Chitinase domain-containing protein 1 (CHID1)
The protein contains 393 amino acids for an estimated molecular weight of 44941 Da.
Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro). (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- 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.
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:rs1127800 | |
| dbSNP:rs6682 |
No binding partner found
Biological Process
Carbohydrate metabolic process
Chitin catabolic process
Innate immune response
Negative regulation of cytokine production involved in inflammatory response
Platelet degranulation
The reference OMIM entry for this protein is 615692
Chitinase domain-containing protein 1; chid1
Stabilin 1-interacting chitinase-like protein; siclp
DESCRIPTION
Mammalian GLYCO18 domain-containing proteins include catalytically active chitinases (e.g., CHIT1; 600031) and chitinase-like proteins (e.g., CHI3L1; 601525) with cytokine activity involved in host defense and Th2 inflammatory reactions. CHID1 is a GLYCO18 domain-containing protein that lacks catalytic amino acids and a chitin-binding domain. CHID1 interacts with the endocytic/sorting receptor stabilin-1 (STAB1; 608560) and is present in late endosomes and secretory lysosomes in alternatively activated macrophages (Kzhyshkowska et al., 2006).CLONING
Using a yeast 2-hybrid screen of a placenta cDNA library with STAB1 as bait, followed by database analysis, Kzhyshkowska et al. (2006) identified human CHID1, which they called SICLP. The deduced 393-amino acid protein has a calculated molecular mass of 44.9 kD. It contains an N-terminal signal sequence and a GLYCO18-like domain, but it lacks a chitin-binding domain and catalytic amino acids. Western blot analysis showed high expression of 33- and 39-kD proteins in human monocyte, embryonic kidney, and B-cell lines, as well as in human bronchoalveolar lavage and peripheral blood cells, but only low levels were detected in T-cell and epithelial cell lines. Immunofluorescence and confocal microscopy demonstrated localization of SICLP in LAMP1 (153330)-positive/CD63 (155740)-positive lysosomes and p62 (SQSTM1; 601530)-positive late endosomes.GENE FUNCTION
Using protein pull-down assays, Kzhyshkowska et al. (2006) confirmed interaction between STAB1 and SICLP and showed that the interaction occurred through fasciclin domain-7 of STAB1. RT-PCR analysis showed upregulated expression of CHID1 in human macrophages after stimulation with IL4 (147780) and/or dexamethasone and revealed that IFNG (147570) suppressed this effect. Knockdown of STAB1 resulted in decreased sorting of CHID1 from late Golgi compartments to lysosomes. Kzhyshkowska et al. (2006) concluded that CHID1 is a chitinase-like secreted protein that interacts with STAB1.BIOCHEMICAL FEATURES
Using the hanging-drop vapor diffusion method, Meng et al. (2009) generated crystal images of SICLP at 2.7-angstrom resolution. Further analysis of the structure by Meng et al. (2010) showed a typical triose-phosphate isomerase barrel fold with an atypically wide and open saccharide-binding cleft. Binding studies indicated a preference for chitotetraose and a capacity to bind lipopolysaccharide (LPS) and neutralize its endotoxin effect on macrophages. Meng et al. (2010) proposed that SICLP may play a role in pathogen sensing.MAPPING
Gross (2014) mapped the CHID1 gene to chromosome 11p15.5 based on an alignment of the CHID1 sequence (GenBank GENBANK BC000001) with the genomic sequence (GRCh37). ... More on the omim web site
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 615692 was added.