Lysosome-associated membrane glycoprotein 1 (LAMP1)
The protein contains 417 amino acids for an estimated molecular weight of 44882 Da.
Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.', '(Microbial infection) Acts as a receptor for Lassa virus protein. (updated: June 2, 2021)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs9577230 |
Biological Process
Autophagic cell death
Autophagy
Establishment of protein localization to organelle
Golgi to lysosome transport
Granzyme-mediated apoptotic signaling pathway
Granzyme-mediated programmed cell death signaling pathway
Neutrophil degranulation
Positive regulation of natural killer cell degranulation
Positive regulation of natural killer cell mediated cytotoxicity
Protein stabilization
Regulation of organelle transport along microtubule
Viral process
Cellular Component
Alveolar lamellar body
Autolysosome
Autophagosome membrane
Azurophil granule membrane
Cytolytic granule
Cytolytic granule membrane
Cytoplasm
Cytosol
Dendrite
Endosome membrane
External side of plasma membrane
Extracellular exosome
Ficolin-1-rich granule membrane
Integral component of plasma membrane
Integral component of synaptic vesicle membrane
Late endosome
Late endosome membrane
Lysosomal membrane
Lysosome
Melanosome
Membrane
Multivesicular body
Neuronal cell body
Perinuclear region of cytoplasm
Phagolysosome membrane
Plasma membrane
Sarcolemma
Synaptic vesicle
The reference OMIM entry for this protein is 153330
Lysosome-associated membrane protein 1; lamp1
Lysosome-associated membrane protein a; lampa
Lysosomal membrane glycoprotein, 120-kd; lgp120
Cd107a
CLONING
The 120-kD lysosomal membrane glycoprotein is an acidic, heavily glycosylated membrane protein enriched in the lysosomal membrane. By using an oligonucleotide probe corresponding to the amino terminus of rat lgp120, Howe et al. (1988) isolated and characterized cDNA clones containing the entire coding region. The deduced amino acid sequence demonstrated that the rat LGP120 contains a putative signal peptide, 18 sites for N-linked glycosylation, a single membrane-spanning segment, and a short (11 amino acid) cytosolic tail. LGP120 showed similarity to 2 other lysosomal membrane proteins and showed a high degree of conservation in domain organization and primary structure with the proteins in other species. Viitala et al. (1988) reported the complete amino acid sequence for the human lysosome-associated membrane glycoprotein with M(r) about 120,000. The amino acid sequence, which was deduced from analysis of the cDNA, contains 385 amino acid residues. Mattei et al. (1990) noted that, although LAMP1 contains a functional hinge region, it has a disulfide arrangement different from that observed in members of the immunoglobulin superfamily and thus may represent a novel family of membrane glycoproteins. The amino acid sequence of LAMP1 is more homologous to corresponding molecules from other species than it is to LAMP2 (309060). Furthermore, LAMP1 and LAMP2 are immunologically distinguishable from each other. Mattei et al. (1990) proposed that LAMP1 and LAMP2 diverged relatively early in evolution, but that LAMP1 (and possibly LAMP2) structures have been strongly conserved.GENE FUNCTION
Yogalingam et al. (2008) stated that LAMP1 is involved in lysosomal exocytosis, movement of lysosomes along microtubules, and fusion of phagosomes with lysosomes. They found that hematopoietic cells from neuraminidase-1 (NEU1; 608272) -/- mice, a model of human sialidosis (256550), showed increased plasma membrane expression of a hypersialylated form of Lamp1 compared with wildtype mice. Yogalingam et al. (2008) confirmed that Lamp1, but not other lysosomal membrane proteins, was an endogenous Neu1 substrate. Accumulation of Lamp1 on the plasma membrane of Neu1 -/- macrophages was associated with enhanced exocytosis of lysosomal hydrolases. Overexpression of wildtype Lamp1 did not fully recapitulate the effects of accumulated hypersialylated Lamp1 on lysosomal exocytosis. Reduced Lamp1 expression in both Neu1 -/- and wildtype mouse macrophages via small interfering RNA reduced lysosomal exocytosis, particularly in Neu1 -/- cells. Yogalingam et al. (2008) found that fibroblasts from 2 patients with early-onset (type II) sialidosis due to mutations that eliminated NEU1 activity showed increased plasma membrane LAMP1 compared with normal fibroblasts. In contrast, fibroblasts from a patient with late-onset (type I) sialidosis with residual NEU1 activity exhibited a more normal LAMP1 distribution. The culture medium of type II sialidosis fibroblasts also showed elevated alpha-mannosidase activity (see 609458), suggesting increased lysosomal exocytosis. Lassa virus, which spreads from rodents to humans, can cause lethal hemorrhagic fever. Despite the broad tropism of the virus, chicken cells were reported 30 years ago to resist infection. Jae et al. (2014) found that Lassa virus readily engaged its cell-surface receptor alpha-dystroglycan (DAG1; 128239) in avian cells, but virus entry in susceptible species involved a pH-dependent swi ... More on the omim web site
July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 153330 was added.