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Q9DCS3

- MECR_MOUSE

UniProt

Q9DCS3 - MECR_MOUSE

Protein

Trans-2-enoyl-CoA reductase, mitochondrial

Gene

Mecr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (26 Apr 2005)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671NADPBy similarity
    Binding sitei368 – 3681NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 1964NADPBy similarity
    Nucleotide bindingi216 – 2183NADPBy similarity
    Nucleotide bindingi285 – 2884NADPBy similarity
    Nucleotide bindingi310 – 3123NADPBy similarity

    GO - Molecular functioni

    1. ligand-dependent nuclear receptor binding Source: MGI
    2. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB-EC
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trans-2-enoyl-CoA reductase, mitochondrial (EC:1.3.1.38)
    Gene namesi
    Name:Mecr
    Synonyms:Nrbf1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1349441. Mecr.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. cytosol Source: MGI
    2. mitochondrion Source: MGI
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353MitochondrionSequence AnalysisAdd
    BLAST
    Chaini54 – 373320Trans-2-enoyl-CoA reductase, mitochondrialPRO_0000000889Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611N6-acetyllysine; alternate1 Publication
    Modified residuei61 – 611N6-succinyllysine; alternate1 Publication
    Modified residuei252 – 2521N6-acetyllysine; alternate1 Publication
    Modified residuei252 – 2521N6-succinyllysine; alternate1 Publication
    Modified residuei267 – 2671N6-acetyllysine; alternate1 Publication
    Modified residuei267 – 2671N6-succinyllysine; alternate1 Publication
    Modified residuei316 – 3161N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9DCS3.
    PaxDbiQ9DCS3.
    PRIDEiQ9DCS3.

    PTM databases

    PhosphoSiteiQ9DCS3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DCS3.
    BgeeiQ9DCS3.
    CleanExiMM_MECR.
    GenevestigatoriQ9DCS3.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiQ9DCS3. 2 interactions.
    MINTiMINT-4128719.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DCS3.
    SMRiQ9DCS3. Positions 38-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0604.
    GeneTreeiENSGT00740000115589.
    HOGENOMiHOG000294683.
    HOVERGENiHBG052446.
    InParanoidiQ9DCS3.
    KOiK07512.
    OMAiCSTLWRV.
    OrthoDBiEOG78M024.
    PhylomeDBiQ9DCS3.
    TreeFamiTF312886.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    Q9DCS3-1 [UniParc]FASTAAdd to Basket

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    MLVSQRVTGA RARAPQLAGL LEAWYRHGRT TSSYSALSEP SRVRALVYGN    50
    HGDPAKVVQL KNLELTAVEG SDVHVRMLAA PINPSDINMI QGNYGLLPKL 100
    PAVGGNEGVG QVIAVGSSVS ALKPGDWVIP ANAGLGTWRT EAVFSEEALI 150
    GIPKDIPLQS AATLGVNPCT AYRMLVDFEQ LQPGDSVIQN ASNSGVGQAV 200
    IQIASALRLK TINVVRDRPD IKKLTDRLKD LGADYVLTEE ELRMPETKTI 250
    FKDLPLPRLA LNCVGGKSST ELLRHLAPGG TMVTYGGMAK QPVTASVSLL 300
    IFKDLKLRGF WLSQWKKNHS PDEFKELILT LCNLIRQGRL TAPSCSEVPL 350
    QGYQQALEAS MKPFVSSKQI LTM 373
    Length:373
    Mass (Da):40,343
    Last modified:April 26, 2005 - v2
    Checksum:iEBA9A61A46386AEE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691E → K in BAB22169. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002533 mRNA. Translation: BAB22169.1.
    BC003864 mRNA. Translation: AAH03864.1.
    CCDSiCCDS18715.1.
    RefSeqiNP_079573.2. NM_025297.2.
    UniGeneiMm.192706.

    Genome annotation databases

    EnsembliENSMUST00000030742; ENSMUSP00000030742; ENSMUSG00000028910.
    GeneIDi26922.
    KEGGimmu:26922.
    UCSCiuc008vae.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002533 mRNA. Translation: BAB22169.1 .
    BC003864 mRNA. Translation: AAH03864.1 .
    CCDSi CCDS18715.1.
    RefSeqi NP_079573.2. NM_025297.2.
    UniGenei Mm.192706.

    3D structure databases

    ProteinModelPortali Q9DCS3.
    SMRi Q9DCS3. Positions 38-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9DCS3. 2 interactions.
    MINTi MINT-4128719.

    PTM databases

    PhosphoSitei Q9DCS3.

    Proteomic databases

    MaxQBi Q9DCS3.
    PaxDbi Q9DCS3.
    PRIDEi Q9DCS3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030742 ; ENSMUSP00000030742 ; ENSMUSG00000028910 .
    GeneIDi 26922.
    KEGGi mmu:26922.
    UCSCi uc008vae.2. mouse.

    Organism-specific databases

    CTDi 51102.
    MGIi MGI:1349441. Mecr.

    Phylogenomic databases

    eggNOGi COG0604.
    GeneTreei ENSGT00740000115589.
    HOGENOMi HOG000294683.
    HOVERGENi HBG052446.
    InParanoidi Q9DCS3.
    KOi K07512.
    OMAi CSTLWRV.
    OrthoDBi EOG78M024.
    PhylomeDBi Q9DCS3.
    TreeFami TF312886.

    Miscellaneous databases

    NextBioi 304813.
    PROi Q9DCS3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DCS3.
    Bgeei Q9DCS3.
    CleanExi MM_MECR.
    Genevestigatori Q9DCS3.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    Pfami PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiMECR_MOUSE
    AccessioniPrimary (citable) accession number: Q9DCS3
    Secondary accession number(s): Q99L39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3