Q9FYE1 · MCA9_ARATH

Function

function

Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. Required for proteolytic processing of GRI (PubMed:25398910).

Activity regulation

Inhibited by serpin ZX and nitric oxide through cysteine nitrosylation.

Features

Showing features for site, active site.

132550100150200250300
TypeIDPosition(s)Description
Site29S-nitrosylation-insensitive cysteine; may replace the S-nitrosylated cysteine residue within the catalytic center (in mature processed form only)
Active site95
Active site147
Site183-184Cleavage; by autolysis

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapoplast
Molecular Functioncysteine-type endopeptidase activity
Molecular Functioncysteine-type peptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      AMC9
    • Synonyms
      MCP2F
    • ORF names
      F21E1.120
    • Ordered locus names
      At5g04200

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9FYE1
  • Secondary accessions
    • Q8LCR8

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis29Reduced proteolytic activity.
Mutagenesis147Loss of autoprocessing and protease activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00003346081-183Metacaspase-9 subunit p20
ChainPRO_00003346071-325Metacaspase-9
Modified residue147S-nitrosocysteine
Glycosylation177N-linked (GlcNAc...) asparagine
ChainPRO_0000334609184-325Metacaspase-9 subunit p10

Post-translational modification

The two subunits are derived from the precursor sequence by an autocatalytic mechanism.
S-nitrosylation at Cys-147 suppresses both autoprocessing and proteolytic activity of the full-length protein, but does not affect the activity of the mature processed form.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in root tips, cauline leaves, flowers and siliques.

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the peptidase C14B family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    325
  • Mass (Da)
    35,505
  • Last updated
    2001-03-01 v1
  • Checksum
    AB574D648EDF3E0E
MDQQGMVKKRLAVLVGCNYPNTRNELHGCINDVLAMKETILSRFGFKQDDIEVLTDEPESKVKPTGANIKAALRRMVDKAQAGSGDILFFHYSGHGTRIPSVKSAHPFKQDEAIVPCDFNLITDVDFRELVNQLPKGTSFTMISDSCHSGGLIDKEKEQIGPSSVSSNISPAIETTNKTITSRALPFKAVLDHLSSLTGITTSDIGTHLLELFGRDAGLKFRLPAMDLMDLLETMTAREKHVDSGILMSGCQADETSADVGVGNGKAYGAFSNAIQRVLNENEGAMKNKQLVMMARDVLERLGFHQHPCLYCSDQNADATFLSQP

Sequence caution

The sequence AAM63441.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY219834
EMBL· GenBank· DDBJ
AAP44522.1
EMBL· GenBank· DDBJ
mRNA
AY322531
EMBL· GenBank· DDBJ
AAP84712.1
EMBL· GenBank· DDBJ
mRNA
AL391716
EMBL· GenBank· DDBJ
CAC05502.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED90710.1
EMBL· GenBank· DDBJ
Genomic DNA
AY063830
EMBL· GenBank· DDBJ
AAL36186.1
EMBL· GenBank· DDBJ
mRNA
AY091308
EMBL· GenBank· DDBJ
AAM14247.1
EMBL· GenBank· DDBJ
mRNA
AY086438
EMBL· GenBank· DDBJ
AAM63441.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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