The PDCD10 gene is 51,688 bp in length, located on the minus strand and spans 9 exons (NCBI, 2016).

3 different alternatively spliced mRNAs (1454, 1313 and 1212 bp long, respectively) that differ only in 5UTRs; 639 bp long open reading frame (NM_007217.3, NM_145859.1, NM_145860.1).

LOC100128686 programmed cell death 10 pseudogene; located on 8q11.21 (NCBI, 2016).

PDCD10 encodes an evolutionarily conserved 212 amino acid long protein (Wang et al, 1999). PDCD10 has an estimated molecular weight of 29 kDa.

PDCD10 is expressed in all tissues including brain, pancreas, breast, ovary, kidney, liver and lungs (The Human Protein Atlas, 2016).

PDCD10 is localized in cytoplasm, near Golgi apparatus and nucleus (Fidalgo et al, 2010).

The PDCD10 protein regulates cell proliferation and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway through interaction with serine/threonine protein kinase STK26 (MST4) (Ma et al, 2007). It also interacts with another serine/threonine kinase, STK25 , and triggers apoptosis under oxidative stress (Zhang et al, 2012). PDCD10 interacts with members of germinal center kinases III subfamily to promote normal Golgi assembly and cell orientation (Fidalgo, 2010). PDCD10 involves in the stabilization of KDR (VEGFR2) signaling and is vital for normal vascular development (He et al, 2010). PDCD10 acts downstream of gamma-protocadherins and regulate neuronal survival (Lin et al, 2010).

Cerebral cavernous malformations are associated with the mutations in 3 loci; one of which is CCM3/PDCD10. Bergametti et al reported a de novo deletion as well as six other deleterious mutations in PDCD10 gene. Three of these mutations were stated as nonsense mutations, two other mutations were reported to generate aberrant splicing in exon 9 with a frameshift and the last one caused an abnormal splicing in exon 5 without frameshift (Bergametti et al, 2005). In a study with 61 families with cerebral caverous malformations, Guclu et al (2005) identified two identical mutations creating a premature stop codon in exon 7, two frameshift mutations in exon 6 and one additional frameshift mutation in exon 9 (Guclu et al, 2005). In patients without KRIT1 (CCM1) and CCM2 mutations, Verlaan et al (2005) identified two mutations in CCM3 which lead to a truncated PDCD10 protein. One of the mutations was a nonsense mutation in exon 7 caused by a transversion o a C to a T that creates a stop codon and the other one was reported to be an invariant splice acceptor site mutation (Verlaan et al, 2005). Riant et al (2013) reported that, in 13 of 54 CCM3-mutated patients, there are deletions in one or several coding exons; 8 of which deletions are whole gene deletions. In 41 patients, several point mutations leading abnormal splicing, nonsense mutations and small insertions and deletions causing frameshifts and premature stop codons were identified. Additionally, they reported deletions in noncoding exons 1-3 in a 5-year old child with cerebral carcinomas (Riant et al, 3013).