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    HLA-A

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    For Research Use Only. Not For Clinical Use.


    Background

    HLA-A belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-A alleles have been described.
    Protein class

    Cancer-related genes, Disease related genes, Human disease related genes, Plasma proteins, Potential drug targets, Transporters

    Predicted location

    Intracellular, Membrane (different isoforms)

    Single cell type specificity

    Cell type enhanced (Proximal enterocytes, Ductal cells)

    Immune cell specificity

    Low immune cell specificity

    Cell line specificity

    Cell line enhanced (A-431, fHDF/TERT166, HBEC3-KT, RPMI-8226, U-266/70)

    Interaction

    Heterotrimer that consists of an alpha chain HLA-A, a beta chain B2M and a peptide (peptide-HLA-A-B2M) (PubMed:7504010, 7679507, 21943705, 19177349, 24395804, 26758806, 7504010, 7506728, 8805302, 7694806, 7935798, 9177355, 18275829, 22245737, 28250417, 11502003, 8906788, 19542454). Early in biogenesis, HLA-A-B2M dimer interacts with the components of the peptide-loading complex composed of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:21263072). Interacts with TAP1-TAP2 transporter via TAPBP; this interaction is obligatory for the loading of peptide epitopes delivered to the ER by TAP1-TAP2 transporter (PubMed:8805302, 8630735, 21263072). Interacts with TAPBPL; TAPBPL binds peptide-free HLA-A-B2M complexes or those loaded with low affinity peptides, likely facilitating peptide exchange for higher affinity peptides (PubMed:26869717). Only optimally assembled peptide-HLA-B2M trimer translocates to the surface of antigen-presenting cells, where it interacts with TCR and CD8 coreceptor on the surface of T cells. HLA-A (via polymorphic alpha-1 and alpha-2 domains) interacts with antigen-specific TCR (via CDR3 domains) (PubMed:22245737, 12796775, 18275829). One HLA-A molecule (mainly via nonpolymorphic alpha-3 domain) interacts with one CD8A homodimer (via CDR-like loop); this interaction insures peptide-HLA-A-B2M recognition by CD8-positive T cells only (PubMed:9177355, 2784196). Alleles A*23:01; A*24:02 and A*32:01 interact (via Bw4 motif) with KIR3DL1 on NK cells; this interaction is direct. (Microbial infection) Interacts with HHV-8 MIR1 protein. (Microbial infection) Interacts with HTLV-1 accessory protein p12I.

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