PPID_HUMAN
ID PPID_HUMAN Reviewed; 370 AA.
AC Q08752; B2R9V2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000305|PubMed:11350175, ECO:0000305|PubMed:20676357};
DE Short=PPIase D {ECO:0000305|PubMed:11350175, ECO:0000305|PubMed:20676357};
DE EC=5.2.1.8 {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:20676357};
DE AltName: Full=40 kDa peptidyl-prolyl cis-trans isomerase;
DE AltName: Full=Cyclophilin-40 {ECO:0000303|PubMed:8509368};
DE Short=CYP-40 {ECO:0000303|PubMed:8509368};
DE AltName: Full=Cyclophilin-related protein;
DE AltName: Full=Rotamase D {ECO:0000305|PubMed:11350175, ECO:0000305|PubMed:20676357};
GN Name=PPID {ECO:0000312|HGNC:HGNC:9257}; Synonyms=CYP40, CYPD;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Pancreas;
RX PubMed=8509368; DOI=10.1016/s0021-9258(18)31389-9;
RA Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E.,
RA Bayney R.M.;
RT "Cyclophilin-40, a protein with homology to the P59 component of the
RT steroid receptor complex. Cloning of the cDNA and further
RT characterization.";
RL J. Biol. Chem. 268:12303-12310(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8812478; DOI=10.1006/geno.1996.0384;
RA Yokoi H., Shimizu Y., Anazawa H., Lefebvre C.A., Korneluk R.G., Ikeda J.E.;
RT "The structure and complete nucleotide sequence of the human cyclophilin 40
RT (PPID) gene.";
RL Genomics 35:448-455(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-49; ILE-302 AND
RP GLU-335.
RG NIEHS SNPs program;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 2-17.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH MYB.
RX PubMed=9659917; DOI=10.1016/s1097-2765(00)80021-0;
RA Leverson J.D., Ness S.A.;
RT "Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative
RT regulatory mechanism.";
RL Mol. Cell 1:203-211(1998).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11525244; DOI=10.1379/1466-1268(2001)006<0059:hciahs>2.0.co;2;
RA Mark P.J., Ward B.K., Kumar P., Lahooti H., Minchin R.F., Ratajczak T.;
RT "Human cyclophilin 40 is a heat shock protein that exhibits altered
RT intracellular localization following heat shock.";
RL Cell Stress Chaperones 6:59-70(2001).
RN [10]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX PubMed=11350175; DOI=10.1006/jmbi.2001.4595;
RA Pirkl F., Buchner J.;
RT "Functional analysis of the Hsp90-associated human peptidyl prolyl
RT cis/trans isomerases FKBP51, FKBP52 and Cyp40.";
RL J. Mol. Biol. 308:795-806(2001).
RN [11]
RP INTERACTION WITH HSP90AB1, AND MUTAGENESIS OF LYS-227; ASN-231; PHE-234;
RP SER-274; ASN-278; LEU-284; LYS-285; LYS-308; ARG-312 AND ASP-329.
RX PubMed=12145316; DOI=10.1074/jbc.m207097200;
RA Ward B.K., Allan R.K., Mok D., Temple S.E., Taylor P., Dornan J.,
RA Mark P.J., Shaw D.J., Kumar P., Walkinshaw M.D., Ratajczak T.;
RT "A structure-based mutational analysis of cyclophilin 40 identifies key
RT residues in the core tetratricopeptide repeat domain that mediate binding
RT to Hsp90.";
RL J. Biol. Chem. 277:40799-40809(2002).
RN [12]
RP IDENTIFICATION IN HSP90 COMPLEXES.
RX PubMed=14580201; DOI=10.1021/bi035001t;
RA Scroggins B.T., Prince T., Shao J., Uma S., Huang W., Guo Y., Yun B.G.,
RA Hedman K., Matts R.L., Hartson S.D.;
RT "High affinity binding of Hsp90 is triggered by multiple discrete segments
RT of its kinase clients.";
RL Biochemistry 42:12550-12561(2003).
RN [13]
RP INTERACTION WITH HSPA8, AND MUTAGENESIS OF LYS-227; ASN-231; PHE-234;
RP SER-274; ASN-278; LEU-284; LYS-285; LYS-308 AND ARG-312.
