[1]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANTS TYR-100; SER-108; MET-141 AND ILE-219. DOI=10.1016/0378-1119(92)90691-H; PubMed=1347277 [NCBI, ExPASy, EBI, Israel, Japan] Prasher D.C., Eckenrode V.K., Ward W.W., Prendergast F.G., Cormier M.J.; "Primary structure of the Aequorea victoria green-fluorescent protein."; Gene 111:229-233(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-5793(94)80472-9; PubMed=8137953 [NCBI, ExPASy, EBI, Israel, Japan] Inouye S., Tsuji F.I.; "Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein."; FEBS Lett. 341:277-280(1994).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1023/A:1005740823703; PubMed=9154981 [NCBI, ExPASy, EBI, Israel, Japan] Rouwendal G.J.A., Mendes O., Wolbert E.J.H., de Boer A.D.; "Enhanced expression in tobacco of the gene encoding green fluorescent protein by modification of its codon usage."; Plant Mol. Biol. 33:989-999(1997).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-65 AND SER-72. DOI=10.1016/0378-1119(95)00685-0; PubMed=8707053 [NCBI, ExPASy, EBI, Israel, Japan] Cormack B.P., Valdivia R.H., Falkow S.; "FACS-optimized mutants of the green fluorescent protein (GFP)."; Gene 173:33-38(1996).
[5]	CHROMOPHORE. DOI=10.1021/bi00056a003; PubMed=8448132 [NCBI, ExPASy, EBI, Israel, Japan] Cody C.W., Prasher D.C., Westler W.M., Prendergast F.G., Ward W.W.; "Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein."; Biochemistry 32:1212-1218(1993).
[6]	BIOTECHNOLOGY. DOI=10.1021/ja0715905; PubMed=17685514 [NCBI, ExPASy, EBI, Israel, Japan] Wong F.H., Banks D.S., Abu-Arish A., Fradin C.; "A molecular thermometer based on fluorescent protein blinking."; J. Am. Chem. Soc. 129:10302-10303(2007).
[7]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-65. DOI=10.1126/science.273.5280.1392; PubMed=8703075 [NCBI, ExPASy, EBI, Israel, Japan] Ormoe M., Cubitt A.B., Kallio K., Gross L.A., Tsien R.Y., Remington S.J.; "Crystal structure of the Aequorea victoria green fluorescent protein."; Science 273:1392-1395(1996).
[8]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1038/nbt1096-1246; PubMed=9631087 [NCBI, ExPASy, EBI, Israel, Japan] Yang F., Moss L.G., Phillips G.N. Jr.; "The molecular structure of green fluorescent protein."; Nat. Biotechnol. 14:1246-1251(1996).
[9]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT WITH YELLOW EMISSION. DOI=10.1016/S0969-2126(98)00127-0; PubMed=9782051 [NCBI, ExPASy, EBI, Israel, Japan] Wachter R.M., Elsliger M.-A., Kallio K., Hanson G.T., Remington S.J.; "Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein."; Structure 6:1267-1277(1998).
[10]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1021/bi9902182; PubMed=10220315 [NCBI, ExPASy, EBI, Israel, Japan] Elsliger M.-A., Wachter R.M., Hanson G.T., Kallio K., Remington S.J.; "Structural and spectral response of green fluorescent protein variants to changes in pH."; Biochemistry 38:5296-5301(1999).

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 Ca(2+)-activated photoprotein aequorin.
BIOPHYSICOCHEMICAL PROPERTIES:

Absorption: Abs(max)=395 nm;
Note=Exhibits a smaller absorbance peak at 470 nm. The fluorescence emission spectrum peaks at 509 nm with a shoulder at 540 nm;
SUBUNIT: Monomer.
TISSUE SPECIFICITY: Photocytes.
PTM: 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.
BIOTECHNOLOGY: 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.
BIOTECHNOLOGY: 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.
SIMILARITY: Belongs to the GFP family.
WEB RESOURCE: Name=Protein Spotlight; Note=The greenest of us all - Issue 11 of June 2001; URL="http://www.expasy.org/spotlight/back_issues/sptlt011.shtml";.
WEB RESOURCE: Name=Wikipedia; Note=Green fluorescent protein entry; URL="http://en.wikipedia.org/wiki/Green_fluorescent_protein";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M62654; AAA27722.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M62653; AAA27721.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29345; AAA58246.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X96418; CAA65278.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U73901; AAB18957.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JS0692; JQ1514.

3D structure databases

PDB

1B9C; X-ray; 2.40 A; A/B/C/D=2-238.	[ExPASy / RCSB / EBI]
1BFP; X-ray; 2.10 A; A=1-238.	[ExPASy / RCSB / EBI]
1C4F; X-ray; 2.25 A; A=1-238.	[ExPASy / RCSB / EBI]
1CV7; X-ray; 2.50 A; A=1-228.	[ExPASy / RCSB / EBI]
1EMA; X-ray; 1.90 A; A=1-238.	[ExPASy / RCSB / EBI]
1EMB; X-ray; 2.13 A; A=1-238.	[ExPASy / RCSB / EBI]
1EMC; X-ray; 2.30 A; A/B/C/D=2-237.	[ExPASy / RCSB / EBI]
1EME; X-ray; 2.50 A; A=2-237.	[ExPASy / RCSB / EBI]
1EMF; X-ray; 2.40 A; A=2-238.	[ExPASy / RCSB / EBI]
1EMG; X-ray; 2.00 A; A=1-238.	[ExPASy / RCSB / EBI]
1EMK; X-ray; 2.10 A; A=2-237.	[ExPASy / RCSB / EBI]
1EML; X-ray; 2.30 A; A=2-237.	[ExPASy / RCSB / EBI]
1EMM; X-ray; 2.30 A; A=2-238.	[ExPASy / RCSB / EBI]
1F09; X-ray; 2.14 A; A=1-238.	[ExPASy / RCSB / EBI]
1F0B; X-ray; 2.10 A; A=1-238.	[ExPASy / RCSB / EBI]
1GFL; X-ray; 1.90 A; A/B=2-238.	[ExPASy / RCSB / EBI]
1H6R; X-ray; 1.50 A; A/B/C=1-238.	[ExPASy / RCSB / EBI]
1HCJ; X-ray; 1.80 A; A/B/C/D=1-238.	[ExPASy / RCSB / EBI]
1HUY; X-ray; 2.20 A; A=2-238.	[ExPASy / RCSB / EBI]
1JBY; X-ray; 1.80 A; A=1-238.	[ExPASy / RCSB / EBI]
1JBZ; X-ray; 1.50 A; A=1-238.	[ExPASy / RCSB / EBI]
1JC0; X-ray; 2.00 A; A/B/C=1-238.	[ExPASy / RCSB / EBI]
1JC1; X-ray; 1.90 A; A/B/C=1-238.	[ExPASy / RCSB / EBI]
1KP5; X-ray; 2.60 A; A/B=3-238.	[ExPASy / RCSB / EBI]
1KYP; X-ray; 1.35 A; A=2-238.	[ExPASy / RCSB / EBI]
1KYR; X-ray; 1.50 A; A=2-238.	[ExPASy / RCSB / EBI]
1KYS; X-ray; 1.44 A; A=2-238.	[ExPASy / RCSB / EBI]
1MYW; X-ray; 2.20 A; A=2-238.	[ExPASy / RCSB / EBI]
1Q4A; X-ray; 1.45 A; A=1-238.	[ExPASy / RCSB / EBI]
1Q4B; X-ray; 1.48 A; A=1-238.	[ExPASy / RCSB / EBI]
1Q4C; X-ray; 1.55 A; A=1-238.	[ExPASy / RCSB / EBI]
1Q4D; X-ray; 1.58 A; A=1-238.	[ExPASy / RCSB / EBI]
1Q4E; X-ray; 1.38 A; A=1-238.	[ExPASy / RCSB / EBI]
1Q73; X-ray; 1.60 A; A=1-238.	[ExPASy / RCSB / EBI]
1QXT; X-ray; 2.00 A; A=2-229.	[ExPASy / RCSB / EBI]
1QY3; X-ray; 2.00 A; A=1-229.	[ExPASy / RCSB / EBI]
1QYF; X-ray; 1.50 A; A=2-227.	[ExPASy / RCSB / EBI]
1QYO; X-ray; 1.80 A; A=1-238.	[ExPASy / RCSB / EBI]
1QYQ; X-ray; 1.80 A; A=2-238.	[ExPASy / RCSB / EBI]
1RM9; X-ray; 2.90 A; A=2-238.	[ExPASy / RCSB / EBI]
1RMM; X-ray; 1.90 A; A=2-229.	[ExPASy / RCSB / EBI]
1RMO; X-ray; 1.80 A; A=2-238.	[ExPASy / RCSB / EBI]
1RMP; X-ray; 3.00 A; A=2-229.	[ExPASy / RCSB / EBI]
1RRX; X-ray; 2.10 A; A=2-229.	[ExPASy / RCSB / EBI]
1W7S; X-ray; 1.85 A; A/B/C/D=1-238.	[ExPASy / RCSB / EBI]
1W7T; X-ray; 1.85 A; A/B/C/D=1-238.	[ExPASy / RCSB / EBI]
1W7U; X-ray; 1.85 A; A/B/C/D=1-238.	[ExPASy / RCSB / EBI]
1YFP; X-ray; 2.50 A; A/B=3-229.	[ExPASy / RCSB / EBI]
1YHG; X-ray; 2.50 A; A/B=2-238.	[ExPASy / RCSB / EBI]
1YHH; X-ray; 1.50 A; A=2-238.	[ExPASy / RCSB / EBI]
1YHI; X-ray; 1.90 A; A=2-238.	[ExPASy / RCSB / EBI]
1YJ2; X-ray; 1.50 A; A=2-238.	[ExPASy / RCSB / EBI]
1YJF; X-ray; 1.35 A; A=2-238.	[ExPASy / RCSB / EBI]
1Z1P; X-ray; 2.00 A; A=1-238.	[ExPASy / RCSB / EBI]
1Z1Q; X-ray; 1.50 A; A=1-238.	[ExPASy / RCSB / EBI]
2AH8; X-ray; 2.24 A; A/B=1-238.	[ExPASy / RCSB / EBI]
2AHA; X-ray; 1.98 A; A/B=1-238.	[ExPASy / RCSB / EBI]
2AWJ; X-ray; 1.60 A; A=2-229.	[ExPASy / RCSB / EBI]
2AWK; X-ray; 1.15 A; A=2-229.	[ExPASy / RCSB / EBI]
2AWL; X-ray; 1.85 A; A=2-229.	[ExPASy / RCSB / EBI]
2AWM; X-ray; 1.70 A; A=2-229.	[ExPASy / RCSB / EBI]
2B3P; X-ray; 1.40 A; A=1-238.	[ExPASy / RCSB / EBI]
2B3Q; X-ray; 2.30 A; A/B/C/D=1-238.	[ExPASy / RCSB / EBI]
2DUE; X-ray; 1.24 A; A=1-238.	[ExPASy / RCSB / EBI]
2DUF; X-ray; 1.50 A; A=1-238.	[ExPASy / RCSB / EBI]
2DUG; X-ray; 1.40 A; A=1-238.	[ExPASy / RCSB / EBI]
2DUH; X-ray; 1.20 A; A=1-238.	[ExPASy / RCSB / EBI]
2DUI; X-ray; 1.36 A; A=1-238.	[ExPASy / RCSB / EBI]
2EMD; X-ray; 2.00 A; A=2-238.	[ExPASy / RCSB / EBI]
2EMN; X-ray; 2.30 A; A=2-238.	[ExPASy / RCSB / EBI]
2EMO; X-ray; 2.60 A; A=2-238.	[ExPASy / RCSB / EBI]
2FWQ; X-ray; 1.40 A; A=2-238.	[ExPASy / RCSB / EBI]
2FZU; X-ray; 1.25 A; A=2-238.	[ExPASy / RCSB / EBI]
2G16; X-ray; 2.00 A; A=2-64, B=68-238.	[ExPASy / RCSB / EBI]
2G2S; X-ray; 1.20 A; A=2-63, B=67-238.	[ExPASy / RCSB / EBI]
2G3D; X-ray; 1.35 A; A=2-63, B=67-238.	[ExPASy / RCSB / EBI]
2G5Z; X-ray; 1.80 A; A=2-64, B=67-238.	[ExPASy / RCSB / EBI]
2G6E; X-ray; 1.30 A; A=2-238.	[ExPASy / RCSB / EBI]
2H6V; X-ray; 1.47 A; A=2-238.	[ExPASy / RCSB / EBI]
2H9W; X-ray; 1.82 A; A=2-237.	[ExPASy / RCSB / EBI]
2HCG; X-ray; 1.35 A; A=2-238.	[ExPASy / RCSB / EBI]
2HFC; X-ray; 1.20 A; A=2-238.	[ExPASy / RCSB / EBI]
2HGD; X-ray; 1.60 A; A=2-238.	[ExPASy / RCSB / EBI]
2HGY; X-ray; 2.05 A; A=2-238.	[ExPASy / RCSB / EBI]
2HJO; X-ray; 1.25 A; A=1-238.	[ExPASy / RCSB / EBI]
2HQZ; X-ray; 1.20 A; A=1-238.	[ExPASy / RCSB / EBI]
2HRS; X-ray; 1.40 A; A=1-238.	[ExPASy / RCSB / EBI]
2O24; X-ray; 1.45 A; A=2-238.	[ExPASy / RCSB / EBI]
2O29; X-ray; 1.80 A; A=2-238.	[ExPASy / RCSB / EBI]
2O2B; X-ray; 1.94 A; A=2-238.	[ExPASy / RCSB / EBI]
2OKW; X-ray; 1.90 A; A/B/C/D/E/F=1-238.	[ExPASy / RCSB / EBI]
2OKY; X-ray; 2.40 A; A/B=1-238.	[ExPASy / RCSB / EBI]
2Q57; X-ray; 2.00 A; A=1-238.	[ExPASy / RCSB / EBI]
2Q6P; X-ray; 2.10 A; A=1-238.	[ExPASy / RCSB / EBI]
2QRF; X-ray; 1.50 A; A=1-230.	[ExPASy / RCSB / EBI]
2QT2; X-ray; 1.31 A; A=1-238.	[ExPASy / RCSB / EBI]
2QU1; X-ray; 1.70 A; A=1-238.	[ExPASy / RCSB / EBI]
2QZ0; X-ray; 1.20 A; A=2-229.	[ExPASy / RCSB / EBI]
2YFP; X-ray; 2.60 A; A=1-238.	[ExPASy / RCSB / EBI]
3CB9; X-ray; 1.31 A; A=2-238.	[ExPASy / RCSB / EBI]
3CBE; X-ray; 1.49 A; A=2-238.	[ExPASy / RCSB / EBI]
3CD1; X-ray; 1.31 A; A=2-238.	[ExPASy / RCSB / EBI]
3CD9; X-ray; 1.50 A; A=2-238.	[ExPASy / RCSB / EBI]
3DPW; X-ray; 1.59 A; A=2-238.	[ExPASy / RCSB / EBI]
3DPX; X-ray; 1.50 A; A=2-238.	[ExPASy / RCSB / EBI]
3DPZ; X-ray; 1.70 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ1; X-ray; 1.70 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ2; X-ray; 1.60 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ3; X-ray; 1.70 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ4; X-ray; 1.47 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ5; X-ray; 1.50 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ6; X-ray; 1.60 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ7; X-ray; 1.23 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ8; X-ray; 1.51 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQ9; X-ray; 1.40 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQA; X-ray; 1.44 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQC; X-ray; 1.49 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQD; X-ray; 1.40 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQE; X-ray; 1.43 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQF; X-ray; 1.46 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQH; X-ray; 1.45 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQI; X-ray; 1.42 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQJ; X-ray; 1.51 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQK; X-ray; 1.40 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQL; X-ray; 1.47 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQM; X-ray; 1.44 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQN; X-ray; 1.44 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQO; X-ray; 1.50 A; A=2-238.	[ExPASy / RCSB / EBI]
3DQU; X-ray; 1.42 A; A=2-238.	[ExPASy / RCSB / EBI]
3ED8; X-ray; 2.70 A; A/B/C/D/E=2-238.	[ExPASy / RCSB / EBI]
3EK4; X-ray; 2.65 A; A=2-238.	[ExPASy / RCSB / EBI]
3EK7; X-ray; 1.85 A; A=2-238.	[ExPASy / RCSB / EBI]
3EK8; X-ray; 2.80 A; A=2-238.	[ExPASy / RCSB / EBI]
3EKH; X-ray; 2.00 A; A=2-238.	[ExPASy / RCSB / EBI]
3EKJ; X-ray; 2.80 A; A=2-238.	[ExPASy / RCSB / EBI]
3EVP; X-ray; 1.45 A; A=2-238.	[ExPASy / RCSB / EBI]
3EVR; X-ray; 2.00 A; A=2-238.	[ExPASy / RCSB / EBI]
3EVU; X-ray; 1.75 A; A=2-238.	[ExPASy / RCSB / EBI]
3EVV; X-ray; 2.60 A; A=2-238.	[ExPASy / RCSB / EBI]
3GJ1; X-ray; 1.80 A; A/B/C/D=1-230.	[ExPASy / RCSB / EBI]
3GJ2; X-ray; 1.90 A; A/B/C/D=1-230.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B9C; -.
1BFP; -.
1C4F; -.
1CV7; -.
1EMA; -.
1EMB; -.
1EMC; -.
1EME; -.
1EMF; -.
1EMG; -.
1EMK; -.
1EML; -.
1EMM; -.
1F09; -.
1F0B; -.
1GFL; -.
1H6R; -.
1HCJ; -.
1HUY; -.
1JBY; -.
1JBZ; -.
1JC0; -.
1JC1; -.
1KP5; -.
1KYP; -.
1KYR; -.
1KYS; -.
1MYW; -.
1Q4A; -.
1Q4B; -.
1Q4C; -.
1Q4D; -.
1Q4E; -.
1Q73; -.
1QXT; -.
1QY3; -.
1QYF; -.
1QYO; -.
1QYQ; -.
1RM9; -.
1RMM; -.
1RMO; -.
1RMP; -.
1RRX; -.
1W7S; -.
1W7T; -.
1W7U; -.
1YFP; -.
1YHG; -.
1YHH; -.
1YHI; -.
1YJ2; -.
1YJF; -.
1Z1P; -.
1Z1Q; -.
2AH8; -.
2AHA; -.
2AWJ; -.
2AWK; -.
2AWL; -.
2AWM; -.
2B3P; -.
2B3Q; -.
2DUE; -.
2DUF; -.
2DUG; -.
2DUH; -.
2DUI; -.
2EMD; -.
2EMN; -.
2EMO; -.
2FWQ; -.
2FZU; -.
2G16; -.
2G2S; -.
2G3D; -.
2G5Z; -.
2G6E; -.
2H6V; -.
2H9W; -.
2HCG; -.
2HFC; -.
2HGD; -.
2HGY; -.
2HJO; -.
2HQZ; -.
2HRS; -.
2O24; -.
2O29; -.
2O2B; -.
2OKW; -.
2OKY; -.
2Q57; -.
2Q6P; -.
2QRF; -.
2QT2; -.
2QU1; -.
2QZ0; -.
2YFP; -.
3CB9; -.
3CBE; -.
3CD1; -.
3CD9; -.
3DPW; -.
3DPX; -.
3DPZ; -.
3DQ1; -.
3DQ2; -.
3DQ3; -.
3DQ4; -.
3DQ5; -.
3DQ6; -.
3DQ7; -.
3DQ8; -.
3DQ9; -.
3DQA; -.
3DQC; -.
3DQD; -.
3DQE; -.
3DQF; -.
3DQH; -.
3DQI; -.
3DQJ; -.
3DQK; -.
3DQL; -.
3DQM; -.
3DQN; -.
3DQO; -.
3DQU; -.
3ED8; -.
3EK4; -.
3EK7; -.
3EK8; -.
3EKH; -.
3EKJ; -.
3EVP; -.
3EVR; -.
3EVU; -.
3EVV; -.
3GJ1; -.
3GJ2; -.

ModBase

P42212.

Ontologies

GO:0008218;	Biological process: bioluminescence (traceable author statement from UniProtKB).
GO:0006091;	Biological process: generation of precursor metabolites and energy (traceable author statement from UniProtKB).
GO:0018298;	Biological process: protein-chromophore linkage (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011584; GFP_related.
IPR000786; Green_fluorescent_prot.
Graphical view of domain structure.

Pfam

PF01353; GFP; 1.
Pfam graphical view of domain structure.

PRINTS

PR01229; GFLUORESCENT.

ProDom

PD013756; Green_fl_protein; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

ProtoNet

P42212.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chromophore; Direct protein sequencing; Luminescence; Photoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 238`	`238`	`Green fluorescent protein.`	`PRO_0000192576`
`MOD_RES`	`66 66`		`(Z)-2,3-didehydrotyrosine.`
`CROSSLNK`	`65 67`		`5-imidazolinone (Ser-Gly).`
`VARIANT`	`100 100`	`1`	`F -> Y.`
`VARIANT`	`108 108`	`1`	`T -> S.`
`VARIANT`	`141 141`	`1`	`L -> M.`
`VARIANT`	`219 219`	`1`	`V -> I.`
`MUTAGEN`	`65 65`		`S->G: In mut3; highly fluorescent mutant when excited at 488 nm; when associated with A-72.`
`MUTAGEN`	`65 65`		`S->T: Increases fluoresence, photostability and shift the major exitation peak to 488 nm.`
`MUTAGEN`	`72 72`		`S->A: In mut3; highly fluorescent mutant when excited at 488 nm; when associated with G-65.`
`CONFLICT`	`2 2`		`S -> G (in Ref. 3; CAA65278).`
`CONFLICT`	`25 25`		`H -> Q (in Ref. 3; CAA65278).`
`CONFLICT`	`80 80`		`Q -> R (in Ref. 3; CAA65278).`
`CONFLICT`	`157 157`		`Q -> P (in Ref. 2; AAA58246).`
`CONFLICT`	`172 172`		`E -> K (in Ref. 2; AAA58246).`
`HELIX`	`5 8`	`4`
`STRAND`	`12 22`	`11`
`STRAND`	`25 36`	`12`
`HELIX`	`37 39`	`3`
`STRAND`	`41 48`	`8`
`HELIX`	`57 60`	`4`
`TURN`	`61 63`	`3`
`HELIX`	`69 71`	`3`
`HELIX`	`76 81`	`6`
`HELIX`	`83 86`	`4`
`TURN`	`87 90`	`4`
`STRAND`	`92 100`	`9`
`STRAND`	`105 115`	`11`
`STRAND`	`118 129`	`12`
`TURN`	`135 139`	`5`
`STRAND`	`149 155`	`7`
`HELIX`	`156 158`	`3`
`STRAND`	`160 171`	`12`
`STRAND`	`176 191`	`16`
`STRAND`	`198 208`	`11`
`STRAND`	`215 228`	`14`
`HELIX`	`233 236`	`4`

Sequence information

Length: 238 AA [This is the length of the unprocessed precursor]

Molecular weight: 26886 Da [This is the MW of the unprocessed precursor]

CRC64: EA5A6F21FBFB6E05 [This is a checksum on the sequence]

        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

P42212 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools