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P42212 (GFP_AEQVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Green fluorescent protein
Gene names
Name:GFP
OrganismAequorea victoria (Jellyfish)
Taxonomic identifier6100 [NCBI]
Taxonomic lineageEukaryotaMetazoaCnidariaHydrozoaHydroidaLeptomedusaeAequoreidaeAequorea

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca2+-activated photoprotein aequorin.

Subunit structure

Monomer.

Tissue specificity

Photocytes.

Post-translational modification

Contains a chromophore consisting of modified amino acid residues. The chromophore is formed by autocatalytic backbone condensation between Ser-65 and Gly-67, and oxidation of Tyr-66 to didehydrotyrosine. Maturation of the chromophore requires nothing other than molecular oxygen.

Biotechnological use

Green fluorescent protein has been engineered to produce a vast number of variously colored mutants, fusion proteins, and biosensors. Fluorescent proteins and its mutated allelic forms, blue, cyan and yellow 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. Ref.6

Can also be used as a molecular thermometer, allowing accurate temperature measurements in fluids. The measurement process relies on the detection of the blinking of GFP using fluorescence correlation spectroscopy. Ref.6

Sequence similarities

Belongs to the GFP family.

Biophysicochemical properties

Absorption:

Abs(max)=395 nm

Exhibits a smaller absorbance peak at 470 nm. The fluorescence emission spectrum peaks at 509 nm with a shoulder at 540 nm.

Ontologies

Keywords
   Biological processLuminescence
   LigandChromophore
   Molecular functionPhotoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processbioluminescence

Traceable author statement Ref.2. Source: UniProtKB

generation of precursor metabolites and energy

Traceable author statement Ref.2. Source: UniProtKB

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Green fluorescent protein
PRO_0000192576

Amino acid modifications

Modified residue661(Z)-2,3-didehydrotyrosine
Cross-link65 ↔ 675-imidazolinone (Ser-Gly)

Natural variations

Natural variant1001F → Y. Ref.1
Natural variant1081T → S. Ref.1
Natural variant1411L → M. Ref.1
Natural variant2191V → I. Ref.1

Experimental info

Mutagenesis651S → G in mut3; highly fluorescent mutant when excited at 488 nm; when associated with A-72. Ref.4
Mutagenesis651S → T: Increases fluoresence, photostability and shift the major exitation peak to 488 nm. Ref.4
Mutagenesis721S → A in mut3; highly fluorescent mutant when excited at 488 nm; when associated with G-65. Ref.4
Sequence conflict21S → G in CAA65278. Ref.3
Sequence conflict251H → Q in CAA65278. Ref.3
Sequence conflict801Q → R in CAA65278. Ref.3
Sequence conflict1571Q → P in AAA58246. Ref.2
Sequence conflict1721E → K in AAA58246. Ref.2

Secondary structure

............................................... 238
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42212 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: EA5A6F21FBFB6E05

FASTA23826,886
        10         20         30         40         50         60 
MSKGEELFTG VVPILVELDG DVNGHKFSVS GEGEGDATYG KLTLKFICTT GKLPVPWPTL 

        70         80         90        100        110        120 
VTTFSYGVQC FSRYPDHMKQ HDFFKSAMPE GYVQERTIFF KDDGNYKTRA EVKFEGDTLV 

       130        140        150        160        170        180 
NRIELKGIDF KEDGNILGHK LEYNYNSHNV YIMADKQKNG IKVNFKIRHN IEDGSVQLAD 

