Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Trans-2-enoyl-CoA reductase, mitochondrial

Gene

MECR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=37 µM for trans-2-hexenoyl-CoA2 Publications
  2. KM=7.1 µM for trans-2-decenoyl-CoA2 Publications
  3. KM=3.6 µM for trans-dodec-2-enoyl-CoA2 Publications
  4. KM=10.4 µM for trans-dec-2-enoyl-CoA2 Publications
  5. KM=10.2 µM for trans-oct-2-enoyl-CoA2 Publications
  6. KM=4.3 µM for trans-tetradec-2-enoyl-CoA2 Publications
  7. KM=6.6 µM for trans-hexadec-2-enoyl-CoA2 Publications
  8. KM=63.5 µM for trans-hex-2-enoyl-CoA2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei167NADPBy similarity1
    Binding sitei368NADPBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi193 – 196NADPBy similarity4
    Nucleotide bindingi216 – 218NADPBy similarity3
    Nucleotide bindingi285 – 288NADPBy similarity4
    Nucleotide bindingi310 – 312NADPBy similarity3

    GO - Molecular functioni

    • trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • fatty acid biosynthetic process Source: UniProtKB-KW
    • fatty acid metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciZFISH:HS04010-MONOMER.
    SABIO-RKQ9BV79.

    Chemistry databases

    SwissLipidsiSLP:000001054.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:MECR
    Synonyms:NBRF1
    ORF Names:CGI-63
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19691. MECR.

    Subcellular locationi

    Isoform 1 :
    Isoform 2 :

    GO - Cellular componenti

    • mitochondrion Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi85S → A: Reduces catalytic activity by 68%. 1 Publication1
    Mutagenesisi94Y → F: Reduces catalytic activity by 95%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication1
    Mutagenesisi129I → 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%. 1 Publication1
    Mutagenesisi165G → 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%. 1 Publication1
    Mutagenesisi170T → A: Reduces catalytic activity by 69%. 1 Publication1
    Mutagenesisi311W → A: Reduces catalytic activity by 98%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication1
    Mutagenesisi311W → L: Reduces catalytic activity by 87%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication1
    Mutagenesisi324F → 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%. 1 Publication1

    Organism-specific databases

    OpenTargetsiENSG00000116353.
    PharmGKBiPA142671471.

    Polymorphism and mutation databases

    DMDMi334302832.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 53MitochondrionSequence analysisAdd BLAST53
    ChainiPRO_000000088854 – 373Trans-2-enoyl-CoA reductase, mitochondrialAdd BLAST320

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei61N6-acetyllysine; alternateBy similarity1
    Modified residuei61N6-succinyllysine; alternateBy similarity1
    Modified residuei252N6-acetyllysine; alternateBy similarity1
    Modified residuei252N6-succinyllysine; alternateBy similarity1
    Modified residuei267N6-acetyllysine; alternateBy similarity1
    Modified residuei267N6-succinyllysine; alternateBy similarity1
    Modified residuei316N6-succinyllysineBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ9BV79.
    MaxQBiQ9BV79.
    PaxDbiQ9BV79.
    PeptideAtlasiQ9BV79.
    PRIDEiQ9BV79.

    PTM databases

    iPTMnetiQ9BV79.
    PhosphoSitePlusiQ9BV79.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal and heart muscle. Expressed at lower level in placenta, liver, kidney and pancreas. Weakly or not expressed in lung.1 Publication

    Gene expression databases

    BgeeiENSG00000116353.
    CleanExiHS_MECR.
    ExpressionAtlasiQ9BV79. baseline and differential.
    GenevisibleiQ9BV79. HS.

    Organism-specific databases

    HPAiHPA022018.
    HPA022030.
    HPA028740.

    Interactioni

    Subunit structurei

    Homodimer. Isoform 2 interacts with PPARA in the nucleus and increases its activity.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi119291. 14 interactors.
    IntActiQ9BV79. 2 interactors.
    STRINGi9606.ENSP00000263702.

