ID   PPIF_HUMAN              Reviewed;         207 AA.
AC   P30405; Q5W131;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-JAN-2012, entry version 111.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase F, mitochondrial;
DE            Short=PPIase F;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin F;
DE   AltName: Full=Rotamase F;
DE   Flags: Precursor;
GN   Name=PPIF; Synonyms=CYP3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92078192; PubMed=1744118;
RA   Bergsma D.J., Eder C., Gross M., Kersten H., Sylvester D.,
RA   Appelbaum E., Cusimano D., Livi G.P., McLauglin M.M., Kasyan K.,
RA   Porter T.G., Silverman C., Dunnington D., Hand A., Prichett W.P.,
RA   Bossard M.J., 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 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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [5]
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.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR   EMBL; M80254; AAA58434.1; -; mRNA.
DR   EMBL; AL133481; CAH72725.1; -; Genomic_DNA.
DR   EMBL; AL391665; CAH72725.1; JOINED; Genomic_DNA.
DR   EMBL; AL391665; CAI40994.1; -; Genomic_DNA.
DR   EMBL; AL133481; CAI40994.1; JOINED; Genomic_DNA.
DR   EMBL; BC005020; AAH05020.1; -; mRNA.
DR   IPI; IPI00026519; -.
DR   PIR; A41581; A41581.
DR   RefSeq; NP_005720.1; NM_005729.3.
DR   UniGene; Hs.381072; -.
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   PDBsum; 2BIT; -.
DR   PDBsum; 2BIU; -.
DR   PDBsum; 2Z6W; -.
DR   PDBsum; 3QYU; -.
DR   ProteinModelPortal; P30405; -.
DR   SMR; P30405; 44-207.
DR   STRING; P30405; -.
DR   PhosphoSite; P30405; -.
DR   DMDM; 231968; -.
DR   OGP; P30405; -.
DR   UCD-2DPAGE; P30405; -.
DR   PeptideAtlas; P30405; -.
DR   PRIDE; P30405; -.
DR   Ensembl; ENST00000225174; ENSP00000225174; ENSG00000108179.
DR   GeneID; 10105; -.
DR   KEGG; hsa:10105; -.
DR   UCSC; uc001kai.1; human.
DR   CTD; 10105; -.
DR   GeneCards; GC10P081107; -.
DR   H-InvDB; HIX0008969; -.
DR   HGNC; HGNC:9259; PPIF.
DR   MIM; 604486; gene.
DR   neXtProt; NX_P30405; -.
DR   PharmGKB; PA33584; -.
DR   eggNOG; prNOG05846; -.
DR   GeneTree; ENSGT00530000062909; -.
DR   HOGENOM; HBG610621; -.
DR   HOVERGEN; HBG001065; -.
DR   InParanoid; P30405; -.
DR   OMA; RACSKGA; -.
DR   OrthoDB; EOG4DJJXN; -.
DR   PhylomeDB; P30405; -.
DR   DrugBank; DB01093; Dimethyl sulfoxide.
DR   DrugBank; DB00172; L-Proline.
DR   NextBio; 38221; -.
DR   ArrayExpress; P30405; -.
DR   Bgee; P30405; -.
DR   CleanEx; HS_PPIF; -.
DR   Genevestigator; P30405; -.
DR   GermOnline; ENSG00000108179; Homo sapiens.
DR   GO; GO:0005624; C:membrane fraction; TAS:ProtInc.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   KO; K09565; -.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; CSA_PPIase; 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; Complete proteome; Cyclosporin; Isomerase;
KW   Mitochondrion; Reference proteome; Rotamase; Transit peptide.
FT   TRANSIT       1     29       Mitochondrion (Potential).
FT   CHAIN        30    207       Peptidyl-prolyl cis-trans isomerase F,
FT                                mitochondrial.
FT                                /FTId=PRO_0000025489.
FT   DOMAIN       49    205       PPIase cyclophilin-type.
FT   MOD_RES     167    167       N6-acetyllysine.
FT   STRAND       47     54
FT   STRAND       57     66
FT   TURN         68     70
FT   HELIX        72     83
FT   TURN         84     86
FT   STRAND       94     99
FT   TURN        100    102
FT   STRAND      103    106
FT   TURN        109    111
FT   STRAND      112    115
FT   STRAND      139    142
FT   STRAND      154    159
FT   HELIX       162    164
FT   TURN        165    167
FT   STRAND      170    176
FT   HELIX       178    186
FT   STRAND      198    205
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
//