PPIF_HUMAN
ID PPIF_HUMAN Reviewed; 207 AA.
AC P30405; Q2YDB7; Q5W131;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase F, mitochondrial;
DE Short=PPIase F;
DE EC=5.2.1.8 {ECO:0000269|PubMed:20676357};
DE AltName: Full=Cyclophilin D;
DE Short=CyP-D;
DE Short=CypD;
DE AltName: Full=Cyclophilin F;
DE AltName: Full=Mitochondrial cyclophilin;
DE Short=CyP-M;
DE AltName: Full=Rotamase F;
DE Flags: Precursor;
GN Name=PPIF; Synonyms=CYP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1744118; DOI=10.1016/s0021-9258(18)54484-7;
RA Bergsma D.J., Eder C., Gross M., Kersten H., Sylvester D., Appelbaum E.,
RA Cusimano D., Livi G.P., McLauglin M.M., Kasyan K., Porter T.G.,
RA Silverman C., Dunnington D., Hand A., Prichett W.P., Bossard M.J.,
RA Brandt M., Levy M.A.;
RT "The cyclophilin multigene family of peptidyl-prolyl isomerases.
RT Characterization of three separate human isoforms.";
RL J. Biol. Chem. 266:23204-23214(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10406942; DOI=10.1046/j.1432-1327.1999.00490.x;
RA Johnson N., Khan A., Virji S., Ward J.M., Crompton M.;
RT "Import and processing of heart mitochondrial cyclophilin D.";
RL Eur. J. Biochem. 263:353-359(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH BCL2.
RX PubMed=19228691; DOI=10.1074/jbc.m808750200;
RA Eliseev R.A., Malecki J., Lester T., Zhang Y., Humphrey J., Gunter T.E.;
RT "Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect.";
RL J. Biol. Chem. 284:9692-9699(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INTERACTION WITH C1QBP.
RX PubMed=20950273; DOI=10.1042/bj20101431;
RA McGee A.M., Baines C.P.;
RT "Complement 1q-binding protein inhibits the mitochondrial permeability
RT transition pore and protects against oxidative stress-induced death.";
RL Biochem. J. 433:119-125(2011).
RN [11]
RP MUTAGENESIS OF CYS-203.
RX PubMed=21930693; DOI=10.1074/jbc.m111.243469;
RA Nguyen T.T., Stevens M.V., Kohr M., Steenbergen C., Sack M.N., Murphy E.;
RT "Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of
RT the mitochondrial permeability transition pore.";
RL J. Biol. Chem. 286:40184-40192(2011).
RN [12]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=22726440; DOI=10.1016/j.cell.2012.05.014;
RA Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S., Moll U.M.;
RT "p53 opens the mitochondrial permeability transition pore to trigger
RT necrosis.";
RL Cell 149:1536-1548(2012).
RN [13]
RP FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL PERMEABILITY TRANSITION PORE
RP COMPLEX, AND INTERACTION WITH SPG7.
RX PubMed=26387735; DOI=10.1016/j.molcel.2015.08.009;
RA Shanmughapriya S., Rajan S., Hoffman N.E., Higgins A.M., Tomar D.,
RA Nemani N., Hines K.J., Smith D.J., Eguchi A., Vallem S., Shaikh F.,
RA Cheung M., Leonard N.J., Stolakis R.S., Wolfers M.P., Ibetti J.,
RA Chuprun J.K., Jog N.R., Houser S.R., Koch W.J., Elrod J.W., Madesh M.;
RT "SPG7 is an essential and conserved component of the mitochondrial
RT permeability transition pore.";
RL Mol. Cell 60:47-62(2015).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP INTERACTION WITH MCUR1.
RX PubMed=26976564; DOI=10.1073/pnas.1602264113;
RA Chaudhuri D., Artiga D.J., Abiria S.A., Clapham D.E.;
RT "Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the calcium
RT threshold for the mitochondrial permeability transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1872-E1880(2016).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 43-207.
