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Q9BV79 (MECR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Alternative name(s):
Nuclear receptor-binding factor 1
Short name=HsNrbf-1
Short name=NRBF-1
Gene names
Name:MECR
Synonyms:NBRF1
ORF Names:CGI-63
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.10

Catalytic activity

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH. Ref.7 Ref.10

Subunit structure

Homodimer. Ref.7 Ref.10

Subcellular location

Mitochondrion Ref.7.

Tissue specificity

Highly expressed in skeletal and heart muscle. Expressed at lower level in placenta, liver, kidney and pancreas. Weakly or not expressed in lung. Ref.7

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=37 µM for trans-2-hexenoyl-CoA (Ref.7) Ref.7 Ref.10

KM=7.1 µM for trans-2-decenoyl-CoA (Ref.7)

KM=3.6 µM for trans-dodec-2-enoyl-CoA (Ref.10)

KM=10.4 µM for trans-dec-2-enoyl-CoA (Ref.10)

KM=10.2 µM for trans-oct-2-enoyl-CoA (Ref.10)

KM=4.3 µM for trans-tetradec-2-enoyl-CoA (Ref.10)

KM=6.6 µM for trans-hexadec-2-enoyl-CoA (Ref.10)

KM=63.5 µM for trans-hex-2-enoyl-CoA (Ref.10)

Sequence caution

The sequence AAD34058.1 differs from that shown. Reason: Frameshift at positions 14 and 19.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BV79-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BV79-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion Potential
Chain54 – 373320Trans-2-enoyl-CoA reductase, mitochondrial
PRO_0000000888

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 By similarity
Modified residue611N6-succinyllysine; alternate By similarity
Modified residue2521N6-acetyllysine; alternate By similarity
Modified residue2521N6-succinyllysine; alternate By similarity
Modified residue2671N6-acetyllysine; alternate By similarity
Modified residue2671N6-succinyllysine; alternate By similarity
Modified residue3161N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 7676Missing in isoform 2.
VSP_041131
Natural variant961F → L. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs1128400 [ dbSNP | Ensembl ].
VAR_027935
Natural variant2271R → K.
Corresponds to variant rs11544658 [ dbSNP | Ensembl ].
VAR_055486
Natural variant2581R → L.
Corresponds to variant rs34835902 [ dbSNP | Ensembl ].
VAR_055487

Experimental info

Mutagenesis851S → A: Reduces catalytic activity by 68%. Ref.10
Mutagenesis941Y → F: Reduces catalytic activity by 95%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. Ref.10
Mutagenesis1291I → M: Strongly increases activity with trans-oct-2-enoyl-CoA. No effect on activity with trans-tetradec-2-enoyl-CoA. Decreases activity with trans-hexadec-2-enoyl-CoA by 20%. Ref.10
Mutagenesis1651G → S: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 73%. Decreases activity with trans-hexadec-2-enoyl-CoA by 80%. Ref.10
Mutagenesis1701T → A: Reduces catalytic activity by 69%. Ref.10
Mutagenesis3111W → A: Reduces catalytic activity by 98%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. Ref.10
Mutagenesis3111W → L: Reduces catalytic activity by 87%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. Ref.10
Mutagenesis3241F → Y: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 25%. Decreases activity with trans-hexadec-2-enoyl-CoA by 68%. Ref.10
Sequence conflict45 – 462AL → GV in AAD34058. Ref.1
Sequence conflict3731M → I in CAG32984. Ref.2

Secondary structure

................................................................. 373
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: DB13F6B0ED54A823

FASTA37340,462
        10         20         30         40         50         60 
MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH HGDPAKVVEL 

        70         80         90        100        110        120 
KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGFLPEL 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 

« Hide

Isoform 2 [UniParc].

Checksum: 1A27621E27728B76
Show »

FASTA29732,228

References

« Hide 'large scale' references
[1]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LEU-96.
Tissue: Hippocampus.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96.
[4]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-96.
[6]"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] (ISOFORM 1), VARIANT LEU-96.
Tissue: Placenta.
[7]"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] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The structure of human mitochondrial 2-enoyl thioester reductase (CGI-63)."
Structural genomics consortium (SGC)
Submitted (JUN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 40-373.
[10]"Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties."
Chen Z.J., Pudas R., Sharma S., Smart O.S., Juffer A.H., Hiltunen J.K., Wierenga R.K., Haapalainen A.M.
J. Mol. Biol. 379:830-844(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 31-373, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-85; TYR-94; ILE-129; GLY-165; THR-170; TRP-311 AND PHE-324.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF151821 mRNA. Translation: AAD34058.1. Frameshift.
AK095099 mRNA. Translation: BAG52984.1.
CR456703 mRNA. Translation: CAG32984.1.
AL590729 Genomic DNA. Translation: CAI14329.1.
AL590729 Genomic DNA. Translation: CAI14330.1.
CH471059 Genomic DNA. Translation: EAX07655.1.
BC001419 mRNA. Translation: AAH01419.1.
RefSeqNP_001019903.2. NM_001024732.2.
NP_057095.3. NM_016011.3.
XP_005245943.1. XM_005245886.1.
XP_005245944.1. XM_005245887.1.
XP_005245945.1. XM_005245888.1.
XP_005245946.1. XM_005245889.1.
UniGeneHs.183646.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSYX-ray1.75A40-373[»]
2VCYX-ray2.41A/B31-373[»]
ProteinModelPortalQ9BV79.
SMRQ9BV79. Positions 40-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119291. 7 interactions.
STRING9606.ENSP00000263702.

PTM databases

PhosphoSiteQ9BV79.

Polymorphism databases

DMDM334302832.

Proteomic databases

PaxDbQ9BV79.
PRIDEQ9BV79.

Protocols and materials databases

DNASU51102.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263702; ENSP00000263702; ENSG00000116353. [Q9BV79-1]
ENST00000373791; ENSP00000362896; ENSG00000116353. [Q9BV79-2]
GeneID51102.
KEGGhsa:51102.
UCSCuc001brp.1. human. [Q9BV79-1]

Organism-specific databases

CTD51102.
GeneCardsGC01M029519.
HGNCHGNC:19691. MECR.
HPAHPA022018.
HPA022030.
HPA028740.
MIM608205. gene.
neXtProtNX_Q9BV79.
PharmGKBPA142671471.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0604.
HOVERGENHBG052446.
InParanoidQ9BV79.
KOK07512.
OMACSTLWRV.
OrthoDBEOG78M024.
PhylomeDBQ9BV79.
TreeFamTF312886.

Enzyme and pathway databases

SABIO-RKQ9BV79.

Gene expression databases

ArrayExpressQ9BV79.
BgeeQ9BV79.
CleanExHS_MECR.
GenevestigatorQ9BV79.

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

EvolutionaryTraceQ9BV79.
GeneWikiMECR.
GenomeRNAi51102.
NextBio53817.
PROQ9BV79.
SOURCESearch...

Entry information

Entry nameMECR_HUMAN
AccessionPrimary (citable) accession number: Q9BV79
Secondary accession number(s): B3KT72 expand/collapse secondary AC list , Q5SYU0, Q5SYU1, Q5SYU2, Q6IBU9, Q9Y373
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 31, 2011
Last modified: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM