Q7S7Z6 · PPIB_NEUCR

Function

function

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

Activity regulation

Inhibited by cyclosporin A (CsA).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum lumen
Cellular Componentmembrane
Molecular Functioncyclosporin A binding
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 B
  • EC number
  • Short names
    PPIase B
  • Alternative names
    • Rotamase B

Gene names

    • Name
      cpr2
    • ORF names
      18F11.170, NCU01200

Organism names

Accessions

  • Primary accession
    Q7S7Z6
  • Secondary accessions
    • A7UWE9
    • A7UWF0
    • Q8X0S3
    • V5IM99
    • V5IP42

Proteomes

    • Identifier
    • Component
      Chromosome 2, Linkage Group V

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane250-270Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_000023304928-285Peptidyl-prolyl cis-trans isomerase B
Glycosylation139N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain38-195PPIase cyclophilin-type
Region217-243Disordered

Sequence similarities

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.

Q7S7Z6-1

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.

  • Name
    Long
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    285
  • Mass (Da)
    30,743
  • Last updated
    2008-01-15 v3
  • Checksum
    C8C6DD66836DBB6F
MFSLRRLLLAATLFLGAMLLFAQSAEAAKGPKITHKVYFDIEQGDKPLGRIVMGLYGKTVPKTAENFRALATGEKGFGYEGSTFHRVIKQFMIQGGDFTKGDGTGGKSIYGDKFPDENFKLKHSKKGLLSMANAGKDTNGSQFFITTVITSWLDGKHVVFGEVLEGYDVVEKIENTKTGPRDAPAEPIKIAKSGELEVPPEGLEGQSEWASPAYANEDEKPAAPVPVTDAKPPAHDSIPAATADDDDTGAPLFAKVLFFGVLVLGLVLYIRLRRAPKGTYGKGME

Q7S7Z6-2

  • Name
    Short
  • Note
    Lacks the C-terminal transmembrane domain, but has an ER retention motif at its extreme C-terminus.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 203-285: LEGQSEWASPAYANEDEKPAAPVPVTDAKPPAHDSIPAATADDDDTGAPLFAKVLFFGVLVLGLVLYIRLRRAPKGTYGKGME → IHVEL

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_029975203-285in isoform Short

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL670011
EMBL· GenBank· DDBJ
CAD21421.1
EMBL· GenBank· DDBJ
Genomic DNA
CM002240
EMBL· GenBank· DDBJ
ESA42515.1
EMBL· GenBank· DDBJ
Genomic DNA
CM002240
EMBL· GenBank· DDBJ
ESA42516.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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