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Reviewed, UniProtKB/Swiss-Prot Q7YS70 (MECR_BOVIN)

Last modified November 25, 2008. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Trans-2-enoyl-CoA reductase, mitochondrial
    EC=1.3.1.38
Alternative name(s):
    BtNrbf-1
      Short name=NRBF-1
Gene names
Name: MECR
Synonyms: NBRF1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids.

Catalytic activity

Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA + NADPH.

Subunit structure

Homodimer.

Subcellular location

MitochondrionBy similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords

   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion Ref.1

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functiontrans-2-enoyl-CoA reductase (NADPH) activity Ref.1

Inferred from direct assay. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion Potential
Chain54 – 373320Trans-2-enoyl-CoA reductase, mitochondrial
PRO_0000000887

Sequences

Sequence LengthMass (Da)Tools
Q7YS70-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7921122C7735A95D

FASTA37340,275
        10         20         30         40         50         60 
MWVCGALCRT RAPAQLGQRL LPESRRRRPA SASFSASAEP SRVRALVYGH HGDPAKVVEL 

        70         80         90        100        110        120 
KNLELAAVGG SHVHVKMLAA PINPSDINMI QGNYGLLPQL PAVGGNEGVG QVVAVGSGVT 

       130        140        150        160        170        180 
GVKPGDWVIP ANPGLGTWRT EAVFGEEELI TVPSDIPLQS AATLGVNPCT AYRMLVDFER 

       190        200        210        220        230        240 
LRPRDSIIQN ASNSGVGQAV IQIAAARGLR TINVLRDTPD LQKLTDTLKN LGANHVVTEE 

       250        260        270        280        290        300 
ELRKPEMKSF FKDVPQPRLA LNCVGGKSST ELLRHLAPGG TMVTYGGMAK QPVIASVSQL 

       310        320        330        340        350        360 
IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSEVPL QDYLCALEAS 

       370 
TQPFVSSKQI LTM 

« Hide

References

[1]"Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II."
Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.
J. Biol. Chem. 278:20154-20161(2003) [PubMed: 12654921] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, ENZYME ACTIVITY, SUBUNIT.
Tissue: Heart.

Cross-references

Sequence databases

AY256973 mRNA. Translation: AAP45003.1.
RefSeqNP_858055.1.
UniGeneBt.18851

3D structure databases

HSSPHSSP built from PDB template 1H0K based on UniProtKB Q8WZM4.
SMRQ7YS70. Positions 40-373.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000017253. Bos taurus. [Contig view]
GeneID353301.
KEGGbta:353301.

Phylogenomic databases

HOVERGENQ7YS70.

Family and domain databases

InterProIPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMECR_BOVIN
AccessionPrimary (citable) accession number: Q7YS70
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: October 1, 2003
Last modified: November 25, 2008
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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