RX PubMed=15497503; DOI=10.1379/csc-26r.1;
RA Carrello A., Allan R.K., Morgan S.L., Owen B.A., Mok D., Ward B.K.,
RA Minchin R.F., Toft D.O., Ratajczak T.;
RT "Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.";
RL Cell Stress Chaperones 9:167-181(2004).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18708059; DOI=10.1016/j.febslet.2008.08.007;
RA Luu T.C., Bhattacharya P., Chan W.K.;
RT "Cyclophilin-40 has a cellular role in the aryl hydrocarbon receptor
RT signaling.";
RL FEBS Lett. 582:3167-3173(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
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 [18]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=19932913; DOI=10.1016/j.virol.2009.10.043;
RA Gaither L.A., Borawski J., Anderson L.J., Balabanis K.A., Devay P.,
RA Joberty G., Rau C., Schirle M., Bouwmeester T., Mickanin C., Zhao S.,
RA Vickers C., Lee L., Deng G., Baryza J., Fujimoto R.A., Lin K., Compton T.,
RA Wiedmann B.;
RT "Multiple cyclophilins involved in different cellular pathways mediate HCV
RT replication.";
RL Virology 397:43-55(2010).
RN [19]
RP INTERACTION WITH ILF2; XRCC6; RACK1 AND RPS3.
RX PubMed=21146485; DOI=10.1016/j.ab.2010.12.007;
RA Park M.S., Chu F., Xie J., Wang Y., Bhattacharya P., Chan W.K.;
RT "Identification of cyclophilin-40-interacting proteins reveals potential
RT cellular function of cyclophilin-40.";
RL Anal. Biochem. 410:257-265(2011).
RN [20]
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 [21]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21711559; DOI=10.1186/1743-422x-8-329;
RA Anderson L.J., Lin K., Compton T., Wiedmann B.;
RT "Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C
RT virus secretion.";
RL Virol. J. 8:329-329(2011).
RN [22]
RP FUNCTION.
RX PubMed=22681779; DOI=10.1186/1471-2407-12-229;
RA Pearson J.D., Mohammed Z., Bacani J.T., Lai R., Ingham R.J.;
RT "The heat shock protein-90 co-chaperone, Cyclophilin 40, promotes ALK-
RT positive, anaplastic large cell lymphoma viability and its expression is
RT regulated by the NPM-ALK oncoprotein.";
RL BMC Cancer 12:229-229(2012).
RN [23]
RP FUNCTION.
RX PubMed=23220213; DOI=10.1016/j.yexcr.2012.11.016;
RA Jandova J., Janda J., Sligh J.E.;
RT "Cyclophilin 40 alters UVA-induced apoptosis and mitochondrial ROS
RT generation in keratinocytes.";
RL Exp. Cell Res. 319:750-760(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-198, AND
RP IDENTIFICATION BY 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 [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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:11350175, PubMed:20676357). Proposed to act as a co-
CC chaperone in HSP90 complexes such as in unligated steroid receptors
CC heterocomplexes. Different co-chaperones seem to compete for
CC association with HSP90 thus establishing distinct HSP90-co-chaperone-
CC receptor complexes with the potential to exert tissue-specific receptor
CC activity control. May have a preference for estrogen receptor complexes
CC and is not found in glucocorticoid receptor complexes. May be involved
CC in cytoplasmic dynein-dependent movement of the receptor from the
CC cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-
CC binding activity. Involved in regulation of AHR signaling by promoting
CC the formation of the AHR:ARNT dimer; the function is independent of
CC HSP90 but requires the chaperone activity. Involved in regulation of UV
CC radiation-induced apoptosis. Promotes cell viability in anaplastic
CC lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL)
CC cell lines. {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:18708059,
CC ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22681779,
CC ECO:0000269|PubMed:23220213, ECO:0000269|PubMed:9659917}.
CC -!- FUNCTION: (Microbial infection) May be involved in hepatitis C virus
CC (HCV) replication and release. {ECO:0000269|PubMed:19932913,
CC ECO:0000269|PubMed:21711559}.
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; Evidence={ECO:0000269|PubMed:11350175,
CC ECO:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Less sensitive to inhibition by cyclosporin A than
CC is CYP-18. {ECO:0000269|PubMed:20676357}.
