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Q9U6Y8

- RFP_DISSP

UniProt

Q9U6Y8 - RFP_DISSP

Protein

Red fluorescent protein drFP583

Gene
N/A
Organism
Discosoma sp. (Sea anemone)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Thought to play a role in photoprotection of the coral's resident symbiont microalgae's photosystems from photoinhibition caused by high light levels found near the surface of coral reefs. In deeper water, the fluorescence may be to convert blue light into longer wavelengths more suitable for use in photosynthesis by the microalgal symbionts.

    Absorptioni

    Abs(max)=558 nm

    Exhibits a smaller absorbance peak at 494 nm. The broad fluorescence emission spectrum peaks at 583 nm.

    GO - Biological processi

    1. bioluminescence Source: UniProtKB-KW
    2. generation of precursor metabolites and energy Source: InterPro
    3. protein-chromophore linkage Source: UniProtKB-KW

    Keywords - Molecular functioni

    Photoprotein

    Keywords - Biological processi

    Luminescence

    Keywords - Ligandi

    Chromophore

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Red fluorescent protein drFP583
    Short name:
    DsRed
    OrganismiDiscosoma sp. (Sea anemone)
    Taxonomic identifieri86600 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaCorallimorphariaDiscosomatidaeDiscosoma

    Pathology & Biotechi

    Biotechnological usei

    Fluorescent proteins have become a useful and ubiquitous tool for making chimeric proteins, where they function as a fluorescent protein tag. Typically they tolerate N- and C-terminal fusion to a broad variety of proteins. They have been expressed in most known cell types and are used as a noninvasive fluorescent marker in living cells and organisms. They enable a wide range of applications where they have functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions.Curated

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 225225Red fluorescent protein drFP583PRO_0000192577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki66 ↔ 682-iminomethyl-5-imidazolinone (Gln-Gly)1 Publication
    Modified residuei67 – 671(Z)-2,3-didehydrotyrosine1 Publication

    Post-translational modificationi

    Contains a chromophore consisting of modified amino acid residues. The chromophore is formed by autocatalytic backbone condensation between Xaa-N and Gly-N+2, oxidation of Tyr-N+1 to didehydrotyrosine, and formation of a double bond to the alpha-amino nitrogen of residue Xaa-N. Maturation of the chromophore requires nothing other than molecular oxygen.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1
    225
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 2213
    Beta strandi25 – 3612
    Turni37 – 404
    Beta strandi41 – 5111
    Helixi58 – 603
    Helixi62 – 643
    Helixi70 – 723
    Helixi82 – 854
    Turni86 – 894
    Beta strandi91 – 999
    Beta strandi104 – 11411
    Beta strandi117 – 12711
    Turni134 – 1385
    Beta strandi140 – 1434
    Beta strandi146 – 1538
    Beta strandi156 – 16712
    Beta strandi170 – 18516
    Beta strandi192 – 20413
    Beta strandi208 – 22013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G7KX-ray2.00A/B/C/D2-225[»]
    1GGXX-ray1.90A/B/C/D1-225[»]
    1ZGOX-ray1.40A/B/C/D1-225[»]
    1ZGPX-ray1.90A/B/C/D1-225[»]
    1ZGQX-ray1.90A/B/C/D/E/F/G/H1-225[»]
    2H5OX-ray1.08A/B8-221[»]
    2H5RX-ray1.60A8-223[»]
    2H8QX-ray2.00A/B/C/D7-225[»]
    2V4EX-ray2.40A/B/C/D/E/F/G/H6-225[»]
    2VADX-ray1.59A7-221[»]
    2VAEX-ray1.64A/B/C/D/E/F/G/H3-225[»]
    4I2YX-ray2.20A/B8-145[»]
    A/B147-221[»]
    4KF4X-ray1.99A/B/C/D/E/F/G/H8-221[»]
    4KF5X-ray2.60C/D8-221[»]
    ProteinModelPortaliQ9U6Y8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9U6Y8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GFP family.Curated

    Family and domain databases

    Gene3Di2.40.155.10. 1 hit.
    InterProiIPR009017. GFP.
    IPR011584. GFP-related.
    IPR023413. GFP_like.
    IPR000786. Green_fluorescent_prot.
    [Graphical view]
    PfamiPF01353. GFP. 1 hit.
    [Graphical view]
    PRINTSiPR01229. GFLUORESCENT.
    SUPFAMiSSF54511. SSF54511. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9U6Y8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSSKNVIKE FMRFKVRMEG TVNGHEFEIE GEGEGRPYEG HNTVKLKVTK    50
    GGPLPFAWDI LSPQFQYGSK VYVKHPADIP DYKKLSFPEG FKWERVMNFE 100
    DGGVVTVTQD SSLQDGCFIY KVKFIGVNFP SDGPVMQKKT MGWEASTERL 150
    YPRDGVLKGE IHKALKLKDG GHYLVEFKSI YMAKKPVQLP GYYYVDSKLD 200
    ITSHNEDYTI VEQYERTEGR HHLFL 225
    Length:225
    Mass (Da):25,931
    Last modified:May 1, 2000 - v1
    Checksum:iFBF9A5369778F689
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF168419 mRNA. Translation: AAF03369.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF168419 mRNA. Translation: AAF03369.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G7K X-ray 2.00 A/B/C/D 2-225 [» ]
    1GGX X-ray 1.90 A/B/C/D 1-225 [» ]
    1ZGO X-ray 1.40 A/B/C/D 1-225 [» ]
    1ZGP X-ray 1.90 A/B/C/D 1-225 [» ]
    1ZGQ X-ray 1.90 A/B/C/D/E/F/G/H 1-225 [» ]
    2H5O X-ray 1.08 A/B 8-221 [» ]
    2H5R X-ray 1.60 A 8-223 [» ]
    2H8Q X-ray 2.00 A/B/C/D 7-225 [» ]
    2V4E X-ray 2.40 A/B/C/D/E/F/G/H 6-225 [» ]
    2VAD X-ray 1.59 A 7-221 [» ]
    2VAE X-ray 1.64 A/B/C/D/E/F/G/H 3-225 [» ]
    4I2Y X-ray 2.20 A/B 8-145 [» ]
    A/B 147-221 [» ]
    4KF4 X-ray 1.99 A/B/C/D/E/F/G/H 8-221 [» ]
    4KF5 X-ray 2.60 C/D 8-221 [» ]
    ProteinModelPortali Q9U6Y8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9U6Y8.

    Family and domain databases

    Gene3Di 2.40.155.10. 1 hit.
    InterProi IPR009017. GFP.
    IPR011584. GFP-related.
    IPR023413. GFP_like.
    IPR000786. Green_fluorescent_prot.
    [Graphical view ]
    Pfami PF01353. GFP. 1 hit.
    [Graphical view ]
    PRINTSi PR01229. GFLUORESCENT.
    SUPFAMi SSF54511. SSF54511. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The structural basis for red fluorescence in the tetrameric GFP homolog DsRed."
      Wall M.A., Socolich M., Ranganathan R.
      Nat. Struct. Biol. 7:1133-1138(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    3. "Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0-A resolution."
      Yarbrough D., Wachter R.M., Kallio K., Matz M.V., Remington S.J.
      Proc. Natl. Acad. Sci. U.S.A. 98:462-467(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiRFP_DISSP
    AccessioniPrimary (citable) accession number: Q9U6Y8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3