ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9DCS3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name MECR_MOUSE
Primary accession number Q9DCS3
Secondary accession number Q99L39
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on April 26, 2005 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 54)
Name and origin of the protein
Protein name Trans-2-enoyl-CoA reductase, mitochondrial [Precursor]
Synonym EC 1.3.1.38
Gene name
Name: Mecr
Synonyms: Nrbf1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK002533; BAB22169.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003864; AAH03864.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_079573.1; -.
UniGene Mm.192706
3D structure databases
HSSP Q8WZM3; 1GU7. [HSSP ENTRY / PDB]
SMR Q9DCS3; 38-373.
ModBase Q9DCS3.
PTM databases
PhosphoSite Q9DCS3; -.
Organism-specific databases
MGI MGI:1349441; Mecr.
Gene expression databases
ArrayExpress Q9DCS3; -.
CleanEx MM_MECR; -.
GermOnline ENSMUSG00000028910; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0019166; Molecular function: trans-2-enoyl-CoA reductase (NADPH) activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
Proteomics databases
PRIDE Q9DCS3; -.
Genome annotation databases
Ensembl ENSMUSG00000028910; Mus musculus. [Contig view]
GeneID 26922; -.
KEGG mmu:26922; -.
Phylogenomic databases
HOGENOM Q9DCS3; -.
HOVERGEN Q9DCS3; -.
Other
NextBio 304813; -.
SOURCE Mecr; Mus musculus.
ProtoNet Q9DCS3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
TRANSIT   1    53  53     Mitochondrion (Potential). 
CHAIN   54   373  320     Trans-2-enoyl-CoA reductase, mitochondrial. PRO_0000000889
CONFLICT   69    69        E -> K (in Ref. 1; BAB22169). 
Sequence information
Length: 373 AA [This is the length of the unprocessed precursor] Molecular weight: 40343 Da [This is the MW of the unprocessed precursor] CRC64: EBA9A61A46386AEE [This is a checksum on the sequence]
        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 

Q9DCS3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!