ID   GFPL_DISST              Reviewed;         232 AA.
AC   Q9U6Y7;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=GFP-like fluorescent chromoprotein dsFP483;
OS   Discosoma striata (Striped mushroom).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Corallimorpharia;
OC   Discosomidae; Discosoma.
OX   NCBI_TaxID=105400;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF03370.1}
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).
CC   -!- FUNCTION: Pigment protein that is green in color.
CC       {ECO:0000269|PubMed:10504696}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=443 nm;
CC         Note=Has a strong fluorescence emission spectrum which peaks at 483
CC         nm.;
CC   -!- TISSUE SPECIFICITY: Oral disk. {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), oxidation of Tyr-(N+1) to
CC       didehydrotyrosine, and formation of a double bond to the alpha-amino
CC       nitrogen of residue Xaa-N. Maturation of the chromophore requires
CC       nothing other than molecular oxygen. The precise stereochemistry of the
CC       tyrosine has not been determined.
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   -!- SIMILARITY: Belongs to the GFP family. {ECO:0000269|PubMed:10504696}.
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DR   EMBL; AF168420; AAF03370.1; -; mRNA.
DR   PDB; 3CGL; X-ray; 2.09 A; A/B/C/D/E/F=1-232.
DR   PDBsum; 3CGL; -.
DR   AlphaFoldDB; Q9U6Y7; -.
DR   SMR; Q9U6Y7; -.
DR   EvolutionaryTrace; Q9U6Y7; -.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro.
DR   Gene3D; 2.40.155.10; -; 1.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR011584; GFP-related.
DR   InterPro; IPR000786; Green_fluorescent_prot.
DR   Pfam; PF01353; GFP; 1.
DR   PRINTS; PR01229; GFLUORESCENT.
DR   SUPFAM; SSF54511; SSF54511; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromophore; Luminescence; Photoprotein.
FT   CHAIN           1..232
FT                   /note="GFP-like fluorescent chromoprotein dsFP483"
FT                   /id="PRO_0000192581"
FT   MOD_RES         67
FT                   /note="2,3-didehydrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT   CROSSLNK        66..68
FT                   /note="2-iminomethyl-5-imidazolinone (Gln-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT   HELIX           3..6
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          10..22
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          25..36
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   TURN            37..40
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          41..51
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   HELIX           58..61
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   HELIX           62..65
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          104..114
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          117..127
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   TURN            134..138
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          146..153
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          156..167
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          172..185
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          193..205
FT                   /evidence="ECO:0007829|PDB:3CGL"
FT   STRAND          209..221
FT                   /evidence="ECO:0007829|PDB:3CGL"
SQ   SEQUENCE   232 AA;  26435 MW;  AA8F18EEE283CE4D CRC64;
     MSCSKSVIKE EMLIDLHLEG TFNGHYFEIK GKGKGQPNEG TNTVTLEVTK GGPLPFGWHI
     LCPQFQYGNK AFVHHPDNIH DYLKLSFPEG YTWERSMHFE DGGLCCITND ISLTGNCFYY
     DIKFTGLNFP PNGPVVQKKT TGWEPSTERL YPRDGVLIGD IHHALTVEGG GHYACDIKTV
     YRAKKAALKM PGYHYVDTKL VIWNNDKEFM KVEEHEIAVA RHHPFYEPKK DK