NFCP_ANESU
ID NFCP_ANESU Reviewed; 232 AA.
AC Q9GZ28;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=GFP-like non-fluorescent chromoprotein FP595;
DE AltName: Full=asFP595;
DE Contains:
DE RecName: Full=GFP-like non-fluorescent chromoprotein FP595 chain 1;
DE Contains:
DE RecName: Full=GFP-like non-fluorescent chromoprotein FP595 chain 2;
OS Anemonia sulcata (Mediterranean snakelocks sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anemonia.
OX NCBI_TaxID=6108;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG02385.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF THR-68 AND ALA-143.
RX PubMed=10852900; DOI=10.1074/jbc.c000338200;
RA Lukyanov K.A., Fradkov A.F., Gurskaya N.G., Matz M.V., Labas Y.A.,
RA Savitsky A.P., Markelov M.L., Zaraisky A.G., Zhao X., Fang Y., Tan W.,
RA Lukyanov S.A.;
RT "Natural animal coloration can be determined by a nonfluorescent green
RT fluorescent protein homolog.";
RL J. Biol. Chem. 275:25879-25882(2000).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND DEHYDROGENATION AT TYR-64.
RX PubMed=15542608; DOI=10.1074/jbc.c400484200;
RA Wilmann P.G., Petersen J., Devenish R.J., Prescott M., Rossjohn J.;
RT "Variations on the GFP chromophore: a polypeptide fragmentation within the
RT chromophore revealed in the 2.1 A crystal structure of a nonfluorescent
RT chromoprotein from Anemonia sulcata.";
RL J. Biol. Chem. 280:2401-2404(2005).
CC -!- FUNCTION: Pigment protein that is intensely purple in color.
CC {ECO:0000269|PubMed:10852900}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=572 nm;
CC Note=Exhibits a smaller absorbance peak at 530 nm. The wild-type has
CC a very weak fluorescence emission spectrum which peaks at 595 nm.;
CC -!- TISSUE SPECIFICITY: Tentacle tips. {ECO:0000269|PubMed:10852900}.
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 Tyr-(N+1). Maturation of the chromophore requires
CC nothing other than molecular oxygen. {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:10852900}.
CC -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC 1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC {ECO:0000305}.
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DR EMBL; AF246709; AAG02385.1; -; mRNA.
DR PDB; 1XMZ; X-ray; 1.38 A; A/B=2-232.
DR PDB; 1XQM; X-ray; 2.10 A; A=5-232.
DR PDB; 2A50; X-ray; 1.30 A; A/C=2-62, B/D=63-232.
DR PDB; 2A52; X-ray; 1.70 A; A/C=2-62, B/D=63-232.
DR PDB; 2A53; X-ray; 1.45 A; A/C=2-62, B/D=63-232.
DR PDB; 2A54; X-ray; 1.45 A; A/C=2-62, B/D=63-232.
DR PDB; 2A56; X-ray; 1.90 A; A/C=2-62, B/D=63-232.
DR PDB; 3CFA; X-ray; 1.75 A; A/B/G/H=63-231, L/M/R/S=14-62.
DR PDB; 3CFF; X-ray; 1.80 A; A/B/G/H=63-231, L/M/R/S=14-62.
DR PDB; 3CFH; X-ray; 1.75 A; A/B/G/H=63-231, L/M/R/S=14-62.
DR PDBsum; 1XMZ; -.
DR PDBsum; 1XQM; -.
DR PDBsum; 2A50; -.
DR PDBsum; 2A52; -.
DR PDBsum; 2A53; -.
DR PDBsum; 2A54; -.
DR PDBsum; 2A56; -.
DR PDBsum; 3CFA; -.
DR PDBsum; 3CFF; -.
DR PDBsum; 3CFH; -.
DR AlphaFoldDB; Q9GZ28; -.
DR SMR; Q9GZ28; -.
DR EvolutionaryTrace; Q9GZ28; -.
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..62
FT /note="GFP-like non-fluorescent chromoprotein FP595 chain
FT 1"
FT /id="PRO_0000010860"
FT CHAIN 63..232
FT /note="GFP-like non-fluorescent chromoprotein FP595 chain
FT 2"
FT /id="PRO_0000010861"
FT SITE 62..63
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:15542608"
FT MOD_RES 64
FT /note="(E)-2,3-didehydrotyrosine"
FT /evidence="ECO:0000269|PubMed:15542608"
FT CROSSLNK 63..65
FT /note="2-iminomethyl-5-imidazolinone (Met-Gly)"
FT /evidence="ECO:0000269|PubMed:15542608"
FT MUTAGEN 68
FT /note="T->A: Increases fluorescence; when associated with
FT S-143."
FT /evidence="ECO:0000269|PubMed:10852900"
FT MUTAGEN 143
FT /note="A->S: Produces a fluorescent form."
FT /evidence="ECO:0000269|PubMed:10852900"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 22..33
FT /evidence="ECO:0007829|PDB:2A50"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:2A50"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:2A50"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2A50"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:2A50"
FT TURN 131..135
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:2A50"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3CFA"
FT STRAND 169..182
FT /evidence="ECO:0007829|PDB:2A50"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 192..206
FT /evidence="ECO:0007829|PDB:2A50"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:2A50"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2A50"
SQ SEQUENCE 232 AA; 25919 MW; CDFE982006F4975E CRC64;
MASFLKKTMP FKTTIEGTVN GHYFKCTGKG EGNPFEGTQE MKIEVIEGGP LPFAFHILST
SCMYGSKTFI KYVSGIPDYF KQSFPEGFTW ERTTTYEDGG FLTAHQDTSL DGDCLVYKVK
ILGNNFPADG PVMQNKAGRW EPATEIVYEV DGVLRGQSLM ALKCPGGRHL TCHLHTTYRS
KKPASALKMP GFHFEDHRIE IMEEVEKGKC YKQYEAAVGR YCDAAPSKLG HN