RX PubMed=15858260; DOI=10.1107/s0907444905003070;
RA Schlatter D., Thoma R., Kung E., Stihle M., Muller F., Borroni E.,
RA Cesura A., Hennig M.;
RT "Crystal engineering yields crystals of cyclophilin D diffracting to 1.7 A
RT resolution.";
RL Acta Crystallogr. D 61:513-519(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) OF 44-207 IN COMPLEX WITH
RP CYCLOSPORIN A.
RX PubMed=18076075; DOI=10.1002/prot.21855;
RA Kajitani K., Fujihashi M., Kobayashi Y., Shimizu S., Tsujimoto Y., Miki K.;
RT "Crystal structure of human cyclophilin D in complex with its inhibitor,
RT cyclosporin A at 0.96-A resolution.";
RL Proteins 70:1635-1639(2008).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 44-207.
RX PubMed=21904027; DOI=10.1107/s0907444911023249;
RA le Maire A., Gelin M., Pochet S., Hoh F., Pirocchi M., Guichou J.F.,
RA Ferrer J.L., Labesse G.;
RT "In-plate protein crystallization, in situ ligand soaking and X-ray
RT diffraction.";
RL Acta Crystallogr. D 67:747-755(2011).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding (PubMed:20676357). Involved in regulation of the mitochondrial
CC permeability transition pore (mPTP) (PubMed:26387735). It is proposed
CC that its association with the mPTP is masking a binding site for
CC inhibiting inorganic phosphate (Pi) and promotes the open probability
CC of the mPTP leading to apoptosis or necrosis; the requirement of the
CC PPIase activity for this function is debated (PubMed:26387735). In
CC cooperation with mitochondrial p53/TP53 is involved in activating
CC oxidative stress-induced necrosis (PubMed:22726440). Involved in
CC modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and
CC regulation of mitochondrial matrix adenine nucleotide levels (By
CC similarity). Has anti-apoptotic activity independently of mPTP and in
CC cooperation with BCL2 inhibits cytochrome c-dependent apoptosis
CC (PubMed:19228691). {ECO:0000250|UniProtKB:Q99KR7,
CC ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:20676357,
CC ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26387735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA)
CC (PubMed:20676357). Is displaced by CsA from the mPTP leading to a lower
CC open probability of the mPTP. {ECO:0000269|PubMed:20676357}.
CC -!- SUBUNIT: Associates with the mitochondrial membrane ATP synthase
CC F(1)F(0) ATP synthase; the association is increased by inorganic
CC phosphate (Pi) and decreased by cyclosporin A (CsA) (By similarity).
CC Interacts with ATP5F1B; ATP5PD and ATP5PO (By similarity). Interacts
CC with SLC25A3; the interaction is impaired by CsA (By similarity).
CC Interacts with BCL2; the interaction is impaired by CsA
CC (PubMed:19228691). Interacts with TP53; the association implicates
CC preferentially tetrameric TP53, is induced by oxidative stress and is
CC impaired by CsA (PubMed:22726440). Interacts with C1QBP
CC (PubMed:20950273). Interacts with MCUR1 (PubMed:26976564). Component of
CC the mitochondrial permeability transition pore complex (mPTPC), at
CC least composed of SPG7, VDAC1 and PPIF (PubMed:26387735). Interacts
CC with SPG7 (PubMed:26387735). {ECO:0000250|UniProtKB:P29117,
CC ECO:0000250|UniProtKB:P30404, ECO:0000250|UniProtKB:Q99KR7,
CC ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:20950273,
CC ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26387735,
CC ECO:0000269|PubMed:26976564}.
CC -!- INTERACTION:
CC P30405; Q9NYB9: ABI2; NbExp=4; IntAct=EBI-5544229, EBI-743598;
CC P30405; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-5544229, EBI-11096309;
CC P30405; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-5544229, EBI-11522760;
CC P30405; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-5544229, EBI-821758;
CC P30405; P53365: ARFIP2; NbExp=3; IntAct=EBI-5544229, EBI-638194;
CC P30405; Q8N9N5: BANP; NbExp=3; IntAct=EBI-5544229, EBI-744695;
CC P30405; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-5544229, EBI-7062247;
CC P30405; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-5544229, EBI-2548702;
CC P30405; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-5544229, EBI-14240149;
CC P30405; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-5544229, EBI-3918971;
CC P30405; P43364: MAGEA11; NbExp=3; IntAct=EBI-5544229, EBI-739552;
CC P30405; P15941-11: MUC1; NbExp=3; IntAct=EBI-5544229, EBI-17263240;
CC P30405; Q04118: PRB3; NbExp=3; IntAct=EBI-5544229, EBI-13360404;
CC P30405; P08247: SYP; NbExp=5; IntAct=EBI-5544229, EBI-9071725;
CC P30405; Q16563: SYPL1; NbExp=3; IntAct=EBI-5544229, EBI-2800683;
CC P30405; P04637: TP53; NbExp=4; IntAct=EBI-5544229, EBI-366083;
CC P30405; O95070: YIF1A; NbExp=3; IntAct=EBI-5544229, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:10406942}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30405-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30405-2; Sequence=VSP_056286;
CC -!- PTM: Acetylated at Lys-167; deacetylated at Lys-167 by SIRT3.
CC {ECO:0000250|UniProtKB:Q99KR7}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; M80254; AAA58434.1; -; mRNA.
DR EMBL; AK296669; BAG59266.1; -; mRNA.
DR EMBL; AL133481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54645.1; -; Genomic_DNA.
DR EMBL; BC005020; AAH05020.1; -; mRNA.
DR EMBL; BC110299; AAI10300.1; -; mRNA.
DR CCDS; CCDS7358.1; -. [P30405-1]
DR PIR; A41581; A41581.
DR RefSeq; NP_005720.1; NM_005729.3. [P30405-1]
DR PDB; 2BIT; X-ray; 1.71 A; X=43-207.
DR PDB; 2BIU; X-ray; 1.71 A; X=43-207.
DR PDB; 2Z6W; X-ray; 0.96 A; A/B=44-207.
DR PDB; 3QYU; X-ray; 1.54 A; A=44-207.
DR PDB; 3R49; X-ray; 1.77 A; A=43-207.
DR PDB; 3R4G; X-ray; 1.05 A; A=43-207.
DR PDB; 3R54; X-ray; 1.35 A; A=43-207.
DR PDB; 3R56; X-ray; 1.40 A; A=43-207.
DR PDB; 3R57; X-ray; 1.71 A; A=43-207.
DR PDB; 3R59; X-ray; 1.10 A; A=43-207.
DR PDB; 3RCF; X-ray; 1.15 A; A=43-207.
DR PDB; 3RCG; X-ray; 0.97 A; A=43-207.
DR PDB; 3RCI; X-ray; 1.44 A; X=43-207.
DR PDB; 3RCK; X-ray; 1.26 A; X=43-207.
DR PDB; 3RCL; X-ray; 1.70 A; A=43-207.
DR PDB; 3RD9; X-ray; 1.40 A; X=43-207.
DR PDB; 3RDA; X-ray; 1.07 A; X=43-207.
DR PDB; 3RDB; X-ray; 1.55 A; A=43-207.
DR PDB; 3RDC; X-ray; 1.94 A; A=43-207.
DR PDB; 4J58; X-ray; 1.28 A; A=44-207.
DR PDB; 4J59; X-ray; 1.92 A; A=44-207.
DR PDB; 4J5A; X-ray; 1.58 A; X=44-207.
DR PDB; 4J5B; X-ray; 2.01 A; A=44-207.
DR PDB; 4J5C; X-ray; 1.03 A; X=44-207.
DR PDB; 4J5D; X-ray; 1.32 A; X=44-207.
DR PDB; 4J5E; X-ray; 0.99 A; X=44-207.
DR PDB; 4O8H; X-ray; 0.85 A; A=43-207.
DR PDB; 4O8I; X-ray; 1.45 A; A=43-207.
DR PDB; 4XNC; X-ray; 2.23 A; A=44-207.
DR PDB; 4ZSC; X-ray; 1.50 A; A=44-207.
