Phosphatidylserine decarboxylase proenzyme, mitochondrial (PISD)
The protein contains 409 amino acids for an estimated molecular weight of 46672 Da.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer) (PubMed:30488656, PubMed:30858161). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. (updated: June 2, 2021)
Protein identification was indicated in the following studies:
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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No binding partner found
The reference OMIM entry for this protein is 612770
Phosphatidylserine decarboxylase; pisd
Psd
Pssc
DESCRIPTION
Phosphatidylserine decarboxylases (PSDs; EC 4.1.1.65) catalyze the formation of phosphatidylethanolamine (PE) by decarboxylation of phosphatidylserine (PS). Type I PSDs, such as PISD, are targeted to the inner mitochondrial membrane by an N-terminal targeting sequence. PISD also contains a conserved LGST motif that functions as an autocatalytic cleavage site where the proenzyme is split into mature alpha and beta subunits (Schuiki and Daum, 2009).CLONING
Kuge et al. (1991) cloned Pisd, which they called Pssc, from Chinese hamster ovary cells. The deduced protein contains at least 370 amino acids. Northern blot analysis detected a transcript of about 2.4 kb. Using real-time PCR, Steenbergen et al. (2005) found that Pisd was expressed in all mouse tissues examined, with highest expression in testis and liver. Expression was lower in embryonic and young mice compared with adult mice. Beta-galactosidase (GLB1; 611458) staining detected high Pisd expression in embryonic heart and in Sertoli cells of adult testis. By PCR of a placenta cDNA library, Forbes et al. (2007) cloned human PISD. The full-length proenzyme contains 409 amino acids and is self-processed into an active heterodimer.GENE FUNCTION
By assaying membranes prepared from transfected human embryonic kidney cells, Forbes et al. (2007) confirmed that human PISD was catalytically active, and they identified several chemical inhibitors of PISD activity. Schuiki and Daum (2009) reviewed PSDs and their role in lipid metabolism.MAPPING
By genomic sequence analysis, Dunham et al. (1999) mapped the PISD gene to chromosome 22q12.ANIMAL MODEL
Steenbergen et al. (2005) found that Pisd -/- mice died between embryonic days 8 and 10. In 8-day-old Pisd -/- embryos, there were no extra-embryonic components, such as placenta or amnion, and the embryo was in direct contact with maternal blood. A large number of mitochondria in Pisd -/- embryos were aberrantly shaped, although the inner and outer membranes were present, and cristae were clearly visible. Mitochondria from embryonic fibroblasts were fragmented and rounded, with irregular diameter, and they were widely dispersed throughout the cell rather than being concentrated near the nucleus. Pisd +/- mice appeared normal, exhibited normal vitality, and had the same phospholipid composition of liver, testis, and brain as wildtype mice. However, the amount of CTP-phosphoethanolamine cytidylyltransferase (PCYT2; 602679) protein, which synthesizes PE through an alternative pathway in the endoplasmic reticulum, was elevated, and the enzymatic activity of Pcyt2 was 100% higher in live homogenates from Pisd +/- mice compared with wildtype. ... More on the omim web site
July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 612770 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).