ID   GFPL1_ZOASP             Reviewed;         231 AA.
AC   Q9U6Y5;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=GFP-like fluorescent chromoprotein FP506;
DE   AltName: Full=zFP506;
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:AAF03372.1}
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 yellow-green in color.
CC       {ECO:0000269|PubMed:10504696}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=492 nm;
CC         Note=Exhibits a smaller absorbance peak at 480 nm. Has a strong
CC         fluorescence emission spectrum which peaks at 506 nm.;
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. Maturation of the chromophore requires nothing other
CC       than molecular oxygen. The precise stereochemistry of the tyrosine has
CC       not been determined. {ECO:0000305}.
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; AF168422; AAF03372.1; -; mRNA.
DR   PDB; 2ICR; X-ray; 1.51 A; A/B/C/D=17-231.
DR   PDB; 2OJK; X-ray; 2.20 A; A/B=1-231.
DR   PDB; 2PXS; X-ray; 2.20 A; A/B=4-231.
DR   PDB; 2PXW; X-ray; 2.40 A; A/B=4-231.
DR   PDBsum; 2ICR; -.
DR   PDBsum; 2OJK; -.
DR   PDBsum; 2PXS; -.
DR   PDBsum; 2PXW; -.
DR   AlphaFoldDB; Q9U6Y5; -.
DR   SMR; Q9U6Y5; -.
DR   PRIDE; Q9U6Y5; -.
DR   EvolutionaryTrace; Q9U6Y5; -.
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; Chromophore; Luminescence; Photoprotein.
FT   CHAIN           1..231
FT                   /note="GFP-like fluorescent chromoprotein FP506"
FT                   /id="PRO_0000192582"
FT   MOD_RES         67
FT                   /note="2,3-didehydrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT   CROSSLNK        66..68
FT                   /note="5-imidazolinone (Asn-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT   STRAND          10..22
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          25..36
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          41..51
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   HELIX           58..64
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:2OJK"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          104..114
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   TURN            115..118
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          119..129
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   TURN            136..140
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   TURN            156..159
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          160..171
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          176..189
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          198..208
FT                   /evidence="ECO:0007829|PDB:2ICR"
FT   STRAND          216..226
FT                   /evidence="ECO:0007829|PDB:2ICR"
SQ   SEQUENCE   231 AA;  26111 MW;  E6B1C029C461C2BC CRC64;
     MAQSKHGLTK EMTMKYRMEG CVDGHKFVIT GEGIGYPFKG KQAINLCVVE GGPLPFAEDI
     LSAAFNYGNR VFTEYPQDIV DYFKNSCPAG YTWDRSFLFE DGAVCICNAD ITVSVEENCM
     YHESKFYGVN FPADGPVMKK MTDNWEPSCE KIIPVPKQGI LKGDVSMYLL LKDGGRLRCQ
     FDTVYKAKSV PRKMPDWHFI QHKLTREDRS DAKNQKWHLT EHAIASGSAL P