBI-719602,EBI-518675
    Stat3P422273EBI-719602,EBI-602878From a different organism.

    Protein-protein interaction databases

    BioGridi108221. 31 interactions.
    IntActiP30084. 18 interactions.
    MINTiMINT-1401929.
    STRINGi9606.ENSP00000357535.

    Structurei

    Secondary structure

    1
    290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 429
    Helixi43 – 453
    Beta strandi47 – 526
    Helixi55 – 573
    Helixi63 – 7816
    Beta strandi84 – 885
    Beta strandi91 – 955
    Helixi100 – 1034
    Helixi108 – 1136
    Turni114 – 1174
    Helixi119 – 1257
    Beta strandi130 – 1345
    Beta strandi136 – 1394
    Helixi141 – 1477
    Beta strandi149 – 1557
    Beta strandi159 – 1613
    Helixi163 – 1675
    Beta strandi172 – 1743
    Turni175 – 1773
    Helixi178 – 1836
    Helixi185 – 19410
    Helixi200 – 2056
    Beta strandi210 – 2134
    Turni215 – 2173
    Helixi218 – 23114
    Helixi234 – 24512
    Helixi246 – 2483
    Helixi252 – 26615
    Helixi270 – 28011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HW5X-ray2.55A/B/C/D/E/F28-290[»]
    ProteinModelPortaliP30084.
    SMRiP30084. Positions 31-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30084.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1014Substrate binding

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1024.
    HOGENOMiHOG000027939.
    HOVERGENiHBG010157.
    InParanoidiP30084.
    KOiK07511.
    OMAiHWDQLTR.
    OrthoDBiEOG7N63NC.
    PhylomeDBiP30084.
    TreeFamiTF314497.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    P30084-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALRVLLSC VRGPLRPPVR CPAWRPFASG ANFEYIIAEK RGKNNTVGLI    50
    QLNRPKALNA LCDGLIDELN QALKTFEEDP AVGAIVLTGG DKAFAAGADI 100
    KEMQNLSFQD CYSSKFLKHW DHLTQVKKPV IAAVNGYAFG GGCELAMMCD 150
    IIYAGEKAQF AQPEILIGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA 200
    QDAKQAGLVS KICPVETLVE EAIQCAEKIA SNSKIVVAMA KESVNAAFEM 250
    TLTEGSKLEK KLFYSTFATD DRKEGMTAFV EKRKANFKDQ 290
    Length:290
    Mass (Da):31,387
    Last modified:April 26, 2005 - v4
    Checksum:i0CCD0C7F891B1704
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841A → G in BAA03001. (PubMed:8012501)Curated
    Sequence conflicti121 – 1211D → G in BAA03001. (PubMed:8012501)Curated
    Sequence conflicti138 – 1381A → P in BAA03001. (PubMed:8012501)Curated
    Sequence conflicti188 – 1892AM → EL in BAA03001. (PubMed:8012501)Curated
    Sequence conflicti197 – 1971R → A in BAA03001. (PubMed:8012501)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111V → A.2 Publications
    Corresponds to variant rs10466126 [ dbSNP | Ensembl ].
    VAR_022273
    Natural varianti75 – 751T → I.5 Publications
    Corresponds to variant rs1049951 [ dbSNP | Ensembl ].
    VAR_022274

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13900 mRNA. Translation: BAA03001.1.
    X98126
    , X98127, X98128, X98129 Genomic DNA. Translation: CAA66808.1.
    BT007123 mRNA. Translation: AAP35787.1.
    AL360181 Genomic DNA. Translation: CAH70286.1.
    BC008906 mRNA. Translation: AAH08906.1.
    CCDSiCCDS7681.1.
    RefSeqiNP_004083.3. NM_004092.3.
    UniGeneiHs.76394.

    Genome annotation databases

    EnsembliENST00000368547; ENSP00000357535; ENSG00000127884.
    GeneIDi1892.
    KEGGihsa:1892.
    UCSCiuc001lmu.3. human.