DR PDB; 4ZSD; X-ray; 1.45 A; A=44-207.
DR PDB; 5A0E; X-ray; 1.25 A; A/B=43-207.
DR PDB; 5CBT; X-ray; 1.45 A; A=44-207.
DR PDB; 5CBU; X-ray; 1.40 A; A=44-207.
DR PDB; 5CBV; X-ray; 1.80 A; A=44-207.
DR PDB; 5CBW; X-ray; 1.80 A; A=44-207.
DR PDB; 5CCN; X-ray; 1.80 A; A=44-207.
DR PDB; 5CCQ; X-ray; 1.80 A; A=44-207.
DR PDB; 5CCR; X-ray; 1.90 A; A=44-207.
DR PDB; 5CCS; X-ray; 2.10 A; X=44-207.
DR PDB; 6R8L; X-ray; 1.64 A; A=44-207.
DR PDB; 6R8O; X-ray; 1.36 A; A=44-207.
DR PDB; 6R8W; X-ray; 1.40 A; A=44-207.
DR PDB; 6R9S; X-ray; 2.00 A; A=44-207.
DR PDB; 6R9U; X-ray; 1.26 A; A=44-207.
DR PDB; 6R9X; X-ray; 1.66 A; A=44-207.
DR PDB; 6RA1; X-ray; 2.00 A; A=44-207.
DR PDB; 6Y3E; X-ray; 1.45 A; A=44-207.
DR PDB; 6YBM; X-ray; 1.41 A; A/B/C=44-207.
DR PDBsum; 2BIT; -.
DR PDBsum; 2BIU; -.
DR PDBsum; 2Z6W; -.
DR PDBsum; 3QYU; -.
DR PDBsum; 3R49; -.
DR PDBsum; 3R4G; -.
DR PDBsum; 3R54; -.
DR PDBsum; 3R56; -.
DR PDBsum; 3R57; -.
DR PDBsum; 3R59; -.
DR PDBsum; 3RCF; -.
DR PDBsum; 3RCG; -.
DR PDBsum; 3RCI; -.
DR PDBsum; 3RCK; -.
DR PDBsum; 3RCL; -.
DR PDBsum; 3RD9; -.
DR PDBsum; 3RDA; -.
DR PDBsum; 3RDB; -.
DR PDBsum; 3RDC; -.
DR PDBsum; 4J58; -.
DR PDBsum; 4J59; -.
DR PDBsum; 4J5A; -.
DR PDBsum; 4J5B; -.
DR PDBsum; 4J5C; -.
DR PDBsum; 4J5D; -.
DR PDBsum; 4J5E; -.
DR PDBsum; 4O8H; -.
DR PDBsum; 4O8I; -.
DR PDBsum; 4XNC; -.
DR PDBsum; 4ZSC; -.
DR PDBsum; 4ZSD; -.
DR PDBsum; 5A0E; -.
DR PDBsum; 5CBT; -.
DR PDBsum; 5CBU; -.
DR PDBsum; 5CBV; -.
DR PDBsum; 5CBW; -.
DR PDBsum; 5CCN; -.
DR PDBsum; 5CCQ; -.
DR PDBsum; 5CCR; -.
DR PDBsum; 5CCS; -.
DR PDBsum; 6R8L; -.
DR PDBsum; 6R8O; -.
DR PDBsum; 6R8W; -.
DR PDBsum; 6R9S; -.
DR PDBsum; 6R9U; -.
DR PDBsum; 6R9X; -.
DR PDBsum; 6RA1; -.
DR PDBsum; 6Y3E; -.
DR PDBsum; 6YBM; -.
DR AlphaFoldDB; P30405; -.
DR BMRB; P30405; -.
DR SMR; P30405; -.
DR BioGRID; 115411; 129.
DR CORUM; P30405; -.
DR IntAct; P30405; 37.
DR MINT; P30405; -.
DR STRING; 9606.ENSP00000225174; -.
DR BindingDB; P30405; -.
DR ChEMBL; CHEMBL3325306; -.
DR DrugBank; DB08168; Coumarin 120.
DR DrugBank; DB00091; Cyclosporine.
