UniProt Accession

 PPID_MOUSE; Q9CR16; Q543G1 

Genbank Protein ID

 AK003402; AK013919; AK051597; BC011499; BC019778 

Genbank Nucleotide ID

 BAB22767.1; BAB29056.1; BAC34686.1; AAH11499.1; AAH19778.1 

Protein Name

 Peptidyl-prolyl cis-trans isomerase D 

Protein Synonyms/Alias

 PPIase D; 40 kDa peptidyl-prolyl cis-trans isomerase; Cyclophilin-40; CYP-40; Rotamase D 

Gene Name

 Ppid 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
9	SHASPAAKPSNSKNP	ubiquitination	[1]
14	AAKPSNSKNPRVFFD	ubiquitination	[1]
64	GTGSTTGKPLHFKGC	acetylation	[2]
145	PTPHLDGKHVVFGQV	acetylation	[3]
154	VVFGQVIKGLGVART	acetylation	[2]
171	NVEVNGEKPAKLCVI	acetylation	[4]
218	IDLKDVDKILLISED	ubiquitination	[1]
227	LLISEDLKNIGNTFF	acetylation	[2]
227	LLISEDLKNIGNTFF	ubiquitination	[1]
283	VLNIGACKLKMSNWQ	ubiquitination	[1]
313	NTKALYRKAQGWQGL	ubiquitination	[1]
331	DQALADLKKAQEIAP	acetylation	[5]
341	QEIAPGDKAIQAELL	acetylation	[5]
341	QEIAPGDKAIQAELL	ubiquitination	[1]
349	AIQAELLKVKQMIKA	acetylation	[2]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria.
 Shulga N, Wilson-Smith R, Pastorino JG.
 J Cell Sci. 2010 Mar 15;123(Pt 6):894-902. [PMID: 20159966]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 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 region. Involved in regulation of UV radiation-induced apoptosis. 

Sequence Annotation

 DOMAIN 19 183 PPIase cyclophilin-type.
 REPEAT 223 256 TPR 1.
 REPEAT 273 306 TPR 2.
 REPEAT 307 340 TPR 3.
 REGION 185 215 Chaperone activity (By similarity).
 REGION 214 370 Interaction with HSP90AB1 (By
 MOD_RES 198 198 Phosphoserine (By similarity).  

Keyword

 Apoptosis; Chaperone; Complete proteome; Cyclosporin; Cytoplasm; Direct protein sequencing; Isomerase; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; Rotamase; TPR repeat; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 370 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0045111; C:intermediate filament cytoskeleton; IEA:Compara.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0030331; F:estrogen receptor binding; ISS:UniProtKB.
 GO:0005528; F:FK506 binding; TAS:MGI.
 GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
 GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
 GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
 GO:0008134; F:transcription factor binding; ISS:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
 GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
 GO:0034389; P:lipid particle organization; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
 GO:0050714; P:positive regulation of protein secretion; IEA:Compara.
 GO:0045070; P:positive regulation of viral genome replication; IEA:Compara.
 GO:0006461; P:protein complex assembly; ISS:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 

Interpro

 IPR002130; Cyclophilin-like_PPIase_dom.
 IPR020892; Cyclophilin-type_PPIase_CS.
 IPR023114; Elongated_TPR_rpt_dom.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 

Pfam

 PF00160; Pro_isomerase
 PF13176; TPR_7 

SMART

 SM00028; TPR 

PROSITE

 PS00170; CSA_PPIASE_1
 PS50072; CSA_PPIASE_2
 PS50005; TPR
 PS50293; TPR_REGION 

PRINTS

 PR00153; CSAPPISMRASE.