Rab-interacting lysosomal protein (RILP)
The protein contains 401 amino acids for an estimated molecular weight of 44200 Da.
Rab effector playing a role in late endocytic transport to degradative compartments (PubMed:11696325, PubMed:14668488, PubMed:27113757, PubMed:11179213, PubMed:12944476). Involved in the regulation of lysosomal morphology and distribution (PubMed:14668488, PubMed:27113757). Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments (PubMed:11179213, PubMed:11696325). Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes (PubMed:12944476). (updated: April 22, 2020)
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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs9909321 | |
| dbSNP:rs34982553 |
Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class II
Cilium assembly
Early endosome to late endosome transport
Endosome to lysosome transport
Endosome transport via multivesicular body sorting pathway
Intralumenal vesicle formation
Negative regulation of protein catabolic process
Positive regulation of protein catabolic process
Protein transport
Regulation of multivesicular body size
The reference OMIM entry for this protein is 607848
Rab-interacting lysosomal protein
Rilp
DESCRIPTION
RILP, along with the GTPase RAB7 (602298), controls late endocytic transport (Cantalupo et al., 2001).CLONING
Using Rab7 as bait in a yeast 2-hybrid screen, followed by screening a HeLa cell cDNA library, Cantalupo et al. (2001) cloned a full-length RILP cDNA. The deduced 401-amino acid protein has a calculated molecular mass of about 45 kD and contains 2 coiled-coil regions. RILP shares significant homology with a mouse protein belonging to the ezrin (123900)-radixin (179410)-moesin (309845) (ERM) family. Northern blot analysis detected transcripts of about 1.2 and 1.8 kb in the 3 tissues tested (lung, spleen, and stomach). Western blot analysis detected a 50-kD RILP protein in all cell lines examined. Immunolocalization colocalized RILP with several late endosomal/lysosomal marker proteins. By RNA dot blot analysis, Bucci et al. (2001) determined that RILP is expressed at varying levels in all tissues examined. Expression was highest in adult heart, stomach, adrenal gland, thyroid gland, salivary gland, liver, and lung, and in fetal heart and liver. Expression was lowest in whole fetal brain and in all adult brain regions. Northern blot analysis confirmed ubiquitous expression of 0.9- and 1.8-kb transcripts. Expression levels of the 2 transcripts varied between tissues. Using PCR, Wang et al. (2004) detected variable RILP expression in all 8 human tissues examined. Database analysis detected orthologs of RILP and RILP-like proteins (RLPs; see 614092) in several multicellular organisms, but not in unicellular organisms. Similarity among the RILP and RLP orthologs was highest in 2 domains that Wang et al. (2004) called RILP homology domain-1 (RH1) and RH2.GENE FUNCTION
Cantalupo et al. (2001) determined that the C-terminal half of RILP interacted with RAB7. It also interacted with a constitutively active GTP-bound RAB7 mutant, but it did not bind an inactive GDP-bound RAB7 mutant or several other RAB proteins. Overexpression of RILP resulted in perinuclear clustering of the late endosomal/lysosomal compartment, which could be reversed by microtubule depolymerization. The perinuclear clustering was similar to that observed in cells expressing wildtype or constitutively active RAB7. Overexpression of the C-terminal half of RILP resulted in lysosome dispersal and inhibition of lysosomal substrate degradation, similar to that observed in cells expressing the inactive GDP-bound RAB7 mutant. Overexpression of RILP was able to prevent or reverse the effects of the inactive RAB7 mutant, leading Cantalupo et al. (2001) to hypothesize that RILP lies downstream of RAB7 in the regulation of late endocytic traffic. Wang et al. (2004) found that overexpression of human RILP in normal rat kidney cells caused enlargement and relocalization of lysosomes. Experiments with chimeric proteins made up of sequences from RILP and RLP1 (RILPL1; 614092) revealed a 62-amino acid domain in RILP that was necessary to regulate lysosome morphology. The ability to regulate lysosomes correlated with the ability of the chimeric protein to interact with GTP-bound RAB7 or both GTP-bound RAB7 and RAB34 (610917) simultaneously, but not GTP-bound RAB34 alone.MAPPING
By radiation hybrid analysis, Bucci et al. (2001) mapped the RILP gene to chromosome 17p13.3. Cantalupo et al. (2001) mapped the mouse Rilp gene to chromosome 11. ... More on the omim web site
April 25, 2020: 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 607848 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed