Anti-SNRPD3/Sm-D3 antibody [EPR7676]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

SNRPD3 also known as Sm-D3 is a protein that plays an important role in the assembly of small nuclear ribonucleoproteins (snRNPs) essential for pre-mRNA splicing. This protein has a molecular mass of approximately 10 kDa. It functions as a core component of the spliceosomal machinery an essential complex in eukaryotic gene expression. You can find SNRPD3 expressed in various tissues where pre-mRNA splicing activity is required reflecting its fundamental role in cellular processes.

Biological function summary

SNRPD3 participates in snRNP assembly by interacting with other Sm proteins to form a heptameric ring structure around small nuclear RNAs (snRNAs). As part of the major spliceosomal snRNPs SNRPD3 contributes to the modification and catalysis of pre-mRNA splicing. The protein also gets involved in RNA stability and regulation. As a member of the spliceosome complex SNRPD3 helps ensure the fidelity and precision of splicing events important for generating mature mRNA molecules.

Pathways

The actions of SNRPD3 lie within the splicing pathway and have implications in the gene expression pathway. Interaction occurs with other proteins such as SNRPD1 and SNRPD2 which are also part of the snRNP complex facilitating effective spliceosomal function. The U1 snRNP specifically involving SNRPD3 plays a part in the recognition of splice sites initiating the splicing of pre-mRNAs.

Associated diseases and disorders

Issues with SNRPD3 function or expression might relate to autoimmune diseases such as lupus and some neurodegenerative conditions. Antinuclear antibodies targeting snRNP components including SNRPD3 are common in systemic lupus erythematosus indicating its involvement in the disease's pathology. Furthermore alterations in splicing mechanisms involving SNRPD3 might influence neurodegenerative disorders due to its role in RNA processing and stability potentially relating to other RNA-binding proteins like hnRNPs.