    Polymorphism databases

    DMDMi62906863.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13900 mRNA. Translation: BAA03001.1 .
    X98126
    , X98127 , X98128 , X98129 Genomic DNA. Translation: CAA66808.1 .
    BT007123 mRNA. Translation: AAP35787.1 .
    AL360181 Genomic DNA. Translation: CAH70286.1 .
    BC008906 mRNA. Translation: AAH08906.1 .
    CCDSi CCDS7681.1.
    RefSeqi NP_004083.3. NM_004092.3.
    UniGenei Hs.76394.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HW5 X-ray 2.55 A/B/C/D/E/F 28-290 [» ]
    ProteinModelPortali P30084.
    SMRi P30084. Positions 31-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108221. 31 interactions.
    IntActi P30084. 18 interactions.
    MINTi MINT-1401929.
    STRINGi 9606.ENSP00000357535.

    PTM databases

    PhosphoSitei P30084.

    Polymorphism databases

    DMDMi 62906863.

    2D gel databases

    DOSAC-COBS-2DPAGE P30084.
    REPRODUCTION-2DPAGE IPI00024993.
    P30084.
    SWISS-2DPAGE P30084.
    UCD-2DPAGE P30084.

    Proteomic databases

    MaxQBi P30084.
    PaxDbi P30084.
    PeptideAtlasi P30084.
    PRIDEi P30084.

    Protocols and materials databases

    DNASUi 1892.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368547 ; ENSP00000357535 ; ENSG00000127884 .
    GeneIDi 1892.
    KEGGi hsa:1892.
    UCSCi uc001lmu.3. human.

    Organism-specific databases

    CTDi 1892.
    GeneCardsi GC10M135175.
    HGNCi HGNC:3151. ECHS1.
    HPAi CAB003783.
    HPA021995.
    HPA022476.
    MIMi 602292. gene.
    neXtProti NX_P30084.
    PharmGKBi PA27597.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1024.
    HOGENOMi HOG000027939.
    HOVERGENi HBG010157.
    InParanoidi P30084.
    KOi K07511.
    OMAi HWDQLTR.
    OrthoDBi EOG7N63NC.
    PhylomeDBi P30084.
    TreeFami TF314497.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:HS05132-MONOMER.
    Reactomei REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
    SABIO-RK P30084.

    Miscellaneous databases

    ChiTaRSi ECHS1. human.
    EvolutionaryTracei P30084.
    GeneWikii ECHS1.
    GenomeRNAii 1892.
    NextBioi 7715.
    PROi P30084.
    SOURCEi Search...

    Gene expression databases

    Bgeei P30084.
    CleanExi HS_ECHS1.
    Genevestigatori P30084.

    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. "Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase."
      Kanazawa M., Ohtake A., Abe H., Yamamoto S., Satoh Y., Takayanagi M., Niimi H., Mori M., Hashimoto T.
      Enzyme Protein 47:9-13(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-11 AND ILE-75.
      Tissue: Liver.
    2. "Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3."
      Janssen U., Davis E.M., le Beau M.M., Stoffel W.
      Genomics 40:470-475(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-11 AND ILE-75.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-75.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      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], VARIANT ILE-75.
      Tissue: Placenta.
    6. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-37.
      Tissue: Liver.
    7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 44-56; 102-115; 158-178; 186-197; 242-257 AND 262-273, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
      Hubbard M.J., McHugh N.J.
      Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 57-63; 75-92 AND 158-178, VARIANT ILE-75, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Liver.
    9. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "The crystal structure of human enoyl-coenzyme A (CoA) hydratase short chain 1, ECHS1."
      Structural genomics consortium (SGC)
      Submitted (AUG-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 24-290 IN COMPLEX WITH CROTONYL COENZYME A, SUBUNIT.

    Entry informationi

    Entry nameiECHM_HUMAN
    AccessioniPrimary (citable) accession number: P30084
    Secondary accession number(s): O00739, Q5VWY1, Q96H54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 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 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3