Tag | Content |
---|
CPLM ID | CPLM-006417 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptidyl-prolyl cis-trans isomerase D |
Protein Synonyms/Alias | PPIase D; Cyclophilin D; Rotamase D |
Gene Name | CPR5 |
Gene Synonyms/Alias | CYP5; CYPD; YDR304C; D9740.14 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
---|
45 | FDINHGDKQIGRIVM | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
Sequence Annotation | DOMAIN 37 195 PPIase cyclophilin-type. MOTIF 222 225 Prevents secretion from ER. CARBOHYD 139 139 N-linked (GlcNAc...) (Potential). |
Keyword | Complete proteome; Cyclosporin; Endoplasmic reticulum; Glycoprotein; Isomerase; Reference proteome; Rotamase; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 225 AA |
Protein Sequence | MKLQFFSFIT LFACLFTTAI FAKEDTAEDP EITHKVYFDI NHGDKQIGRI VMGLYGLTTP 60 QTVENFYQLT ISRDPKMGYL NSIFHRVIPN FMIQGGDFTH RSGIGGKSIF GNTFKDENFD 120 VKHDKPGRLS MANRGKNTNG SQFFITTVPC PWLDGKHVVF GEVLDGMDVV HYIENVKTDS 180 RNMPVKEVII VESGELETVP LDNKDAAKLQ EEIKAEASEA AHDEL 225 |
Gene Ontology | GO:0005783; C:endoplasmic reticulum; IDA:SGD. GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. GO:0042277; F:peptide binding; IEA:UniProtKB-KW. GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:SGD. GO:0006457; P:protein folding; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |