RFP_ENTQU
ID RFP_ENTQU Reviewed; 231 AA.
AC Q8ISF8;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Red fluorescent protein eqFP611;
DE AltName: Full=GFP-like chromoprotein;
OS Entacmaea quadricolor (Bubble-tip anemone) (Parasicyonis actinostoloides).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Entacmaea.
OX NCBI_TaxID=6118;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN05449.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX PubMed=12185250; DOI=10.1073/pnas.182157199;
RA Wiedenmann J., Schenk A., Roecker C., Girod A., Spindler K.-D.,
RA Nienhaus G.U.;
RT "A far-red fluorescent protein with fast maturation and reduced
RT oligomerization tendency from Entacmaea quadricolor (Anthozoa,
RT Actinaria).";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11646-11651(2002).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DEHYDROGENATION AT TYR-64.
RX PubMed=12909624; DOI=10.1074/jbc.m307896200;
RA Petersen J., Wilmann P.G., Beddoe T., Oakley A.J., Devenish R.J.,
RA Prescott M., Rossjohn J.;
RT "The 2.0-A crystal structure of eqFP611, a far red fluorescent protein from
RT the sea anemone Entacmaea quadricolor.";
RL J. Biol. Chem. 278:44626-44631(2003).
CC -!- FUNCTION: Pigment protein. {ECO:0000269|PubMed:12185250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=559 nm;
CC Note=Exhibits a smaller absorbance peak at 525 nm. Has a strong
CC fluorescence emission spectrum which peaks at 611 nm.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12185250}.
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 -!- MISCELLANEOUS: The emission does not change over the pH range of 4 to
CC 10. Maturation occurs via a green intermediate and is complete within
CC 12 hours. Recombinant expression at high temperatures induces
CC oligomerization. {ECO:0000269|PubMed:12185250}.
CC -!- SIMILARITY: Belongs to the GFP family. {ECO:0000269|PubMed:12185250}.
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DR EMBL; AY130757; AAN05449.1; -; mRNA.
DR PDB; 1UIS; X-ray; 2.00 A; A/B=1-231.
DR PDB; 3E5T; X-ray; 1.10 A; A=1-231.
DR PDB; 3E5V; X-ray; 2.10 A; A=1-231.
DR PDB; 3E5W; X-ray; 1.71 A; A/B/C/D=1-231.
DR PDB; 3IP2; X-ray; 1.60 A; A=34-229.
DR PDB; 3U0L; X-ray; 1.25 A; A=1-224.
DR PDB; 3U0M; X-ray; 1.65 A; A=1-224.
DR PDB; 3U0N; X-ray; 1.60 A; A=1-224.
DR PDB; 6XWY; X-ray; 1.75 A; A/B/C/D=4-222.
DR PDBsum; 1UIS; -.
DR PDBsum; 3E5T; -.
DR PDBsum; 3E5V; -.
DR PDBsum; 3E5W; -.
DR PDBsum; 3IP2; -.
DR PDBsum; 3U0L; -.
DR PDBsum; 3U0M; -.
DR PDBsum; 3U0N; -.
DR PDBsum; 6XWY; -.
DR AlphaFoldDB; Q8ISF8; -.
DR SMR; Q8ISF8; -.
DR EvolutionaryTrace; Q8ISF8; -.
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..231
FT /note="Red fluorescent protein eqFP611"
FT /id="PRO_0000192578"
FT MOD_RES 64
FT /note="(E)-2,3-didehydrotyrosine"
FT /evidence="ECO:0000269|PubMed:12909624"
FT CROSSLNK 63..65
FT /note="2-iminomethyl-5-imidazolinone (Met-Gly)"
FT /evidence="ECO:0000269|PubMed:12909624"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1UIS"
FT STRAND 7..19
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 22..33
FT /evidence="ECO:0007829|PDB:3E5T"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:3E5T"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:3E5T"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6XWY"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3IP2"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3E5T"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:3E5T"
FT TURN 131..135
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:3E5T"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3U0L"
FT STRAND 169..182
FT /evidence="ECO:0007829|PDB:3E5T"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 192..205
FT /evidence="ECO:0007829|PDB:3E5T"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:3E5T"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3E5T"
SQ SEQUENCE 231 AA; 26053 MW; 86467A7EB5D6DD60 CRC64;
MNSLIKENMR MMVVMEGSVN GYQFKCTGEG DGNPYMGTQT MRIKVVEGGP LPFAFDILAT
SFMYGSKTFI KHTKGIPDFF KQSFPEGFTW ERVTRYEDGG VFTVMQDTSL EDGCLVYHAK
VTGVNFPSNG AVMQKKTKGW EPNTEMLYPA DGGLRGYSQM ALNVDGGGYL SCSFETTYRS
KKTVENFKMP GFHFVDHRLE RLEESDKEMF VVQHEHAVAK FCDLPSKLGR L
