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Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Cyclophilin-related protein) (Rotamase D)

 PPID_HUMAN              Reviewed;         370 AA.
Q08752; B2R9V2;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 173.
RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
Short=PPIase D;
EC=5.2.1.8 {ECO:0000269|PubMed:11350175};
AltName: Full=40 kDa peptidyl-prolyl cis-trans isomerase;
AltName: Full=Cyclophilin-40;
Short=CYP-40;
AltName: Full=Cyclophilin-related protein;
AltName: Full=Rotamase D;
Name=PPID; Synonyms=CYP40, CYPD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Pancreas;
PubMed=8509368;
Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E.,
Bayney R.M.;
"Cyclophilin-40, a protein with homology to the P59 component of the
steroid receptor complex. Cloning of the cDNA and further
characterization.";
J. Biol. Chem. 268:12303-12310(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8812478; DOI=10.1006/geno.1996.0384;
Yokoi H., Shimizu Y., Anazawa H., Lefebvre C.A., Korneluk R.G.,
Ikeda J.E.;
"The structure and complete nucleotide sequence of the human
cyclophilin 40 (PPID) gene.";
Genomics 35:448-455(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-49; ILE-302 AND
GLU-335.
NIEHS SNPs program;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-17.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
FUNCTION, AND INTERACTION WITH MYB.
PubMed=9659917; DOI=10.1016/S1097-2765(00)80021-0;
Leverson J.D., Ness S.A.;
"Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative
regulatory mechanism.";
Mol. Cell 1:203-211(1998).
[9]
SUBCELLULAR LOCATION.
PubMed=11525244; DOI=10.1379/1466-1268(2001)006<0059:HCIAHS>2.0.CO;2;
Mark P.J., Ward B.K., Kumar P., Lahooti H., Minchin R.F.,
Ratajczak T.;
"Human cyclophilin 40 is a heat shock protein that exhibits altered
intracellular localization following heat shock.";
Cell Stress Chaperones 6:59-70(2001).
[10]
CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
PubMed=11350175; DOI=10.1006/jmbi.2001.4595;
Pirkl F., Buchner J.;
"Functional analysis of the Hsp90-associated human peptidyl prolyl
cis/trans isomerases FKBP51, FKBP52 and Cyp40.";
J. Mol. Biol. 308:795-806(2001).
[11]
INTERACTION WITH HSP90AB1, AND MUTAGENESIS OF LYS-227; ASN-231;
PHE-234; SER-274; ASN-278; LEU-284; LYS-285; LYS-308; ARG-312 AND
ASP-329.
PubMed=12145316; DOI=10.1074/jbc.M207097200;
Ward B.K., Allan R.K., Mok D., Temple S.E., Taylor P., Dornan J.,
Mark P.J., Shaw D.J., Kumar P., Walkinshaw M.D., Ratajczak T.;
"A structure-based mutational analysis of cyclophilin 40 identifies
key residues in the core tetratricopeptide repeat domain that mediate
binding to Hsp90.";
J. Biol. Chem. 277:40799-40809(2002).
[12]
IDENTIFICATION IN HSP90 COMPLEXES.
PubMed=14580201; DOI=10.1021/bi035001t;
Scroggins B.T., Prince T., Shao J., Uma S., Huang W., Guo Y.,
Yun B.G., Hedman K., Matts R.L., Hartson S.D.;
"High affinity binding of Hsp90 is triggered by multiple discrete
segments of its kinase clients.";
Biochemistry 42:12550-12561(2003).
[13]
INTERACTION WITH HSPA8, AND MUTAGENESIS OF LYS-227; ASN-231; PHE-234;
SER-274; ASN-278; LEU-284; LYS-285; LYS-308 AND ARG-312.
PubMed=15497503; DOI=10.1379/CSC-26R.1;
Carrello A., Allan R.K., Morgan S.L., Owen B.A., Mok D., Ward B.K.,
Minchin R.F., Toft D.O., Ratajczak T.;
"Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.";
Cell Stress Chaperones 9:167-181(2004).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18708059; DOI=10.1016/j.febslet.2008.08.007;
Luu T.C., Bhattacharya P., Chan W.K.;
"Cyclophilin-40 has a cellular role in the aryl hydrocarbon receptor
signaling.";
FEBS Lett. 582:3167-3173(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
FUNCTION.
PubMed=19932913; DOI=10.1016/j.virol.2009.10.043;
Gaither L.A., Borawski J., Anderson L.J., Balabanis K.A., Devay P.,
Joberty G., Rau C., Schirle M., Bouwmeester T., Mickanin C., Zhao S.,
Vickers C., Lee L., Deng G., Baryza J., Fujimoto R.A., Lin K.,
Compton T., Wiedmann B.;
"Multiple cyclophilins involved in different cellular pathways mediate
HCV replication.";
Virology 397:43-55(2010).
[18]
INTERACTION WITH ILF2; XRCC6; RACK1 AND RPS3.