CC -!- SUBUNIT: Identified in ESR1 or NR3C1/GCR steroid receptor-chaperone
CC complexes. Found in HSP90 chaperone complexes with kinase clients LCK
CC or EIF2AK1. Two monomers associate with one HSP90 homodimer. Interacts
CC with HSP90AA1. Interacts with HSP90AB1; PPID and FKBP4 compete for
CC binding to HSP90AB1 and the interaction is mutually exclusive with the
CC PPID:HSPA8 interaction. Interacts with HSPA8; PPID and STIP1 but not
CC FKBP4 compete for binding to HSPA8 and the interaction is mutually
CC exclusive with the PPID:HSP90AB1 interaction. Interacts with S100A1 and
CC S100A2; the interactions dissociate the PPID:HSP90AA1 interaction.
CC Interacts with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3.
CC Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or
CC DYNC1I2). {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:12145316,
CC ECO:0000269|PubMed:14580201, ECO:0000269|PubMed:15497503,
CC ECO:0000269|PubMed:21146485, ECO:0000269|PubMed:9659917}.
CC -!- INTERACTION:
CC Q08752; PRO_0000000092 [P05067]: APP; NbExp=4; IntAct=EBI-716596, EBI-821758;
CC Q08752; PRO_0000000093 [P05067]: APP; NbExp=2; IntAct=EBI-716596, EBI-2431589;
CC Q08752; P48047: ATP5PO; NbExp=3; IntAct=EBI-716596, EBI-355815;
CC Q08752; Q12905: ILF2; NbExp=4; IntAct=EBI-716596, EBI-357925;
CC Q08752; P63244: RACK1; NbExp=4; IntAct=EBI-716596, EBI-296739;
CC Q08752; P23396: RPS3; NbExp=4; IntAct=EBI-716596, EBI-351193;
CC Q08752; P12956: XRCC6; NbExp=4; IntAct=EBI-716596, EBI-353208;
CC Q08752; P01103: MYB; Xeno; NbExp=2; IntAct=EBI-716596, EBI-6502562;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11525244,
CC ECO:0000269|PubMed:18708059}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein should not be confused with mitochondrial
CC peptidyl-prolyl cis-trans isomerase F (PPIF) which is often referred to
CC as cyclophilin D or CypD. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ppid/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry;
CC URL="https://en.wikipedia.org/wiki/Cyclophilin";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L11667; AAA35731.1; -; mRNA.
DR EMBL; D63861; BAA09923.1; -; Genomic_DNA.
DR EMBL; AY714221; AAT97986.1; -; Genomic_DNA.
DR EMBL; AK313929; BAG36649.1; -; mRNA.
DR EMBL; CH471056; EAX04853.1; -; Genomic_DNA.
DR EMBL; BC030707; AAH30707.1; -; mRNA.
DR CCDS; CCDS3801.1; -.
DR PIR; A45981; A45981.
DR RefSeq; NP_005029.1; NM_005038.2.
DR AlphaFoldDB; Q08752; -.
DR SMR; Q08752; -.
DR BioGRID; 111477; 88.
DR DIP; DIP-34893N; -.
DR IntAct; Q08752; 40.
DR MINT; Q08752; -.
DR STRING; 9606.ENSP00000303754; -.
DR BindingDB; Q08752; -.
DR ChEMBL; CHEMBL1697657; -.
DR DrugCentral; Q08752; -.
DR GuidetoPHARMACOLOGY; 3179; -.
DR GlyGen; Q08752; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08752; -.
DR MetOSite; Q08752; -.
DR PhosphoSitePlus; Q08752; -.
DR BioMuta; PPID; -.
DR DMDM; 729274; -.
DR REPRODUCTION-2DPAGE; IPI00003927; -.
DR EPD; Q08752; -.
DR jPOST; Q08752; -.
DR MassIVE; Q08752; -.
DR MaxQB; Q08752; -.
DR PaxDb; Q08752; -.
DR PeptideAtlas; Q08752; -.
DR PRIDE; Q08752; -.
DR ProteomicsDB; 58647; -.
DR Antibodypedia; 16935; 371 antibodies from 37 providers.
DR DNASU; 5481; -.
DR Ensembl; ENST00000307720.4; ENSP00000303754.3; ENSG00000171497.5.
