GFPL_CLASP
ID GFPL_CLASP Reviewed; 266 AA.
AC Q9U6Y3;
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 cFP484;
OS Clavularia sp. (Brown star polyp).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Alcyonacea;
OC Stolonifera; Clavulariidae; Clavularia; unclassified Clavularia.
OX NCBI_TaxID=86521;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF03374.1}
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)=458 nm;
CC Note=Has a strong fluorescence emission spectrum which peaks at 486
CC 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), 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; AF168424; AAF03374.1; -; mRNA.
DR PDB; 2HQK; X-ray; 1.19 A; A=44-266.
DR PDB; 2OTB; X-ray; 1.79 A; A/B=44-259.
DR PDB; 2OTE; X-ray; 1.47 A; A/B=44-259.
DR PDB; 4Q9W; X-ray; 1.00 A; A/B=44-260.
DR PDB; 4Q9X; X-ray; 1.90 A; A=44-260.
DR PDB; 4R6D; X-ray; 1.55 A; A=44-258.
DR PDB; 6FP7; X-ray; 1.58 A; A=41-260.
DR PDB; 6FP8; X-ray; 1.85 A; A=41-260.
DR PDB; 6QSL; X-ray; 1.60 A; A=44-260.
DR PDB; 6QSM; X-ray; 1.65 A; A=44-260.
DR PDB; 6QSO; X-ray; 1.80 A; A=44-260.
DR PDBsum; 2HQK; -.
DR PDBsum; 2OTB; -.
DR PDBsum; 2OTE; -.
DR PDBsum; 4Q9W; -.
DR PDBsum; 4Q9X; -.
DR PDBsum; 4R6D; -.
DR PDBsum; 6FP7; -.
DR PDBsum; 6FP8; -.
DR PDBsum; 6QSL; -.
DR PDBsum; 6QSM; -.
DR PDBsum; 6QSO; -.
DR AlphaFoldDB; Q9U6Y3; -.
DR SMR; Q9U6Y3; -.
DR ABCD; Q9U6Y3; 3 sequenced antibodies.
DR EvolutionaryTrace; Q9U6Y3; -.
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..266
FT /note="GFP-like fluorescent chromoprotein cFP484"
FT /id="PRO_0000192580"
FT MOD_RES 105
FT /note="2,3-didehydrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT CROSSLNK 104..106
FT /note="2-iminomethyl-5-imidazolinone (Gln-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q9U6Y8"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:6FP7"
FT STRAND 48..60
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:4Q9W"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:4Q9W"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2OTE"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:4Q9W"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:4Q9W"
FT TURN 172..176
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 210..223
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 230..242
FT /evidence="ECO:0007829|PDB:4Q9W"
FT STRAND 246..260
FT /evidence="ECO:0007829|PDB:4Q9W"
SQ SEQUENCE 266 AA; 30450 MW; B4E97406E2708854 CRC64;
MKCKFVFCLS FLVLAITNAN IFLRNEADLE EKTLRIPKAL TTMGVIKPDM KIKLKMEGNV
NGHAFVIEGE GEGKPYDGTH TLNLEVKEGA PLPFSYDILS NAFQYGNRAL TKYPDDIADY
FKQSFPEGYS WERTMTFEDK GIVKVKSDIS MEEDSFIYEI RFDGMNFPPN GPVMQKKTLK
WEPSTEIMYV RDGVLVGDIS HSLLLEGGGH YRCDFKSIYK AKKVVKLPDY HFVDHRIEIL
NHDKDYNKVT LYENAVARYS LLPSQA