PubMed=21146485; DOI=10.1016/j.ab.2010.12.007;
Park M.S., Chu F., Xie J., Wang Y., Bhattacharya P., Chan W.K.;
"Identification of cyclophilin-40-interacting proteins reveals
potential cellular function of cyclophilin-40.";
Anal. Biochem. 410:257-265(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION.
PubMed=21711559; DOI=10.1186/1743-422X-8-329;
Anderson L.J., Lin K., Compton T., Wiedmann B.;
"Inhibition of cyclophilins alters lipid trafficking and blocks
hepatitis C virus secretion.";
Virol. J. 8:329-329(2011).
[21]
FUNCTION.
PubMed=22681779; DOI=10.1186/1471-2407-12-229;
Pearson J.D., Mohammed Z., Bacani J.T., Lai R., Ingham R.J.;
"The heat shock protein-90 co-chaperone, Cyclophilin 40, promotes ALK-
positive, anaplastic large cell lymphoma viability and its expression
is regulated by the NPM-ALK oncoprotein.";
BMC Cancer 12:229-229(2012).
[22]
FUNCTION.
PubMed=23220213; DOI=10.1016/j.yexcr.2012.11.016;
Jandova J., Janda J., Sligh J.E.;
"Cyclophilin 40 alters UVA-induced apoptosis and mitochondrial ROS
generation in keratinocytes.";
Exp. Cell Res. 319:750-760(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-198, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides. Proposed to act as a co-chaperone in HSP90
complexes such as in unligated steroid receptors heterocomplexes.
Different co-chaperones seem to compete for association with HSP90
thus establishing distinct HSP90-co-chaperone-receptor complexes
with the potential to exert tissue-specific receptor activity
control. May have a preference for estrogen receptor complexes and
is not found in glucocorticoid receptor complexes. May be involved
in cytoplasmic dynein-dependent movement of the receptor from the
cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-
binding activity. Involved in regulation of AHR signaling by
promoting the formation of the AHR:ARNT dimer; the function is
independent of HSP90 but requires the chaperone activity. Involved
in regulation of UV radiation-induced apoptosis. Promotes cell
viability in anaplastic lymphoma kinase-positive anaplastic large-
cell lymphoma (ALK+ ALCL) cell lines. May be involved in hepatitis
C virus (HCV) replication and release.
{ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:18708059,
ECO:0000269|PubMed:19932913, ECO:0000269|PubMed:21711559,
ECO:0000269|PubMed:22681779, ECO:0000269|PubMed:23220213,
ECO:0000269|PubMed:9659917}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0). {ECO:0000269|PubMed:11350175}.
-!- ENZYME REGULATION: Less sensitive to inhibition by cyclosporin A
than is CYP-18.
-!- SUBUNIT: Identified in ESR1 or NR3C1/GCR steroid receptor-
chaperone complexes. Found in HSP90 chaperone complexes with
kinase clients LCK or EIF2AK1. Two monomers associate with one
HSP90 homodimer. Interacts with HSP90AA1. Interacts with HSP90AB1;
PPID and FKBP4 compete for binding to HSP90AB1 and the interaction
is mutually exclusive with the PPID:HSPA8 interaction. Interacts
with HSPA8; PPID and STIP1 but not FKBP4 compete for binding to
HSPA8 and the interaction is mutually exclusive with the
PPID:HSP90AB1 interaction. Interacts with S100A1 and S100A2; the
interactions dissociate the PPID:HSP90AA1 interaction. Interacts
with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3.
Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or
DYNC1I2). {ECO:0000269|PubMed:11350175,
ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:14580201,
ECO:0000269|PubMed:15497503, ECO:0000269|PubMed:21146485,
ECO:0000269|PubMed:9659917}.
-!- INTERACTION:
Q12905:ILF2; NbExp=4; IntAct=EBI-716596, EBI-357925;
P01103:MYB (xeno); NbExp=2; IntAct=EBI-716596, EBI-6502562;
P63244:RACK1; NbExp=4; IntAct=EBI-716596, EBI-296739;
P23396:RPS3; NbExp=4; IntAct=EBI-716596, EBI-351193;
P12956:XRCC6; NbExp=4; IntAct=EBI-716596, EBI-353208;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11525244,
ECO:0000269|PubMed:18708059}. Nucleus, nucleolus
{ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:11525244,
ECO:0000269|PubMed:18708059}.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
D subfamily. {ECO:0000305}.
-!- CAUTION: This protein should not be confused with mitochondrial
peptidyl-prolyl cis-trans isomerase F (PPIF) which is often
referred to as cyclophilin D or CypD. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ppid/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry;
URL="https://en.wikipedia.org/wiki/Cyclophilin";
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EMBL; L11667; AAA35731.1; -; mRNA.
EMBL; D63861; BAA09923.1; -; Genomic_DNA.
EMBL; AY714221; AAT97986.1; -; Genomic_DNA.
EMBL; AK313929; BAG36649.1; -; mRNA.
EMBL; CH471056; EAX04853.1; -; Genomic_DNA.
EMBL; BC030707; AAH30707.1; -; mRNA.
CCDS; CCDS3801.1; -.
PIR; A45981; A45981.
