A0A1I9R3Y5 · PXG_PINEL

Function

function

Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Features

Showing features for binding site.

123420406080100120140160180200220
TypeIDPosition(s)Description
Binding site64Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site69Ca2+ (UniProtKB | ChEBI)
Binding site71Ca2+ (UniProtKB | ChEBI)
Binding site73Ca2+ (UniProtKB | ChEBI)
Binding site80Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentmembrane
Cellular Componentmonolayer-surrounded lipid storage body
Molecular Functioncalcium ion binding
Molecular Functionheme binding
Molecular Functionmonooxygenase activity
Molecular Functionplant seed peroxygenase activity
Molecular Functionprotein homodimerization activity
Biological Processnegative regulation of lipid storage

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxygenase
  • EC number
  • Alternative names
    • Caleosin

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Pinopsida > Pinidae > Conifers I > Pinales > Pinaceae > Pinus > Pinus subgen. Pinus

Accessions

  • Primary accession
    A0A1I9R3Y5

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00004500652-234Peroxygenase

Keywords

Expression

Tissue specificity

Expressed in pollen (at protein level).

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain56-91EF-hand
Motif112-121Proline-knot

Domain

Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
The proline-knot motif may be involved in targeting to lipid bodies.

Sequence similarities

Belongs to the caleosin family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    234
  • Mass (Da)
    26,544
  • Last updated
    2017-02-15 v1
  • MD5 Checksum
    040CF69FBC7FAC87493CFEC6F091D9ED
MASNESLQTTAAMAPVTIERRVNPNLDDELPKPFLPRALVAVDTEHPSGTPGHQHGDMSVLQQHVAFFDRNNDGIVYPWETFLGLRAVGFNIIISFFGCLIINISLSYATLPGWIPSPFFPIYIDRIHRAKHGSDSEVYDTEGRFVPSKFEEIFTKNARTHPDKLSFSELWNLTEHNRNALDPLGWVAAKLEWFLLYLLAKDPHGFVPKEAARGVFDGSLFEFCEKSRRSNKQQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KX688795
EMBL· GenBank· DDBJ
AOZ15520.1
EMBL· GenBank· DDBJ
mRNA

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.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help