CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005749
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase F, mitochondrial 
Protein Synonyms/Alias
 PPIase F; Cyclophilin D; CyP-D; CypD; Cyclophilin F; Rotamase F 
Gene Name
 Ppif 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
66GRVVLELKADVVPKTacetylation[1]
85RALCTGEKGFGYKGSacetylation[1]
90GEKGFGYKGSTFHRVacetylation[1]
166KTDWLDGKHVVFGHVacetylation[1]
174HVVFGHVKEGMDVVKacetylation[1]
181KEGMDVVKKIESFGSacetylation[1]
182EGMDVVKKIESFGSKacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 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 probablity 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 F(1)F(0) 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. 
Sequence Annotation
 DOMAIN 48 204 PPIase cyclophilin-type.
 MOD_RES 166 166 N6-acetyllysine (By similarity).
 MOD_RES 202 202 S-nitrosocysteine (By similarity).  
Keyword
 Acetylation; Apoptosis; Complete proteome; Cyclosporin; Direct protein sequencing; Isomerase; Mitochondrion; Necrosis; Reference proteome; Rotamase; S-nitrosylation; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 206 AA 
Protein Sequence
MLALRCGPRL LGLLSGPRSA PLLLSTTRTC SDGGARGANS SSQNPLVYLD VGADGQPLGR 60
VVLELKADVV PKTAENFRAL CTGEKGFGYK GSTFHRVIPA FMCQAGDFTN HNGTGGKSIY 120
GSRFPDENFT LKHVGPGVLS MANAGPNTNG SQFFICTIKT DWLDGKHVVF GHVKEGMDVV 180
KKIESFGSKS GKTSKKIVIT DCGQLS 206 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
 GO:0005759; C:mitochondrial matrix; IDA:RGD.
 GO:0016018; F:cyclosporin A binding; IDA:RGD.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:RGD.
 GO:0008637; P:apoptotic mitochondrial changes; IEA:Compara.
 GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
 GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
 GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0032780; P:negative regulation of ATPase activity; ISS:UniProtKB.
 GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
 GO:0090324; P:negative regulation of oxidative phosphorylation; ISS:UniProtKB.
 GO:2000276; P:negative regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
 GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
 GO:0010940; P:positive regulation of necrotic cell death; ISS:UniProtKB.
 GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:RGD.
 GO:0010849; P:regulation of proton-transporting ATPase activity, rotational mechanism; ISS:UniProtKB.
 GO:0002931; P:response to ischemia; ISS:UniProtKB. 
Interpro
 IPR002130; Cyclophilin-like_PPIase_dom.
 IPR024936; Cyclophilin-type_PPIase.
 IPR020892; Cyclophilin-type_PPIase_CS. 
Pfam
 PF00160; Pro_isomerase 
SMART
  
PROSITE
 PS00170; CSA_PPIASE_1
 PS50072; CSA_PPIASE_2 
PRINTS
 PR00153; CSAPPISMRASE.