ERp29 (also known as ERp28 and ERp31) is a ubiquitously expressed endoplasmic reticulum protein found in mammals []. This protein has an N-terminal thioredoxin-like domain, which is homologous to the domain of human protein disulphide isomerase (PDI). ERp29 may help mediate the chaperone function of PDI. The C-terminal Erp29 domain has a 5-helical bundle fold. ERp29 is thought to form part of the thyroglobulin folding complex []. The Drosophila homologue, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe [].
ERp29 (also known as ERp28 and ERp31) is a ubiquitously expressed endoplasmic reticulum protein found in mammals []. This protein has an N-terminal thioredoxin-like domain, which is homologous to the domain of human protein disulphide isomerase (PDI). ERp29 may help mediate the chaperone function of PDI. The C-terminal Erp29 domain has a 5-helical bundle fold. ERp29 is thought to form part of the thyroglobulin folding complex []. The Drosophila homologue, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe [].
ERp29 (also known as ERp28 and ERp31) is a ubiquitously expressed endoplasmic reticulum protein found in mammals []. This protein has an N-terminal thioredoxin-like domain, which is homologous to the domain of human protein disulphide isomerase (PDI). ERp29 may help mediate the chaperone function of PDI. The C-terminal Erp29 domain has a 5-helical bundle fold. ERp29 is thought to form part of the thyroglobulin folding complex []. The Drosophila homologue, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe [].
ERp29 () is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle [, ]. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organised into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI) []. However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that the function of ERp29 is similar to the chaperone function of PDI []. The N-terminal domain is exclusively responsible for the homodimerisation of the protein, without covalent linkages or additional contacts with other domains [].The Drosophila homologue, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase [].
Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2), where a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system, the NADP/thioredoxin system, and the glutathione/glutaredoxin system []. Several of these disulphide proteins share a common structure, consisting of a three-layer α/β/α core. Proteins that contain domains with a thioredoxin-like fold include:Arsenate reductase (ArsC) []Calsequestrin (contains three tandem repeats of this fold) []Circadian oscillation regulator KaiB []Disulphide bond isomerase DsbC and DsbG (C-terminal domain) [, ]Disulphide bond facilitator DsbA (contains an α-helical insertion) []Endoplasmic reticulum protein ERP29 (N-terminal domain) []Glutathione S-transferase (GST) (N-terminal domain) []Mitochondrial ribosomal protein L51/S25/CI-B8 domain (variable positions for Cys residues in active site) []Phosducin []Protein disulphide isomerase (PDI) (contains two tandem repeats of this fold) []Glutathione peroxidase-like enzymes []Selenoprotein W-related []SH3-binding glutamic acid-rich protein like (SH3BGR) (lacks both conserved Cys residues) []Spliceosomal protein U5-15Kd []Thioltransferases, including thioredoxin [], glutaredoxin [], hybrid peroxiredoxin hyPrx5 []Thioredoxin-like 2Fe-2S ferredoxin []
