| ID | Sequence | Length | GC content |
|---|---|---|---|
| GUAGAUGUAUCUCUCCAGGAAGCGCUGUGUCCCAUUAAACGCGUAGCAU… | 1742 nt | 0.4845 | |
| GUAGAUGUAUCUCUCCAGGAAGCGCUGUGUCCCAUUAAACGCGUAGCAU… | 1666 nt | 0.4814 | |
| AGUCUCAUCUGCCUCCACUCGGCCUCAGUUCCUCAUCACUGUUCCUGUG… | 1852 nt | 0.4492 | |
| AGUCUCAUCUGCCUCCACUCGGCCUCAGUUCCUCAUCACUGUUCCUGUG… | 1653 nt | 0.4822 |
HLA-DPA1 belongs to the HLA class II alpha chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DPA) and a beta (DPB) chain, both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The alpha chain is approximately 33-35 kDa and its gene contains 5 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and the cytoplasmic tail. Within the DP molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to 4 different molecules. [provided by RefSeq, Jul 2008]
A study in humans analyzing sepsis patient blood samples via single-cell and bulk RNA sequencing identified HLA-DPA1 as a gene with reduced expression in CHIT1+ neutrophils from sepsis non-survivors compared to other myeloid cells [Li et al. DOI:10.1038/s41598-025-99619-z]. In a separate human study, HLA-DPA1 was identified as a ligand binding to the CD4 receptor, participating in the MHC-II signaling pathway within monocytes, which are key signal transmitters and receivers in sepsis [Liu et al. DOI:10.1590/1414-431X2025e14930].