DR GeneID; 5481; -.
DR KEGG; hsa:5481; -.
DR MANE-Select; ENST00000307720.4; ENSP00000303754.3; NM_005038.3; NP_005029.1.
DR UCSC; uc003iqc.4; human.
DR CTD; 5481; -.
DR DisGeNET; 5481; -.
DR GeneCards; PPID; -.
DR HGNC; HGNC:9257; PPID.
DR HPA; ENSG00000171497; Low tissue specificity.
DR MIM; 601753; gene.
DR neXtProt; NX_Q08752; -.
DR OpenTargets; ENSG00000171497; -.
DR PharmGKB; PA33582; -.
DR VEuPathDB; HostDB:ENSG00000171497; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000154672; -.
DR HOGENOM; CLU_012062_37_1_1; -.
DR InParanoid; Q08752; -.
DR OMA; CKDFGNK; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q08752; -.
DR TreeFam; TF324493; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; Q08752; -.
DR Reactome; R-HSA-8939211; ESR-mediated signaling.
DR SignaLink; Q08752; -.
DR BioGRID-ORCS; 5481; 15 hits in 1079 CRISPR screens.
DR ChiTaRS; PPID; human.
DR GeneWiki; PPID; -.
DR GenomeRNAi; 5481; -.
DR Pharos; Q08752; Tchem.
DR PRO; PR:Q08752; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q08752; protein.
DR Bgee; ENSG00000171497; Expressed in right lobe of liver and 203 other tissues.
DR ExpressionAtlas; Q08752; baseline and differential.
DR Genevisible; Q08752; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071492; P:cellular response to UV-A; IMP:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; TAS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF13176; TPR_7; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Chaperone; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Isomerase; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Rotamase; TPR repeat;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..370
FT /note="Peptidyl-prolyl cis-trans isomerase D"
FT /id="PRO_0000064153"
FT DOMAIN 19..183
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 223..256
FT /note="TPR 1"
FT REPEAT 273..306
FT /note="TPR 2"
FT REPEAT 307..340
FT /note="TPR 3"
FT REGION 185..215
FT /note="Chaperone activity"
FT /evidence="ECO:0000250"
FT REGION 214..370
FT /note="Interaction with HSP90AB1"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR16"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VARIANT 49
FT /note="R -> C (in dbSNP:rs2070631)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_021021"
FT VARIANT 196
FT /note="D -> V (in dbSNP:rs2230222)"
FT /id="VAR_051771"
FT VARIANT 302
FT /note="L -> I (in dbSNP:rs9410)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_021022"
FT VARIANT 335
FT /note="G -> E (in dbSNP:rs17843956)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_021023"
FT MUTAGEN 227
FT /note="K->A: Abolishes interaction with HSP90AB1 and
FT impairs interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 231
FT /note="N->A: Abolishes interaction with HSP90AB1 and
FT impairs interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 234
FT /note="F->A: Impairs interaction with HSP90AB1 and HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 274
FT /note="S->L: Impairs interaction with HSP90AB1 and HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 278
FT /note="N->A: Abolishes interaction with HSP90AB1."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 284
FT /note="L->A: Impairs interaction with HSP90AB1 and HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 285
FT /note="K->A: Impairs interaction with HSP90AB1 and HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 308
FT /note="K->A: Abolishes interaction with HSP90AB1 and
FT impairs interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 312
FT /note="R->A: Abolishes interaction with HSP90AB1 and
FT impairs interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12145316,
FT ECO:0000269|PubMed:15497503"
FT MUTAGEN 329
FT /note="D->A: Impairs interaction with HSP90AB1."
FT /evidence="ECO:0000269|PubMed:12145316"
SQ SEQUENCE 370 AA; 40764 MW; 39D4100748B35D48 CRC64;
MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGH
TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSM
ANAGRNTNGS QFFITTVPTP HLDGKHVVFG QVIKGIGVAR ILENVEVKGE KPAKLCVIAE
CGELKEGDDG GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LITEDLKNIG NTFFKSQNWE
MAIKKYAEVL RYVDSSKAVI ETADRAKLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL
ELDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQGIAPED KAIQAELLKV KQKIKAQKDK
EKAVYAKMFA
