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Protein
Submitted name:

Fluorescent protein Dronpa

Gene

Dronpa

Organism
Echinophyllia sp. SC22
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Fluorescent protein DronpaImported
Gene namesi
Name:DronpaImported
OrganismiEchinophyllia sp. SC22Imported
Taxonomic identifieri301887 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaScleractiniaFaviinaLobophylliidaeEchinophyllia

Interactioni

Protein-protein interaction databases

DIPiDIP-46137N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GX0X-ray1.90A/B/C/D2-224[»]
2GX2X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-224[»]
2IE2X-ray1.70A/B/C/D/E/F1-224[»]
2IOVX-ray1.80A/B/C/D1-224[»]
2POXX-ray1.95A/B/C/D1-224[»]
2Z1OX-ray1.75A/B/C/D1-224[»]
2Z6XX-ray2.30A/B/C/D/E/F/G/H1-224[»]
2Z6YX-ray2.00A/B/C/D1-224[»]
2Z6ZX-ray1.80A/B/C/D/E/F1-224[»]
3ZUFX-ray2.20A/B/C/D/E/F2-93[»]
A/B/C/D/E/F95-140[»]
A/B/C/D/E/F142-218[»]
3ZUJX-ray2.35A/B/C/D/E/F2-93[»]
A/B/C/D/E/F95-140[»]
A/B/C/D/E/F142-217[»]
3ZULX-ray2.30A/B/C/D/E/F2-93[»]
A/B/C/D/E/F95-140[»]
A/B/C/D/E/F142-224[»]
4EMQX-ray1.95A/B/C/D/E/F1-224[»]
4HQ8X-ray1.95A/B/C/D/E/F1-101[»]
A/B/C/D/E/F103-224[»]
4HQ9X-ray2.07A/B/C/D/E/F1-101[»]
A/B/C/D/E/F103-224[»]
4HQCX-ray2.05A/B/C/D/E/F1-101[»]
A/B/C/D/E/F103-224[»]
4IZNX-ray2.15A/B/C/D/E/F/G/H/I/J/K/L1-101[»]
A/B/C/D/E/F/G/H/I/J/K/L103-224[»]
4UTSX-ray2.03A/B/C/D2-217[»]
ProteinModelPortaliQ5TLG6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5TLG6.

Family & Domainsi

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q5TLG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVIKPDMKI KLRMEGAVNG HPFAIEGVGL GKPFEGKQSM DLKVKEGGPL
60 70 80 90 100
PFAYDILTTV FCYGNRVFAK YPENIVDYFK QSFPEGYSWE RSMNYEDGGI
110 120 130 140 150
CNATNDITLD GDCYIYEIRF DGVNFPANGP VMQKRTVKWE PSTEKLYVRD
160 170 180 190 200
GVLKGDVNMA LSLEGGGHYR CDFKTTYKAK KVVQLPDYHF VDHHIEIKSH
210 220
DKDYSNVNLH EHAEAHSELP RQAK
Length:224
Mass (Da):25,481
Last modified:December 21, 2004 - v1
Checksum:i9091A477C9A99D98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB180726 Genomic DNA. Translation: BAD72874.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB180726 Genomic DNA. Translation: BAD72874.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GX0X-ray1.90A/B/C/D2-224[»]
2GX2X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-224[»]
2IE2X-ray1.70A/B/C/D/E/F1-224[»]
2IOVX-ray1.80A/B/C/D1-224[»]
2POXX-ray1.95A/B/C/D1-224[»]
2Z1OX-ray1.75A/B/C/D1-224[»]
2Z6XX-ray2.30A/B/C/D/E/F/G/H1-224[»]
2Z6YX-ray2.00A/B/C/D1-224[»]
2Z6ZX-ray1.80A/B/C/D/E/F1-224[»]
3ZUFX-ray2.20A/B/C/D/E/F2-93[»]
A/B/C/D/E/F95-140[»]
A/B/C/D/E/F142-218[»]
3ZUJX-ray2.35A/B/C/D/E/F2-93[»]
A/B/C/D/E/F95-140[»]
A/B/C/D/E/F142-217[»]
3ZULX-ray2.30A/B/C/D/E/F2-93[»]
A/B/C/D/E/F95-140[»]
A/B/C/D/E/F142-224[»]
4EMQX-ray1.95A/B/C/D/E/F1-224[»]
4HQ8X-ray1.95A/B/C/D/E/F1-101[»]
A/B/C/D/E/F103-224[»]
4HQ9X-ray2.07A/B/C/D/E/F1-101[»]
A/B/C/D/E/F103-224[»]
4HQCX-ray2.05A/B/C/D/E/F1-101[»]
A/B/C/D/E/F103-224[»]
4IZNX-ray2.15A/B/C/D/E/F/G/H/I/J/K/L1-101[»]
A/B/C/D/E/F/G/H/I/J/K/L103-224[»]
4UTSX-ray2.03A/B/C/D2-217[»]
ProteinModelPortaliQ5TLG6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46137N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ5TLG6.

Family and domain databases

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

Publicationsi

  1. "Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting."
    Ando R., Mizuno H., Miyawaki A.
    Science 306:1370-1373(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: SC22Imported.
  2. "The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein."
    Wilmann P.G., Turcic K., Battad J.M., Wilce M.C., Devenish R.J., Prescott M., Rossjohn J.
    J. Mol. Biol. 364:213-224(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
  3. "Structural characterization of the photoswitchable fluorescent protein Dronpa-C62S."
    Nam K.H., Kwon O.Y., Sugiyama K., Lee W.H., Kim Y.K., Song H.K., Kim E.E., Park S.Y., Jeon H., Hwang K.Y.
    Biochem. Biophys. Res. Commun. 354:962-967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-224.
  4. "1.8 A bright-state structure of the reversibly switchable fluorescent protein Dronpa guides the generation of fast switching variants."
    Stiel A.C., Trowitzsch S., Weber G., Andresen M., Eggeling C., Hell S.W., Jakobs S., Wahl M.C.
    Biochem. J. 402:35-42(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
  5. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
  6. "Light-dependent regulation of structural flexibility in a photochromic fluorescent protein."
    Mizuno H., Mal T.K., Walchli M., Kikuchi A., Fukano T., Ando R., Jeyakanthan J., Taka J., Shiro Y., Ikura M., Miyawaki A.
    Proc. Natl. Acad. Sci. U.S.A. 105:9227-9232(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
  7. "Low-temperature chromophore isomerization reveals the photoswitching mechanism of the fluorescent protein Padron."
    Faro A.R., Carpentier P., Jonasson G., Pompidor G., Arcizet D., Demachy I., Bourgeois D.
    J. Am. Chem. Soc. 133:16362-16365(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-93; 95-140 AND 142-218.
  8. "Structural basis for the influence of a single mutation K145N on the oligomerization and photoswitching rate of Dronpa."
    Nguyen Bich N., Moeyaert B., Van Hecke K., Dedecker P., Mizuno H., Hofkens J., Van Meervelt L.
    Acta Crystallogr. D 68:1653-1659(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
  9. "Green-to-red photoconvertible Dronpa mutant for multimodal super-resolution fluorescence microscopy."
    Moeyaert B., Nguyen Bich N., De Zitter E., Rocha S., Clays K., Mizuno H., van Meervelt L., Hofkens J., Dedecker P.
    ACS Nano 8:1664-1673(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-101 AND 103-224.
  10. "Room temperature crystal structure of the fast switching M159T mutant of the fluorescent protein dronpa."
    Kaucikas M., Fitzpatrick A., Bryan E., Struve A., Henning R., Kosheleva I., Srajer V., Groenhof G., Van Thor J.J.
    Proteins 83:397-402(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-217.

Entry informationi

Entry nameiQ5TLG6_9CNID
AccessioniPrimary (citable) accession number: Q5TLG6
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: July 22, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.