TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
8.A.165.1.1 | Calnexin (CANX) of 627 aas and 2 TMSs, one at the N-terminus, and one near the C-terminus. It is a calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum (ER). It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. It is associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, and may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse. (See family description for more details). Calnexin aids in the folding of transport proteins (see TC#s 2.A.22.2.10 and 9.A.49.1.2 and 3) and in the proper insertion of ER membrane glycoproteins via the general secretory pathway (TC# 3.A.5) (Lee et al. 2020). The ER protein CANX (calnexin)-mediates autophagy and protects against alzheimer disease (AD) (Shen et al. 2025). | Eukaryota |
Metazoa, Chordata | CONX of Homo sapiens |
8.A.165.1.2 | Calreticulin (CRT) of 417 aas and one N-terminal TMS. Calreticulin is a sugar-binding protein chaparone (a lectin-like chaperone) that functions in peptide-loading to the major histocompatibility complex encoded class I (MHC-I) molecules (Margulies et al. 2020). The uterine sacroplasmic reticulum (SR) takes up and stores calcium [Ca], using the SERCA ATPase and the Ca-buffering proteins, calsequestrin and calreticulin. This stored Ca can be released via IP(3)-gated Ca channels (Noble et al. 2009), so calreticulin serves as an intermediate between the SERCA ATPase and Ca channels such as IP930-gated channels. The pre-apoptotic translocation of intracellular calreticulin (endo-CRT) to the plasma membrane surface (ecto-CRT) is critical for the recognition and engulfment of dying tumor cells by dendritic cells (Obeid et al. 2007). | Eukaryota |
Metazoa, Chordata | CRT of Homo sapiens |
8.A.165.1.3 | Calreticulin family protein of 437 aas and 4 TMSs, three N-terminal and one C-terminal. The similarity with other members of the family are in the central hydrophilc region of the protein. | Eukaryota |
Apicomplexa | Calreticulin-like protein of Toxoplasma gondii |
8.A.165.1.4 | Uncharacterized protein of 382 aas and at least two TMSs, N- and C-terminal. | Eukaryota |
Fungi, Ascomycota | UP of Candida glabrata |
8.A.165.1.5 | Uncharacterized protein of 382 aas and 0 TM | Eukaryota |
Viridiplantae, Streptophyta | UP of Prunus mume |
8.A.165.1.6 | Calreticulin family protein of 682 aas and 3 TMSs, 1 (or 2) N-terminal and 2 C-terminal. | Eukaryota |
Apicomplexa | Calreticulin family protein of Cystoisospora suis |
8.A.165.1.7 | Sphingomyelin phosphodiesterase 2 of 563 aas and 3 TMSs, one N-terminal and two at residues 320 - 365. | Eukaryota |
Metazoa, Arthropoda | SPD2 of Trichonephila clavipes |