NFCP_MONEF
ID NFCP_MONEF Reviewed; 221 AA.
AC P83690;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=GFP-like non-fluorescent chromoprotein;
DE AltName: Full=Non-fluorescent pocilloporin;
DE AltName: Full=Rtms 5;
OS Montipora efflorescens (Pore coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Acroporidae; Montipora.
OX NCBI_TaxID=105610;
RN [1] {ECO:0000305}
RP CRYSTALLIZATION.
RX PubMed=12595737; DOI=10.1107/s0907444902023466;
RA Beddoe T., Ling M., Dove S., Hoegh-Guldberg O., Devenish R.J., Prescott M.,
RA Rossjohn J.;
RT "The production, purification and crystallization of a pocilloporin pigment
RT from a reef-forming coral.";
RL Acta Crystallogr. D 59:597-599(2003).
RN [2] {ECO:0000305, ECO:0000312|PDB:1MOU}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, MUTAGENESIS OF HIS-142 AND
RP PHE-158, AND DEHYDROGENATION AT TYR-63.
RX PubMed=12623015; DOI=10.1016/s0969-2126(03)00028-5;
RA Prescott M., Ling M., Beddoe T., Oakley A.J., Dove S., Hoegh-Guldberg O.,
RA Devenish R.J., Rossjohn J.;
RT "The 2.2 A crystal structure of a pocilloporin pigment reveals a nonplanar
RT chromophore conformation.";
RL Structure 11:275-284(2003).
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.
CC {ECO:0000303|PubMed:12595737}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12623015}.
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 wild-type form is non-fluorescent with the color
CC being pH dependent, ranging from yellow at low pH, through red to blue
CC at high pH. The His-142 mutation produces a fluorescent form.
CC {ECO:0000269|PubMed:12595737, ECO:0000269|PubMed:12623015}.
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 PDB; 1MOU; X-ray; 2.20 A; A=3-221.
DR PDB; 1MOV; X-ray; 2.40 A; A=3-221.
DR PDB; 2ARL; X-ray; 2.00 A; A=2-221.
DR PDB; 2P4M; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-221.
DR PDB; 3VIC; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-221.
DR PDB; 3VK1; X-ray; 2.20 A; A=1-221.
DR PDBsum; 1MOU; -.
DR PDBsum; 1MOV; -.
DR PDBsum; 2ARL; -.
DR PDBsum; 2P4M; -.
DR PDBsum; 3VIC; -.
DR PDBsum; 3VK1; -.
DR AlphaFoldDB; P83690; -.
DR SMR; P83690; -.
DR EvolutionaryTrace; P83690; -.
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..221
FT /note="GFP-like non-fluorescent chromoprotein"
FT /id="PRO_0000192586"
FT MOD_RES 63
FT /note="(E)-2,3-didehydrotyrosine"
FT /evidence="ECO:0000269|PubMed:12623015"
FT CROSSLNK 62..64
FT /note="2-iminomethyl-5-imidazolinone (Gln-Gly)"
FT /evidence="ECO:0000269|PubMed:12623015"
FT MUTAGEN 142
FT /note="H->S: Produces a fluorescent form."
FT /evidence="ECO:0000269|PubMed:12623015"
FT MUTAGEN 158
FT /note="F->H: Produces a homodimeric form."
FT /evidence="ECO:0000269|PubMed:12623015"
FT STRAND 6..18
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:2P4M"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:2P4M"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2P4M"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2P4M"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2P4M"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:2P4M"
FT TURN 130..134
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 152..163
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 168..181
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 188..200
FT /evidence="ECO:0007829|PDB:2P4M"
FT STRAND 204..217
FT /evidence="ECO:0007829|PDB:2P4M"
SQ SEQUENCE 221 AA; 24911 MW; 626B1A7BEDD7393B CRC64;
MSVIATQMTY KVYMSGTVNG HYFEVEGDGK GRPYEGEQTV KLTVTKGGPL PFAWDILSPQ
CQYGSIPFTK YPEDIPDYVK QSFPEGFTWE RIMNFEDGAV CTVSNDSSIQ GNCFTYHVKF
SGLNFPPNGP VMQKKTQGWE PHSERLFARG GMLIGNNFMA LKLEGGGHYL CEFKTTYKAK
KPVKMPGYHY VDRKLDVTNH NKDYTSVEQC EISIARKPVV A
