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Protein

Peptidyl-prolyl cis-trans isomerase F, mitochondrial

Gene

PPIF

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Binds cyclosporin A (CsA). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Apoptosis, Necrosis

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase F, mitochondrial (EC:5.2.1.8)
Short name:
PPIase F
Alternative name(s):
Cyclophilin D
Short name:
CyP-D
Short name:
CypD
Cyclophilin F
Rotamase F
Gene namesi
Name:PPIF
Synonyms:CYP3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 28

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionAdd
BLAST
Chaini31 – 208178Peptidyl-prolyl cis-trans isomerase F, mitochondrialPRO_0000064149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-acetyllysine; alternateBy similarity
Modified residuei68 – 681N6-succinyllysine; alternateBy similarity
Modified residuei87 – 871N6-succinyllysineBy similarity
Modified residuei168 – 1681N6-acetyllysineBy similarity
Modified residuei176 – 1761N6-succinyllysineBy similarity
Modified residuei191 – 1911N6-succinyllysineBy similarity
Modified residuei204 – 2041S-nitrosocysteineBy similarity

Post-translational modificationi

Deacteylated at Lys-168 by SIRT3.By similarity

Keywords - PTMi

Acetylation, S-nitrosylation

Proteomic databases

PaxDbiP30404.
PeptideAtlasiP30404.
PRIDEiP30404.

Interactioni

Subunit structurei

Believed to associate with the mitochondrial permeability transition pore complex (PTPC). Associates with the mitochondrial membrane ATP synthase F1F0 ATP synthase; the association is increased by inorganic phosphate (Pi) and decreased by cyclosporin A (CsA). Interacts with ATP5B; ATP5H and ATP5O. Interacts with SLC25A3; the interaction is impaired by CsA. Interacts with BCL2; the interaction is impaired by CsA. Interacts with TP53; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by CsA. Interacts with C1QBP.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022213.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 206157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.Curated
Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP30404.
KOiK09565.
OMAiDMTADNE.
OrthoDBiEOG79GT7W.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLALRCGPR LLGLLSGPRS AHLRLPAVRA CSSGSGSHGS SSSSGNPLVY
60 70 80 90 100
LDVGADGQPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI
110 120 130 140 150
PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FKLKHEGPGV LSMANAGPNT
160 170 180 190 200
NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGKTSKKIV

ITDCGQLS
Length:208
Mass (Da):22,019
Last modified:March 6, 2013 - v3
Checksum:i087239A93D68A512
GO

Sequence cautioni

The sequence AAT02663.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301A → V in AAT02663 (Ref. 1) Curated
Sequence conflicti30 – 301A → V in EH176460 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY594335 mRNA. Translation: AAT02663.1. Sequence problems.
EH176460 mRNA. No translation available.
AAFC03123307 Genomic DNA. No translation available.
PIRiPC1237.
RefSeqiNP_001001597.1. NM_001001597.1.
UniGeneiBt.9791.

Genome annotation databases

EnsembliENSBTAT00000022213; ENSBTAP00000022213; ENSBTAG00000016711.
GeneIDi414346.
KEGGibta:414346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY594335 mRNA. Translation: AAT02663.1. Sequence problems.
EH176460 mRNA. No translation available.
AAFC03123307 Genomic DNA. No translation available.
PIRiPC1237.
RefSeqiNP_001001597.1. NM_001001597.1.
UniGeneiBt.9791.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022213.

Proteomic databases

PaxDbiP30404.
PeptideAtlasiP30404.
PRIDEiP30404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022213; ENSBTAP00000022213; ENSBTAG00000016711.
GeneIDi414346.
KEGGibta:414346.

Organism-specific databases

CTDi10105.

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP30404.
KOiK09565.
OMAiDMTADNE.
OrthoDBiEOG79GT7W.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bos taurus peptidylprolyl isomerase F."
    Zhang W., Xiao Y., Ren Z., Wang J., Wu Z., Cheng J., Wang Y.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Colon.
  3. "The genome sequence of taurine cattle: a window to ruminant biology and evolution."
    The bovine genome sequencing and analysis consortium
    Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  4. "Isolation of mitochondrial cyclophilin from bovine heart."
    Inoue T., Yoshida Y., Isaka Y., Tagawa K.
    Biochem. Biophys. Res. Commun. 190:857-863(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE.
    Tissue: Heart.
  5. "Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex."
    Giorgio V., Bisetto E., Soriano M.E., Dabbeni-Sala F., Basso E., Petronilli V., Forte M.A., Bernardi P., Lippe G.
    J. Biol. Chem. 284:33982-33988(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATP5B; ATP5H AND ATP5O.

Entry informationi

Entry nameiPPIF_BOVIN
AccessioniPrimary (citable) accession number: P30404
Secondary accession number(s): Q6PMK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 6, 2013
Last modified: July 6, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.