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GFP-like non-fluorescent chromoprotein FP595 (asFP595) [Cleaved into: GFP-like non-fluorescent chromoprotein FP595 chain 1; GFP-like non-fluorescent chromoprotein FP595 chain 2]

 NFCP_ANESU              Reviewed;         232 AA.
Q9GZ28;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
31-JAN-2018, entry version 70.
RecName: Full=GFP-like non-fluorescent chromoprotein FP595;
AltName: Full=asFP595;
Contains:
RecName: Full=GFP-like non-fluorescent chromoprotein FP595 chain 1;
Contains:
RecName: Full=GFP-like non-fluorescent chromoprotein FP595 chain 2;
Anemonia sulcata (Mediterranean snakelocks sea anemone).
Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
Actiniidae; Anemonia.
NCBI_TaxID=6108;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG02385.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF THR-68 AND ALA-143.
PubMed=10852900; DOI=10.1074/jbc.C000338200;
Lukyanov K.A., Fradkov A.F., Gurskaya N.G., Matz M.V., Labas Y.A.,
Savitsky A.P., Markelov M.L., Zaraisky A.G., Zhao X., Fang Y., Tan W.,
Lukyanov S.A.;
"Natural animal coloration can be determined by a nonfluorescent green
fluorescent protein homolog.";
J. Biol. Chem. 275:25879-25882(2000).
[2] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND DEHYDROGENATION AT TYR-64.
PubMed=15542608; DOI=10.1074/jbc.C400484200;
Wilmann P.G., Petersen J., Devenish R.J., Prescott M., Rossjohn J.;
"Variations on the GFP chromophore: a polypeptide fragmentation within
the chromophore revealed in the 2.1 A crystal structure of a
nonfluorescent chromoprotein from Anemonia sulcata.";
J. Biol. Chem. 280:2401-2404(2005).
-!- FUNCTION: Pigment protein that is intensely purple in color.
{ECO:0000269|PubMed:10852900}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=572 nm;
Note=Exhibits a smaller absorbance peak at 530 nm. The wild-type
has a very weak fluorescence emission spectrum which peaks at
595 nm.;
-!- TISSUE SPECIFICITY: Tentacle tips. {ECO:0000269|PubMed:10852900}.
-!- PTM: Contains a chromophore consisting of modified amino acid
residues. The chromophore is formed by autocatalytic backbone
condensation between Xaa-N and Gly-(N+2), oxidation of Tyr-(N+1)
to didehydrotyrosine, and formation of a double bond to the alpha-
amino nitrogen of residue Tyr-(N+1). Maturation of the chromophore
requires nothing other than molecular oxygen. {ECO:0000305}.
-!- BIOTECHNOLOGY: Fluorescent proteins have become a useful and
ubiquitous tool for making chimeric proteins, where they function
as a fluorescent protein tag. Typically they tolerate N- and C-
terminal fusion to a broad variety of proteins. They have been
expressed in most known cell types and are used as a noninvasive
fluorescent marker in living cells and organisms. They enable a
wide range of applications where they have functioned as a cell
lineage tracer, reporter of gene expression, or as a measure of
protein-protein interactions. {ECO:0000305}.
-!- SIMILARITY: Belongs to the GFP family.
{ECO:0000269|PubMed:10852900}.
-!- CAUTION: Opinions are divided on whether Anemonia viridis
(Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate
species. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF246709; AAG02385.1; -; mRNA.
PDB; 1XMZ; X-ray; 1.38 A; A/B=2-232.
PDB; 1XQM; X-ray; 2.10 A; A=5-232.
PDB; 2A50; X-ray; 1.30 A; A/C=2-62, B/D=63-232.
PDB; 2A52; X-ray; 1.70 A; A/C=2-62, B/D=63-232.
PDB; 2A53; X-ray; 1.45 A; A/C=2-62, B/D=63-232.
PDB; 2A54; X-ray; 1.45 A; A/C=2-62, B/D=63-232.
PDB; 2A56; X-ray; 1.90 A; A/C=2-62, B/D=63-232.
PDB; 3CFA; X-ray; 1.75 A; A/B/G/H=63-231, L/M/R/S=14-62.
PDB; 3CFF; X-ray; 1.80 A; A/B/G/H=63-231, L/M/R/S=14-62.
PDB; 3CFH; X-ray; 1.75 A; A/B/G/H=63-231, L/M/R/S=14-62.
PDBsum; 1XMZ; -.
PDBsum; 1XQM; -.
PDBsum; 2A50; -.
PDBsum; 2A52; -.
PDBsum; 2A53; -.
PDBsum; 2A54; -.
PDBsum; 2A56; -.
PDBsum; 3CFA; -.
PDBsum; 3CFF; -.
PDBsum; 3CFH; -.
ProteinModelPortal; Q9GZ28; -.
SMR; Q9GZ28; -.
EvolutionaryTrace; Q9GZ28; -.
GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
InterPro; IPR009017; GFP.
InterPro; IPR011584; GFP-related.
Pfam; PF01353; GFP; 1.
SUPFAM; SSF54511; SSF54511; 1.
1: Evidence at protein level;
3D-structure; Chromophore; Luminescence; Photoprotein.
CHAIN 1 62 GFP-like non-fluorescent chromoprotein
FP595 chain 1.
/FTId=PRO_0000010860.
CHAIN 63 232 GFP-like non-fluorescent chromoprotein
FP595 chain 2.
/FTId=PRO_0000010861.
SITE 62 63 Cleavage. {ECO:0000269|PubMed:15542608}.
MOD_RES 64 64 (E)-2,3-didehydrotyrosine.
{ECO:0000269|PubMed:15542608}.
CROSSLNK 63 65 2-iminomethyl-5-imidazolinone (Met-Gly).
{ECO:0000269|PubMed:15542608}.
MUTAGEN 68 68 T->A: Increases fluorescence; when
associated with S-143.
{ECO:0000269|PubMed:10852900}.
MUTAGEN 143 143 A->S: Produces a fluorescent form.
{ECO:0000269|PubMed:10852900}.
HELIX 2 4 {ECO:0000244|PDB:2A50}.
STRAND 9 19 {ECO:0000244|PDB:2A50}.
STRAND 22 33 {ECO:0000244|PDB:2A50}.
TURN 34 37 {ECO:0000244|PDB:2A50}.
STRAND 38 48 {ECO:0000244|PDB:2A50}.
HELIX 55 61 {ECO:0000244|PDB:2A50}.
HELIX 81 83 {ECO:0000244|PDB:2A50}.
TURN 84 86 {ECO:0000244|PDB:2A50}.
STRAND 88 96 {ECO:0000244|PDB:2A50}.
STRAND 101 111 {ECO:0000244|PDB:2A50}.
STRAND 114 124 {ECO:0000244|PDB:2A50}.
TURN 131 135 {ECO:0000244|PDB:2A50}.
STRAND 143 150 {ECO:0000244|PDB:2A50}.
STRAND 153 163 {ECO:0000244|PDB:2A50}.
TURN 165 167 {ECO:0000244|PDB:3CFA}.
STRAND 169 182 {ECO:0000244|PDB:2A50}.
HELIX 184 186 {ECO:0000244|PDB:2A50}.
STRAND 192 206 {ECO:0000244|PDB:2A50}.
TURN 207 209 {ECO:0000244|PDB:2A50}.
STRAND 210 220 {ECO:0000244|PDB:2A50}.
STRAND 228 230 {ECO:0000244|PDB:2A50}.
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


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