TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
8.A.125.1.1









Clptm1 of 669 aas and 9 - 11 TMSs.  Plays a direct role in trafficking and activity of the GABAA receptor (TC 1.A.9.5.2) by binding to it (Ge et al. 2018)

Eukaryota
Metazoa
Clptm1 of Homo sapiens
8.A.125.1.2









ClptM1-like protein of 745 aas and 9 - 11 TMSs.

Eukaryota
Apicomplexa
Clptm1 of Plasmodium gonderi
8.A.125.1.3









Clptm1 of 593 aas and 9 - 11 TMSs.

Eukaryota
Viridiplantae
Clptm1 of Arabidopsis thaliana (Mouse-ear cress)
8.A.125.1.4









ClpM1 of 657 aas and ~ 9 TMSs.

Eukaryota
Fungi
ClpM1 of Neurospora crassa
8.A.125.1.5









Cleft lip and palate transmembrane protein 1-like protein, Clptm1L, of 538 aas and possibly 7 TMSs in a 1 (N-terminal) + 3 + 3 TMS arrangement.  It enhances cisplatin-mediated apoptosis, when overexpressed (Yamamoto et al. 2001). It is a lipid scramblase, required for efficient glycosylphosphatidylinositol biosynthesis (Wang et al. 2022). Scramblases translocate lipids across the lipid bilayer without consumption of ATP, thereby regulating lipid distributions in cellular membranes. Cytosol-to-lumen translocation across the endoplasmic reticulum (ER) membrane is a common process among lipid glycoconjugates involved in posttranslational protein modifications in eukaryotes. These translocations are thought to be mediated by specific ER-resident scramblases.  Wang et al. 2022 showed that CLPTM1L, an integral membrane protein with seven or eight putative TMSs, is the major lipid scramblase involved in efficient glycosylphosphatidylinositol biosynthesis in the ER membrane. These results validate the long-standing hypothesis that lipid scramblases ensure the efficient translocations of lipid glycoconjugates across the ER membrane for protein glycosylation pathways.

 

Eukaryota
Opisthokonta
CLPTM1L of Homo sapiens