Calpain-1 catalytic subunit (CAPN1)
The protein contains 714 amino acids for an estimated molecular weight of 81890 Da.
Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (PubMed:21531719, PubMed:2400579). Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409' (PubMed:23707407). (updated: Feb. 10, 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.
- 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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| dbSNP:rs17885718 | |
| dbSNP:rs10895991 | |
| dbSNP:rs17883283 | |
| dbSNP:rs17884773 | |
| SPG76 |
Biological Process
Cornification
Extracellular matrix disassembly
Extracellular matrix organization
Mammary gland involution
Neutrophil degranulation
Positive regulation of cell population proliferation
Proteolysis
Receptor catabolic process
Regulation of catalytic activity
Regulation of macroautophagy
Regulation of NMDA receptor activity
Self proteolysis
The reference OMIM entry for this protein is 114220
Calpain 1; capn1
Calpain, large polypeptide l1
Calpain i, large subunit; canpl1
Calcium-activated neutral protease 1, catalytic subunit; canp1
DESCRIPTION
Calpain (calcium-dependent protease; EC 3.4.22.17) is an intracellular protease that requires calcium for its catalytic activity. Two isozymes, calpain I (mu-calpain) and calpain II (m-calpain), with different calcium requirements, have been identified. Both are heterodimers composed of L (large, catalytic, 80 kD) and S (small, regulatory, 30 kD) subunits. The isozymes share an identical S subunit (CAPNS1; 114170), with the differences arising from the L subunits, L1 (CAPN1) and L2 (CAPN2; 114230) (summary by Ohno et al., 1990).GENE FUNCTION
By quantitative RT-PCR, Ueyama et al. (1998) found that expression of calpain-1 and calpain-2 mRNA was significantly increased in muscle biopsy samples derived from 5 men with progressive muscular dystrophy (e.g., DMD; 310200) and 2 men and 3 women with amyotrophic lateral sclerosis (ALS; 105400) compared with controls. Using cell biologic, pharmacologic, and genetic methods, Chandramohanadas et al. (2009) found that the apicomplexan parasites Plasmodium falciparum and Toxoplasma gondii, the causative agents of malaria and toxoplasmosis, respectively, used host cell calpains to facilitate parasite egress. Immunodepletion and inhibition experiments showed that calpain-1 was required for escape of P. falciparum from human erythrocytes. Similarly, elimination of both calpain-1 and calpain-2 via small interfering RNA against the common regulatory subunit CAPNS1 in human osteosarcoma cells or deletion of Capns1 in mouse embryonic fibroblasts blocked egress of T. gondii. Chandramohanadas et al. (2009) concluded that P. falciparum and T. gondii both exploit host cell calpains to facilitate escape from intracellular parasitophorous vacuoles and/or the host plasma membrane, a process required for parasite proliferation.MAPPING
Using cDNA clones as probes, Ohno et al. (1989, 1990) mapped the CANPL1 and CANPL2 genes as well as the CANPS gene and a gene for another protein, L3 (CAPN3; 114240), that is homologous to the other 2 L subunits. They used a combination of spot-blot hybridization with sorted chromosomes and Southern hybridization with human-mouse cell hybrid DNAs. In this way they were able to assign CANPL1 to chromosome 11, CANPL2 to chromosome 1, CANPL3 to chromosome 15, and CANPS to chromosome 19. Courseaux et al. (1996) used a combination of methods to refine maps of an approximately 5-Mb region of 11q13. They mapped the CAPN1 gene within this region, telomeric to the FAU gene (134690) and centromeric to the MLK3 (MAP3K11; 600050) and RELA (164014) genes. ... More on the omim web site
Feb. 16, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
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
Oct. 26, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 114220 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed