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 24-JAN-2024, entry version 81. 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. 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 PDB; 5LK4; X-ray; 1.47 A; A=7-221. DR PDB; 7OIN; X-ray; 1.40 A; B=7-221. DR PDB; 7ZCT; X-ray; 1.33 A; A/B=7-224. DR PDB; 8ARM; X-ray; 1.41 A; A=7-221. DR PDB; 8B65; X-ray; 1.55 A; A=8-221. DR PDB; 8B7G; X-ray; 1.30 A; A=8-221. DR PDB; 8BGL; X-ray; 2.00 A; A/B=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 PDBsum; 5LK4; -. DR PDBsum; 7OIN; -. DR PDBsum; 7ZCT; -. DR PDBsum; 8ARM; -. DR PDBsum; 8B65; -. DR PDBsum; 8B7G; -. DR PDBsum; 8BGL; -. DR AlphaFoldDB; Q9U6Y8; -. DR EMDB; EMD-3334; -. DR EMDB; EMD-3335; -. DR EMDB; EMD-3336; -. DR SMR; 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; 3.30.1300.40; -; 1. DR Gene3D; 2.40.155.10; Green fluorescent protein; 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; GFP-like; 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:7ZCT" FT STRAND 25..36 FT /evidence="ECO:0007829|PDB:7ZCT" FT TURN 37..40 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 41..51 FT /evidence="ECO:0007829|PDB:7ZCT" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:7ZCT" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:1ZGO" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:7ZCT" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:7ZCT" FT TURN 86..89 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 91..99 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 104..114 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 117..127 FT /evidence="ECO:0007829|PDB:7ZCT" FT TURN 134..138 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 146..153 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 156..167 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 170..185 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 192..204 FT /evidence="ECO:0007829|PDB:7ZCT" FT STRAND 208..224 FT /evidence="ECO:0007829|PDB:7ZCT" 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 //