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Q9SUM3

- NCPR2_ARATH

UniProt

Q9SUM3 - NCPR2_ARATH

Protein

NADPH--cytochrome P450 reductase 2

Gene

ATR2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and dichloroindophenol.5 Publications

    Catalytic activityi

    NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.

    Cofactori

    FAD.1 Publication
    FMN.1 Publication

    Kineticsi

    1. KM=23 µM for NADPH (at pH 7.7 and 28 degrees Celsius)4 Publications
    2. KM=2.0 µM for NADPH (at pH 7.25 and 25 degrees Celsius)4 Publications
    3. KM=15 µM for cytochrome c (at pH 7.7 and 30 degrees Celsius)4 Publications
    4. KM=16 µM for cytochrome c (at pH 7.0 and 25 degrees Celsius)4 Publications
    5. KM=22.5 µM for cytochrome c (at pH 7.7 and 28 degrees Celsius)4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi111 – 1155FMNPROSITE-ProRule annotation
    Nucleotide bindingi201 – 23232FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi346 – 35712FADBy similarityAdd
    BLAST
    Nucleotide bindingi486 – 49611FADBy similarityAdd
    BLAST
    Nucleotide bindingi564 – 58219NADPBy similarityAdd
    BLAST
    Nucleotide bindingi658 – 67417NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. FMN binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. NADPH-hemoprotein reductase activity Source: TAIR

    GO - Biological processi

    1. oxidation-reduction process Source: GOC
    2. phenylpropanoid metabolic process Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Phenylpropanoid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyciARA:GQT-1816-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductase 2 (EC:1.6.2.4)
    Gene namesi
    Name:ATR2
    Synonyms:AR2
    Ordered Locus Names:At4g30210
    ORF Names:F9N11.60
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G30210.

    Subcellular locationi

    Endoplasmic reticulum membrane Curated; Peripheral membrane protein Curated
    Note: Anchored to the ER membrane by its N-terminal hydrophobic region.By similarity

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. endoplasmic reticulum Source: TAIR
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 711711NADPH--cytochrome P450 reductase 2PRO_0000416840Add
    BLAST

    Proteomic databases

    PRIDEiQ9SUM3.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems, flowers and siliques.1 Publication

    Inductioni

    By wounding and transition from dark to light.1 Publication

    Gene expression databases

    ArrayExpressiQ9SUM3.
    GenevestigatoriQ9SUM3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SUM3.
    SMRiQ9SUM3. Positions 96-711.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini105 – 255151Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini310 – 556247FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOGENOMiHOG000282027.
    KOiK00327.
    OMAiHEFLQSK.
    PhylomeDBiQ9SUM3.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR023208. P450R.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000208. P450R. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9SUM3-1) [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

    MSSSSSSSTS MIDLMAAIIK GEPVIVSDPA NASAYESVAA ELSSMLIENR    50
    QFAMIVTTSI AVLIGCIVML VWRRSGSGNS KRVEPLKPLV IKPREEEIDD 100
    GRKKVTIFFG TQTGTAEGFA KALGEEAKAR YEKTRFKIVD LDDYAADDDE 150
    YEEKLKKEDV AFFFLATYGD GEPTDNAARF YKWFTEGNDR GEWLKNLKYG 200
    VFGLGNRQYE HFNKVAKVVD DILVEQGAQR LVQVGLGDDD QCIEDDFTAW 250
    REALWPELDT ILREEGDTAV ATPYTAAVLE YRVSIHDSED AKFNDINMAN 300
    GNGYTVFDAQ HPYKANVAVK RELHTPESDR SCIHLEFDIA GSGLTYETGD 350
    HVGVLCDNLS ETVDEALRLL DMSPDTYFSL HAEKEDGTPI SSSLPPPFPP 400
    CNLRTALTRY ACLLSSPKKS ALVALAAHAS DPTEAERLKH LASPAGKDEY 450
    SKWVVESQRS LLEVMAEFPS AKPPLGVFFA GVAPRLQPRF YSISSSPKIA 500
    ETRIHVTCAL VYEKMPTGRI HKGVCSTWMK NAVPYEKSEN CSSAPIFVRQ 550
    SNFKLPSDSK VPIIMIGPGT GLAPFRGFLQ ERLALVESGV ELGPSVLFFG 600
    CRNRRMDFIY EEELQRFVES GALAELSVAF SREGPTKEYV QHKMMDKASD 650
    IWNMISQGAY LYVCGDAKGM ARDVHRSLHT IAQEQGSMDS TKAEGFVKNL 700
    QTSGRYLRDV W 711
    Length:711
    Mass (Da):78,927
    Last modified:May 1, 2000 - v1
    Checksum:iF0503108EB7F508F
    GO
    Isoform 2 (identifier: Q9SUM3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         447-447: K → KV

    Note: May be due to a competing donor splice site. No experimental confirmation available.

