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Protein

GFP-like fluorescent chromoprotein cFP484

Gene
N/A
Organism
Clavularia sp. (Brown star polyp)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Pigment protein that is green in color.1 Publication

Absorptioni

Abs(max)=458 nm

Has a strong fluorescence emission spectrum which peaks at 486 nm.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Photoprotein

Keywords - Biological processi

Luminescence

Keywords - Ligandi

Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
GFP-like fluorescent chromoprotein cFP484
OrganismiClavularia sp. (Brown star polyp)
Taxonomic identifieri86521 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaOctocoralliaAlcyonaceaStoloniferaClavulariidaeClavularia

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266GFP-like fluorescent chromoprotein cFP484PRO_0000192580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki104 ↔ 1062-iminomethyl-5-imidazolinone (Gln-Gly)By similarity
Modified residuei105 – 10512,3-didehydrotyrosineBy similarity

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. The precise stereochemistry of the tyrosine has not been determined.

Expressioni

Tissue specificityi

Tentacle and oral disk.1 Publication

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 6013Combined sources
Beta strandi63 – 7412Combined sources
Turni75 – 784Combined sources
Beta strandi79 – 8911Combined sources
Helixi97 – 1004Combined sources
Beta strandi110 – 1123Combined sources
Helixi120 – 1234Combined sources
Turni124 – 1274Combined sources
Beta strandi129 – 1379Combined sources
Beta strandi142 – 15211Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi162 – 1654Combined sources
Turni172 – 1765Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi184 – 1918Combined sources
Beta strandi194 – 20512Combined sources
Beta strandi210 – 22314Combined sources
Beta strandi230 – 24213Combined sources
Beta strandi246 – 26015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQKX-ray1.19A44-266[»]
2OTBX-ray1.79A/B44-259[»]
2OTEX-ray1.47A/B44-259[»]
4Q9WX-ray1.00A/B44-160[»]
A/B162-260[»]
4Q9XX-ray1.90A44-160[»]
A162-260[»]
4R6DX-ray1.55A44-160[»]
A162-258[»]
ProteinModelPortaliQ9U6Y3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U6Y3.

Family & Domainsi

Sequence similaritiesi

Belongs to the GFP family.1 Publication

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR009017. GFP.
IPR023413. GFP-like.
IPR011584. GFP-related.
IPR000786. Green_fluorescent_prot.
[Graphical view]
PfamiPF01353. GFP. 1 hit.
[Graphical view]
PRINTSiPR01229. GFLUORESCENT.
SUPFAMiSSF54511. SSF54511. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9U6Y3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCKFVFCLS FLVLAITNAN IFLRNEADLE EKTLRIPKAL TTMGVIKPDM
60 70 80 90 100
KIKLKMEGNV NGHAFVIEGE GEGKPYDGTH TLNLEVKEGA PLPFSYDILS
110 120 130 140 150
NAFQYGNRAL TKYPDDIADY FKQSFPEGYS WERTMTFEDK GIVKVKSDIS
160 170 180 190 200
MEEDSFIYEI RFDGMNFPPN GPVMQKKTLK WEPSTEIMYV RDGVLVGDIS
210 220 230 240 250
HSLLLEGGGH YRCDFKSIYK AKKVVKLPDY HFVDHRIEIL NHDKDYNKVT
260
LYENAVARYS LLPSQA
Length:266
Mass (Da):30,450
Last modified:May 1, 2000 - v1
Checksum:iB4E97406E2708854
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168424 mRNA. Translation: AAF03374.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168424 mRNA. Translation: AAF03374.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQKX-ray1.19A44-266[»]
2OTBX-ray1.79A/B44-259[»]
2OTEX-ray1.47A/B44-259[»]
4Q9WX-ray1.00A/B44-160[»]
A/B162-260[»]
4Q9XX-ray1.90A44-160[»]
A162-260[»]
4R6DX-ray1.55A44-160[»]
A162-258[»]
ProteinModelPortaliQ9U6Y3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U6Y3.

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR009017. GFP.
IPR023413. GFP-like.
IPR011584. GFP-related.
IPR000786. Green_fluorescent_prot.
[Graphical view]
PfamiPF01353. GFP. 1 hit.
[Graphical view]
PRINTSiPR01229. GFLUORESCENT.
SUPFAMiSSF54511. SSF54511. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGFPL_CLASP
AccessioniPrimary (citable) accession number: Q9U6Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.