Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30084 (ECHM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ECHS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homohexamer; dimer of trimers. Ref.11

Subcellular location

Mitochondrion matrix.

Tissue specificity

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

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Molecular functionLyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Traceable author statement PubMed 16130169. Source: UniProtKB

   Molecular_functionenoyl-CoA hydratase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAT3P407633EBI-719602,EBI-518675
Stat3P422273EBI-719602,EBI-602878From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Ref.6
Chain28 – 290263Enoyl-CoA hydratase, mitochondrial
PRO_0000007411

Regions

Region98 – 1014Substrate binding

Sites

Binding site1411Substrate; via amide nitrogen
Site1641Important for catalytic activity By similarity

Amino acid modifications

Modified residue1011N6-acetyllysine; alternate By similarity
Modified residue1011N6-succinyllysine; alternate By similarity
Modified residue1151N6-acetyllysine; alternate By similarity
Modified residue1151N6-succinyllysine; alternate By similarity
Modified residue1181N6-acetyllysine Ref.9
Modified residue2041N6-succinyllysine By similarity
Modified residue2111N6-acetyllysine By similarity

Natural variations

Natural variant111V → A. Ref.1 Ref.2
Corresponds to variant rs10466126 [ dbSNP | Ensembl ].
VAR_022273
Natural variant751T → I. Ref.1 Ref.2 Ref.3 Ref.5 Ref.8
Corresponds to variant rs1049951 [ dbSNP | Ensembl ].
VAR_022274

Experimental info

Sequence conflict841A → G in BAA03001. Ref.1
Sequence conflict1211D → G in BAA03001. Ref.1
Sequence conflict1381A → P in BAA03001. Ref.1
Sequence conflict188 – 1892AM → EL in BAA03001. Ref.1
Sequence conflict1971R → A in BAA03001. Ref.1

Secondary structure

..................................................... 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30084 [UniParc].

Last modified April 26, 2005. Version 4.
Checksum: 0CCD0C7F891B1704

FASTA29031,387
        10         20         30         40         50         60 
MAALRVLLSC VRGPLRPPVR CPAWRPFASG ANFEYIIAEK RGKNNTVGLI QLNRPKALNA 

        70         80         90        100        110        120 
LCDGLIDELN QALKTFEEDP AVGAIVLTGG DKAFAAGADI KEMQNLSFQD CYSSKFLKHW 

       130        140        150        160        170        180 
DHLTQVKKPV IAAVNGYAFG GGCELAMMCD IIYAGEKAQF AQPEILIGTI PGAGGTQRLT 

       190        200        210        220        230        240 
RAVGKSLAME MVLTGDRISA QDAKQAGLVS KICPVETLVE EAIQCAEKIA SNSKIVVAMA 

       250        260        270        280        290 
KESVNAAFEM TLTEGSKLEK KLFYSTFATD DRKEGMTAFV EKRKANFKDQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13900 mRNA. Translation: BAA03001.1.
X98126 expand/collapse EMBL AC list , X98127, X98128, X98129 Genomic DNA. Translation: CAA66808.1.
BT007123 mRNA. Translation: AAP35787.1.
AL360181 Genomic DNA. Translation: CAH70286.1.
BC008906 mRNA. Translation: AAH08906.1.
RefSeqNP_004083.3. NM_004092.3.
UniGeneHs.76394.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HW5X-ray2.55A/B/C/D/E/F28-290[»]
ProteinModelPortalP30084.
SMRP30084. Positions 31-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108221. 30 interactions.
IntActP30084. 16 interactions.
MINTMINT-1401929.
STRING9606.ENSP00000357535.

PTM databases

PhosphoSiteP30084.

Polymorphism databases

DMDM62906863.

2D gel databases

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

Proteomic databases

PaxDbP30084.
PeptideAtlasP30084.
PRIDEP30084.

Protocols and materials databases

DNASU1892.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368547; ENSP00000357535; ENSG00000127884.
GeneID1892.
KEGGhsa:1892.
UCSCuc001lmu.3. human.

Organism-specific databases

CTD1892.
GeneCardsGC10M135175.
HGNCHGNC:3151. ECHS1.
HPACAB003783.
HPA021995.
HPA022476.
MIM602292. gene.
neXtProtNX_P30084.
PharmGKBPA27597.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1024.
HOGENOMHOG000027939.
HOVERGENHBG010157.
InParanoidP30084.
KOK07511.
OMANVGFIQL.
OrthoDBEOG7N63NC.
PhylomeDBP30084.
TreeFamTF314497.

Enzyme and pathway databases

BioCycMetaCyc:HS05132-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP30084.
UniPathwayUPA00659.

Gene expression databases

BgeeP30084.
CleanExHS_ECHS1.
GenevestigatorP30084.

Family and domain databases

InterProIPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSECHS1. human.
EvolutionaryTraceP30084.
GeneWikiECHS1.
GenomeRNAi1892.
NextBio7715.
PROP30084.
SOURCESearch...

Entry information

Entry nameECHM_HUMAN
AccessionPrimary (citable) accession number: P30084
Secondary accession number(s): O00739, Q5VWY1, Q96H54
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 151 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM