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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) (Mitochondrial cyclophilin) (CyP-M) (Rotamase F)

 PPIF_HUMAN              Reviewed;         207 AA.
P30405; Q2YDB7; Q5W131;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
20-JUN-2018, entry version 173.
RecName: Full=Peptidyl-prolyl cis-trans isomerase F, mitochondrial;
Short=PPIase F;
EC=5.2.1.8 {ECO:0000269|PubMed:20676357};
AltName: Full=Cyclophilin D;
Short=CyP-D;
Short=CypD;
AltName: Full=Cyclophilin F;
AltName: Full=Mitochondrial cyclophilin;
Short=CyP-M;
AltName: Full=Rotamase F;
Flags: Precursor;
Name=PPIF; Synonyms=CYP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1744118;
Bergsma D.J., Eder C., Gross M., Kersten H., Sylvester D.,
Appelbaum E., Cusimano D., Livi G.P., McLauglin M.M., Kasyan K.,
Porter T.G., Silverman C., Dunnington D., Hand A., Prichett W.P.,
Bossard M.J., Brandt M., Levy M.A.;
"The cyclophilin multigene family of peptidyl-prolyl isomerases.
Characterization of three separate human isoforms.";
J. Biol. Chem. 266:23204-23214(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Blood, and Ovary;
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).
[6]
SUBCELLULAR LOCATION.
PubMed=10406942; DOI=10.1046/j.1432-1327.1999.00490.x;
Johnson N., Khan A., Virji S., Ward J.M., Crompton M.;
"Import and processing of heart mitochondrial cyclophilin D.";
Eur. J. Biochem. 263:353-359(1999).
[7]
FUNCTION, 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).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J.,
Paramanathan R., Bernstein G., MacKenzie F., Tempel W., Ouyang H.,
Lee W.H., Eisenmesser E.Z., Dhe-Paganon S.;
"Structural and biochemical characterization of the human cyclophilin
family of peptidyl-prolyl isomerases.";
PLoS Biol. 8:e1000439-e1000439(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INTERACTION WITH C1QBP.
PubMed=20950273; DOI=10.1042/BJ20101431;
McGee A.M., Baines C.P.;
"Complement 1q-binding protein inhibits the mitochondrial permeability
transition pore and protects against oxidative stress-induced death.";
Biochem. J. 433:119-125(2011).
[11]
MUTAGENESIS OF CYS-203.
PubMed=21930693; DOI=10.1074/jbc.M111.243469;
Nguyen T.T., Stevens M.V., Kohr M., Steenbergen C., Sack M.N.,
Murphy E.;
"Cysteine 203 of cyclophilin D is critical for cyclophilin D
activation of the mitochondrial permeability transition pore.";
J. Biol. Chem. 286:40184-40192(2011).
[12]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=22726440; DOI=10.1016/j.cell.2012.05.014;
Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S.,
Moll U.M.;
"p53 opens the mitochondrial permeability transition pore to trigger
necrosis.";
Cell 149:1536-1548(2012).
[13]
FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL PERMEABILITY TRANSITION
PORE COMPLEX, AND INTERACTION WITH SPG7.
PubMed=26387735; DOI=10.1016/j.molcel.2015.08.009;
Shanmughapriya S., Rajan S., Hoffman N.E., Higgins A.M., Tomar D.,
Nemani N., Hines K.J., Smith D.J., Eguchi A., Vallem S., Shaikh F.,
Cheung M., Leonard N.J., Stolakis R.S., Wolfers M.P., Ibetti J.,
Chuprun J.K., Jog N.R., Houser S.R., Koch W.J., Elrod J.W., Madesh M.;
"SPG7 is an essential and conserved component of the mitochondrial
permeability transition pore.";
Mol. Cell 60:47-62(2015).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
INTERACTION WITH MCUR1.
PubMed=26976564; DOI=10.1073/pnas.1602264113;
Chaudhuri D., Artiga D.J., Abiria S.A., Clapham D.E.;
"Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the
calcium threshold for the mitochondrial permeability transition.";
Proc. Natl. Acad. Sci. U.S.A. 113:E1872-E1880(2016).
[16]
X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 43-207.
PubMed=15858260; DOI=10.1107/S0907444905003070;
Schlatter D., Thoma R., Kung E., Stihle M., Muller F., Borroni E.,
Cesura A., Hennig M.;
"Crystal engineering yields crystals of cyclophilin D diffracting to
1.7 A resolution.";
Acta Crystallogr. D 61:513-519(2005).
[17]
X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) OF 44-207 IN COMPLEX WITH
CYCLOSPORIN A.
PubMed=18076075; DOI=10.1002/prot.21855;
Kajitani K., Fujihashi M., Kobayashi Y., Shimizu S., Tsujimoto Y.,
Miki K.;
"Crystal structure of human cyclophilin D in complex with its
inhibitor, cyclosporin A at 0.96-A resolution.";
Proteins 70:1635-1639(2008).
[18]
X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 44-207.
PubMed=21904027; DOI=10.1107/S0907444911023249;
le Maire A., Gelin M., Pochet S., Hoh F., Pirocchi M., Guichou J.F.,
Ferrer J.L., Labesse G.;
"In-plate protein crystallization, in situ ligand soaking and X-ray
diffraction.";
Acta Crystallogr. D 67:747-755(2011).
-!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of
proline imidic peptide bonds in oligopeptides and may therefore
assist protein folding (PubMed:20676357). 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:19228691, ECO:0000269|PubMed:20676357,
ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26387735}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0). {ECO:0000269|PubMed:20676357}.
-!- ENZYME REGULATION: Inhibited by cyclosporin A (CsA)
(PubMed:20676357). Is displaced by CsA from the mPTP leading to a
lower open probability of the mPTP. {ECO:0000269|PubMed:20676357}.
-!- 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 ATP5F1B; 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 (PubMed:26976564). Component of the
mitochondrial permeability transition pore complex (mPTPC), at
least composed of SPG7, VDAC1 and PPIF (PubMed:26387735).
Interacts with SPG7 (PubMed:26387735).
{ECO:0000269|PubMed:18076075, ECO:0000269|PubMed:19228691,
ECO:0000269|PubMed:20950273, ECO:0000269|PubMed:22726440,
ECO:0000269|PubMed:26387735, ECO:0000269|PubMed:26976564}.
-!- INTERACTION:
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-5544229, EBI-743598;
Q8N9N5:BANP; NbExp=3; IntAct=EBI-5544229, EBI-744695;
Q96DZ9:CMTM5; NbExp=3; IntAct=EBI-5544229, EBI-2548702;
P04637:TP53; NbExp=4; IntAct=EBI-5544229, EBI-366083;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:10406942}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P30405-1; Sequence=Displayed;
Name=2;
IsoId=P30405-2; Sequence=VSP_056286;
-!- PTM: Deacteylated at Lys-167 by SIRT3. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
{ECO:0000305}.
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EMBL; M80254; AAA58434.1; -; mRNA.
EMBL; AK296669; BAG59266.1; -; mRNA.
EMBL; AL133481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54645.1; -; Genomic_DNA.
EMBL; BC005020; AAH05020.1; -; mRNA.
EMBL; BC110299; AAI10300.1; -; mRNA.
CCDS; CCDS7358.1; -. [P30405-1]
PIR; A41581; A41581.
RefSeq; NP_005720.1; NM_005729.3. [P30405-1]
UniGene; Hs.381072; -.
PDB; 2BIT; X-ray; 1.71 A; X=43-207.
PDB; 2BIU; X-ray; 1.71 A; X=43-207.
PDB; 2Z6W; X-ray; 0.96 A; A/B=44-207.
PDB; 3QYU; X-ray; 1.54 A; A=44-207.
PDB; 3R49; X-ray; 1.77 A; A=43-207.
PDB; 3R4G; X-ray; 1.05 A; A=43-207.
PDB; 3R54; X-ray; 1.35 A; A=43-207.
PDB; 3R56; X-ray; 1.40 A; A=43-207.
PDB; 3R57; X-ray; 1.71 A; A=43-207.
PDB; 3R59; X-ray; 1.10 A; A=43-207.
PDB; 3RCF; X-ray; 1.15 A; A=43-207.
PDB; 3RCG; X-ray; 0.97 A; A=43-207.
PDB; 3RCI; X-ray; 1.44 A; X=43-207.
PDB; 3RCK; X-ray; 1.26 A; X=43-207.
PDB; 3RCL; X-ray; 1.70 A; A=43-207.
PDB; 3RD9; X-ray; 1.40 A; X=43-207.
PDB; 3RDA; X-ray; 1.07 A; X=43-207.
PDB; 3RDB; X-ray; 1.55 A; A=43-207.
PDB; 3RDC; X-ray; 1.94 A; A=43-207.
PDB; 4J58; X-ray; 1.28 A; A=44-207.
PDB; 4J59; X-ray; 1.92 A; A=44-207.
PDB; 4J5A; X-ray; 1.58 A; X=44-207.
PDB; 4J5B; X-ray; 2.01 A; A=44-207.
PDB; 4J5C; X-ray; 1.03 A; X=44-207.
PDB; 4J5D; X-ray; 1.32 A; X=44-207.
PDB; 4J5E; X-ray; 0.99 A; X=44-207.
PDB; 4O8H; X-ray; 0.85 A; A=43-207.
PDB; 4O8I; X-ray; 1.45 A; A=43-207.
PDB; 4XNC; X-ray; 2.23 A; A=44-207.
PDB; 4ZSC; X-ray; 1.50 A; A=44-207.
PDB; 4ZSD; X-ray; 1.45 A; A=44-207.
PDB; 5A0E; X-ray; 1.25 A; A/B=43-207.
PDB; 5CBT; X-ray; 1.45 A; A=44-207.
PDB; 5CBU; X-ray; 1.40 A; A=44-207.
PDB; 5CBV; X-ray; 1.80 A; A=44-207.
PDB; 5CBW; X-ray; 1.80 A; A=44-207.
PDB; 5CCN; X-ray; 1.80 A; A=44-207.
PDB; 5CCQ; X-ray; 1.80 A; A=44-207.
PDB; 5CCR; X-ray; 1.90 A; A=44-207.
PDB; 5CCS; X-ray; 2.10 A; X=44-207.
PDBsum; 2BIT; -.
PDBsum; 2BIU; -.
PDBsum; 2Z6W; -.
PDBsum; 3QYU; -.
PDBsum; 3R49; -.
PDBsum; 3R4G; -.
PDBsum; 3R54; -.
PDBsum; 3R56; -.
PDBsum; 3R57; -.
PDBsum; 3R59; -.
PDBsum; 3RCF; -.
PDBsum; 3RCG; -.
PDBsum; 3RCI; -.
PDBsum; 3RCK; -.
PDBsum; 3RCL; -.
PDBsum; 3RD9; -.
PDBsum; 3RDA; -.
PDBsum; 3RDB; -.
PDBsum; 3RDC; -.
PDBsum; 4J58; -.
PDBsum; 4J59; -.
PDBsum; 4J5A; -.
PDBsum; 4J5B; -.
PDBsum; 4J5C; -.
PDBsum; 4J5D; -.
PDBsum; 4J5E; -.
PDBsum; 4O8H; -.
PDBsum; 4O8I; -.
PDBsum; 4XNC; -.
PDBsum; 4ZSC; -.
PDBsum; 4ZSD; -.
PDBsum; 5A0E; -.
PDBsum; 5CBT; -.
PDBsum; 5CBU; -.
PDBsum; 5CBV; -.
PDBsum; 5CBW; -.
PDBsum; 5CCN; -.
PDBsum; 5CCQ; -.
PDBsum; 5CCR; -.
PDBsum; 5CCS; -.
ProteinModelPortal; P30405; -.
SMR; P30405; -.
BioGrid; 115411; 36.
CORUM; P30405; -.
IntAct; P30405; 19.
STRING; 9606.ENSP00000225174; -.
BindingDB; P30405; -.
ChEMBL; CHEMBL3325306; -.
DrugBank; DB02078; 1-Methoxy-2-[2-(2-Methoxy-Ethoxy]-Ethane.
DrugBank; DB08168; 7-AMINO-4-METHYL-CHROMEN-2-ONE.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB00172; L-Proline.
iPTMnet; P30405; -.
PhosphoSitePlus; P30405; -.
SwissPalm; P30405; -.
BioMuta; PPIF; -.
DMDM; 231968; -.
OGP; P30405; -.
UCD-2DPAGE; P30405; -.
EPD; P30405; -.
MaxQB; P30405; -.
PaxDb; P30405; -.
PeptideAtlas; P30405; -.
PRIDE; P30405; -.
ProteomicsDB; 54662; -.
TopDownProteomics; P30405-1; -. [P30405-1]
DNASU; 10105; -.
Ensembl; ENST00000225174; ENSP00000225174; ENSG00000108179. [P30405-1]
GeneID; 10105; -.
KEGG; hsa:10105; -.
UCSC; uc001kai.4; human. [P30405-1]
CTD; 10105; -.
DisGeNET; 10105; -.
EuPathDB; HostDB:ENSG00000108179.13; -.
GeneCards; PPIF; -.
HGNC; HGNC:9259; PPIF.
HPA; HPA077416; -.
MIM; 604486; gene.
neXtProt; NX_P30405; -.
OpenTargets; ENSG00000108179; -.
PharmGKB; PA33584; -.
eggNOG; KOG0865; Eukaryota.
eggNOG; COG0652; LUCA.
GeneTree; ENSGT00760000119119; -.
HOGENOM; HOG000065981; -.
HOVERGEN; HBG001065; -.
InParanoid; P30405; -.
KO; K09565; -.
OMA; ELKHTGS; -.
OrthoDB; EOG091G0BGL; -.
PhylomeDB; P30405; -.
TreeFam; TF312801; -.
BRENDA; 5.2.1.8; 2681.
ChiTaRS; PPIF; human.
EvolutionaryTrace; P30405; -.
GeneWiki; PPIF; -.
GenomeRNAi; 10105; -.
PRO; PR:P30405; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000108179; -.
CleanEx; HS_PPIF; -.
ExpressionAtlas; P30405; baseline and differential.
Genevisible; P30405; HS.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
GO; GO:0005757; C:mitochondrial permeability transition pore complex; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
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; IMP:UniProtKB.
GO; GO:1902686; P:mitochondrial outer membrane permeabilization involved in programmed cell death; IMP:UniProtKB.
GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0032780; P:negative regulation of ATPase activity; ISS:UniProtKB.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP: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; IDA: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:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB.
GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; IMP:UniProtKB.
GO; GO:0010939; P:regulation of necrotic cell death; IEA:Ensembl.
GO; GO:0010849; P:regulation of proton-transporting ATPase activity, rotational mechanism; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
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; Alternative splicing; Apoptosis;
Complete proteome; Isomerase; Mitochondrion; Necrosis;
Reference proteome; Rotamase; S-nitrosylation; Transit peptide.
TRANSIT 1 29 Mitochondrion. {ECO:0000255}.
CHAIN 30 207 Peptidyl-prolyl cis-trans isomerase F,
mitochondrial.
/FTId=PRO_0000025489.
DOMAIN 49 205 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
MOD_RES 67 67 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 67 67 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 86 86 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 167 167 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 175 175 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 190 190 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99KR7}.
MOD_RES 203 203 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q99KR7}.
VAR_SEQ 139 207 VLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMD
VVKKIESFGSKSGRTSKKIVITDCGQLS -> WMASMLCSV
TSKRAWTS (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_056286.
MUTAGEN 203 203 C->S: Blocks Ca(2+)-induced mPTP opening
and reduces hydrogen peroxide-induced
cell death.
{ECO:0000269|PubMed:21930693}.
STRAND 47 54 {ECO:0000244|PDB:4O8H}.
STRAND 57 66 {ECO:0000244|PDB:4O8H}.
TURN 68 70 {ECO:0000244|PDB:4O8H}.
HELIX 72 83 {ECO:0000244|PDB:4O8H}.
TURN 84 86 {ECO:0000244|PDB:4O8H}.
STRAND 94 99 {ECO:0000244|PDB:4O8H}.
TURN 100 102 {ECO:0000244|PDB:4O8H}.
STRAND 103 106 {ECO:0000244|PDB:4O8H}.
TURN 109 111 {ECO:0000244|PDB:4O8H}.
STRAND 112 115 {ECO:0000244|PDB:4O8H}.
STRAND 120 123 {ECO:0000244|PDB:4J5E}.
STRAND 139 142 {ECO:0000244|PDB:4O8H}.
STRAND 144 146 {ECO:0000244|PDB:2Z6W}.
STRAND 150 152 {ECO:0000244|PDB:4O8H}.
STRAND 154 159 {ECO:0000244|PDB:4O8H}.
HELIX 162 164 {ECO:0000244|PDB:4O8H}.
TURN 165 167 {ECO:0000244|PDB:4O8H}.
STRAND 170 176 {ECO:0000244|PDB:4O8H}.
HELIX 178 186 {ECO:0000244|PDB:4O8H}.
STRAND 198 205 {ECO:0000244|PDB:4O8H}.
SEQUENCE 207 AA; 22040 MW; D7C76F1D4049F16A CRC64;
MLALRCGSRW LGLLSVPRSV PLRLPAARAC SKGSGDPSSS SSSGNPLVYL DVDANGKPLG
RVVLELKADV VPKTAENFRA LCTGEKGFGY KGSTFHRVIP SFMCQAGDFT NHNGTGGKSI
YGSRFPDENF TLKHVGPGVL SMANAGPNTN GSQFFICTIK TDWLDGKHVV FGHVKEGMDV
VKKIESFGSK SGRTSKKIVI TDCGQLS


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