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Q99MZ7

- PECR_MOUSE

UniProt

Q99MZ7 - PECR_MOUSE

Protein

Peroxisomal trans-2-enoyl-CoA reductase

Gene

Pecr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity By similarity.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei179 – 1791Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 4725NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid elongation Source: MGI
    2. phytol metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal trans-2-enoyl-CoA reductase (EC:1.3.1.38)
    Short name:
    TERP
    Gene namesi
    Name:Pecr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:2148199. Pecr.

    Subcellular locationi

    Peroxisome By similarity

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: UniProtKB
    2. mitochondrion Source: UniProtKB
    3. peroxisomal membrane Source: UniProtKB
    4. peroxisome Source: MGI

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 303302Peroxisomal trans-2-enoyl-CoA reductasePRO_0000054741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei5 – 51N6-succinyllysine1 Publication
    Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
    Modified residuei17 – 171N6-succinyllysine; alternate1 Publication
    Modified residuei32 – 321N6-succinyllysine1 Publication
    Modified residuei83 – 831N6-acetyllysine1 Publication
    Modified residuei97 – 971N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99MZ7.
    PaxDbiQ99MZ7.
    PRIDEiQ99MZ7.

    2D gel databases

    REPRODUCTION-2DPAGEQ99MZ7.

    PTM databases

    PhosphoSiteiQ99MZ7.

    Expressioni

    Tissue specificityi

    Highly expressed in liver and kidney. Expressed at lowe level in heart and skeletal muscle. Expressed at weak level in other tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ99MZ7.
    BgeeiQ99MZ7.
    CleanExiMM_PECR.
    GenevestigatoriQ99MZ7.

    Interactioni

    Subunit structurei

    Interacts with PEX5, probably required to target it into peroxisomes.By similarity

    Protein-protein interaction databases

    IntActiQ99MZ7. 2 interactions.
    MINTiMINT-2514438.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99MZ7.
    SMRiQ99MZ7. Positions 7-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi301 – 3033Microbody targeting signalBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00740000115347.
    HOVERGENiHBG105268.
    InParanoidiQ99MZ7.
    KOiK07753.
    OMAiXREIALA.
    PhylomeDBiQ99MZ7.
    TreeFamiTF315256.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.

    Sequencei

    Sequence statusi: Complete.

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

    Q99MZ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSWKTGQSY LAAGLLKNQV AVVTGGGTGI GKAVSRELLH LGCNVVIASR    50
    KLDRLTAAVD ELRASLPPSS SAEVSAIQCN IRKEEEVSNL VKSTLAKYGK 100
    INFLVNNGGG QFMAPVEDIT AKGWHAVIET NLTGTFYMCK EVYNSWMREH 150
    GGSIVNIIVL LNNGFPTAAH TGAAREGVYN LTKSMALAWA SSGVRINCVA 200
    PGTIYSQTAV DNYGEMGQTL FEMAFDSIPA KRLGVPEEIS PLVCFLLSPA 250
    ASYITGQLIN VDGGQALYTH AFSIPDHDNW PVGAGDLSIV KRIKESFKKK 300
    AKL 303
    Length:303
    Mass (Da):32,410
    Last modified:June 1, 2001 - v1
    Checksum:i97AD4047A20B30D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891N → Y in BAB26803. (PubMed:16141072)Curated
    Sequence conflicti230 – 2323AKR → VSA in AAF69800. (PubMed:10811639)Curated
    Sequence conflicti241 – 2444PLVC → LLAR in AAF69800. (PubMed:10811639)Curated
    Sequence conflicti268 – 2681Y → H in AAF69800. (PubMed:10811639)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF232011 mRNA. Translation: AAF69800.1.
    AF242204 mRNA. Translation: AAK28336.1.
    AK010260 mRNA. Translation: BAB26803.1.
    BC013530 mRNA. Translation: AAH13530.1.
    CCDSiCCDS35607.1.
    RefSeqiNP_076012.3. NM_023523.5.
    UniGeneiMm.281738.

    Genome annotation databases

    EnsembliENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189.
    GeneIDi111175.
    KEGGimmu:111175.
    UCSCiuc007bki.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF232011 mRNA. Translation: AAF69800.1 .
    AF242204 mRNA. Translation: AAK28336.1 .
    AK010260 mRNA. Translation: BAB26803.1 .
    BC013530 mRNA. Translation: AAH13530.1 .
    CCDSi CCDS35607.1.
    RefSeqi NP_076012.3. NM_023523.5.
    UniGenei Mm.281738.

    3D structure databases

    ProteinModelPortali Q99MZ7.
    SMRi Q99MZ7. Positions 7-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99MZ7. 2 interactions.
    MINTi MINT-2514438.

    PTM databases

    PhosphoSitei Q99MZ7.

    2D gel databases

    REPRODUCTION-2DPAGE Q99MZ7.

    Proteomic databases

    MaxQBi Q99MZ7.
    PaxDbi Q99MZ7.
    PRIDEi Q99MZ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027381 ; ENSMUSP00000027381 ; ENSMUSG00000026189 .
    GeneIDi 111175.
    KEGGi mmu:111175.
    UCSCi uc007bki.2. mouse.

    Organism-specific databases

    CTDi 55825.
    MGIi MGI:2148199. Pecr.

    Phylogenomic databases

    eggNOGi COG1028.
    GeneTreei ENSGT00740000115347.
    HOVERGENi HBG105268.
    InParanoidi Q99MZ7.
    KOi K07753.
    OMAi XREIALA.
    PhylomeDBi Q99MZ7.
    TreeFami TF315256.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .

    Miscellaneous databases

    NextBioi 365461.
    PROi Q99MZ7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99MZ7.
    Bgeei Q99MZ7.
    CleanExi MM_PECR.
    Genevestigatori Q99MZ7.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs."
      Das A.K., Uhler M.D., Hajra A.K.
      J. Biol. Chem. 275:24333-24340(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology."
      Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M.
      Comb. Chem. High Throughput Screen. 4:545-552(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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.
    4. "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: Kidney.
    5. "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 GLY-2, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-17 AND LYS-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "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-17; LYS-83 AND LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiPECR_MOUSE
    AccessioniPrimary (citable) accession number: Q99MZ7
    Secondary accession number(s): Q9CX01, Q9JIF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3