1.A.94.1.1 Non-structural glycoprotein 4, NSP4 or enterotoxin, of 175 aas and 2 TMSs (Hyser et al. 2012). A pentatmeric structure of a 53 aas NSP4 fragment has been solved (3MIW). NSP4 viroporin is involved in activation. It increases the endoplasmic reticulum (ER) permeability, resulting in decreased ER
calcium stores and activation of plasma membrane (PM) calcium influx
channels, ultimately causing the elevation in cytoplasmic
calcium (Hyser et al. 2013). It activates ER calcium store-operated calcium entry (Hyser et al. 2013). NSP4 VPD is a Ca2+/Ba2+-conducting cation-selective viroporin that transports monovalent and divalent cations equally well (Pham et al. 2017). It may be involved in particle production (Scott and Griffin 2015).
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Accession Number: | P04512 |
Protein Name: | Non-structural glycoprotein 4 |
Length: | 175 |
Molecular Weight: | 20267.00 |
Species: | Rotavirus A (strain SA11-Both G3-P5B[2]-I2-R2-C5-M5-A5-N2-T5-E2-H5) (RV-A) [37137] |
Number of TMSs: | 2 |
Location1 / Topology2 / Orientation3: |
Host rough endoplasmic reticulum membrane1 / Single-pass type III membrane protein2 |
Substrate |
monoatomic dication, calcium(2+), monoatomic monocation |
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1: MEKLTDLNYT LSVITLMNNT LHTILEDPGM AYFPYIASVL TGLFALNKAS IPTMKIALKT
61: SKCSYKVVKY CIVTIFNTLL KLAGYKEQIT TKDEIEKQMD RVVKEMRRQL EMIDKLTTRE
121: IEQVELLKRI YDKLTVQTTG EIDMTKEINQ KNVRTLEEWE SGKNPYEPRE VTAAM