TRAPPC6A (trafficking protein particle complex 6A), also known as TRS33 or HSPC289, is a 159 amino acid protein that localizes to the Golgi apparatus and endoplasmic reticulum. Belonging to the TRAPP small subunits family and the BET3 subfamily, TRAPPC6A may play a role in vesicular transport during the biogenesis of melanosomes. TRAPPC6A is part of the multisubunit TRAPP tethering complex, which acts as a GTP exchange factor. TRAPPC6A exists as a heterodimer with TRAPPC3 and undergoes alternative splicing to produce two isoforms. TRAPPC6A is encoded by a gene located on human chromosome 19, which consists of approximately 63 million bases and makes up over 2% of human genomic DNA.
The transport protein particle (TRAPP) complex was initially identified as a tethering factor for COPII vesicle. Subsequently, three forms (TRAPPI, II, and III) have been found and TRAPPIII has been reported to serve as a regulator in autophagy. This study investigates a new role of mammalian TRAPPIII in ciliogenesis. We found a ciliopathy protein, oral-facial-digital syndrome 1 (OFD1), interacting with the TRAPPIII-specific subunits TRAPPC8 and TRAPPC12. TRAPPC8 is necessary for the association of OFD1 with pericentriolar material 1 (PCM1).
Trefoil Factor 1 (TFF1) belongs to the three structurally related secreted proteins that contain trefoil domains. TFF1 is an approximately 7 kDa peptide that plays an important role in epithelial regeneration and wound healing. It is highly expressed in goblet cells of the gastric and intestinal mucosa and by conjunctival goblet cells. By conserving intrachain disulfide bonds, human TFF1 formed a three-leaved conformation held together.It is a copper-binding protein that can form disulfide-linked homodimers, associate into disulfide-linked complexes with Gastrokine 2, and form non-covalent complexes with the mucin MUC5AC. TFF1 is down-regulated during the progression from gastritis to gastric dysplasia to gastric cancer, although it is up-regulated in breast and prostate cancers.
Trefoil Factor 2 (TFF2) is a member of the trefoil family and contains two P-type (trefoil) domains. Members of this family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. TFF2 is a secreted protein and specifically expressed in the stomach. TFF2 inhibits gastrointestinal motility and gastric acid secretion. TFF2 could function as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains.
Trefoil Factor 3 (TFF3) is one of three trefoil peptides secreted by epithelial cells that line mucus membranes. Trefoils contribute to protection and repair of the gastrointestinal tract. TFF3 is secreted by mucus-producing goblet cells in the large and small intestines and lower respiratory tract. It is mainly active as a disulfide-linked homodimer. The mature 59 aa, 6.5 kDa human TFF3 contains one trefoil structure formed by intramolecular disulfides and shows 76% aa identity with mouse TFF3.
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