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GFP-like fluorescent chromoprotein FP538 (zFP538) [Cleaved into: GFP-like fluorescent chromoprotein FP538 chain 1; GFP-like fluorescent chromoprotein FP538 chain 2]

 GFPL2_ZOASP             Reviewed;         231 AA.
Q9U6Y4;
21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 55.
RecName: Full=GFP-like fluorescent chromoprotein FP538;
AltName: Full=zFP538;
Contains:
RecName: Full=GFP-like fluorescent chromoprotein FP538 chain 1;
Contains:
RecName: Full=GFP-like fluorescent chromoprotein FP538 chain 2;
Zoanthus sp. (Green polyp).
Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Zoantharia;
Zoanthidae; Zoanthus.
NCBI_TaxID=105402;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF03373.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10504696; DOI=10.1038/13657;
Matz M.V., Fradkov A.F., Labas Y.A., Savitsky A.P., Zaraisky A.G.,
Markelov M.L., Lukyanov S.A.;
"Fluorescent proteins from nonbioluminescent Anthozoa species.";
Nat. Biotechnol. 17:969-973(1999).
[2]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, AMIDATION AT PHE-65, CHROMOPHORE STRUCTURE, AND
MUTAGENESIS OF LYS-66.
PubMed=15628861; DOI=10.1021/bi048383r;
Remington S.J., Wachter R.M., Yarbrough D.K., Branchaud B.,
Anderson D.C., Kallio K., Lukyanov K.A.;
"zFP538, a yellow-fluorescent protein from Zoanthus, contains a novel
three-ring chromophore.";
Biochemistry 44:202-212(2005).
-!- FUNCTION: Pigment protein that is yellow in color.
{ECO:0000269|PubMed:10504696, ECO:0000269|PubMed:15628861}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=528 nm {ECO:0000269|PubMed:15628861};
Note=Exhibits a smaller absorbance peak at 494 nm. Has a strong
fluorescence emission spectrum which peaks at 538 nm.;
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15628861}.
-!- TISSUE SPECIFICITY: Tentacle and oral disk.
{ECO:0000269|PubMed:10504696}.
-!- PTM: Contains a chromophore consisting of modified amino acid
residues. The chromophore is formed by autocatalytic backbone
condensation between Xaa-N and Gly-(N+2), and oxidation of Tyr-
(N+1) to didehydrotyrosine. In addition, the residue N lysine
undergoes cyclization. The alpha-amino nitrogen is replaced by the
epsilon-amino nitrogen, the peptide chain is broken, residue N-1
is released as an amide, and a double bond is formed between the
alpha-carbon and the nitrogen so that a tetrahydropyridine ring
results. Maturation of the chromophore requires nothing other than
molecular oxygen.
-!- BIOTECHNOLOGY: 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. {ECO:0000305}.
-!- MISCELLANEOUS: Fluorescence excitation of the Glu-66 mutant is at
493 nm and 550 nm with intense green emission at 405 nm and a weak
red emission at 576 nm. Fluorescence emission of the Asp-66 mutant
is at 524 nm and 552 nm and with a broad red emission shoulder
extending from 650 nm.
-!- SIMILARITY: Belongs to the GFP family.
{ECO:0000269|PubMed:10504696}.
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EMBL; AF168423; AAF03373.1; -; mRNA.
PDB; 1XA9; X-ray; 2.50 A; A=1-231.
PDB; 1XAE; X-ray; 2.70 A; A/B=1-231.
PDB; 2OGR; X-ray; 1.80 A; A/B/C/D=1-231.
PDB; 5Y8Q; X-ray; 2.90 A; A/B=1-231.
PDB; 5Y8R; X-ray; 2.30 A; A=1-231.
PDBsum; 1XA9; -.
PDBsum; 1XAE; -.
PDBsum; 2OGR; -.
PDBsum; 5Y8Q; -.
PDBsum; 5Y8R; -.
ProteinModelPortal; Q9U6Y4; -.
SMR; Q9U6Y4; -.
EvolutionaryTrace; Q9U6Y4; -.
GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
InterPro; IPR009017; GFP.
InterPro; IPR011584; GFP-related.
Pfam; PF01353; GFP; 1.
SUPFAM; SSF54511; SSF54511; 1.
1: Evidence at protein level;
3D-structure; Amidation; Chromophore; Luminescence; Photoprotein.
CHAIN 1 65 GFP-like fluorescent chromoprotein FP538
chain 1.
/FTId=PRO_0000010858.
CHAIN 66 231 GFP-like fluorescent chromoprotein FP538
chain 2.
/FTId=PRO_0000010859.
SITE 65 66 Cleavage.
MOD_RES 65 65 Phenylalanine amide; atypical.
{ECO:0000305|PubMed:15628861}.
MOD_RES 67 67 2,3-didehydrotyrosine.
{ECO:0000250|UniProtKB:Q9U6Y8}.
CROSSLNK 66 68 2-tetrahydro-2-pyridyl-5-imidazolinone
(Lys-Gly). {ECO:0000269|PubMed:15628861}.
MUTAGEN 66 66 K->A,C,F,G,H,L,N,S,T,P,Q: Changes
fluorescence emission from yellow to
green. {ECO:0000269|PubMed:15628861}.
MUTAGEN 66 66 K->E,D: Changes fluorescence emission
from yellow to green with a weak red
peak. {ECO:0000269|PubMed:15628861}.
MUTAGEN 66 66 K->I,R,W,Y: Produces a non-fluorescent
form. {ECO:0000269|PubMed:15628861}.
STRAND 10 22 {ECO:0000244|PDB:2OGR}.
STRAND 25 36 {ECO:0000244|PDB:2OGR}.
HELIX 37 39 {ECO:0000244|PDB:2OGR}.
STRAND 41 51 {ECO:0000244|PDB:2OGR}.
HELIX 58 64 {ECO:0000244|PDB:2OGR}.
HELIX 70 72 {ECO:0000244|PDB:5Y8R}.
HELIX 82 85 {ECO:0000244|PDB:2OGR}.
TURN 86 89 {ECO:0000244|PDB:2OGR}.
STRAND 91 99 {ECO:0000244|PDB:2OGR}.
STRAND 104 114 {ECO:0000244|PDB:2OGR}.
TURN 115 118 {ECO:0000244|PDB:2OGR}.
STRAND 119 129 {ECO:0000244|PDB:2OGR}.
TURN 136 140 {ECO:0000244|PDB:2OGR}.
STRAND 142 145 {ECO:0000244|PDB:2OGR}.
STRAND 148 154 {ECO:0000244|PDB:2OGR}.
TURN 156 158 {ECO:0000244|PDB:2OGR}.
STRAND 161 171 {ECO:0000244|PDB:2OGR}.
STRAND 176 189 {ECO:0000244|PDB:2OGR}.
STRAND 197 208 {ECO:0000244|PDB:2OGR}.
STRAND 216 226 {ECO:0000244|PDB:2OGR}.
SEQUENCE 231 AA; 26171 MW; 1C011421C448F65D CRC64;
MAHSKHGLKE EMTMKYHMEG CVNGHKFVIT GEGIGYPFKG KQTINLCVIE GGPLPFSEDI
LSAGFKYGDR IFTEYPQDIV DYFKNSCPAG YTWGRSFLFE DGAVCICNVD ITVSVKENCI
YHKSIFNGMN FPADGPVMKK MTTNWEASCE KIMPVPKQGI LKGDVSMYLL LKDGGRYRCQ
FDTVYKAKSV PSKMPEWHFI QHKLLREDRS DAKNQKWQLT EHAIAFPSAL A


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