Peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3)
The protein contains 161 amino acids for an estimated molecular weight of 18155 Da.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs7562391 |
Biological Process
MRNA splicing, via spliceosome
Protein folding
Protein peptidyl-prolyl isomerization
The reference OMIM entry for this protein is 615811
Peptidyl-prolyl isomerase-like 3; ppil3
DESCRIPTION
PPIL3 shares sequence similarity with peptidyl-prolyl cis/trans isomerases (see 123840). These enzymes catalyze interconversion of the cis and trans isomers of peptidyl-prolyl imide bonds in peptide and protein substrates and are predicted to assist in protein folding (Zhou et al., 2001).CLONING
By sequencing clones obtained from a human fetal brain cDNA library, followed by 5-prime RACE, Zhou et al. (2001) obtained clones representing 2 splice variants of PPIL3. PPIL3a encodes a deduced 165-amino acid protein with a calculated molecular mass of 18.6 kD. PPIL3b encodes a deduced 161-amino acid protein with a calculated molecular mass of 18.2 kD. The proteins have identical N- and C-terminal regions, but they differ in the sequence of an internal stretch. Both PPIL3a and PPIL3b have a putative PPI catalytic domain, but they contain 6 and 3 altered amino acids, respectively, in this normally highly conserved domain. RT-PCR detected variable expression of both transcripts in all 16 human tissues examined. Expression of PPIL3a was higher than PPIL3b in skeletal muscle, thymus, prostate, small intestine, colon, and peripheral blood leukocytes. Expression of PPIL3b predominated in heart, brain, liver, kidney, pancreas, spleen, and testis.GENE STRUCTURE
Zhou et al. (2001) determined that the PPIL3 gene spans more than 18 kb and contains 8 exons, including alternate exons 4a and 4b, which are used by PPIL3a and PPIL3b transcripts, respectively.MAPPING
By genomic sequence analysis, Zhou et al. (2001) mapped the PPIL3 gene to chromosome 2q33. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 615811 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).