Entry sw:PPIH_HUMAN

ID   PPIH_HUMAN              Reviewed;         177 AA.
AC   O43447; A6NNE7;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   18-JAN-2017, entry version 153.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE            Short=PPIase H;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase H;
DE   AltName: Full=Small nuclear ribonucleoprotein particle-specific cyclophilin H;
DE            Short=CypH;
DE   AltName: Full=U-snRNP-associated cyclophilin SnuCyp-20;
DE            Short=USA-CYP;
GN   Name=PPIH; Synonyms=CYP20, CYPH;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 154-164,
RP   AND INTERACTION WITH PRPF3; PRPF4 AND U4/U6 SNRNPS.
RC   TISSUE=Liver;
RX   PubMed=9404889;
RA   Horowitz D.S., Kobayashi R., Krainer A.R.;
RT   "A new cyclophilin and the human homologues of yeast Prp3 and Prp4
RT   form a complex associated with U4/U6 snRNPs.";
RL   RNA 3:1374-1387(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 62-67;
RP   71-81 AND 153-164, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH THE U4/U5/U6 TRI-SNRNP COMPLEX.
RC   TISSUE=Liver;
RX   PubMed=9570313;
RA   Teigelkamp S., Achsel T., Mundt C., Goethel S.-F., Cronshagen U.,
RA   Lane W.S., Marahiel M., Luehrmann R.;
RT   "The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel
RT   cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD
RT   proteins.";
RL   RNA 4:127-141(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Amygdala;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [7]
RP   FUNCTION, MUTAGENESIS OF TRP-133, AND INTERACTION WITH PRPF4 AND
RP   PRPF18.
RX   PubMed=11823439; DOI=10.1093/emboj/21.3.470;
RA   Horowitz D.S., Lee E.J., Mabon S.A., Misteli T.;
RT   "A cyclophilin functions in pre-mRNA splicing.";
RL   EMBO J. 21:470-480(2002).
RN   [8]
RP   SUBUNIT.
RX   PubMed=16723661; DOI=10.1261/rna.55406;
RA   Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT   "The network of protein-protein interactions within the human U4/U6.U5
RT   tri-snRNP.";
RL   RNA 12:1418-1430(2006).
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.,
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).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., 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   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177.
RX   PubMed=10713041; DOI=10.1074/jbc.275.11.7439;
RA   Reidt U., Reuter K., Achsel T., Ingelfinger D., Luehrmann R.,
RA   Ficner R.;
RT   "Crystal structure of the human U4/U6 small nuclear ribonucleoprotein
RT   particle-specific SnuCyp-20, a nuclear cyclophilin.";
RL   J. Biol. Chem. 275:7439-7442(2000).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4,
RP   AND FUNCTION.
RX   PubMed=12875835; DOI=10.1016/S0022-2836(03)00684-3;
RA   Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R.,
RA   Ficner R.;
RT   "Crystal structure of a complex between human spliceosomal cyclophilin
RT   H and a U4/U6 snRNP-60K peptide.";
RL   J. Mol. Biol. 331:45-56(2003).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Participates in pre-mRNA splicing. May play a role
CC       in the assembly of the U4/U5/U6 tri-snRNP complex, one of the
CC       building blocks of the spliceosome. May act as a chaperone.
CC       {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835,
CC       ECO:0000269|PubMed:9570313}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited by cyclosporin A.
CC   -!- SUBUNIT: Interacts directly with PRPF4. Part of a heteromeric
CC       complex containing PPIH, PRPF3 and PRPF4 that is stable in the
CC       absence of RNA. Component of the U4/U6-U5 tri-snRNP complex
CC       composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4,
CC       PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2,
CC       PPIH, SNU13, EFTUD2, SART1 and USP39. Heterodimer with PRPF18.
CC       {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835,
CC       ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:9404889,
CC       ECO:0000269|PubMed:9570313}.
CC   -!- INTERACTION:
CC       Q92802:N4BP2L2; NbExp=5; IntAct=EBI-1055615, EBI-2514973;
CC       Q99633:PRPF18; NbExp=4; IntAct=EBI-1055615, EBI-2798416;
CC       O43172:PRPF4; NbExp=2; IntAct=EBI-1055615, EBI-718395;
CC       P98170:XIAP; NbExp=4; IntAct=EBI-1055615, EBI-517127;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle
CC       {ECO:0000269|PubMed:9570313}. Cytoplasm
CC       {ECO:0000269|PubMed:9570313}. Note=Colocalizes with spliceosomal
CC       snRNPs. A small proportion may also be cytoplasmic.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O43447-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43447-2; Sequence=VSP_056587;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       H subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00156}.
DR   EMBL; AF016371; AAC51927.1; -; mRNA.
DR   EMBL; AF036331; AAC60793.1; -; mRNA.
DR   EMBL; AK294288; BAH11725.1; -; mRNA.
DR   EMBL; AC098484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07155.1; -; Genomic_DNA.
DR   EMBL; BC003412; AAH03412.1; -; mRNA.
DR   CCDS; CCDS469.1; -. [O43447-1]
DR   CCDS; CCDS81308.1; -. [O43447-2]
DR   RefSeq; NP_001317439.1; NM_001330510.1. [O43447-2]
DR   RefSeq; NP_006338.1; NM_006347.3. [O43447-1]
DR   RefSeq; XP_005270419.1; XM_005270362.1. [O43447-1]
DR   RefSeq; XP_016855546.1; XM_017000057.1. [O43447-1]
DR   RefSeq; XP_016855547.1; XM_017000058.1. [O43447-2]
DR   RefSeq; XP_016855548.1; XM_017000059.1. [O43447-2]
DR   UniGene; Hs.256639; -.
