| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
9.B.188.1.1 | The transmembrane (2 TMSs, N- and C-termini) Emp24 domain-containing protein 1, TMED1 of 227 aas. | Eukaryota |
Metazoa | TMED1 of Homo sapiens |
|
9.B.188.1.2 | The transmembrane (2 TMSs, N- and C-termini) Emp24 domain-containing protein 2, TMED2 or RNP24 of 201 aas. A role for TMED2 in liver health has been suggested (Hou et al. 2017). The structure, topology, and dynamics of membrane-inserted polypeptides and lipids have been examined by solid-state NMR spectroscopy, specifically with respect to the transmembrane domains of the DQ Beta-1 subunit of the MHC II receptor and the COP I protein, p24 (Salnikov et al. 2019). The role of the p24/transmembrane emp24 domain (TMED) family of cargo receptors in development and disease has been reviewed (Aber et al. 2019). TMED2/emp24 is required in both the chorion and the allantois for placental labyrinth layer development involving membrane fusion (Hou and Jerome-Majewska 2018). Circular RNA circ_0008305 aggravates hepatocellular carcinoma growth through binding to miR-186 and inducing TMED2 (Zhang et al. 2022). | Eukaryota |
Metazoa | TMED2 of Homo sapiens |
|
9.B.188.1.3 | The transmembrane (2 TMSs, N- and C-termini) Emp24 domain-containing protein 3, TMED3 of 217 aas. | Eukaryota |
Metazoa | TMED3 of Homo sapiens |
|
9.B.188.1.4 | Transmembrane emp24 domain-containing protein 10 precursor, Tmed10 or TMP21, of 219 aas and 2 TMSs, N- and C-terminal. It is involved in vesicular protein trafficking in the early secretory pathway, probably as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles (Luo et al. 2011). The TMP21 transmembrane domain promotes its association with the presenilin complex that results in decreased gamma-cleavage activity (Pardossi-Piquard et al. 2009). Thus, TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity (Chen et al. 2006). TMP21 modulates cell growth of papillary thyroid cancer cells by inducing autophagy through activation of the AMPK/mTOR pathway (Xu et al. 2015). TMED2 may regulate inflammation in lung adenocarcinoma (LUAD) through the TLR4/NF-kappaB signaling pathway and enhance the proliferation, development, and prognosis of LUAD by regulating inflammation (Feng et al. 2022).
| Eukaryota |
Metazoa | Tmed10 of Homo sapiens |
|
9.B.188.1.5 | Transmembrane emp24 domain-containing protein, eclair or Eca, of 216 aas and 2 TMSs, N- and C-terminal. Eca and Bai are essential, though not redundant, for dorsoventral patterning of the embryo. They are required during early embryogenesis for the activity of maternal Tkv receptor (TC# 8.B.23.1.27), while the zygotic Tkv is not affected (Bartoszewski et al. 2004). It may also be involved in Golgi organization (Kondylis et al. 2011). Ecla and Bai are involved in the early secretory pathway of Wingless/Wnt, but only Bai interacts with wingless (Wg) (Li et al. 2015). | Eukaryota |
Metazoa | EMP24 of Drosophila melanogaster (Fruit fly) |
|
9.B.188.1.6 | Transmembrane emp24 domain-containing protein Baiser or Bai, of 206 aas and 2 TMSs, N- and C-terminal. Eca (TC# 9.B.188.1.5) and Bai are essential, though not redundant, for dorsoventral patterning of the embryo (Bartoszewski et al. 2004). They are specifically required during early embryogenesis for the activity of the maternal Kkv receptor, while the zygotic Tkv is not affected. Ecla and Bai are involved in the early secretory pathway of Wingless/Wnt, but only Bai interacts with wingless (Wg) (Li et al. 2015). | Eukaryota |
Metazoa | Bai of Drosophila melanogaster |
|
9.B.188.1.7 | p24 protein (EMP24-1; GP25) of 210 aas and 2 TMSs, N- and C-terminal. It is a cargo receptor involved in ER to golgi vesticle transport (Carney and Bowen 2004). The p24/transmembrane emp24 domain (TMED) family of cargo receptors has been shown to be important in development and disease (Aber et al. 2019). | Eukaryota |
Metazoa | p24 of Drosophila melanogaster (Fruit fly) |
|
9.B.188.1.8 | Transmembrane emp24 domain-containing protein 7, TMED7, of 224 aas and 2 TMSs, N- and C-terminal. It plays a role in vesicular protein trafficking, mainly in
the early secretory pathway. It appears to function in the biosynthesis
of secreted cargo including processing and post-translational
modifications and thereby in embyogenesis (Nie et al. 2020). | Eukaryota |
Opisthokonta | TMED7 of Homo sapiens |
|
9.B.188.1.9 | Transmembrane emp24 domain-containing protein 9 of 235 aas and 2 TMSs, N- and C-terminal, TMED9. The secretory pathway is an intracellular highway for the vesicular transport of newly synthesized proteins that span the ER, Golgi, lysosomes and cell surface. A variety of cargo receptors, chaperones, and quality control proteins maintain the smooth flow of cargo along this route. Among these is vesicular transport protein TMED9, which belongs to the p24/transmembrane emp24 domain (TMED) family of proteins. It is expressed across vertebrate species (Roberts and Satpute-Krishnan 2022). The TMED family consists of structurally-related type I transmembrane proteins with a luminal N-terminal Golgi-dynamics domain, a luminal coiled-coil domain, a transmembrane domain and a short cytosolic C-terminal tail that binds COPI and COPII coat proteins. TMED9, like other members of the TMED family, was first identified as an abundant constituent of the COPI and COPII coated vesicles that mediate traffic between the ER and the Golgi. TMED9 is typically purified in hetero-oligomers together with TMED family members, suggesting that it may function as part of a complex. TMED family members play various roles in secretory pathway homeostasis including secreted protein processing, quality control and degradation of misfolded proteins, and post-Golgi trafficking. In particular, TMED9 has been implicated in autophagy, lysosomal sorting, viral replication and cancer (Roberts and Satpute-Krishnan 2022). | Eukaryota |
Opisthokonta | TMED9 of Homo sapiens |