RFP_DISSP
ID RFP_DISSP Reviewed; 225 AA.
AC Q9U6Y8;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Red fluorescent protein drFP583;
DE Short=DsRed;
OS Discosoma sp. (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Corallimorpharia;
OC Discosomidae; Discosoma; unclassified Discosoma.
OX NCBI_TaxID=86600;
RN [1] {ECO:0000312|EMBL:AAF03369.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=11101896; DOI=10.1038/81992;
RA Wall M.A., Socolich M., Ranganathan R.;
RT "The structural basis for red fluorescence in the tetrameric GFP homolog
RT DsRed.";
RL Nat. Struct. Biol. 7:1133-1138(2000).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, AND DEHYDROGENATION AT
RP TYR-67.
RX PubMed=11209050; DOI=10.1073/pnas.98.2.462;
RA Yarbrough D., Wachter R.M., Kallio K., Matz M.V., Remington S.J.;
RT "Refined crystal structure of DsRed, a red fluorescent protein from coral,
RT at 2.0-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:462-467(2001).
CC -!- FUNCTION: Thought to play a role in photoprotection of the coral's
CC resident symbiont microalgae's photosystems from photoinhibition caused
CC by high light levels found near the surface of coral reefs. In deeper
CC water, the fluorescence may be to convert blue light into longer
CC wavelengths more suitable for use in photosynthesis by the microalgal
CC symbionts.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=558 nm;
CC Note=Exhibits a smaller absorbance peak at 494 nm. The broad
CC fluorescence emission spectrum peaks at 583 nm.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11209050}.
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.
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:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF168419; AAF03369.1; -; mRNA.
DR PDB; 1G7K; X-ray; 2.00 A; A/B/C/D=2-225.
DR PDB; 1GGX; X-ray; 1.90 A; A/B/C/D=1-225.
DR PDB; 1ZGO; X-ray; 1.40 A; A/B/C/D=1-225.
DR PDB; 1ZGP; X-ray; 1.90 A; A/B/C/D=1-225.
DR PDB; 1ZGQ; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-225.
DR PDB; 2H5O; X-ray; 1.08 A; A/B=8-221.
DR PDB; 2H5R; X-ray; 1.60 A; A=8-223.
DR PDB; 2H8Q; X-ray; 2.00 A; A/B/C/D=7-225.
DR PDB; 2V4E; X-ray; 2.40 A; A/B/C/D/E/F/G/H=6-225.
DR PDB; 2VAD; X-ray; 1.59 A; A=7-221.
DR PDB; 2VAE; X-ray; 1.64 A; A/B/C/D/E/F/G/H=3-225.
DR PDB; 4I2Y; X-ray; 2.20 A; A/B=8-145.
DR PDB; 4KF4; X-ray; 1.99 A; A/B/C/D/E/F/G/H=8-221.
DR PDB; 4KF5; X-ray; 2.60 A; C/D=8-221.
DR PDBsum; 1G7K; -.
DR PDBsum; 1GGX; -.
DR PDBsum; 1ZGO; -.
DR PDBsum; 1ZGP; -.
DR PDBsum; 1ZGQ; -.
DR PDBsum; 2H5O; -.
DR PDBsum; 2H5R; -.
DR PDBsum; 2H8Q; -.
DR PDBsum; 2V4E; -.
DR PDBsum; 2VAD; -.
DR PDBsum; 2VAE; -.
DR PDBsum; 4I2Y; -.
DR PDBsum; 4KF4; -.
DR PDBsum; 4KF5; -.
DR AlphaFoldDB; Q9U6Y8; -.
DR SMR; Q9U6Y8; -.
DR PRIDE; Q9U6Y8; -.
DR EvolutionaryTrace; Q9U6Y8; -.
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..225
FT /note="Red fluorescent protein drFP583"
FT /id="PRO_0000192577"
FT MOD_RES 67
FT /note="(Z)-2,3-didehydrotyrosine"
FT /evidence="ECO:0000269|PubMed:11209050"
FT CROSSLNK 66..68
FT /note="2-iminomethyl-5-imidazolinone (Gln-Gly)"
FT /evidence="ECO:0000269|PubMed:11209050"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:2VAD"
FT STRAND 10..22
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:1ZGO"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:1ZGO"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1ZGO"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2VAD"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1ZGO"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1ZGO"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1ZGO"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 104..114
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:1ZGO"
FT TURN 134..138
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 156..167
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 170..185
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 192..204
FT /evidence="ECO:0007829|PDB:1ZGO"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:1ZGO"
SQ SEQUENCE 225 AA; 25931 MW; FBF9A5369778F689 CRC64;
MRSSKNVIKE FMRFKVRMEG TVNGHEFEIE GEGEGRPYEG HNTVKLKVTK GGPLPFAWDI
LSPQFQYGSK VYVKHPADIP DYKKLSFPEG FKWERVMNFE DGGVVTVTQD SSLQDGCFIY
KVKFIGVNFP SDGPVMQKKT MGWEASTERL YPRDGVLKGE IHKALKLKDG GHYLVEFKSI
YMAKKPVQLP GYYYVDSKLD ITSHNEDYTI VEQYERTEGR HHLFL
