A0A087RGC0 · A0A087RGC0_APTFO

Function

function

Proteolytically removes the C-terminal three residues of farnesylated proteins.

Catalytic activity

  • Hydrolyzes the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic side chains and P3' is any C-terminal residue.
    EC:3.4.24.84 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

142750100150200250300350400
TypeIDPosition(s)Description
Binding site287Zn2+ (UniProtKB | ChEBI); catalytic
Active site288
Binding site291Zn2+ (UniProtKB | ChEBI); catalytic
Binding site367Zn2+ (UniProtKB | ChEBI); catalytic
Active site371Proton donor

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological ProcessCAAX-box protein processing

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    CAAX prenyl protease
  • EC number

Gene names

    • ORF names
      AS27_10073

Organism names

  • Taxonomic identifier
  • Strain
    • BGI_AS27
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Aequornithes > Sphenisciformes > Spheniscidae > Aptenodytes

Accessions

  • Primary accession
    A0A087RGC0

Proteomes

Subcellular Location

Endoplasmic reticulum membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane80-104Helical
Transmembrane131-149Helical
Transmembrane155-176Helical
Transmembrane309-331Helical
Transmembrane337-362Helical

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-185CAAX prenyl protease 1 N-terminal
Domain188-423Peptidase M48
Region253-273Disordered

Sequence similarities

Belongs to the peptidase M48A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    427
  • Mass (Da)
    48,961
  • Last updated
    2014-10-29 v1
  • Checksum
    7170162821E9445C
QRRVYRTTTHVPRELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSEVEGTMILLCGGIPFLWNLSGQISGRAGFGPEYEIVQSLVFLLLATLFSAVTGLPWSLYNTFVIEEKHGFNQQTLGFFFKDAIKKFIVTQCILLPVTSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFIPLPEGELKQQIETMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEDYSALNKEPAEGEDGENEETKSKTKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDTQPTLIGLMIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKELGKAKDLYSALIKLNKDNLGFPVSDWIFSMWHYSHPPLLERLQALKDAKQE

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue427

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KL226349
EMBL· GenBank· DDBJ
KFM12524.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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