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Database: UniProt
Entry: Q9Y3C6
LinkDB: Q9Y3C6
Original site: Q9Y3C6 
ID   PPIL1_HUMAN             Reviewed;         166 AA.
AC   Q9Y3C6; O15001; Q5TDC9;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   29-SEP-2021, entry version 193.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 1;
DE            Short=PPIase;
DE            EC=5.2.1.8 {ECO:0000269|PubMed:16595688};
DE   AltName: Full=Rotamase PPIL1;
GN   Name=PPIL1; Synonyms=CYPL1; ORFNames=CGI-124, UNQ2425/PRO4984;
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].
RC   TISSUE=Fetal brain;
RX   PubMed=8978786; DOI=10.1159/000134199;
RA   Ozaki K., Fujiwara T., Kawai A., Shimizu F., Takami S., Okuno S.,
RA   Takeda S., Shimada Y., Nagata M., Watanabe T., Takaichi A., Takahashi E.,
RA   Nakamura Y., Shin S.;
RT   "Cloning, expression and chromosomal mapping of a novel cyclophilin-related
RT   gene (PPIL1) from human fetal brain.";
RL   Cytogenet. Cell Genet. 72:242-245(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph;
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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, ACTIVITY REGULATION,
RP   CYCLOSPORIN A BINDING, INTERACTION WITH SNW1, AND STRUCTURE BY NMR.
RX   PubMed=16595688; DOI=10.1074/jbc.m511155200;
RA   Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y., Huang Q.,
RA   Zhang Q.;
RT   "Solution structure of human peptidyl prolyl isomerase-like protein 1 and
RT   insights into its interaction with SKIP.";
RL   J. Biol. Chem. 281:15900-15908(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP   COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11991638; DOI=10.1017/s1355838202021088;
RA   Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT   "Purification and characterization of native spliceosomes suitable for
RT   three-dimensional structural analysis.";
RL   RNA 8:426-439(2002).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), AND INTERACTION WITH SNW1.
RX   PubMed=20368803; DOI=10.1371/journal.pone.0010013;
RA   Stegmann C.M., Luhrmann R., Wahl M.C.;
RT   "The crystal structure of PPIL1 bound to cyclosporine A suggests a binding
RT   mode for a linear epitope of the SKIP protein.";
RL   PLoS ONE 5:E10013-E10013(2010).
RN   [12] {ECO:0007744|PDB:5XJC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA   Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT   "An Atomic Structure of the Human Spliceosome.";
RL   Cell 169:918-929(2017).
RN   [13] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28076346; DOI=10.1038/nature21079;
RA   Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA   Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT   "Cryo-EM structure of a human spliceosome activated for step 2 of
RT   splicing.";
RL   Nature 542:318-323(2017).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC       (PubMed:11991638, PubMed:28502770, PubMed:28076346). PPIases accelerate
CC       the folding of proteins. It catalyzes the cis-trans isomerization of
CC       proline imidic peptide bonds in oligopeptides (PubMed:16595688).
CC       {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16595688,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
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:16595688};
CC   -!- ACTIVITY REGULATION: Inhibited by Cyclosporin A.
