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Protein

GFP-like non-fluorescent chromoprotein

Gene
N/A
Organism
Montipora efflorescens (Coral)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Thought to play a role in photoprotection of the coral's resident symbiont microalgae's photosystems from photoinhibition caused by high light levels found near the surface of coral reefs.1 Publication

GO - Biological processi

  • bioluminescence Source: UniProtKB-KW
  • photoprotection Source: UniProtKB
  • protein-chromophore linkage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Photoprotein

Keywords - Biological processi

Luminescence

Keywords - Ligandi

Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
GFP-like non-fluorescent chromoprotein
Alternative name(s):
Non-fluorescent pocilloporin
Rtms 5
OrganismiMontipora efflorescens (Coral)
Taxonomic identifieri105610 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaScleractiniaAstrocoeniinaAcroporidaeMontipora

Subcellular locationi

GO - Cellular componenti

  • host Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Biotechnological usei

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.Curated

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi142H → S: Produces a fluorescent form. 1 Publication1
Mutagenesisi158F → H: Produces a homodimeric form. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001925861 – 221GFP-like non-fluorescent chromoproteinAdd BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki62 ↔ 642-iminomethyl-5-imidazolinone (Gln-Gly)1 Publication
Modified residuei63(E)-2,3-didehydrotyrosine1 Publication1

Post-translational modificationi

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 Xaa-N. Maturation of the chromophore requires nothing other than molecular oxygen.

Proteomic databases

PRIDEiP83690.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1221
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 18Combined sources13
Beta strandi21 – 32Combined sources12
Turni33 – 36Combined sources4
Beta strandi37 – 47Combined sources11
Helixi54 – 56Combined sources3
Helixi58 – 60Combined sources3
Helixi78 – 81Combined sources4
Turni82 – 85Combined sources4
Beta strandi87 – 95Combined sources9
Beta strandi100 – 110Combined sources11
Beta strandi113 – 123Combined sources11
Turni130 – 134Combined sources5
Beta strandi136 – 139Combined sources4
Beta strandi142 – 149Combined sources8
Beta strandi152 – 163Combined sources12
Beta strandi168 – 181Combined sources14
Beta strandi188 – 200Combined sources13
Beta strandi204 – 217Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MOUX-ray2.20A3-221[»]
1MOVX-ray2.40A3-221[»]
2ARLX-ray2.00A2-221[»]
2P4MX-ray1.80A/B/C/D/E/F/G/H1-221[»]
3VICX-ray2.20A/B/C/D/E/F/G/H1-221[»]
3VK1X-ray2.20A1-221[»]
ProteinModelPortaliP83690.
SMRiP83690.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83690.

Family & Domainsi

Sequence similaritiesi

Belongs to the GFP family.Curated

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR009017. GFP.
IPR023413. GFP-like.
IPR011584. GFP-related.
[Graphical view]
PfamiPF01353. GFP. 1 hit.
[Graphical view]
SUPFAMiSSF54511. SSF54511. 1 hit.

Sequencei

Sequence statusi: Complete.

P83690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVIATQMTY KVYMSGTVNG HYFEVEGDGK GRPYEGEQTV KLTVTKGGPL
60 70 80 90 100
PFAWDILSPQ CQYGSIPFTK YPEDIPDYVK QSFPEGFTWE RIMNFEDGAV
110 120 130 140 150
CTVSNDSSIQ GNCFTYHVKF SGLNFPPNGP VMQKKTQGWE PHSERLFARG
160 170 180 190 200
GMLIGNNFMA LKLEGGGHYL CEFKTTYKAK KPVKMPGYHY VDRKLDVTNH
210 220
NKDYTSVEQC EISIARKPVV A
Length:221
Mass (Da):24,911
Last modified:November 23, 2004 - v2
Checksum:i626B1A7BEDD7393B
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MOUX-ray2.20A3-221[»]
1MOVX-ray2.40A3-221[»]
2ARLX-ray2.00A2-221[»]
2P4MX-ray1.80A/B/C/D/E/F/G/H1-221[»]
3VICX-ray2.20A/B/C/D/E/F/G/H1-221[»]
3VK1X-ray2.20A1-221[»]
ProteinModelPortaliP83690.
SMRiP83690.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP83690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP83690.

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR009017. GFP.
IPR023413. GFP-like.
IPR011584. GFP-related.
[Graphical view]
PfamiPF01353. GFP. 1 hit.
[Graphical view]
SUPFAMiSSF54511. SSF54511. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNFCP_MONEF
AccessioniPrimary (citable) accession number: P83690
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: November 2, 2016
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The wild-type form is non-fluorescent with the color being pH dependent, ranging from yellow at low pH, through red to blue at high pH. The His-142 mutation produces a fluorescent form.2 Publications

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.