The domain within your query sequence starts at position 34 and ends at position 210; the E-value for the MHC_I domain shown below is 5.9e-33.
GTHTLRYNVRAHSLEGSEKTQLLVLIYVDEELFLKYNGDSRETEPLGCWIKGHGGNETCA RETNNLLKVEEKLRGMMAEVINQKSQEEGLHTLQATLGCELLSNGSTRGFWHLGYDGQNF LTFDQKTLTWTVDGPSTQQNKMFWKTHAPRADLVKTFLDDICPAHLQRYLASLRNGL
MHC_I |
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PFAM accession number: | PF00129 |
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Interpro abstract (IPR011161): | Class I MHC glycoproteins are expressed on the surface of all somatic nucleated cells, with the exception of neurons. MHC class I receptors present peptide antigens that are synthesised in the cytoplasm, which includes self-peptides (presented for self-tolerance) as well as foreign peptides (such as viral proteins). These antigens are generated from degraded protein fragments that are transported to the endoplasmic reticulum by TAP proteins (transporter of antigenic peptides), where they can bind MHC I molecules, before being transported to the cell surface via the Golgi apparatus [ (PUBMED:9485452) (PUBMED:15526153) ]. MHC class I receptors display antigens for recognition by cytotoxic T cells, which have the ability to destroy viral-infected or malignant (surfeit of self-peptides) cells. MHC class I molecules are comprised of two chains: a MHC alpha chain (heavy chain), and a beta2-microglobulin chain (light chain), where only the alpha chain spans the membrane. The alpha chain has three extracellular domains (alpha 1-3, with alpha1 being at the N terminus), a transmembrane region and a C-terminal cytoplasmic tail. The soluble extracellular beta-2 microglobulin chain associates primarily with the alpha-3 domain and is necessary for MHC stability. The alpha1 and alpha2 domains of the alpha chain are referred to as the recognition region, because the peptide antigen binds in a deep groove between these two domains. This entry represents MHC antigen-recognition-like domains from:
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This is a PFAM domain. For full annotation and more information, please see the PFAM entry MHC_I