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Q8ISF8

- RFP_ENTQU

UniProt

Q8ISF8 - RFP_ENTQU

Protein

Red fluorescent protein eqFP611

Gene
N/A
Organism
Entacmaea quadricolor (Bubble-tip anemone) (Parasicyonis actinostoloides)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Pigment protein.1 Publication

    Absorptioni

    Abs(max)=559 nm

    Exhibits a smaller absorbance peak at 525 nm. Has a strong fluorescence emission spectrum which peaks at 611 nm.

    GO - Biological processi

    1. bioluminescence Source: UniProtKB-KW
    2. 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 eqFP611
    Alternative name(s):
    GFP-like chromoprotein
    OrganismiEntacmaea quadricolor (Bubble-tip anemone) (Parasicyonis actinostoloides)
    Taxonomic identifieri6118 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaNynantheaeActiniidaeEntacmaea

    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 – 231231Red fluorescent protein eqFP611PRO_0000192578Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki63 ↔ 652-iminomethyl-5-imidazolinone (Met-Gly)1 Publication
    Modified residuei64 – 641(E)-2,3-didehydrotyrosine

    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

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    231
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi7 – 1913
    Beta strandi22 – 3312
    Turni34 – 374
    Beta strandi38 – 4811
    Helixi55 – 617
    Turni73 – 753
    Helixi81 – 833
    Turni84 – 863
    Beta strandi88 – 969
    Beta strandi101 – 11111
    Beta strandi114 – 12411
    Turni131 – 1355
    Beta strandi137 – 1404
    Beta strandi143 – 1508
    Beta strandi153 – 16412
    Turni165 – 1673
    Beta strandi169 – 18214
    Helixi184 – 1863
    Beta strandi192 – 20514
    Turni206 – 2094
    Beta strandi210 – 22011
    Beta strandi227 – 2293

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UISX-ray2.00A/B1-231[»]
    3E5TX-ray1.10A1-231[»]
    3E5VX-ray2.10A1-231[»]
    3E5WX-ray1.71A/B/C/D1-231[»]
    3IP2X-ray1.60A34-229[»]
    3U0LX-ray1.25A1-224[»]
    3U0MX-ray1.65A1-224[»]
    3U0NX-ray1.60A1-224[»]
    ProteinModelPortaliQ8ISF8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8ISF8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GFP family.1 Publication

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q8ISF8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSLIKENMR MMVVMEGSVN GYQFKCTGEG DGNPYMGTQT MRIKVVEGGP    50
    LPFAFDILAT SFMYGSKTFI KHTKGIPDFF KQSFPEGFTW ERVTRYEDGG 100
    VFTVMQDTSL EDGCLVYHAK VTGVNFPSNG AVMQKKTKGW EPNTEMLYPA 150
    DGGLRGYSQM ALNVDGGGYL SCSFETTYRS KKTVENFKMP GFHFVDHRLE 200
    RLEESDKEMF VVQHEHAVAK FCDLPSKLGR L 231
    Length:231
    Mass (Da):26,053
    Last modified:March 1, 2003 - v1
    Checksum:i86467A7EB5D6DD60
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY130757 mRNA. Translation: AAN05449.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY130757 mRNA. Translation: AAN05449.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UIS X-ray 2.00 A/B 1-231 [» ]
    3E5T X-ray 1.10 A 1-231 [» ]
    3E5V X-ray 2.10 A 1-231 [» ]
    3E5W X-ray 1.71 A/B/C/D 1-231 [» ]
    3IP2 X-ray 1.60 A 34-229 [» ]
    3U0L X-ray 1.25 A 1-224 [» ]
    3U0M X-ray 1.65 A 1-224 [» ]
    3U0N X-ray 1.60 A 1-224 [» ]
    ProteinModelPortali Q8ISF8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q8ISF8.

    Family and domain databases

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

    Publicationsi

    1. "A far-red fluorescent protein with fast maturation and reduced oligomerization tendency from Entacmaea quadricolor (Anthozoa, Actinaria)."
      Wiedenmann J., Schenk A., Roecker C., Girod A., Spindler K.-D., Nienhaus G.U.
      Proc. Natl. Acad. Sci. U.S.A. 99:11646-11651(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
    2. "The 2.0-A crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor."
      Petersen J., Wilmann P.G., Beddoe T., Oakley A.J., Devenish R.J., Prescott M., Rossjohn J.
      J. Biol. Chem. 278:44626-44631(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiRFP_ENTQU
    AccessioniPrimary (citable) accession number: Q8ISF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    The emission does not change over the pH range of 4 to 10. Maturation occurs via a green intermediate and is complete within 12 hours. Recombinant expression at high temperatures induces oligomerization.1 Publication

    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