ZSWIM9

The high concentration of arginine residues influences the protein's charge, binding properties, and potential regulatory functions.

Arginine-rich proteins can play crucial roles in cell differentiation during embryonic development due to their involvement in processes that regulate gene expression, chromatin remodeling, and signaling pathways.

[8] ZSWIM9 contains a zinc finger SWIM-type profile, a pattern recognized in human protein ZSWIM9 and its orthologs that represent a shared zinc-binding motif.

[9][10] The acronym "SWIM" stands for SWI2/SNF2 and MuDR and detects conserved cysteine- and histidine-rich regions involved in zinc coordination, which facilitates protein-DNA or protein-protein interactions.

This structure, coupled with its FAR1-like DNA-binding domain, suggests ZSWIM9 functions as a transcriptional regulator, potentially co-opted from transposases to play roles in gene expression, DNA repair, or transposon splicing.

[19] Higher expression suggests that ZSWIM9 may have a role in the muscle’s response to chronic disease-related stress, regeneration process, or damage repair.

[23] The presence of an NES indicates the protein may shuttle between the nucleus and cytoplasm, depending on cellular conditions or specific signals (e.g., stress, phosphorylation).

[28] Zinc-finger proteins contain a short finger-like structural motif stabilized by zinc-ions [1] which are involved in critical biological processes including cell differentiation[29] and embryonic development.

[32] One study associate a SNP in ZSWIM9 with acute Graft versus Host Disease (aGvHD) which affects patients undergoing allogeneic hematopoietic stem-cell transplantation (allo-HSCT).

[33] This could be associated with proteins involved in cell differentiation through several mechanisms related to DNA repair, gene expression regulation, and cellular responses to stress or injury.

DNA sequences of ZSWIM9 transcript variants with their exons labeled. Transcript variant 1 is labeled with a red box. Each exon (1-4) is labeled above, as well as the other variants.
Multiple sequence alignment (MSA) of ZSWIM9 and its close orthologs, specifically showing the conserved FAR1 domain from amino acids 97-128.
Schematic illustration of human protein ZSWIM9 with important domains, motifs, and post-translational modifications identified.
Phylogenetic tree showing the evolutionary history of ZSWIM9 protein in humans and its orthologs. Each circle shows taxonomic groups represented by orthologs found in table 1. Some orthologs were not including due to crowding, but each taxonomic group within the twenty orthologs of ZSWIM9 is represented.
Graph of the estimated date of divergence linearly, based on ZSWIM9 compared to Cytochrome C and Fibrinogen Alpha. ZSWIM9 mutates faster than Cytochrome C but not faster than Fibrinogen Alpha. The ZSWIM gene family likely appeared around 350 million years ago due to the fact that it doesn’t have known orthologs before amphibians.