Q07488 · BCB1_ARATH
- ProteinBlue copper protein
- GeneBCB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids196 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Probably acts as an electron carrier.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | plant-type vacuole | |
Cellular Component | plasma membrane | |
Cellular Component | plastid | |
Cellular Component | side of membrane | |
Molecular Function | electron transfer activity | |
Molecular Function | metal ion binding | |
Biological Process | aluminum cation transport | |
Biological Process | cellular response to cold | |
Biological Process | cellular response to hypoxia | |
Biological Process | regulation of lignin biosynthetic process | |
Biological Process | response to absence of light | |
Biological Process | response to oomycetes | |
Biological Process | response to oxidative stress |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBlue copper protein
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ07488
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MAGVFKTVTFLVLVFAAVVVFA | ||||||
Chain | PRO_0000002866 | 23-174 | Blue copper protein | |||
Sequence: EDYDVGDDTEWTRPMDPEFYTTWATGKTFRVGDELEFDFAAGRHDVAVVSEAAFENCEKEKPISHMTVPPVKIMLNTTGPQYFICTVGDHCRFGQKLSITVVAAGATGGATPGAGATPAPGSTPSTGGTTPPTAGGTTTPSGSSGTTTPAGN | ||||||
Disulfide bond | 79↔113 | |||||
Sequence: CEKEKPISHMTVPPVKIMLNTTGPQYFICTVGDHC | ||||||
Glycosylation | 98 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 174 | GPI-anchor amidated asparagine | ||||
Sequence: N | ||||||
Propeptide | PRO_0000002867 | 175-196 | Removed in mature form | |||
Sequence: AASSLGGATFLVAFVSAVVALF |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By dark adaptation. This gives a 20-fold increase in expression.
Developmental stage
Maximum levels are found in 35 day old plantlets when the rosette is mature, consisting of 8-10 fully expanded leaves, and as the floral stem starts to form. This level remains constant during the further life span of the plant.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-125 | Phytocyanin | ||||
Sequence: EDYDVGDDTEWTRPMDPEFYTTWATGKTFRVGDELEFDFAAGRHDVAVVSEAAFENCEKEKPISHMTVPPVKIMLNTTGPQYFICTVGDHCRFGQKLSITVVA | ||||||
Region | 133-173 | Disordered | ||||
Sequence: TPGAGATPAPGSTPSTGGTTPPTAGGTTTPSGSSGTTTPAG | ||||||
Compositional bias | 140-173 | Polar residues | ||||
Sequence: PAPGSTPSTGGTTPPTAGGTTTPSGSSGTTTPAG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length196
- Mass (Da)20,054
- Last updated2002-05-27 v2
- Checksum05100B50518F0A56
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 44 | in Ref. 1; CAA78771 | ||||
Sequence: T → S | ||||||
Sequence conflict | 134 | in Ref. 1; CAA78771 | ||||
Sequence: P → L | ||||||
Compositional bias | 140-173 | Polar residues | ||||
Sequence: PAPGSTPSTGGTTPPTAGGTTTPSGSSGTTTPAG | ||||||
Sequence conflict | 142 | in Ref. 1; CAA78771 | ||||
Sequence: P → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z15058 EMBL· GenBank· DDBJ | CAA78771.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y18227 EMBL· GenBank· DDBJ | CAA77089.1 EMBL· GenBank· DDBJ | mRNA | ||
AB035137 EMBL· GenBank· DDBJ | BAA86999.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF296825 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CP002688 EMBL· GenBank· DDBJ | AED92816.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY052681 EMBL· GenBank· DDBJ | AAK96585.1 EMBL· GenBank· DDBJ | mRNA | ||
AY034986 EMBL· GenBank· DDBJ | AAK59491.1 EMBL· GenBank· DDBJ | mRNA | ||
AY142577 EMBL· GenBank· DDBJ | AAN13146.1 EMBL· GenBank· DDBJ | mRNA | ||
AY088549 EMBL· GenBank· DDBJ | AAM66081.1 EMBL· GenBank· DDBJ | mRNA |