CC       {ECO:0000269|PubMed:16595688}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=230 uM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
CC         {ECO:0000269|PubMed:16595688};
CC   -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
CC       PubMed:28502770, PubMed:28076346). Interacts with SNW1
CC       (PubMed:16595688, PubMed:20368803). {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:16595688, ECO:0000269|PubMed:20368803,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC   -!- INTERACTION:
CC       Q9Y3C6; Q9UMD9: COL17A1; NbExp=3; IntAct=EBI-2557649, EBI-2528742;
CC       Q9Y3C6; Q16630: CPSF6; NbExp=3; IntAct=EBI-2557649, EBI-358410;
CC       Q9Y3C6; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-2557649, EBI-742054;
CC       Q9Y3C6; Q5T749: KPRP; NbExp=3; IntAct=EBI-2557649, EBI-10981970;
CC       Q9Y3C6; P50458: LHX2; NbExp=3; IntAct=EBI-2557649, EBI-12179869;
CC       Q9Y3C6; Q92802: N4BP2L2; NbExp=3; IntAct=EBI-2557649, EBI-2514973;
CC       Q9Y3C6; P78424: POU6F2; NbExp=3; IntAct=EBI-2557649, EBI-12029004;
CC       Q9Y3C6; P0CG20: PRR35; NbExp=3; IntAct=EBI-2557649, EBI-11986293;
CC       Q9Y3C6; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-2557649, EBI-10182375;
CC       Q9Y3C6; Q13573: SNW1; NbExp=15; IntAct=EBI-2557649, EBI-632715;
CC       Q9Y3C6; A6NLX3: SPDYE4; NbExp=3; IntAct=EBI-2557649, EBI-12047907;
CC       Q9Y3C6; P15884: TCF4; NbExp=3; IntAct=EBI-2557649, EBI-533224;
CC       Q9Y3C6; P15884-3: TCF4; NbExp=3; IntAct=EBI-2557649, EBI-13636688;
CC       Q9Y3C6; Q9BRX9: WDR83; NbExp=2; IntAct=EBI-2557649, EBI-7705033;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with the most abundant expression in
CC       heart and skeletal muscle.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF151882; AAD34119.1; -; mRNA.
DR   EMBL; AY359032; AAQ89391.1; -; mRNA.
DR   EMBL; Z85996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL122034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03916.1; -; Genomic_DNA.
DR   EMBL; BC003048; AAH03048.1; -; mRNA.
DR   CCDS; CCDS4826.1; -.
DR   RefSeq; NP_057143.1; NM_016059.4.
DR   PDB; 1XWN; NMR; -; A=1-166.
DR   PDB; 2K7N; NMR; -; A=1-166.
DR   PDB; 2X7K; X-ray; 1.15 A; A=1-166.
DR   PDB; 5MQF; EM; 5.90 A; V=1-166.
DR   PDB; 5XJC; EM; 3.60 A; S=1-166.
DR   PDB; 5YZG; EM; 4.10 A; S=1-166.
DR   PDB; 5Z56; EM; 5.10 A; S=1-166.
DR   PDB; 5Z57; EM; 6.50 A; S=1-166.
DR   PDB; 6FF4; EM; 16.00 A; V=1-166.
DR   PDB; 6FF7; EM; 4.50 A; V=1-166.
DR   PDB; 6ICZ; EM; 3.00 A; S=1-166.
DR   PDB; 6ID0; EM; 2.90 A; S=1-166.
DR   PDB; 6ID1; EM; 2.86 A; S=1-166.
DR   PDB; 6QDV; EM; 3.30 A; i=3-164.
DR   PDB; 6ZYM; EM; 3.40 A; V=1-166.
DR   PDBsum; 1XWN; -.
DR   PDBsum; 2K7N; -.
DR   PDBsum; 2X7K; -.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5XJC; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 6FF4; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 6QDV; -.
DR   PDBsum; 6ZYM; -.
DR   BMRB; Q9Y3C6; -.
DR   SMR; Q9Y3C6; -.
DR   BioGRID; 119654; 59.
DR   CORUM; Q9Y3C6; -.
DR   IntAct; Q9Y3C6; 35.
DR   STRING; 9606.ENSP00000362803; -.
DR   BindingDB; Q9Y3C6; -.
DR   GlyGen; Q9Y3C6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y3C6; -.
DR   MetOSite; Q9Y3C6; -.
DR   PhosphoSitePlus; Q9Y3C6; -.
DR   SwissPalm; Q9Y3C6; -.
DR   BioMuta; PPIL1; -.
DR   DMDM; 20177874; -.
DR   EPD; Q9Y3C6; -.
DR   jPOST; Q9Y3C6; -.