       190        200        210        220        230 
HYQQNTPIGD GPVLLPDNHY LSTQSALSKD PNEKRDHMVL LEFVTAAGIT HGMDELYK 

« Hide

References

[1]"Primary structure of the Aequorea victoria green-fluorescent protein."
Prasher D.C., Eckenrode V.K., Ward W.W., Prendergast F.G., Cormier M.J.
Gene 111:229-233(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS TYR-100; SER-108; MET-141 AND ILE-219.
[2]"Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein."
Inouye S., Tsuji F.I.
FEBS Lett. 341:277-280(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Enhanced expression in tobacco of the gene encoding green fluorescent protein by modification of its codon usage."
Rouwendal G.J.A., Mendes O., Wolbert E.J.H., de Boer A.D.
Plant Mol. Biol. 33:989-999(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"FACS-optimized mutants of the green fluorescent protein (GFP)."
Cormack B.P., Valdivia R.H., Falkow S.
Gene 173:33-38(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-65 AND SER-72.
[5]"Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein."
Cody C.W., Prasher D.C., Westler W.M., Prendergast F.G., Ward W.W.
Biochemistry 32:1212-1218(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOPHORE.
[6]"A molecular thermometer based on fluorescent protein blinking."
Wong F.H., Banks D.S., Abu-Arish A., Fradin C.
J. Am. Chem. Soc. 129:10302-10303(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOTECHNOLOGY.
[7]"Crystal structure of the Aequorea victoria green fluorescent protein."
Ormoe M., Cubitt A.B., Kallio K., Gross L.A., Tsien R.Y., Remington S.J.
Science 273:1392-1395(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-65.
[8]"The molecular structure of green fluorescent protein."
Yang F., Moss L.G., Phillips G.N. Jr.
Nat. Biotechnol. 14:1246-1251(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[9]"Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein."
Wachter R.M., Elsliger M.-A., Kallio K., Hanson G.T., Remington S.J.
Structure 6:1267-1277(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT WITH YELLOW EMISSION.
[10]"Structural and spectral response of green fluorescent protein variants to changes in pH."
Elsliger M.-A., Wachter R.M., Hanson G.T., Kallio K., Remington S.J.
Biochemistry 38:5296-5301(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Protein Spotlight

