Q94A16 · CP21C_ARATH

Function

function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Activity regulation

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase (By similarity).

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 ComponentGolgi apparatus
Cellular ComponentGolgi cis cisterna
Cellular Componentmitochondrion
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial
  • EC number
  • Short names
    PPIase CYP21-3
  • Alternative names
    • Cyclophilin of 21 kDa 3
    • Rotamase CYP21-3

Gene names

    • Name
      CYP21-3
    • ORF names
      T8I13.16
    • Ordered locus names
      At2g47320

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
    Q94A16
  • Secondary accessions
    • C0Z333
    • O22906

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, transit peptide.

TypeIDPosition(s)Description
ChainPRO_0000044628?-230Peptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial
Transit peptide1-?Mitochondrion

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous, mostly in aerial organs.

Induction

Repressed by the munition hexahydro-1,3,5-trinitro-1,3,5-triazine, also known as Royal Demolition eXplosive (RDX).

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain76-226PPIase cyclophilin-type

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q94A16-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    230
  • Mass (Da)
    26,042
  • Last updated
    2005-12-20 v2
  • Checksum
    6198D43EE5B9552F
MAKIKPQALLQQSKKKKGPSRISITNIVIYTLAVLLLVFVLFSAYRRWTHRSEIPTHNGRSVLEDAAFPGMKNVDLPRFATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWALDRKNIDTSLKHEEFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVTLLQDM

Q94A16-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAK91465.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAK91465.1 differs from that shown. Reason: Erroneous termination Truncated C-terminus.

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0553891-70in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY568520
EMBL· GenBank· DDBJ
AAS75303.1
EMBL· GenBank· DDBJ
mRNA
AC002337
EMBL· GenBank· DDBJ
AAB63832.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002685
EMBL· GenBank· DDBJ
AEC10827.1
EMBL· GenBank· DDBJ
Genomic DNA
AY050450
EMBL· GenBank· DDBJ
AAK91465.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AY097351
EMBL· GenBank· DDBJ
AAM19867.1
EMBL· GenBank· DDBJ
mRNA
AK318997
EMBL· GenBank· DDBJ
BAH57112.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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