DR   UniGene; Hs.729213; -.
DR   PDB; 1MZW; X-ray; 2.00 A; A=1-177.
DR   PDB; 1QOI; X-ray; 2.00 A; A=1-177.
DR   PDBsum; 1MZW; -.
DR   PDBsum; 1QOI; -.
DR   ProteinModelPortal; O43447; -.
DR   SMR; O43447; -.
DR   BioGrid; 115728; 27.
DR   IntAct; O43447; 18.
DR   MINT; MINT-270606; -.
DR   STRING; 9606.ENSP00000306614; -.
DR   BindingDB; O43447; -.
DR   DrugBank; DB00172; L-Proline.
DR   iPTMnet; O43447; -.
DR   PhosphoSitePlus; O43447; -.
DR   BioMuta; PPIH; -.
DR   EPD; O43447; -.
DR   PaxDb; O43447; -.
DR   PeptideAtlas; O43447; -.
DR   PRIDE; O43447; -.
DR   DNASU; 10465; -.
DR   Ensembl; ENST00000304979; ENSP00000306614; ENSG00000171960. [O43447-1]
DR   Ensembl; ENST00000372550; ENSP00000361630; ENSG00000171960. [O43447-2]
DR   GeneID; 10465; -.
DR   KEGG; hsa:10465; -.
DR   UCSC; uc009vwl.3; human. [O43447-1]
DR   CTD; 10465; -.
DR   GeneCards; PPIH; -.
DR   HGNC; HGNC:14651; PPIH.
DR   HPA; HPA059019; -.
DR   MIM; 606095; gene.
DR   neXtProt; NX_O43447; -.
DR   OpenTargets; ENSG00000171960; -.
DR   PharmGKB; PA33586; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   eggNOG; COG0652; LUCA.
DR   GeneTree; ENSGT00760000119072; -.
DR   HOGENOM; HOG000065981; -.
DR   HOVERGEN; HBG001065; -.
DR   InParanoid; O43447; -.
DR   KO; K09567; -.
DR   OMA; PTWNQIQ; -.
DR   OrthoDB; EOG091G0BGL; -.
DR   PhylomeDB; O43447; -.
DR   TreeFam; TF312958; -.
DR   BioCyc; ZFISH:HS10424-MONOMER; -.
DR   BRENDA; 5.2.1.8; 2681.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   ChiTaRS; PPIH; human.
DR   EvolutionaryTrace; O43447; -.
DR   GeneWiki; PPIH; -.
DR   GenomeRNAi; 10465; -.
DR   PRO; PR:O43447; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000171960; -.
DR   CleanEx; HS_PPIH; -.
DR   ExpressionAtlas; O43447; baseline and differential.
DR   Genevisible; O43447; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005681; C:spliceosomal complex; IC:BHF-UCL.
DR   GO; GO:0071001; C:U4/U6 snRNP; IDA:BHF-UCL.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:BHF-UCL.
DR   GO; GO:0016018; F:cyclosporin A binding; TAS:ProtInc.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:BHF-UCL.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR   GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR   GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PTHR11071; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 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; Chaperone;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; Isomerase;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Rotamase;
KW   Spliceosome.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378,
FT                                ECO:0000244|PubMed:25944712}.
FT   CHAIN         2    177       Peptidyl-prolyl cis-trans isomerase H.
FT                                /FTId=PRO_0000064162.
FT   DOMAIN       14    176       PPIase cyclophilin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00156}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22814378,
FT                                ECO:0000244|PubMed:25944712}.
FT   VAR_SEQ       1     51       MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAE
FT                                NFRQFCTGEF -> MIAGDSDR (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056587.
FT   MUTAGEN     133    133       W->F: Abolishes inhibition by cyclosporin
FT                                A. {ECO:0000269|PubMed:11823439}.
FT   STRAND       12     19       {ECO:0000244|PDB:1MZW}.
FT   STRAND       22     31       {ECO:0000244|PDB:1MZW}.
FT   TURN         33     35       {ECO:0000244|PDB:1MZW}.
FT   HELIX        37     48       {ECO:0000244|PDB:1MZW}.
FT   STRAND       67     69       {ECO:0000244|PDB:1MZW}.
FT   TURN         70     72       {ECO:0000244|PDB:1MZW}.
FT   STRAND       73     76       {ECO:0000244|PDB:1MZW}.
FT   TURN         79     81       {ECO:0000244|PDB:1MZW}.
FT   STRAND       82     84       {ECO:0000244|PDB:1MZW}.
FT   STRAND      109    112       {ECO:0000244|PDB:1MZW}.
FT   STRAND      124    129       {ECO:0000244|PDB:1MZW}.
FT   HELIX       132    134       {ECO:0000244|PDB:1MZW}.
FT   TURN        135    137       {ECO:0000244|PDB:1MZW}.
FT   STRAND      140    146       {ECO:0000244|PDB:1MZW}.
FT   HELIX       148    155       {ECO:0000244|PDB:1MZW}.
FT   HELIX       161    163       {ECO:0000244|PDB:1MZW}.
FT   STRAND      165    167       {ECO:0000244|PDB:1MZW}.
FT   STRAND      169    176       {ECO:0000244|PDB:1MZW}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        14    176       iprf:CSA_PPIASE_2 [T]
FT   MYHIT        21    175       ipfam:Pro_isomerase [T]
FT   MYHIT        60     77       ipat:CSA_PPIASE_1 [T]
SQ   SEQUENCE   177 AA;  19208 MW;  566BCE6361E0F339 CRC64;
     MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE FRKDGVPIGY
     KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN
     GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM
//