| Post Translational Modifications | N-glycosylated. Glycosylation is not essential for interaction with KLRK1/NKG2D but enhances complex formation. Proteolytically cleaved and released from the cell surface of tumor cells which impairs KLRK1/NKG2D expression and T-cell activation. Palmitoylated on cysteine residues in the cytoplasmic tail leading to its association with membrane microdomains enriched in cholesterol. N-glycosylation is necessary for cell surface expression. (Microbial infection) Ubiquitinated by human herpesvirus 8 protein K5, leading to degradation. |
| Function | Widely expressed membrane-bound protein which acts as a ligand to stimulate an activating receptor KLRK1/NKG2D, expressed on the surface of essentially all human natural killer (NK), gammadelta T and CD8 alphabeta T-cells. Up-regulated in stressed conditions, such as viral and bacterial infections or DNA damage response, serves as signal of cellular stress, and engagement of KLRK1/NKG2D by MICA triggers NK-cells resulting in a range of immune effector functions, such as cytotoxicity and cytokine production. |
| Protein Name | Mhc Class I Polypeptide-Related Sequence AMic-A |
| Database Links | Reactome: R-HSA-198933 |
| Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinCytoplasmExpressed On The Cell Surface In Gastric EpitheliumEndothelial Cells And Fibroblasts And In The Cytoplasm In Keratinocytes And MonocytesInfection With Human Adenovirus 5 Suppresses Cell Surface Expression Due To The Adenoviral E3-19k Protein Which Causes Retention In The Endoplasmic Reticulum |
| Alternative Protein Names | Mhc Class I Polypeptide-Related Sequence A proteinMic-A proteinMICA proteinPERB11.1 protein |
Information sourced from Uniprot.org
