TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(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