DR   MassIVE; Q9Y3C6; -.
DR   MaxQB; Q9Y3C6; -.
DR   PaxDb; Q9Y3C6; -.
DR   PeptideAtlas; Q9Y3C6; -.
DR   PRIDE; Q9Y3C6; -.
DR   ProteomicsDB; 86015; -.
DR   Antibodypedia; 29729; 266 antibodies.
DR   DNASU; 51645; -.
DR   Ensembl; ENST00000373699; ENSP00000362803; ENSG00000137168.
DR   GeneID; 51645; -.
DR   KEGG; hsa:51645; -.
DR   UCSC; uc003omu.3; human.
DR   CTD; 51645; -.
DR   DisGeNET; 51645; -.
DR   GeneCards; PPIL1; -.
DR   HGNC; HGNC:9260; PPIL1.
DR   HPA; ENSG00000137168; Low tissue specificity.
DR   MIM; 601301; gene.
DR   neXtProt; NX_Q9Y3C6; -.
DR   OpenTargets; ENSG00000137168; -.
DR   PharmGKB; PA33587; -.
DR   VEuPathDB; HostDB:ENSG00000137168; -.
DR   eggNOG; KOG0881; Eukaryota.
DR   GeneTree; ENSGT00940000153189; -.
DR   HOGENOM; CLU_012062_16_3_1; -.
DR   InParanoid; Q9Y3C6; -.
DR   OMA; PTPYLDN; -.
DR   PhylomeDB; Q9Y3C6; -.
DR   TreeFam; TF300200; -.
DR   BRENDA; 5.2.1.8; 2681.
DR   PathwayCommons; Q9Y3C6; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SABIO-RK; Q9Y3C6; -.
DR   BioGRID-ORCS; 51645; 516 hits in 1033 CRISPR screens.
DR   ChiTaRS; PPIL1; human.
DR   EvolutionaryTrace; Q9Y3C6; -.
DR   GeneWiki; PPIL1; -.
DR   GenomeRNAi; 51645; -.
DR   Pharos; Q9Y3C6; Tbio.
DR   PRO; PR:Q9Y3C6; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9Y3C6; protein.
DR   Bgee; ENSG00000137168; Expressed in heart right ventricle and 211 other tissues.
DR   ExpressionAtlas; Q9Y3C6; baseline and differential.
DR   Genevisible; Q9Y3C6; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 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; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Rotamase; Spliceosome.
FT   CHAIN           1..166
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 1"
FT                   /id="PRO_0000064164"
FT   DOMAIN          10..164
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          54..65
FT                   /note="Cyclosporin A binding"
FT                   /evidence="ECO:0000305|PubMed:16595688"
FT   REGION          70..71
FT                   /note="Cyclosporin A binding"
FT                   /evidence="ECO:0000305|PubMed:16595688"
FT   REGION          99..104
FT                   /note="Cyclosporin A binding"
FT                   /evidence="ECO:0000305|PubMed:16595688"
FT   REGION          109..113
FT                   /note="Cyclosporin A binding"
FT                   /evidence="ECO:0000305|PubMed:16595688"
FT   BINDING         119
FT                   /note="Cyclosporin A"
FT                   /evidence="ECO:0000305|PubMed:16595688"
FT   BINDING         125
FT                   /note="Cyclosporin A"
FT                   /evidence="ECO:0000305|PubMed:16595688"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         36
FT                   /note="C -> S (in dbSNP:rs12194408)"
FT                   /id="VAR_051772"
FT   STRAND          12..18
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          21..27
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   HELIX           33..45
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   TURN            46..50
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   TURN            123..125
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   HELIX           136..142
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:1XWN"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:2X7K"
FT   STRAND          158..164
FT                   /evidence="ECO:0007829|PDB:2X7K"
SQ   SEQUENCE   166 AA;  18237 MW;  2872DC3336CD05E4 CRC64;
     MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF
     MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ
     WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSG
//
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