Lysosome-associated membrane glycoprotein

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Lysosome-associated membrane glycoprotein (Lamp)
Symbol Lamp
Pfam PF01299
InterPro IPR002000
TCDB 9.A.16

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.

  +-----+            +-----+         +-----+            +-----+
  |     |            |     |         |     |            |     |

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 (

Human proteins containing this domain[edit]



  1. ^ Fukuda M (1991). "Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking". J. Biol. Chem. 266 (32): 21327–21330. PMID 1939168. 
  2. ^ Holness CL, da Silva RP, Fawcett J, Gordon S, Simmons DL (1993). "Macrosialin, a mouse macrophage-restricted glycoprotein, is a member of the lamp/lgp family". J. Biol. Chem. 268 (13): 9661–9666. PMID 8486654. 

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