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 Q9BV79


[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_HUMAN
Primary accession number Q9BV79
Secondary accession numbers Q5SYU0 Q5SYU1 Q5SYU2 Q6IBU9 Q9Y373
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 63)
Name and origin of the protein
Protein name Trans-2-enoyl-CoA reductase, mitochondrial [Precursor]
Synonyms HsNrbf-1
EC 1.3.1.38
NRBF-1
Gene name
Name: MECR
Synonyms: NBRF1
ORFNames: CGI-63
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.10.5.703; PubMed=10810093 [NCBI, ExPASy, EBI, Israel, Japan]
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-96.
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[5]
ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M302851200; PubMed=12654921 [NCBI, ExPASy, EBI, Israel, Japan]
Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.;
"Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II.";
J. Biol. Chem. 278:20154-20161(2003).
[6]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 40-373.
Structural genomics consortium (SGC);
"The structure of human mitochondrial 2-enoyl thioester reductase (CGI-63).";
Submitted (JUN-2005) to the PDB data bank.
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
AF151821; AAD34058.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456703; CAG32984.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590729; CAI14329.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590729; CAI14330.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001419; AAH01419.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Hs.183646
3D structure databases
PDB
1ZSY; X-ray; 1.75 A; A=40-373.[ExPASy / RCSB / EBI]
PDBsum 1ZSY; -.
ModBase Q9BV79.
Organism-specific databases
H-InvDB HIX0000345; -.
HGNC HGNC:19691; MECR.
GenAtlas MECR.
MIM 608205; gene. [NCBI / EBI]
PharmGKB PA142671471; -.
GeneCards Q9BV79.
Gene expression databases
ArrayExpress Q9BV79; -.
CleanEx HS_MECR; -.
GermOnline ENSG00000116353; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0019166; Molecular function: trans-2-enoyl-CoA reductase (NADPH) activity (inferred from direct assay from UniProtKB).
GO:0006631; Biological process: fatty acid metabolic process (inferred from direct assay from UniProtKB).
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.
BLOCKS Q9BV79.
Genome annotation databases
Ensembl ENSG00000116353; Homo sapiens. [Contig view]
Phylogenomic databases
HOGENOM Q9BV79; -.
HOVERGEN Q9BV79; -.
Other
SOURCE MECR; Homo sapiens.
ProtoNet Q9BV79.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; Oxidoreductase; Polymorphism; 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_0000000888
VARIANT   96    96  1     L -> F (in dbSNP:rs1128400 [NCBI]). VAR_027935 [3D]
CONFLICT   45    46        AL -> GV (in Ref. 1; AAD34058). 
CONFLICT   373   373        M -> I (in Ref. 2; CAG32984). 
STRAND   43    52  10      
HELIX   54    57  4      
STRAND   58    63  6      
STRAND   72    81  10      
HELIX   84    91  8      
STRAND   100   103  4      
STRAND   109   115  7      
STRAND   127   133  7      
STRAND   138   145  8      
HELIX   146   148  3      
STRAND   149   152  4      
STRAND   154   156  3      
HELIX   158   163  6      
HELIX   167   177  11      
STRAND   186   191  6      
HELIX   195   207  13      
STRAND   210   215  6      
HELIX   221   230  10      
STRAND   234   238  5      
HELIX   239   243  5      
HELIX   245   249  5      
STRAND   252   254  3      
STRAND   258   264  7      
HELIX   266   273  8      
STRAND   281   284  4      
STRAND   293   295  3      
HELIX   297   302  6      
STRAND   306   309  4      
HELIX   312   318  7      
HELIX   321   336  16      
STRAND   345   349  5      
HELIX   350   352  3      
HELIX   353   360  8      
STRAND   362   364  3      
STRAND   366   372  7      
Sequence information
Length: 373 AA [This is the length of the unprocessed precursor] Molecular weight: 40428 Da [This is the MW of the unprocessed precursor] CRC64: 591758FA0D57CBA3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH HGDPAKVVEL 

        70         80         90        100        110        120 
KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGLLPEL PAVGGNEGVA QVVAVGSNVT 

       130        140        150        160        170        180 
GLKPGDWVIP ANAGLGTWRT EAVFSEEALI QVPSDIPLQS AATLGVNPCT AYRMLMDFEQ 

       190        200        210        220        230        240 
LQPGDSVIQN ASNSGVGQAV IQIAAALGLR TINVVRDRPD IQKLSDRLKS LGAEHVITEE 

       250        260        270        280        290        300 
ELRRPEMKNF FKDMPQPRLA LNCVGGKSST ELLRQLARGG TMVTYGGMAK QPVVASVSLL 

       310        320        330        340        350        360 
IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSQVPL QDYQSALEAS 

       370 
MKPFISSKQI LTM 

Q9BV79 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 ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!