Charged multivesicular body protein 1a (CHMP1A)
The protein contains 196 amino acids for an estimated molecular weight of 21703 Da.
Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing. (updated: April 1, 2015)
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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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Biological Process
Carbon catabolite repression of transcription by glucose
Cell division
Endosome transport via multivesicular body sorting pathway
ESCRT III complex disassembly
Gene silencing
Late endosome to vacuole transport
Midbody abscission
Mitotic chromosome condensation
Mitotic metaphase plate congression
Multivesicular body assembly
Negative regulation of cell cycle
Negative regulation of transcription, DNA-templated
Nucleus organization
Protein transport
Proteolysis
Regulation of centrosome duplication
Regulation of mitotic spindle assembly
Septum digestion after cytokinesis
Transcription, DNA-templated
Vacuolar transport
Vesicle-mediated transport
Viral budding via host ESCRT complex
Viral process
The reference OMIM entry for this protein is 164010
Chmp family, member 1a; chmp1a
Chromatin-modifying protein 1a
Charged multivesicular body protein 1a
Chmp1
Procollagen, type iii, n-endopeptidase; pcoln3
Metalloprotease 1; prsm1
Metalloprotease, 33-kd
DESCRIPTION
CHMP1A belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs, including CHMP1A, have both nuclear and cytoplasmic/vesicular distributions, and CHMP1A is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006).CLONING
Halila et al. (1989) isolated a cDNA for PCOLN3 from a human placenta cDNA library. By screening a human placenta cDNA library with polyclonal antibodies raised against human PCOLN3 and using 5-prime RACE and primer extension strategies on the isolated cDNAs, Scott et al. (1996) cloned PCOLN3, which they called PRSM1. PRSM1 belongs to the gluzincin subfamily of metallopeptidases. The zincin superfamily comprises metallopeptidases that contain an HEXXH zinc-binding consensus sequence, and gluzincins have glutamic acid as a third zinc ligand. The full-length sequence of PRSM1 encodes a deduced 318-amino acid protein with an HELGH pentapeptide fitting the consensus sequence characteristic of zincins, and a glutamic acid 25 residues C-terminal of the first histidine, fitting the pattern of gluzincins for a third zinc-binding ligand. PRSM1 contains 3 clusters of cysteine residues: 1 cluster of 4 residues and 1 cluster of 6 residues at the N terminus, and a cluster of 6 residues at the C terminus. However, the predicted sequence lacks potential glycosylation sites. Immunoblot analysis of placenta revealed an approximately 30-kD protein. Northern blot analysis of human fibroblast culture mRNA detected a transcript of approximately 2.5 kb. By Northern blot analysis, Nomura et al. (1994) found that PRSM1, which they designated KIAA0047, was expressed ubiquitously, with highest levels in lung and kidney and in HeLa and KG-1 cell lines. By yeast 2-hybrid screening of a mouse embryo cDNA library using the mouse Polycomb group (PcG) protein Pcl1 (PHF1; 602881) as bait, followed by RT-PCR of human placenta RNA, Stauffer et al. (2001) cloned a variant of PRSM1 that they called CHMP1. CHMP1 uses an alternative reading frame distinct from that of PRSM1. The deduced 196-amino acid CHMP1 protein contains an N-terminal nuclear localization signal. CHMP1 is most closely related to CHMP1B (606486) and BC2 (CHMP2A; 610893), and more distantly related to S. cerevisiae proteins involved in vesicle trafficking. Western blot analysis of HEK293 human embryonic kidney cells showed a doublet of 32- and 35-kD CHMP1 proteins. Subcellular fractionation of HEK293 cells and several other human cell lines revealed that the 35-kD protein was exclusively nuclear, whereas the 32-kD protein was predominantly cytoplasmic, with a detectable level present in the nuclear fraction. Analysis of mouse whole tissue extracts showed that both Chmp1 proteins were widely expressed, with increased levels of the 35-kD form in heart, kidney, and liver. Mochida et al. (2012) found that the subcellular localization of CHMP1A appears to vary depending on cell type. In mouse embryonic 3T3 cells, Chmp1a was excluded from the nucleus where Bmi1 (164831) was detected. In human HEK 293T cells, CHMP1A showed prominent cytoplasmic and some nuclear immunoreactivity. Primary cultures of cerebellar granule cells from mice showed predominantly cytoplasmic ... More on the omim web site
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 164010 was added.