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Protein

Red fluorescent protein eqFP611

Gene
N/A
Organism
Entacmaea quadricolor (Bubble-tip anemone) (Parasicyonis actinostoloides)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Complete GO annotation...

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001925781 – 231Red fluorescent protein eqFP611Add BLAST231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki63 ↔ 652-iminomethyl-5-imidazolinone (Met-Gly)1 Publication
Modified residuei64(E)-2,3-didehydrotyrosine1

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

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi7 – 19Combined sources13
Beta strandi22 – 33Combined sources12
Turni34 – 37Combined sources4
Beta strandi38 – 48Combined sources11
Helixi55 – 61Combined sources7
Turni73 – 75Combined sources3
Helixi81 – 83Combined sources3
Turni84 – 86Combined sources3
Beta strandi88 – 96Combined sources9
Beta strandi101 – 111Combined sources11
Beta strandi114 – 124Combined sources11
Turni131 – 135Combined sources5
Beta strandi137 – 140Combined sources4
Beta strandi143 – 150Combined sources8
Beta strandi153 – 164Combined sources12
Turni165 – 167Combined sources3
Beta strandi169 – 182Combined sources14
Helixi184 – 186Combined sources3
Beta strandi192 – 205Combined sources14
Turni206 – 209Combined sources4
Beta strandi210 – 220Combined sources11
Beta strandi227 – 229Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiQ8ISF8.
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.
IPR023413. GFP-like.
IPR011584. GFP-related.
[Graphical view]
PfamiPF01353. GFP. 1 hit.
[Graphical view]
SUPFAMiSSF54511. SSF54511. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8ISF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSLIKENMR MMVVMEGSVN GYQFKCTGEG DGNPYMGTQT MRIKVVEGGP
60 70 80 90 100
LPFAFDILAT SFMYGSKTFI KHTKGIPDFF KQSFPEGFTW ERVTRYEDGG
110 120 130 140 150
VFTVMQDTSL EDGCLVYHAK VTGVNFPSNG AVMQKKTKGW EPNTEMLYPA
160 170 180 190 200
DGGLRGYSQM ALNVDGGGYL SCSFETTYRS KKTVENFKMP GFHFVDHRLE
210 220 230
RLEESDKEMF VVQHEHAVAK FCDLPSKLGR L
Length:231
Mass (Da):26,053
Last modified:March 1, 2003 - v1
Checksum:i86467A7EB5D6DD60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY130757 mRNA. Translation: AAN05449.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY130757 mRNA. Translation: AAN05449.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiQ8ISF8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ISF8.

Family and domain databases

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

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: November 2, 2016
This is version 51 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.