Q6Q152 · CPY57_ARATH

Function

function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Involved in plant response to pathogen infection by increasing PAD4 expression in absence of EDS1 up-regulation

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 Componentcytoplasm
Cellular Componentnucleus
Cellular Componentplasmodesma
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Biological Processprotein folding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase CYP57
  • EC number
  • Short names
    PPIase CYP57
  • Alternative names
    • Cyclophilin of 57 kDa
    • Cyclophilin-57

Gene names

    • Name
      CYP57
    • ORF names
      F4I10.3
    • Ordered locus names
      At4g33060

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
    Q6Q152
  • Secondary accessions
    • O82646
    • Q0WU97

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Increased susceptibility to P.syringae infection.

Variants

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

The viewer provides 34 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00004299422-504Peptidyl-prolyl cis-trans isomerase CYP57

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Induction

Up-regulated upon pathogen infection.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, coiled coil, compositional bias, region.

TypeIDPosition(s)Description
Domain16-167PPIase cyclophilin-type
Coiled coil204-274
Compositional bias237-274Basic and acidic residues
Region237-374Disordered
Compositional bias295-318Basic and acidic residues
Compositional bias325-374Basic and acidic residues
Compositional bias416-433Polar residues
Region416-441Disordered
Region482-504Disordered

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q6Q152-1

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
    504
  • Mass (Da)
    56,515
  • Last updated
    2004-07-05 v1
  • Checksum
    824E62DA59EB113B
MSTVYVLEPPTKGKVIVNTTHGPIDVELWPKEAPKSVRNFVQLCLEGYFDNTIFHRVIPGFLVQGGDPTGSGTGGDSIYGGVFADEFHSRLRFSHRGIVAMANASSPNSNGSQFFFTLDKCDWLDKKHTIFGKVTGDSIYNLLRLGEVDTSKDDRPLDPAPKILSVEVLWNPFEDIVPRVLAKTSEESAAEIKEPPTKPVKKLNLLSFGEEAEEEEKELAVVKQKIKSSHDVLNDPRLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDKSFSVSDTVGNSDDDDDGEDETKFDAKMRNQVLSRRKEIGDTPSKPTQKKKSSSLKGREESTQRSDAVSSEDEKPRMEKLSLKKKGIGSEAKAEHMEKGDTDLQLYNASERARQLHKLKKRRLQGNEDSVLAKLEKFKQSISAKPFTSSNEPVVLTSSSEPVDNKEEDLSDWKNVKLKFAPERGKDKMSRRDDPDAYMVVDPLLEKGKEKFNRMQAKQKRREREWSGKSLA

Q6Q152-2

Sequence caution

The sequence CAA21215.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB80023.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict59in Ref. 5; BAE99301
Compositional bias237-274Basic and acidic residues
Alternative sequenceVSP_055393249-252in isoform 2
Alternative sequenceVSP_055394253-504in isoform 2
Compositional bias295-318Basic and acidic residues
Compositional bias325-374Basic and acidic residues
Compositional bias416-433Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY568525
EMBL· GenBank· DDBJ
AAS75308.1
EMBL· GenBank· DDBJ
mRNA
AL031804
EMBL· GenBank· DDBJ
CAA21215.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL161582
EMBL· GenBank· DDBJ
CAB80023.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002687
EMBL· GenBank· DDBJ
AEE86168.1
EMBL· GenBank· DDBJ
Genomic DNA
BT025329
EMBL· GenBank· DDBJ
ABF57285.1
EMBL· GenBank· DDBJ
mRNA
AK227277
EMBL· GenBank· DDBJ
BAE99301.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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