Peptidyl-prolyl cis-trans isomerase F, mitochondrial

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Caution

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• [protein]-peptidylproline (ω=180)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  = [protein]-peptidylproline (ω=0)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  By similarity

  <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:P30405 (PPIF_HUMAN)
  EC:5.2.1.8
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  By similarity

  Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:P30405 (PPIF_HUMAN)
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  [protein]-peptidylproline (ω=180)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  

  peptidylproline (ω=180) residue

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  =

  [protein]-peptidylproline (ω=0)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  

  peptidylproline (ω=0) residue

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• cyclosporin A binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.3

    "Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin."
    Connern C.P., Halestrap A.P.
    Biochem. J. 284:381-385(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 30-58.
• peptide binding Source: RGDInferred from direct assayⁱ
  • "Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis."
    Li Y., Johnson N., Capano M., Edwards M., Crompton M.
    Biochem J 383:101-109(2004) [PubMed] [Europe PMC] [Abstract]
• peptidyl-prolyl cis-trans isomerase activity Source: RGDInferred from direct assayⁱ
  • "Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis."
    Li Y., Johnson N., Capano M., Edwards M., Crompton M.
    Biochem J 383:101-109(2004) [PubMed] [Europe PMC] [Abstract]
  • Ref.3

    "Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin."
    Connern C.P., Halestrap A.P.
    Biochem. J. 284:381-385(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 30-58.

GO - Biological processⁱ

• apoptotic mitochondrial changes Source: RGD
• cellular response to arsenic-containing substance Source: UniProtKB
• cellular response to calcium ion Source: UniProtKB
• cellular response to hydrogen peroxide Source: UniProtKB
• mitochondrial outer membrane permeabilization involved in programmed cell death Source: UniProtKB
• necroptotic process Source: RGD
• negative regulation of apoptotic process Source: UniProtKB
• negative regulation of ATPase activity Source: UniProtKB
• negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
• negative regulation of oxidative phosphorylation Source: UniProtKB
• negative regulation of oxidative phosphorylation uncoupler activity Source: UniProtKB
• negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
• positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
• protein folding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• protein peptidyl-prolyl isomerization Source: RGD
• regulation of apoptotic process Source: RGDInferred from direct assayⁱ
  • "Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis."
    Li Y., Johnson N., Capano M., Edwards M., Crompton M.
    Biochem J 383:101-109(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of mitochondrial membrane permeability Source: RGDInferred from direct assayⁱ
  • "Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis."
    Li Y., Johnson N., Capano M., Edwards M., Crompton M.
    Biochem J 383:101-109(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of mitochondrial membrane permeability involved in programmed necrotic cell death Source: UniProtKB
• regulation of necrotic cell death Source: RGD
• regulation of proton-transporting ATPase activity, rotational mechanism Source: UniProtKB
• response to ischemia Source: UniProtKB
• response to oxidative stress Source: RGD

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MLALRCGPRL LGLLSGPRSA PLLLSTTRTC SDGGARGANS SSQNPLVYLD 
        60         70         80         90        100
VGADGQPLGR VVLELKADVV PKTAENFRAL CTGEKGFGYK GSTFHRVIPA 
       110        120        130        140        150
FMCQAGDFTN HNGTGGKSIY GSRFPDENFT LKHVGPGVLS MANAGPNTNG 
       160        170        180        190        200
SQFFICTIKT DWLDGKHVVF GHVKEGMDVV KKIESFGSKS GKTSKKIVIT 

DCGQLS                                                 

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families