CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014889
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
257LRYLDSSKAVIEKADacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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 308 340 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
MSHPSPAGKP SNSKNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGTGP 60
TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSM 120
ANAGPNTNGS QFFITTVPTP HLDGKHVVFG QVIKGLGVAR MLENVEVNGE KPAKLCVIAE 180
CGELKEGDEW GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LISEDLKNIG NTFFKSQNWE 240
MAIKKYAKVL RYLDSSKAVI EKADVSRLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL 300
EMDPSNTKAL YRKAQGWQGL KEYDQALADL KKAQEIAPGD KAIQAELLKV KQMIKAQKDK 360
EKAVYAKMFA 370 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:RGD.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0030331; F:estrogen receptor binding; ISS:UniProtKB.
 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; IDA:RGD.
 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:0043066; P:negative regulation of apoptotic process; IMP:RGD.
 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:0006461; P:protein complex assembly; ISS:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0051881; P:regulation of mitochondrial membrane potential; IMP:RGD.
 GO:0006979; P:response to oxidative stress; IMP:RGD. 
Interpro
 IPR002130; Cyclophilin-like_PPIase_dom.
 IPR020892; Cyclophilin-type_PPIase_CS.
 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.