    Structurei

    Secondary structure

    1373
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi43 – 52Combined sources10
    Helixi54 – 57Combined sources4
    Beta strandi58 – 63Combined sources6
    Beta strandi72 – 81Combined sources10
    Helixi84 – 91Combined sources8
    Beta strandi100 – 103Combined sources4
    Beta strandi109 – 115Combined sources7
    Beta strandi127 – 133Combined sources7
    Beta strandi138 – 145Combined sources8
    Helixi146 – 148Combined sources3
    Beta strandi149 – 152Combined sources4
    Beta strandi154 – 156Combined sources3
    Helixi158 – 163Combined sources6
    Helixi167 – 177Combined sources11
    Beta strandi186 – 191Combined sources6
    Helixi195 – 207Combined sources13
    Beta strandi210 – 215Combined sources6
    Helixi221 – 230Combined sources10
    Beta strandi234 – 238Combined sources5
    Helixi239 – 243Combined sources5
    Helixi245 – 249Combined sources5
    Beta strandi252 – 254Combined sources3
    Beta strandi258 – 264Combined sources7
    Helixi266 – 273Combined sources8
    Beta strandi281 – 284Combined sources4
    Beta strandi293 – 295Combined sources3
    Helixi297 – 302Combined sources6
    Beta strandi306 – 309Combined sources4
    Helixi312 – 318Combined sources7
    Helixi321 – 336Combined sources16
    Beta strandi345 – 349Combined sources5
    Helixi350 – 352Combined sources3
    Helixi353 – 360Combined sources8
    Beta strandi362 – 364Combined sources3
    Beta strandi366 – 372Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ZSYX-ray1.75A40-373[»]
    2VCYX-ray2.41A/B31-373[»]
    ProteinModelPortaliQ9BV79.
    SMRiQ9BV79.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BV79.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG0025. Eukaryota.
    COG0604. LUCA.
    GeneTreeiENSGT00550000074483.
    HOVERGENiHBG052446.
    InParanoidiQ9BV79.
    KOiK07512.
    OMAiHQLCRAW.
    OrthoDBiEOG091G0BAE.
    PhylomeDBiQ9BV79.
    TreeFamiTF312886.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9BV79-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH
    60 70 80 90 100
    HGDPAKVVEL KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGFLPEL
    110 120 130 140 150
    PAVGGNEGVA QVVAVGSNVT GLKPGDWVIP ANAGLGTWRT EAVFSEEALI
    160 170 180 190 200
    QVPSDIPLQS AATLGVNPCT AYRMLMDFEQ LQPGDSVIQN ASNSGVGQAV
    210 220 230 240 250
    IQIAAALGLR TINVVRDRPD IQKLSDRLKS LGAEHVITEE ELRRPEMKNF
    260 270 280 290 300
    FKDMPQPRLA LNCVGGKSST ELLRQLARGG TMVTYGGMAK QPVVASVSLL
    310 320 330 340 350
    IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSQVPL
    360 370
    QDYQSALEAS MKPFISSKQI LTM
    Length:373
    Mass (Da):40,462
    Last modified:May 31, 2011 - v2
    Checksum:iDB13F6B0ED54A823
    GO
    Isoform 2 (identifier: Q9BV79-2) [UniParc]FASTAAdd to basket
    Also known as: cMECR

    The sequence of this isoform differs from the canonical sequence as follows:
         1-76: Missing.

    Show »
    Length:297
    Mass (Da):32,228
    Checksum:i1A27621E27728B76
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti45 – 46AL → GV in AAD34058 (PubMed:10810093).Curated2
    Sequence conflicti373M → I in CAG32984 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_02793596F → L.5 PublicationsCorresponds to variant rs1128400dbSNPEnsembl.1
    Natural variantiVAR_055486227R → K.Corresponds to variant rs11544658dbSNPEnsembl.1
    Natural variantiVAR_055487258R → L.Corresponds to variant rs34835902dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0411311 – 76Missing in isoform 2. 1 PublicationAdd BLAST76

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS30659.1. [Q9BV79-1]
    CCDS30660.1. [Q9BV79-2]
    RefSeqiNP_001019903.2. NM_001024732.2.
    NP_057095.3. NM_016011.3.
    XP_005245944.1. XM_005245887.2. [Q9BV79-2]
    XP_016856902.1. XM_017001413.1. [Q9BV79-2]
    XP_016856903.1. XM_017001414.1. [Q9BV79-2]
    XP_016856904.1. XM_017001415.1. [Q9BV79-2]
    UniGeneiHs.183646.

