| Lysosome-associated membrane glycoprotein (Lamp) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Lamp, LAMP (root symbol of family) | ||||||||
| Pfam | PF01299 | ||||||||
| InterPro | IPR002000 | ||||||||
| PROSITE | PDOC00280 | ||||||||
| TCDB | 9.A.16 | ||||||||
| OPM superfamily | 423 | ||||||||
| OPM protein | 2mom | ||||||||
| Membranome | 51 | ||||||||
| |||||||||
Lysosome-associated membrane glycoproteins (LAMPs)[1][2][3][4] 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.
CD68 (also called gp110 or macrosialin)[5] 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/).
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Cotranslational protein translocation
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Endomembrane system | Structure of a cell | Biology | Khan Academy
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CELL ORGANELLS _PART 02
Transcription
Human proteins containing this domain
References
- ^ Iwamoto, Tomotada; Sonobe, Toshiaki; Hayashi, Kozaburo (June 2003). "Loop-Mediated Isothermal Amplification for Direct Detection of Mycobacterium tuberculosis Complex, M. avium, and M. intracellulare in Sputum Samples". Journal of Clinical Microbiology. 41 (6): 2616–2622. doi:10.1128/JCM.41.6.2616-2622.2003. PMC 156570. PMID 12791888.
- ^ Nagamine, K.; Hase, T.; Notomi, T. (June 2002). "Accelerated reaction by loop-mediated isothermal amplification using loop primers". Molecular and Cellular Probes. 16 (3): 223–229. doi:10.1006/mcpr.2002.0415. PMID 12144774.
- ^ Notomi, Tsugunori; Okayama, Hiroto; Masubuchi, Harumi; et al. (2000). "Loop-mediated isothermal amplification of DNA". DNA. Nucleic Acids Res. 28 (12): e63. doi:10.1093/nar/28.12.e63. PMC 102748. PMID 10871386.
- ^ Fukuda Minoru (November 1991). "Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking". J. Biol. Chem. 266 (32): 21327–21330. doi:10.1016/S0021-9258(18)54636-6. PMID 1939168.
- ^ 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. doi:10.1016/S0021-9258(18)98400-0. PMID 8486654.
This page was last edited on 10 May 2024, at 13:35