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Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Rotamase F)

 PPIF_RAT                Reviewed;         206 AA.
P29117;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 143.
RecName: Full=Peptidyl-prolyl cis-trans isomerase F, mitochondrial;
Short=PPIase F;
EC=5.2.1.8;
AltName: Full=Cyclophilin D;
Short=CyP-D;
Short=CypD;
AltName: Full=Cyclophilin F;
AltName: Full=Rotamase F;
Flags: Precursor;
Name=Ppif;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Skeletal muscle;
Price N.T., Woodfield K.Y., Halestrap A.P.;
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 30-58.
TISSUE=Liver;
PubMed=1599421; DOI=10.1042/bj2840381;
Connern C.P., Halestrap A.P.;
"Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-
isomerase from rat liver mitochondrial matrix reveals the existence of
a distinct mitochondrial cyclophilin.";
Biochem. J. 284:381-385(1992).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8567677; DOI=10.1074/jbc.271.4.2185;
Nicolli A., Basso E., Petronilli V., Wenger R.M., Bernardi P.;
"Interactions of cyclophilin with the mitochondrial inner membrane and
regulation of the permeability transition pore, and cyclosporin A-
sensitive channel.";
J. Biol. Chem. 271:2185-2192(1996).
[5]
FUNCTION.
PubMed=9309684; DOI=10.1023/A:1006887921810;
Scorrano L., Nicolli A., Basso E., Petronilli V., Bernardi P.;
"Two modes of activation of the permeability transition pore: the role
of mitochondrial cyclophilin.";
Mol. Cell. Biochem. 174:181-184(1997).
[6]
FUNCTION.
PubMed=9820802; DOI=10.1042/bj3360287;
Woodfield K., Ruck A., Brdiczka D., Halestrap A.P.;
"Direct demonstration of a specific interaction between cyclophilin-D
and the adenine nucleotide translocase confirms their role in the
mitochondrial permeability transition.";
Biochem. J. 336:287-290(1998).
[7]
INTERACTION WITH VDAC1.
PubMed=9874241; DOI=10.1046/j.1432-1327.1998.2580729.x;
Crompton M., Virji S., Ward J.M.;
"Cyclophilin-D binds strongly to complexes of the voltage-dependent
anion channel and the adenine nucleotide translocase to form the
permeability transition pore.";
Eur. J. Biochem. 258:729-735(1998).
[8]
INTERACTION WITH SLC25A3.
PubMed=18667415; DOI=10.1074/jbc.M805235200;
Leung A.W., Varanyuwatana P., Halestrap A.P.;
"The mitochondrial phosphate carrier interacts with cyclophilin D and
may play a key role in the permeability transition.";
J. Biol. Chem. 283:26312-26323(2008).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH BCL2.
PubMed=19228691; DOI=10.1074/jbc.M808750200;
Eliseev R.A., Malecki J., Lester T., Zhang Y., Humphrey J.,
Gunter T.E.;
"Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic
effect.";
J. Biol. Chem. 284:9692-9699(2009).
-!- FUNCTION: 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
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. {ECO:0000269|PubMed:8567677,
ECO:0000269|PubMed:9309684, ECO:0000269|PubMed:9820802}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Binds cyclosporin A (CsA). Is displaced by CsA
from the mPTP leading to a lower open probability of the mPTP.
-!- SUBUNIT: Associates with the mitochondrial membrane ATP synthase
F(1)F(0) 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.
Interacts with MCUR1. Component of the mitochondrial permeability
transition pore complex (mPTPC), at least composed of SPG7, VDAC1
and PPIF. Interacts with SPG7 (By similarity).
{ECO:0000250|UniProtKB:P30405, ECO:0000269|PubMed:18667415,
ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:9874241}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:8567677}.
-!- PTM: Deacteylated at Lys-166 by SIRT3 (By similarity). Interacts
with BCL2; the interaction is impaired by CsA. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
{ECO:0000305}.
-!- CAUTION: The polyclonal antibody used in PubMed:9820802 and
PubMed:9874241 and initially thought to detect SLC25A4/ANT1 in
interactions with Ppif/CyP-D is rather detecting SLC25A3.
{ECO:0000305|PubMed:18667415}.
-----------------------------------------------------------------------
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EMBL; U68544; AAB08453.1; -; mRNA.
EMBL; BC086977; AAH86977.1; -; mRNA.
PIR; S23122; S23122.
RefSeq; NP_758443.1; NM_172243.1.
UniGene; Rn.2923; -.
PDB; 4TOT; X-ray; 2.39 A; A/B/C/D=43-206.
PDBsum; 4TOT; -.
ProteinModelPortal; P29117; -.
SMR; P29117; -.
IntAct; P29117; 5.
MINT; MINT-1542363; -.
STRING; 10116.ENSRNOP00000014382; -.
iPTMnet; P29117; -.
PhosphoSitePlus; P29117; -.
PaxDb; P29117; -.
PRIDE; P29117; -.
Ensembl; ENSRNOT00000014382; ENSRNOP00000014382; ENSRNOG00000010558.
GeneID; 282819; -.
KEGG; rno:282819; -.
UCSC; RGD:628670; rat.
CTD; 10105; -.
RGD; 628670; Ppif.
eggNOG; KOG0865; Eukaryota.
eggNOG; COG0652; LUCA.
GeneTree; ENSGT00760000119119; -.
HOGENOM; HOG000065981; -.
HOVERGEN; HBG001065; -.
InParanoid; P29117; -.
KO; K09565; -.
OMA; DIEWEGP; -.
OrthoDB; EOG091G0BGL; -.
PhylomeDB; P29117; -.
TreeFam; TF312801; -.
PRO; PR:P29117; -.
Proteomes; UP000002494; Chromosome 16.
Bgee; ENSRNOG00000010558; -.
Genevisible; P29117; RN.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0016018; F:cyclosporin A binding; IDA:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:RGD.
GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:1902686; P:mitochondrial outer membrane permeabilization involved in programmed cell death; ISS:UniProtKB.
GO; GO:0070266; P:necroptotic process; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0032780; P:negative regulation of ATPase activity; ISS:UniProtKB.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISS:UniProtKB.
GO; GO:2000276; P:negative regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:RGD.
GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; ISS:UniProtKB.
GO; GO:0010939; P:regulation of necrotic cell death; ISO:RGD.
GO; GO:0010849; P:regulation of proton-transporting ATPase activity, rotational mechanism; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom_sf.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
PANTHER; PTHR11071; PTHR11071; 1.
Pfam; PF00160; Pro_isomerase; 1.
PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
PRINTS; PR00153; CSAPPISMRASE.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Complete proteome;
Direct protein sequencing; Isomerase; Mitochondrion; Necrosis;
Reference proteome; Rotamase; S-nitrosylation; Transit peptide.
TRANSIT 1 29 Mitochondrion.
{ECO:0000269|PubMed:1599421}.
CHAIN 30 206 Peptidyl-prolyl cis-trans isomerase F,
mitochondrial.
/FTId=PRO_0000025491.
DOMAIN 48 204 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
MOD_RES 66 66 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 66 66 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 85 85 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 166 166 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 174 174 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 189 189 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 202 202 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q99KR7}.
VARIANT 30 39 Missing (in a minor form).
VARIANT 31 31 S -> R.
CONFLICT 30 30 C -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 46 53 {ECO:0000244|PDB:4TOT}.
STRAND 56 65 {ECO:0000244|PDB:4TOT}.
TURN 67 69 {ECO:0000244|PDB:4TOT}.
HELIX 71 82 {ECO:0000244|PDB:4TOT}.
TURN 83 85 {ECO:0000244|PDB:4TOT}.
STRAND 96 98 {ECO:0000244|PDB:4TOT}.
TURN 99 101 {ECO:0000244|PDB:4TOT}.
STRAND 102 105 {ECO:0000244|PDB:4TOT}.
STRAND 109 114 {ECO:0000244|PDB:4TOT}.
STRAND 119 122 {ECO:0000244|PDB:4TOT}.
STRAND 138 141 {ECO:0000244|PDB:4TOT}.
STRAND 143 145 {ECO:0000244|PDB:4TOT}.
STRAND 153 158 {ECO:0000244|PDB:4TOT}.
HELIX 161 163 {ECO:0000244|PDB:4TOT}.
TURN 164 166 {ECO:0000244|PDB:4TOT}.
STRAND 169 175 {ECO:0000244|PDB:4TOT}.
HELIX 177 185 {ECO:0000244|PDB:4TOT}.
STRAND 197 206 {ECO:0000244|PDB:4TOT}.
SEQUENCE 206 AA; 21810 MW; 69048482631B9FAD CRC64;
MLALRCGPRL LGLLSGPRSA PLLLSTTRTC SDGGARGANS SSQNPLVYLD VGADGQPLGR
VVLELKADVV PKTAENFRAL CTGEKGFGYK GSTFHRVIPA FMCQAGDFTN HNGTGGKSIY
GSRFPDENFT LKHVGPGVLS MANAGPNTNG SQFFICTIKT DWLDGKHVVF GHVKEGMDVV
KKIESFGSKS GKTSKKIVIT DCGQLS


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