RefSeq; NP_005029.1; NM_005038.2.
UniGene; Hs.183958; -.
ProteinModelPortal; Q08752; -.
SMR; Q08752; -.
BioGrid; 111477; 60.
DIP; DIP-34893N; -.
IntAct; Q08752; 26.
MINT; MINT-1399772; -.
STRING; 9606.ENSP00000303754; -.
BindingDB; Q08752; -.
ChEMBL; CHEMBL1697657; -.
iPTMnet; Q08752; -.
PhosphoSitePlus; Q08752; -.
BioMuta; PPID; -.
DMDM; 729274; -.
REPRODUCTION-2DPAGE; IPI00003927; -.
EPD; Q08752; -.
MaxQB; Q08752; -.
PaxDb; Q08752; -.
PeptideAtlas; Q08752; -.
PRIDE; Q08752; -.
DNASU; 5481; -.
Ensembl; ENST00000307720; ENSP00000303754; ENSG00000171497.
GeneID; 5481; -.
KEGG; hsa:5481; -.
UCSC; uc003iqc.4; human.
CTD; 5481; -.
DisGeNET; 5481; -.
EuPathDB; HostDB:ENSG00000171497.4; -.
GeneCards; PPID; -.
HGNC; HGNC:9257; PPID.
HPA; HPA019520; -.
HPA; HPA019692; -.
MIM; 601753; gene.
neXtProt; NX_Q08752; -.
OpenTargets; ENSG00000171497; -.
PharmGKB; PA33582; -.
eggNOG; KOG0546; Eukaryota.
eggNOG; COG0652; LUCA.
GeneTree; ENSGT00550000074595; -.
HOGENOM; HOG000065980; -.
HOVERGEN; HBG053654; -.
InParanoid; Q08752; -.
KO; K05864; -.
OMA; GLDKYQK; -.
OrthoDB; EOG091G0BGL; -.
PhylomeDB; Q08752; -.
TreeFam; TF324493; -.
BRENDA; 5.2.1.8; 2681.
ChiTaRS; PPID; human.
GeneWiki; PPID; -.
GenomeRNAi; 5481; -.
PRO; PR:Q08752; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000171497; -.
CleanEx; HS_PPID; -.
ExpressionAtlas; Q08752; baseline and differential.
Genevisible; Q08752; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016018; F:cyclosporin A binding; TAS:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; ISS:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071492; P:cellular response to UV-A; IMP:UniProtKB.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:0034389; P:lipid particle organization; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
GO; GO:0006457; P:protein folding; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0019076; P:viral release from host cell; TAS:UniProtKB.
Gene3D; 1.25.40.10; -; 1.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom_sf.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR11071; PTHR11071; 1.
Pfam; PF00160; Pro_isomerase; 1.
Pfam; PF13176; TPR_7; 1.
PRINTS; PR00153; CSAPPISMRASE.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
Acetylation; Apoptosis; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Isomerase; Nucleus; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat; Rotamase;
TPR repeat; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801}.
CHAIN 2 370 Peptidyl-prolyl cis-trans isomerase D.
/FTId=PRO_0000064153.
DOMAIN 19 183 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
REPEAT 223 256 TPR 1.
REPEAT 273 306 TPR 2.
REPEAT 307 340 TPR 3.
REGION 185 215 Chaperone activity. {ECO:0000250}.
REGION 214 370 Interaction with HSP90AB1. {ECO:0000250}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CR16}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VARIANT 49 49 R -> C (in dbSNP:rs2070631).
{ECO:0000269|Ref.3}.
/FTId=VAR_021021.
VARIANT 196 196 D -> V (in dbSNP:rs2230222).
/FTId=VAR_051771.
VARIANT 302 302 L -> I (in dbSNP:rs9410).
{ECO:0000269|Ref.3}.
/FTId=VAR_021022.
VARIANT 335 335 G -> E (in dbSNP:rs17843956).
{ECO:0000269|Ref.3}.
/FTId=VAR_021023.
MUTAGEN 227 227 K->A: Abolishes interaction with HSP90AB1
and impairs interaction with HSPA8.
{ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 231 231 N->A: Abolishes interaction with HSP90AB1
and impairs interaction with HSPA8.
{ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 234 234 F->A: Impairs interaction with HSP90AB1
and HSPA8. {ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 274 274 S->L: Impairs interaction with HSP90AB1
and HSPA8. {ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 278 278 N->A: Abolishes interaction with
HSP90AB1. {ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 284 284 L->A: Impairs interaction with HSP90AB1
and HSPA8. {ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 285 285 K->A: Impairs interaction with HSP90AB1
and HSPA8. {ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 308 308 K->A: Abolishes interaction with HSP90AB1
and impairs interaction with HSPA8.
{ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 312 312 R->A: Abolishes interaction with HSP90AB1
and impairs interaction with HSPA8.
{ECO:0000269|PubMed:12145316,
ECO:0000269|PubMed:15497503}.
MUTAGEN 329 329 D->A: Impairs interaction with HSP90AB1.
{ECO:0000269|PubMed:12145316}.
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


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