DR DrugBank; DB00172; Proline.
DR DrugBank; DB02078; Triglyme.
DR GlyGen; P30405; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30405; -.
DR PhosphoSitePlus; P30405; -.
DR SwissPalm; P30405; -.
DR BioMuta; PPIF; -.
DR DMDM; 231968; -.
DR OGP; P30405; -.
DR UCD-2DPAGE; P30405; -.
DR EPD; P30405; -.
DR jPOST; P30405; -.
DR MassIVE; P30405; -.
DR MaxQB; P30405; -.
DR PaxDb; P30405; -.
DR PeptideAtlas; P30405; -.
DR PRIDE; P30405; -.
DR ProteomicsDB; 54662; -. [P30405-1]
DR ProteomicsDB; 61549; -.
DR TopDownProteomics; P30405-1; -. [P30405-1]
DR Antibodypedia; 29865; 439 antibodies from 34 providers.
DR DNASU; 10105; -.
DR Ensembl; ENST00000225174.8; ENSP00000225174.3; ENSG00000108179.14. [P30405-1]
DR GeneID; 10105; -.
DR KEGG; hsa:10105; -.
DR MANE-Select; ENST00000225174.8; ENSP00000225174.3; NM_005729.4; NP_005720.1.
DR UCSC; uc001kai.4; human. [P30405-1]
DR CTD; 10105; -.
DR DisGeNET; 10105; -.
DR GeneCards; PPIF; -.
DR HGNC; HGNC:9259; PPIF.
DR HPA; ENSG00000108179; Low tissue specificity.
DR MIM; 604486; gene.
DR neXtProt; NX_P30405; -.
DR OpenTargets; ENSG00000108179; -.
DR PharmGKB; PA33584; -.
DR VEuPathDB; HostDB:ENSG00000108179; -.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00940000156008; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; P30405; -.
DR OMA; CKGTVVN; -.
DR PhylomeDB; P30405; -.
DR TreeFam; TF312801; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; P30405; -.
DR SignaLink; P30405; -.
DR SIGNOR; P30405; -.
DR BioGRID-ORCS; 10105; 13 hits in 1087 CRISPR screens.
DR ChiTaRS; PPIF; human.
DR EvolutionaryTrace; P30405; -.
DR GeneWiki; PPIF; -.
DR GenomeRNAi; 10105; -.
DR Pharos; P30405; Tchem.
DR PRO; PR:P30405; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P30405; protein.
DR Bgee; ENSG00000108179; Expressed in amniotic fluid and 203 other tissues.
DR ExpressionAtlas; P30405; baseline and differential.
DR Genevisible; P30405; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:1902686; P:mitochondrial outer membrane permeabilization involved in programmed cell death; IMP:UniProtKB.
DR GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISS:UniProtKB.
DR GO; GO:2000276; P:negative regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB.
DR GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; IMP:UniProtKB.
DR GO; GO:0010939; P:regulation of necrotic cell death; IEA:Ensembl.
DR GO; GO:0010849; P:regulation of proton-transporting ATPase activity, rotational mechanism; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Isomerase;
KW Mitochondrion; Necrosis; Reference proteome; Rotamase; S-nitrosylation;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..207
FT /note="Peptidyl-prolyl cis-trans isomerase F,
FT mitochondrial"
FT /id="PRO_0000025489"
FT DOMAIN 49..205
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOD_RES 67
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 67
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 86
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 167
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 175
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 190
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 203
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT VAR_SEQ 139..207
FT /note="VLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSK
FT SGRTSKKIVITDCGQLS -> WMASMLCSVTSKRAWTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056286"
FT MUTAGEN 203
FT /note="C->S: Blocks Ca(2+)-induced mPTP opening and reduces
FT hydrogen peroxide-induced cell death."
FT /evidence="ECO:0000269|PubMed:21930693"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:4O8H"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4O8H"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:4O8H"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4O8H"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4O8H"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4J5E"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2Z6W"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:4O8H"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4O8H"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:4O8H"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:4O8H"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:4O8H"
SQ 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