The greenest of us all - Issue 11 of June 2001

Protein Spotlight

Paint my thoughts - Issue 108 of August 2009

Wikipedia

Green fluorescent protein entry

Protein Spotlight

Paint my thoughts - Issue 108 of November 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62654 mRNA. Translation: AAA27722.1.
M62653 mRNA. Translation: AAA27721.1.
L29345 mRNA. Translation: AAA58246.1.
X96418 mRNA. Translation: CAA65278.1.
U73901 Genomic DNA. Translation: AAB18957.1.
PIRJQ1514. JS0692.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9CX-ray2.40A/B/C/D1-238[»]
1BFPX-ray2.10A1-238[»]
1C4FX-ray2.25A1-238[»]
1CV7X-ray2.50A1-228[»]
1EMAX-ray1.90A1-238[»]
1EMBX-ray2.13A1-238[»]
1EMCX-ray2.30A/B/C/D2-237[»]
1EMEX-ray2.50A2-237[»]
1EMFX-ray2.40A2-238[»]
1EMGX-ray2.00A1-229[»]
1EMKX-ray2.10A2-237[»]
1EMLX-ray2.30A2-237[»]
1EMMX-ray2.30A2-238[»]
1F09X-ray2.14A1-238[»]
1F0BX-ray2.10A1-238[»]
1GFLX-ray1.90A/B2-238[»]
1H6RX-ray1.50A/B/C1-238[»]
1HCJX-ray1.80A/B/C/D1-238[»]
1HUYX-ray2.20A2-238[»]
1JBYX-ray1.80A1-238[»]
1JBZX-ray1.50A1-238[»]
1JC0X-ray2.00A/B/C1-238[»]
1JC1X-ray1.90A/B/C1-238[»]
1KP5X-ray2.60A/B1-238[»]
1KYPX-ray1.35A2-238[»]
1KYRX-ray1.50A2-238[»]
1KYSX-ray1.44A2-238[»]
1MYWX-ray2.20A2-238[»]
1Q4AX-ray1.45A1-238[»]
1Q4BX-ray1.48A1-238[»]
1Q4CX-ray1.55A1-238[»]
1Q4DX-ray1.58A1-238[»]
1Q4EX-ray1.38A1-238[»]
1Q73X-ray1.60A1-238[»]
1QXTX-ray2.00A2-229[»]
1QY3X-ray2.00A1-229[»]
1QYFX-ray1.50A1-227[»]
1QYOX-ray1.80A1-238[»]
1QYQX-ray1.80A2-238[»]
1RM9X-ray2.90A2-236[»]
1RMMX-ray1.90A2-227[»]
1RMOX-ray1.80A2-236[»]
1RMPX-ray3.00A2-229[»]
1RRXX-ray2.10A2-227[»]
1S6ZX-ray1.50A1-238[»]
1W7SX-ray1.85A/B/C/D1-238[»]
1W7TX-ray1.85A/B/C/D1-238[»]
1W7UX-ray1.85A/B/C/D1-238[»]
1YFPX-ray2.50A/B3-229[»]
1YHGX-ray2.50A/B2-238[»]
1YHHX-ray1.50A2-238[»]
1YHIX-ray1.90A2-238[»]
1YJ2X-ray1.50A2-238[»]
1YJFX-ray1.35A2-238[»]
1Z1PX-ray2.00A1-238[»]
1Z1QX-ray1.50A1-238[»]
2AH8X-ray2.24A/B1-238[»]
2AHAX-ray1.98A/B1-238[»]
2AWJX-ray1.60A2-229[»]
2AWKX-ray1.15A1-229[»]
2AWLX-ray1.85A1-229[»]
2AWMX-ray1.70A1-229[»]
2B3PX-ray1.40A1-238[»]
2B3QX-ray2.30A/B/C/D1-238[»]
2DUEX-ray1.24A1-238[»]
2DUFX-ray1.50A1-238[»]
2DUGX-ray1.40A1-238[»]
2DUHX-ray1.20A1-238[»]
2DUIX-ray1.36A1-238[»]
2EMDX-ray2.00A1-238[»]
2EMNX-ray2.30A1-238[»]
2EMOX-ray2.60A1-238[»]
2FWQX-ray1.40A2-238[»]
2FZUX-ray1.25A2-238[»]
2G16X-ray2.00A2-64[»]
B67-238[»]
2G2SX-ray1.20A2-63[»]
B66-238[»]
2G3DX-ray1.35A2-63[»]
B66-238[»]
2G5ZX-ray1.80A2-65[»]
B66-238[»]
2G6EX-ray1.30A2-238[»]
2H6VX-ray1.47A2-238[»]
2H9WX-ray1.82A2-237[»]
2HCGX-ray1.35A2-238[»]
2HFCX-ray1.20A2-238[»]
2HGDX-ray1.60A2-238[»]
2HGYX-ray2.05A2-238[»]
2HJOX-ray1.25A1-238[»]
2HQZX-ray1.20A1-238[»]
2HRSX-ray1.40A1-238[»]
2JADX-ray2.70A1-238[»]
2O24X-ray1.45A2-238[»]
2O29X-ray1.80A2-238[»]
2O2BX-ray1.94A2-238[»]
2OKWX-ray1.90A/B/C/D/E/F1-238[»]
2OKYX-ray2.40A/B1-238[»]
2Q57X-ray2.00A1-238[»]
2Q6PX-ray2.10A1-238[»]
2QRFX-ray1.50A1-230[»]
2QT2X-ray1.31A1-238[»]
2QU1X-ray1.70A1-238[»]
2QZ0X-ray1.20A2-229[»]
2WSNX-ray1.37A2-238[»]
2WSOX-ray1.15A2-238[»]
2WURX-ray0.90A1-237[»]
2Y0GX-ray1.50A2-238[»]
2YDZX-ray1.59A2-238[»]
2YE0X-ray1.47A2-238[»]
2YE1X-ray1.63A2-238[»]
2YFPX-ray2.60A1-238[»]
3CB9X-ray1.31A2-238[»]
3CBEX-ray1.49A2-238[»]
3CD1X-ray1.31A2-238[»]
3CD9X-ray1.50A2-238[»]
3DPWX-ray1.59A2-238[»]
3DPXX-ray1.50A2-238[»]
3DPZX-ray1.70A2-238[»]
