P48451 · CANB1_DROME

Function

function

Calcineurin is a calcium-binding and calmodulin-binding protein found in all cells from yeast to mammals, and a calcium-dependent, calmodulin-stimulated protein phosphatase.

Miscellaneous

This protein has four functional calcium-binding sites.

Features

Showing features for binding site.

117020406080100120140160
TypeIDPosition(s)Description
Binding site31Ca2+ 1 (UniProtKB | ChEBI)
Binding site33Ca2+ 1 (UniProtKB | ChEBI)
Binding site35Ca2+ 1 (UniProtKB | ChEBI)
Binding site42Ca2+ 1 (UniProtKB | ChEBI)
Binding site63Ca2+ 2 (UniProtKB | ChEBI)
Binding site65Ca2+ 2 (UniProtKB | ChEBI)
Binding site67Ca2+ 2 (UniProtKB | ChEBI)
Binding site69Ca2+ 2 (UniProtKB | ChEBI)
Binding site74Ca2+ 2 (UniProtKB | ChEBI)
Binding site100Ca2+ 3 (UniProtKB | ChEBI)
Binding site102Ca2+ 3 (UniProtKB | ChEBI)
Binding site104Ca2+ 3 (UniProtKB | ChEBI)
Binding site106Ca2+ 3 (UniProtKB | ChEBI)
Binding site111Ca2+ 3 (UniProtKB | ChEBI)
Binding site141Ca2+ 4 (UniProtKB | ChEBI)
Binding site143Ca2+ 4 (UniProtKB | ChEBI)
Binding site145Ca2+ 4 (UniProtKB | ChEBI)
Binding site147Ca2+ 4 (UniProtKB | ChEBI)
Binding site152Ca2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcalcineurin complex
Cellular Componentsynaptic vesicle
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent protein serine/threonine phosphatase regulator activity
Molecular Functioncalmodulin binding
Molecular Functionphosphatase binding
Biological Processcalcineurin-mediated signaling
Biological Processneurotransmitter secretion
Biological Processsleep
Biological Processvesicle-mediated transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Calcineurin subunit B type 1
  • Alternative names
    • Protein phosphatase 2B regulatory subunit 1

Gene names

    • Name
      CanB
    • Synonyms
      CANB1, CNB, CNB1
    • ORF names
      CG4209

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    P48451
  • Secondary accessions
    • Q9W4D0

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000734881-170Calcineurin subunit B type 1

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-46EF-hand 1
Domain50-85EF-hand 2
Domain87-122EF-hand 3
Domain128-163EF-hand 4

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    170
  • Mass (Da)
    19,341
  • Last updated
    1996-02-01 v1
  • Checksum
    77D89BE9BD961900
MGNETSLPMDMCSNFDADEIRRLGKRFRKLDLDNSGALSIDEFMSLPELQQNPLVQRVIDIFDADGNGEVDFKEFIQGVSQFSVRGDKLSKLRFAFRIYDMDNDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTICFADKDEDGKISFDEFCSVVGNTDIHKKMVVDV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
M9NFW6M9NFW6_DROMECanB170

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M97215
EMBL· GenBank· DDBJ
AAA28411.1
EMBL· GenBank· DDBJ
mRNA
AE014298
EMBL· GenBank· DDBJ
AAF46026.1
EMBL· GenBank· DDBJ
Genomic DNA
AY070642
EMBL· GenBank· DDBJ
AAL48113.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp