Lysosome-associated membrane glycoprotein

{{Pfam_box

| Symbol = Lamp, LAMP ([https://www.genenames.org/cgi-bin/genefamilies/ root symbol] of family)

| Name = Lysosome-associated membrane glycoprotein (Lamp)

| image =

| width =

| caption =

| Pfam= PF01299

| InterPro= IPR002000

| SMART=

| Prosite = PDOC00280

| SCOP =

| TCDB = 9.A.16

| OPM family= 423

| OPM protein= 2mom

| PDB=

| Membranome family =51

}}

Lysosome-associated membrane glycoproteins (LAMPs){{cite journal |last1=Iwamoto |first1=Tomotada |last2=Sonobe |first2=Toshiaki |last3=Hayashi |first3=Kozaburo |date=June 2003 |title=Loop-Mediated Isothermal Amplification for Direct Detection of Mycobacterium tuberculosis Complex, M. avium, and M. intracellulare in Sputum Samples |journal=Journal of Clinical Microbiology |volume=41 |issue=6 |pages=2616–2622 |doi=10.1128/JCM.41.6.2616-2622.2003 |pmc=156570 |pmid=12791888}}{{cite journal |last1=Nagamine |first1=K. |last2=Hase |first2=T. |last3=Notomi |first3=T. |date=June 2002 |title=Accelerated reaction by loop-mediated isothermal amplification using loop primers |journal=Molecular and Cellular Probes |volume=16 |issue=3 |pages=223–229 |doi=10.1006/mcpr.2002.0415 |pmid=12144774}}{{cite journal |last1=Notomi |first1=Tsugunori |last2=Okayama |first2=Hiroto |last3=Masubuchi |first3=Harumi |last4=Yonekawa |first4=Toshihiro |last5=Watanabe |first5=Keiko |last6=Amino |first6=Nobuyuki |last7=Hase |first7=Tetsu |display-authors=3 |date=2000 |title=Loop-mediated isothermal amplification of DNA |journal=DNA. Nucleic Acids Res. |volume=28 |issue=12 |page=e63 |doi=10.1093/nar/28.12.e63 |pmc=102748 |pmid=10871386}}{{cite journal |author=Fukuda Minoru |title=Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking |journal=J. Biol. Chem. |volume=266 |issue=32 |pages=21327–21330 |date=November 1991 |doi=10.1016/S0021-9258(18)54636-6 |pmid=1939168 |url=http://www.jbc.org/content/266/32/21327.full.pdf+html |doi-access=free }} 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.

+-----+ +-----+ +-----+ +-----+

| | | | | | | |

{{not a typo|xCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxxxCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxx}}

+--------------------------++Hinge++--------------------------++TM++C+

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

CD68 (also called gp110 or macrosialin){{cite journal |vauthors=Holness CL, da Silva RP, Fawcett J, Gordon S, Simmons DL |title=Macrosialin, a mouse macrophage-restricted glycoprotein, is a member of the lamp/lgp family |journal=J. Biol. Chem. |volume=268 |issue=13 |pages=9661–9666 |year=1993 |doi=10.1016/S0021-9258(18)98400-0 |pmid=8486654 |url=http://www.jbc.org/content/268/13/9661.full.pdf+html |doi-access=free }} 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 antigen nomenclature is updated at Protein Reviews On The Web (https://web.archive.org/web/20080920090434/http://mpr.nci.nih.gov/prow/).