Lysosome-associated membrane glycoprotein

Lysosome-associated membrane glycoproteins (lamp)^[1] 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 (TM) followed by a very short cytoplasmic tail (C). In each of the duplicated domains, there are two conserved disulfide bonds. This structure is schematically represented in the figure below.

  +-----+            +-----+         +-----+            +-----+
  |     |            |     |         |     |            |     |
 xCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxxxCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxx
 +--------------------------++Hinge++--------------------------++TM++C+

In mammals, there are two closely related types of lamp: LAMP1 and LAMP2.

CD69 (also called gp110 or macrosialin)^[2] 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 (http://mpr.nci.nih.gov/prow/).

Human proteins containing this domain

CD68; LAMP1; LAMP2; LAMP3;

References

This article incorporates text from the public domain Pfam and InterPro IPR002000