GFPL_ANEMA
ID GFPL_ANEMA Reviewed; 229 AA.
AC Q9U6Y6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=GFP-like fluorescent chromoprotein amFP486;
OS Anemonia manjano (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anemonia.
OX NCBI_TaxID=105399;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF03371.1}
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 (1.65 ANGSTROMS) OF 2-229, AND MUTAGENESIS OF
RP GLU-150; ALA-165; HIS-199 AND GLU-217.
RX PubMed=16120682; DOI=10.1073/pnas.0502250102;
RA Henderson J.N., Remington S.J.;
RT "Crystal structures and mutational analysis of amFP486, a cyan fluorescent
RT protein from Anemonia majano.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12712-12717(2005).
CC -!- FUNCTION: Pigment protein that is green in color.
CC {ECO:0000269|PubMed:10504696}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=458 nm;
CC Note=Has a strong fluorescence emission spectrum which peaks at 486
CC nm.;
CC -!- TISSUE SPECIFICITY: Tentacle tip. {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; AF168421; AAF03371.1; -; mRNA.
DR PDB; 2A46; X-ray; 1.65 A; A=2-227.
DR PDB; 2A47; X-ray; 1.72 A; A=2-227.
DR PDB; 2A48; X-ray; 2.00 A; A=2-227.
DR PDBsum; 2A46; -.
DR PDBsum; 2A47; -.
DR PDBsum; 2A48; -.
DR AlphaFoldDB; Q9U6Y6; -.
DR SMR; Q9U6Y6; -.
DR EvolutionaryTrace; Q9U6Y6; -.
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..229
FT /note="GFP-like fluorescent chromoprotein amFP486"
FT /id="PRO_0000192579"
FT MOD_RES 69
FT /note="2,3-didehydrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT CROSSLNK 68..70
FT /note="5-imidazolinone (Lys-Gly)"
FT MUTAGEN 150
FT /note="E->Q: Shifts fluorescence to 506 nm."
FT /evidence="ECO:0000269|PubMed:16120682"
FT MUTAGEN 165
FT /note="A->M,I: Shifts fluorescence to higher wavelength."
FT /evidence="ECO:0000269|PubMed:16120682"
FT MUTAGEN 199
FT /note="H->T: Shifts fluorescence to 515 nm."
FT /evidence="ECO:0000269|PubMed:16120682"
FT MUTAGEN 217
FT /note="E->Q: Shifts fluorescence to 495 nm."
FT /evidence="ECO:0000269|PubMed:16120682"
FT STRAND 10..22
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:2A46"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:2A46"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2A47"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2A46"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:2A46"
FT TURN 136..140
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 174..187
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:2A46"
FT STRAND 212..223
FT /evidence="ECO:0007829|PDB:2A46"
SQ SEQUENCE 229 AA; 25317 MW; AC412B4DFFFAA6B3 CRC64;
MALSNKFIGD DMKMTYHMDG CVNGHYFTVK GEGNGKPYEG TQTSTFKVTM ANGGPLAFSF
DILSTVFKYG NRCFTAYPTS MPDYFKQAFP DGMSYERTFT YEDGGVATAS WEISLKGNCF
EHKSTFHGVN FPADGPVMAK KTTGWDPSFE KMTVCDGILK GDVTAFLMLQ GGGNYRCQFH
TSYKTKKPVT MPPNHVVEHR IARTDLDKGG NSVQLTEHAV AHITSVVPF