    Genome annotation databases

    EnsembliENST00000263702; ENSP00000263702; ENSG00000116353. [Q9BV79-1]
    ENST00000373791; ENSP00000362896; ENSG00000116353. [Q9BV79-2]
    GeneIDi51102.
    KEGGihsa:51102.
    UCSCiuc001brp.3. human. [Q9BV79-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS30659.1. [Q9BV79-1]
    CCDS30660.1. [Q9BV79-2]
    RefSeqiNP_001019903.2. NM_001024732.2.
    NP_057095.3. NM_016011.3.
    XP_005245944.1. XM_005245887.2. [Q9BV79-2]
    XP_016856902.1. XM_017001413.1. [Q9BV79-2]
    XP_016856903.1. XM_017001414.1. [Q9BV79-2]
    XP_016856904.1. XM_017001415.1. [Q9BV79-2]
    UniGeneiHs.183646.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ZSYX-ray1.75A40-373[»]
    2VCYX-ray2.41A/B31-373[»]
    ProteinModelPortaliQ9BV79.
    SMRiQ9BV79.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119291. 14 interactors.
    IntActiQ9BV79. 2 interactors.
    STRINGi9606.ENSP00000263702.

    Chemistry databases

    SwissLipidsiSLP:000001054.

    PTM databases

    iPTMnetiQ9BV79.
    PhosphoSitePlusiQ9BV79.

    Polymorphism and mutation databases

    DMDMi334302832.

    Proteomic databases

    EPDiQ9BV79.
    MaxQBiQ9BV79.
    PaxDbiQ9BV79.
    PeptideAtlasiQ9BV79.
    PRIDEiQ9BV79.

    Protocols and materials databases

    DNASUi51102.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000263702; ENSP00000263702; ENSG00000116353. [Q9BV79-1]
    ENST00000373791; ENSP00000362896; ENSG00000116353. [Q9BV79-2]
    GeneIDi51102.
    KEGGihsa:51102.
    UCSCiuc001brp.3. human. [Q9BV79-1]

    Organism-specific databases

    CTDi51102.
    GeneCardsiMECR.
    HGNCiHGNC:19691. MECR.
    HPAiHPA022018.
    HPA022030.
    HPA028740.
    MIMi608205. gene.
    neXtProtiNX_Q9BV79.
    OpenTargetsiENSG00000116353.
    PharmGKBiPA142671471.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0025. Eukaryota.
    COG0604. LUCA.
    GeneTreeiENSGT00550000074483.
    HOVERGENiHBG052446.
    InParanoidiQ9BV79.
    KOiK07512.
    OMAiHQLCRAW.
    OrthoDBiEOG091G0BAE.
    PhylomeDBiQ9BV79.
    TreeFamiTF312886.

    Enzyme and pathway databases

    BioCyciZFISH:HS04010-MONOMER.
    SABIO-RKQ9BV79.

    Miscellaneous databases

    EvolutionaryTraceiQ9BV79.
    GeneWikiiMECR.
    GenomeRNAii51102.
    PROiQ9BV79.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000116353.
    CleanExiHS_MECR.
    ExpressionAtlasiQ9BV79. baseline and differential.
    GenevisibleiQ9BV79. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMECR_HUMAN
    AccessioniPrimary (citable) accession number: Q9BV79
    Secondary accession number(s): B3KT72
    , Q5SYU0, Q5SYU1, Q5SYU2, Q6IBU9, Q9Y373
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: May 31, 2011
    Last modified: November 2, 2016
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.