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Q9DCS3 (MECR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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

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) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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

Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion Potential
Chain54 – 373320Trans-2-enoyl-CoA reductase, mitochondrial
PRO_0000000889

Regions

Nucleotide binding193 – 1964NADP By similarity
Nucleotide binding216 – 2183NADP By similarity
Nucleotide binding285 – 2884NADP By similarity
Nucleotide binding310 – 3123NADP By similarity

Sites

Binding site1671NADP By similarity
Binding site3681NADP By similarity

Amino acid modifications

Modified residue611N6-acetyllysine; alternate Ref.4
Modified residue611N6-succinyllysine; alternate Ref.3
Modified residue2521N6-acetyllysine; alternate Ref.4
Modified residue2521N6-succinyllysine; alternate Ref.3
Modified residue2671N6-acetyllysine; alternate Ref.3
Modified residue2671N6-succinyllysine; alternate Ref.3
Modified residue3161N6-succinyllysine Ref.3

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-252; LYS-267 AND LYS-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[4]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61 AND LYS-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002533 mRNA. Translation: BAB22169.1.
BC003864 mRNA. Translation: AAH03864.1.
CCDSCCDS18715.1.
RefSeqNP_079573.2. NM_025297.2.
UniGeneMm.192706.

3D structure databases

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

Protein-protein interaction databases

IntActQ9DCS3. 2 interactions.
MINTMINT-4128719.

PTM databases

PhosphoSiteQ9DCS3.

Proteomic databases

MaxQBQ9DCS3.
PaxDbQ9DCS3.
PRIDEQ9DCS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030742; ENSMUSP00000030742; ENSMUSG00000028910.
GeneID26922.
KEGGmmu:26922.
UCSCuc008vae.2. mouse.

Organism-specific databases

CTD51102.
MGIMGI:1349441. Mecr.

Phylogenomic databases

eggNOGCOG0604.
GeneTreeENSGT00740000115589.
HOGENOMHOG000294683.
HOVERGENHBG052446.
InParanoidQ9DCS3.
KOK07512.
OMACSTLWRV.
OrthoDBEOG78M024.
PhylomeDBQ9DCS3.
TreeFamTF312886.

Gene expression databases

ArrayExpressQ9DCS3.
BgeeQ9DCS3.
CleanExMM_MECR.
GenevestigatorQ9DCS3.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
ProtoNetSearch...

Other

NextBio304813.
PROQ9DCS3.
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: July 9, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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