    Show »
    Length:712
    Mass (Da):79,026
    Checksum:i75656CFE0CC4DB63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti297 – 2982NM → TL in CAA46815. (PubMed:9235908)Curated
    Sequence conflicti346 – 3483YET → MKL in CAA46815. (PubMed:9235908)Curated
    Sequence conflicti540 – 5445NCSSA → KLFLGR in CAA46815. (PubMed:9235908)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei447 – 4471K → KV in isoform 2. CuratedVSP_042906

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66017 mRNA. Translation: CAA46815.1.
    AL109796 Genomic DNA. Translation: CAB52465.1.
    AL161576 Genomic DNA. Translation: CAB81014.1.
    CP002687 Genomic DNA. Translation: AEE85737.1.
    CP002687 Genomic DNA. Translation: AEE85738.1.
    AF325101 mRNA. Translation: AAK17169.1.
    PIRiS21531.
    T14081.
    RefSeqiNP_194750.1. NM_119167.3. [Q9SUM3-1]
    NP_849472.2. NM_179141.2. [Q9SUM3-2]
    UniGeneiAt.145.

    Genome annotation databases

    EnsemblPlantsiAT4G30210.2; AT4G30210.2; AT4G30210. [Q9SUM3-1]
    GeneIDi829144.
    KEGGiath:AT4G30210.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66017 mRNA. Translation: CAA46815.1 .
    AL109796 Genomic DNA. Translation: CAB52465.1 .
    AL161576 Genomic DNA. Translation: CAB81014.1 .
    CP002687 Genomic DNA. Translation: AEE85737.1 .
    CP002687 Genomic DNA. Translation: AEE85738.1 .
    AF325101 mRNA. Translation: AAK17169.1 .
    PIRi S21531.
    T14081.
    RefSeqi NP_194750.1. NM_119167.3. [Q9SUM3-1 ]
    NP_849472.2. NM_179141.2. [Q9SUM3-2 ]
    UniGenei At.145.

    3D structure databases

    ProteinModelPortali Q9SUM3.
    SMRi Q9SUM3. Positions 96-711.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9SUM3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G30210.2 ; AT4G30210.2 ; AT4G30210 . [Q9SUM3-1 ]
    GeneIDi 829144.
    KEGGi ath:AT4G30210.

    Organism-specific databases

    TAIRi AT4G30210.

    Phylogenomic databases

    HOGENOMi HOG000282027.
    KOi K00327.
    OMAi HEFLQSK.
    PhylomeDBi Q9SUM3.

    Enzyme and pathway databases

    BioCyci ARA:GQT-1816-MONOMER.

    Gene expression databases

    ArrayExpressi Q9SUM3.
    Genevestigatori Q9SUM3.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProi IPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR023208. P450R.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000208. P450R. 1 hit.
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMi SSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5."
      Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D.
      J. Biol. Chem. 272:19176-19186(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Strain: cv. Landsberg erecta.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    5. "Differential redox and electron-transfer properties of purified yeast, plant and human NADPH-cytochrome P-450 reductases highly modulate cytochrome P-450 activities."
      Louerat-Oriou B., Perret A., Pompon D.
      Eur. J. Biochem. 258:1040-1049(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    6. "Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation."
      Mizutani M., Ohta D.
      Plant Physiol. 116:357-367(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION.
    7. "Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis."
      Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.
      Plant Physiol. 119:353-361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2."
      Hull A.K., Celenza J.L.
      Protein Expr. Purif. 18:310-315(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiNCPR2_ARATH
    AccessioniPrimary (citable) accession number: Q9SUM3
    Secondary accession number(s): F4JPK2, Q39036
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2012
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3