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Q9U6Y8

- RFP_DISSP

UniProt

Q9U6Y8 - RFP_DISSP

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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

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
Complete GO annotation...

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 – 2213Combined sources
Beta strandi25 – 3612Combined sources
Turni37 – 404Combined sources
Beta strandi41 – 5111Combined sources
Helixi58 – 603Combined sources
Helixi62 – 643Combined sources
Helixi70 – 723Combined sources
Helixi82 – 854Combined sources
Turni86 – 894Combined sources
Beta strandi91 – 999Combined sources
Beta strandi104 – 11411Combined sources
Beta strandi117 – 12711Combined sources
Turni134 – 1385Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi146 – 1538Combined sources
Beta strandi156 – 16712Combined sources
Beta strandi170 – 18516Combined sources
Beta strandi192 – 20413Combined sources
Beta strandi208 – 22013Combined sources

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/B8-221[»]
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

        10         20         30         40         50
MRSSKNVIKE FMRFKVRMEG TVNGHEFEIE GEGEGRPYEG HNTVKLKVTK
60 70 80 90 100
GGPLPFAWDI LSPQFQYGSK VYVKHPADIP DYKKLSFPEG FKWERVMNFE
110 120 130 140 150
DGGVVTVTQD SSLQDGCFIY KVKFIGVNFP SDGPVMQKKT MGWEASTERL
160 170 180 190 200
YPRDGVLKGE IHKALKLKDG GHYLVEFKSI YMAKKPVQLP GYYYVDSKLD
210 220
ITSHNEDYTI VEQYERTEGR HHLFL
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 8-221 [» ]
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 29, 2014
This is version 58 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