3DQ1X-ray1.70A2-238[»]
3DQ2X-ray1.60A2-238[»]
3DQ3X-ray1.70A2-238[»]
3DQ4X-ray1.47A2-238[»]
3DQ5X-ray1.50A2-238[»]
3DQ6X-ray1.60A2-238[»]
3DQ7X-ray1.23A2-238[»]
3DQ8X-ray1.51A2-238[»]
3DQ9X-ray1.40A2-238[»]
3DQAX-ray1.44A2-238[»]
3DQCX-ray1.49A2-238[»]
3DQDX-ray1.40A2-238[»]
3DQEX-ray1.43A2-238[»]
3DQFX-ray1.46A2-238[»]
3DQHX-ray1.45A2-238[»]
3DQIX-ray1.42A2-238[»]
3DQJX-ray1.51A2-238[»]
3DQKX-ray1.40A2-238[»]
3DQLX-ray1.47A2-238[»]
3DQMX-ray1.44A2-238[»]
3DQNX-ray1.44A2-238[»]
3DQOX-ray1.50A2-238[»]
3DQUX-ray1.42A2-238[»]
3ED8X-ray2.70A/B/C/D/E2-238[»]
3EK4X-ray2.65A2-238[»]
3EK7X-ray1.85A2-238[»]
3EK8X-ray2.80A2-238[»]
3EKHX-ray2.00A2-238[»]
3EKJX-ray2.80A2-238[»]
3EVPX-ray1.45A2-144[»]
3EVRX-ray2.00A2-144[»]
3EVUX-ray1.75A2-144[»]
3EVVX-ray2.60A2-238[»]
3G9AX-ray1.61A1-238[»]
3GEXX-ray1.60A1-238[»]
3GJ1X-ray1.80A/B/C/D1-230[»]
3GJ2X-ray1.90A/B/C/D1-230[»]
3I19X-ray1.36A1-238[»]
3K1KX-ray2.15A/B1-238[»]
3LA1X-ray1.29A1-238[»]
3O77X-ray2.35A2-238[»]
3O78X-ray2.60A/B2-237[»]
3OGOX-ray2.80A/B/C/D1-238[»]
3OSQX-ray1.90A2-238[»]
3OSRX-ray2.00A/B2-238[»]
3P28X-ray1.80A3-229[»]
3SG2X-ray2.00A2-238[»]
3SG3X-ray2.10A2-238[»]
3SG4X-ray2.40A2-238[»]
3SG5X-ray1.90A2-238[»]
3SG6X-ray1.70A2-238[»]
3SG7X-ray1.90A2-238[»]
3SRYX-ray1.16A2-238[»]
3SS0X-ray1.49A2-238[»]
3SSHX-ray1.28A2-238[»]
3SSKX-ray1.36A2-238[»]
3SSLX-ray1.45A2-238[»]
3SSPX-ray1.63A2-238[»]
3SSTX-ray1.40A2-238[»]
3SSVX-ray1.86A2-238[»]
3SSYX-ray1.77A2-238[»]
3ST0X-ray1.19A2-238[»]
3SV5X-ray1.53A2-238[»]
3SVBX-ray1.30A2-238[»]
3SVCX-ray1.31A2-238[»]
3SVDX-ray1.78A2-238[»]
3SVEX-ray1.49A2-238[»]
3U8PX-ray2.75A/B/C2-238[»]
3UFZX-ray1.85A2-229[»]
3UG0X-ray2.09A2-229[»]
3V3DX-ray1.95A2-238[»]
3VHTX-ray2.40A1-230[»]
3W1CX-ray1.30A2-238[»]
3W1DX-ray1.50A2-238[»]
3WLCX-ray2.49A2-238[»]
3WLDX-ray2.70A2-144[»]
3ZTFX-ray1.31A2-238[»]
4ANJX-ray2.60A1-238[»]
4AR7X-ray1.23A2-238[»]
4AS8X-ray1.02A2-238[»]
4B5YX-ray1.45A2-238[»]
4BDUX-ray3.00A/B/C/D1-230[»]
4EN1X-ray1.62A/B2-238[»]
4EULX-ray1.35A2-238[»]
4GESX-ray1.23B1-238[»]
4GF6X-ray1.10B1-237[»]
4H47X-ray1.90A1-238[»]
4H48X-ray1.45A1-238[»]
4IK3X-ray2.01A149-238[»]
A2-142[»]
4IK9X-ray1.80A2-144[»]
4J88X-ray2.08A/B2-238[»]
4J89X-ray2.10A/B2-238[»]
4J8AX-ray1.26A2-238[»]
4JFGX-ray3.00A/B/C/D/E/F/G/H1-238[»]
4JRBX-ray2.41A1-229[»]
4KA9X-ray1.58A5-238[»]
4KF5X-ray2.60A/B1-196[»]
4KW4X-ray1.75A2-238[»]
4KW8X-ray2.46A2-238[»]
4KW9X-ray1.80A2-238[»]
4L12X-ray1.78A2-230[»]
4L13X-ray1.66A2-230[»]
4L1IX-ray1.20A2-230[»]
4LQTX-ray1.10A2-238[»]
4LQUX-ray1.60A/B/C/D2-238[»]
4LW5X-ray2.55A/B/C/D/E2-238[»]
4OGSX-ray2.21A/B1-238[»]
4P7HX-ray3.20A/B5-238[»]
ProteinModelPortalP42212.
SMRP42212. Positions 2-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP42212. 1 interaction.

Proteomic databases

PRIDEP42212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.155.10. 1 hit.
InterProIPR009017. GFP.
IPR011584. GFP-related.
IPR023413. GFP_like.
IPR000786. Green_fluorescent_prot.
[Graphical view]
PfamPF01353. GFP. 1 hit.
[Graphical view]
PRINTSPR01229. GFLUORESCENT.
SUPFAMSSF54511. SSF54511. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP42212.

Entry information

Entry nameGFP_AEQVI
AccessionPrimary (citable) accession number: P42212
Secondary accession number(s): Q17104, Q27903, Q93125
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references