Lysosome-associated membrane glycoprotein


Lysosome-associated membrane glycoproteins are integral membrane proteins, specific to lysosomes, and whose exact biological function is not yet clear. Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal extremity there is a transmembrane region followed by a very short cytoplasmic tail. In each of the duplicated domains, there are two conserved disulfide bonds. This structure is schematically represented in the figure below.
+-----+ +-----+ +-----+ +-----+
| | | | | | | |

+--------------------------++Hinge++--------------------------++TM++C+
In mammals, there are two closely related types of lamp: LAMP1 and LAMP2.
CD69 is a heavily glycosylated integral membrane protein whose structure consists of a mucin-like domain followed by a proline-rich hinge; a single lamp-like domain; a transmembrane region and a short cytoplasmic tail.
CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at Protein Reviews On The Web.

Human proteins containing this domain