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Reviewed, UniProtKB/Swiss-Prot Q8BH95 (ECHM_MOUSE)

Last modified January 19, 2010. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Enoyl-CoA hydratase, mitochondrial
    EC=4.2.1.17
Alternative name(s):
    Short chain enoyl-CoA hydratase
      Short name=SCEH
    Enoyl-CoA hydratase 1
Gene names
Name: Echs1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

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

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General annotation (Comments)

Function

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

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 By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Acetylation of Lys-101 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionLyase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionenoyl-CoA hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 290263Enoyl-CoA hydratase, mitochondrial
PRO_0000007412

Regions

Region98 – 1014Substrate binding By similarity

Sites

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

Amino acid modifications

Modified residue1011N6-acetyllysine Ref.4

Experimental info

Sequence conflict711Q → L in AAH02178. Ref.2
Sequence conflict1721G → R in AAH72658. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q8BH95-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3E51E529CE756C68

FASTA29031,474
        10         20         30         40         50         60 
MAALRALLPR ACSSLLSSVR CPELRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA 

        70         80         90        100        110        120 
LCNGLIEELN QALETFEQDP AVGAIVLTGG DKAFAAGADI KEMQNRTFQD CYSSKFLSHW 

       130        140        150        160        170        180 
DHITRVKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILLGTI PGAGGTQRLT 

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

       250        260        270        280        290 
KESVNAAFEM TLTEGNKLEK RLFYSTFATD DRREGMTAFV EKRKANFKDH

« Hide

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References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Liver and Thymus.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Mammary gland.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 116-125; 158-178 AND 274-282, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK040391 mRNA. Translation: BAC30583.1.
AK044954 mRNA. Translation: BAC32157.1.
AK088018 mRNA. Translation: BAC40099.1.
AK167404 mRNA. Translation: BAE39493.1.
BC002178 mRNA. Translation: AAH02178.1.
BC057971 mRNA. Translation: AAH57971.1.
BC072658 mRNA. Translation: AAH72658.1.
IPIIPI00454049.
RefSeqNP_444349.1.
UniGeneMm.24452

3D structure databases

SMRQ8BH95. Positions 31-290.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BH95.

PTM databases

PhosphoSiteQ8BH95.

2-D gel databases

REPRODUCTION-2DPAGEQ8BH95.

Proteomic databases

PRIDEQ8BH95.

Genome annotation databases

EnsemblENSMUST00000026538; ENSMUSP00000026538; ENSMUSG00000025465; Mus musculus. [Genome view]
GeneID93747.
KEGGmmu:93747.
NMPDRfig|10090.3.peg.17872.
UCSCuc009kgx.1. mouse.

Organism-specific databases

CTD93747.
MGIMGI:2136460. Echs1.

Phylogenomic databases

eggNOGroNOG08852.
HOGENOMHBG748731.
HOVERGENQ8BH95.
InParanoidQ8BH95.
OMAHTFQDCY.
OrthoDBEOG9JWXZS.
PhylomeDBQ8BH95.

Enzyme and pathway databases

BRENDA4.2.1.17. 244.

Gene expression databases

ArrayExpressQ8BH95.
BgeeQ8BH95.
GenevestigatorQ8BH95.
GermOnlineENSMUSG00000025465. Mus musculus.

Family and domain databases

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

Other Resources

NextBio351613.
SOURCESearch...

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Entry information

Entry nameECHM_MOUSE
AccessionPrimary (citable) accession number: Q8BH95
Secondary accession number(s): Q3TJK2 expand/collapse secondary AC list , Q6GQS2, Q6PEN1, Q99LX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2003
Last modified: January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents