GFPL2_ZOASP
ID GFPL2_ZOASP Reviewed; 231 AA.
AC Q9U6Y4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=GFP-like fluorescent chromoprotein FP538;
DE AltName: Full=zFP538;
DE Contains:
DE RecName: Full=GFP-like fluorescent chromoprotein FP538 chain 1;
DE Contains:
DE RecName: Full=GFP-like fluorescent chromoprotein FP538 chain 2;
OS Zoanthus sp. (Green polyp).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Zoantharia;
OC Zoanthidae; Zoanthus; unclassified Zoanthus.
OX NCBI_TaxID=105402;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF03373.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10504696; DOI=10.1038/13657;
RA Matz M.V., Fradkov A.F., Labas Y.A., Savitsky A.P., Zaraisky A.G.,
RA Markelov M.L., Lukyanov S.A.;
RT "Fluorescent proteins from nonbioluminescent Anthozoa species.";
RL Nat. Biotechnol. 17:969-973(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AMIDATION AT PHE-65, CHROMOPHORE STRUCTURE, AND
RP MUTAGENESIS OF LYS-66.
RX PubMed=15628861; DOI=10.1021/bi048383r;
RA Remington S.J., Wachter R.M., Yarbrough D.K., Branchaud B., Anderson D.C.,
RA Kallio K., Lukyanov K.A.;
RT "zFP538, a yellow-fluorescent protein from Zoanthus, contains a novel
RT three-ring chromophore.";
RL Biochemistry 44:202-212(2005).
CC -!- FUNCTION: Pigment protein that is yellow in color.
CC {ECO:0000269|PubMed:10504696, ECO:0000269|PubMed:15628861}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=528 nm {ECO:0000269|PubMed:15628861};
CC Note=Exhibits a smaller absorbance peak at 494 nm. Has a strong
CC fluorescence emission spectrum which peaks at 538 nm.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15628861}.
CC -!- TISSUE SPECIFICITY: Tentacle and oral disk.
CC {ECO:0000269|PubMed:10504696}.
CC -!- PTM: Contains a chromophore consisting of modified amino acid residues.
CC The chromophore is formed by autocatalytic backbone condensation
CC between Xaa-N and Gly-(N+2), and oxidation of Tyr-(N+1) to
CC didehydrotyrosine. In addition, the residue N lysine undergoes
CC cyclization. The alpha-amino nitrogen is replaced by the epsilon-amino
CC nitrogen, the peptide chain is broken, residue N-1 is released as an
CC amide, and a double bond is formed between the alpha-carbon and the
CC nitrogen so that a tetrahydropyridine ring results. Maturation of the
CC chromophore requires nothing other than molecular oxygen.
CC -!- BIOTECHNOLOGY: Fluorescent proteins have become a useful and ubiquitous
CC tool for making chimeric proteins, where they function as a fluorescent
CC protein tag. Typically they tolerate N- and C-terminal fusion to a
CC broad variety of proteins. They have been expressed in most known cell
CC types and are used as a noninvasive fluorescent marker in living cells
CC and organisms. They enable a wide range of applications where they have
CC functioned as a cell lineage tracer, reporter of gene expression, or as
CC a measure of protein-protein interactions. {ECO:0000305}.
CC -!- MISCELLANEOUS: Fluorescence excitation of the Glu-66 mutant is at 493
CC nm and 550 nm with intense green emission at 405 nm and a weak red
CC emission at 576 nm. Fluorescence emission of the Asp-66 mutant is at
CC 524 nm and 552 nm and with a broad red emission shoulder extending from
CC 650 nm.
CC -!- SIMILARITY: Belongs to the GFP family. {ECO:0000269|PubMed:10504696}.
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DR EMBL; AF168423; AAF03373.1; -; mRNA.
DR PDB; 1XA9; X-ray; 2.50 A; A=1-231.
DR PDB; 1XAE; X-ray; 2.70 A; A/B=1-231.
DR PDB; 2OGR; X-ray; 1.80 A; A/B/C/D=1-231.
DR PDB; 5Y8Q; X-ray; 2.90 A; A/B=1-231.
DR PDB; 5Y8R; X-ray; 2.30 A; A=1-231.
DR PDBsum; 1XA9; -.
DR PDBsum; 1XAE; -.
DR PDBsum; 2OGR; -.
DR PDBsum; 5Y8Q; -.
DR PDBsum; 5Y8R; -.
DR AlphaFoldDB; Q9U6Y4; -.
DR SMR; Q9U6Y4; -.
DR EvolutionaryTrace; Q9U6Y4; -.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR Gene3D; 2.40.155.10; -; 1.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR011584; GFP-related.
DR Pfam; PF01353; GFP; 1.
DR SUPFAM; SSF54511; SSF54511; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Chromophore; Luminescence; Photoprotein.
FT CHAIN 1..65
FT /note="GFP-like fluorescent chromoprotein FP538 chain 1"
FT /id="PRO_0000010858"
FT CHAIN 66..231
FT /note="GFP-like fluorescent chromoprotein FP538 chain 2"
FT /id="PRO_0000010859"
FT SITE 65..66
FT /note="Cleavage"
FT MOD_RES 65
FT /note="Phenylalanine amide; atypical"
FT /evidence="ECO:0000305|PubMed:15628861"
FT MOD_RES 67
FT /note="2,3-didehydrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT CROSSLNK 66..68
FT /note="2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly)"
FT /evidence="ECO:0000269|PubMed:15628861"
FT MUTAGEN 66
FT /note="K->A,C,F,G,H,L,N,S,T,P,Q: Changes fluorescence
FT emission from yellow to green."
FT /evidence="ECO:0000269|PubMed:15628861"
FT MUTAGEN 66
FT /note="K->E,D: Changes fluorescence emission from yellow to
FT green with a weak red peak."
FT /evidence="ECO:0000269|PubMed:15628861"
FT MUTAGEN 66
FT /note="K->I,R,W,Y: Produces a non-fluorescent form."
FT /evidence="ECO:0000269|PubMed:15628861"
FT STRAND 10..22
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:2OGR"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:2OGR"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2OGR"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5Y8R"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2OGR"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 104..114
FT /evidence="ECO:0007829|PDB:2OGR"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:2OGR"
FT TURN 136..140
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:2OGR"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 176..189
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:2OGR"
FT STRAND 216..226
FT /evidence="ECO:0007829|PDB:2OGR"
SQ 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
