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Q9DCS3 (MECR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trans-2-enoyl-CoA reductase, mitochondrial
EC=1.3.1.38
Gene names
Name:Mecr
Synonyms:Nrbf1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By 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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

trans-2-enoyl-CoA reductase (NADPH) activity

Inferred from electronic annotation. Source: EC

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_0000000889

Experimental info

Sequence conflict691E → K in BAB22169. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DCS3 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: EBA9A61A46386AEE

FASTA37340,343
        10         20         30         40         50         60 
MLVSQRVTGA RARAPQLAGL LEAWYRHGRT TSSYSALSEP SRVRALVYGN HGDPAKVVQL 

        70         80         90        100        110        120 
KNLELTAVEG SDVHVRMLAA PINPSDINMI QGNYGLLPKL PAVGGNEGVG QVIAVGSSVS 

       130        140        150        160        170        180 
ALKPGDWVIP ANAGLGTWRT EAVFSEEALI GIPKDIPLQS AATLGVNPCT AYRMLVDFEQ 

       190        200        210        220        230        240 
LQPGDSVIQN ASNSGVGQAV IQIASALRLK TINVVRDRPD IKKLTDRLKD LGADYVLTEE 

       250        260        270        280        290        300 
ELRMPETKTI FKDLPLPRLA LNCVGGKSST ELLRHLAPGG TMVTYGGMAK QPVTASVSLL 

       310        320        330        340        350        360 
IFKDLKLRGF WLSQWKKNHS PDEFKELILT LCNLIRQGRL TAPSCSEVPL QGYQQALEAS 

       370 
MKPFVSSKQI LTM

« Hide

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.
Tissue: Kidney.
[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: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK002533 mRNA. Translation: BAB22169.1.
BC003864 mRNA. Translation: AAH03864.1.
IPIIPI00121276.
RefSeqNP_079573.2. NM_025297.2.
UniGeneMm.192706.

3D structure databases

ProteinModelPortalQ9DCS3.
SMRQ9DCS3. Positions 38-373.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9DCS3. 1 interaction.
STRINGQ9DCS3.

Proteomic databases

PRIDEQ9DCS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030742; ENSMUSP00000030742; ENSMUSG00000028910.
GeneID26922.
KEGGmmu:26922.

Organism-specific databases

CTD51102.
MGIMGI:1349441. Mecr.

Phylogenomic databases

GeneTreeENSGT00550000074938.
HOGENOMHBG753318.
HOVERGENHBG052446.
InParanoidQ9DCS3.
OMARGFWMTR.
OrthoDBEOG43N7DB.
PhylomeDBQ9DCS3.

Gene expression databases

ArrayExpressQ9DCS3.
BgeeQ9DCS3.
CleanExMM_MECR.
GenevestigatorQ9DCS3.
GermOnlineENSMUSG00000028910. Mus musculus.

Family and domain databases

InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK07512.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
ProtoNetSearch...

Other

NextBio304813.
SOURCESearch...

Entry information

Entry nameMECR_MOUSE
AccessionPrimary (citable) accession number: Q9DCS3
Secondary accession number(s): Q99L39
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: December 14, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents