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NSP4_ROTGA
ID   NSP4_ROTGA              Reviewed;         219 AA.
AC   Q5QGZ2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   29-SEP-2021, entry version 41.
DE   RecName: Full=Non-structural glycoprotein 4 {ECO:0000255|HAMAP-Rule:MF_04091};
DE            Short=NSP4 {ECO:0000255|HAMAP-Rule:MF_04091};
DE   AltName: Full=NCVP5 {ECO:0000255|HAMAP-Rule:MF_04091};
DE   AltName: Full=NS28 {ECO:0000255|HAMAP-Rule:MF_04091};
OS   Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B
OS   (isolate adult diarrhea rotavirus)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=10942;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15845266; DOI=10.1016/j.virusres.2005.02.005;
RA   Guzman E., McCrae M.A.;
RT   "Molecular characterization of the rotavirus NSP4 enterotoxin homologue
RT   from group B rotavirus.";
RL   Virus Res. 110:151-160(2005).
CC   -!- FUNCTION: Plays an essential role in the virus replication cycle by
CC       acting as a viroporin. Creates a pore in the host reticulum endoplasmic
CC       and as a consequence releases Ca(2+) in the cytoplasm of infected cell.
CC       In turn, high levels of cytoplasmic calcium trigger membrane
CC       trafficking and transport of viral ER-associated proteins to
CC       viroplasms, sites of viral genome replication and immature particle
CC       assembly. {ECO:0000255|HAMAP-Rule:MF_04091}.
CC   -!- FUNCTION: The secreted form acts as an enterotoxin that causes
CC       phospholipase C-dependent elevation of the intracellular calcium
CC       concentration in host intestinal mucosa cells. Increased concentration
CC       of intracellular calcium disrupts the cytoskeleton and the tight
CC       junctions, raising the paracellular permeability. Potentiates chloride
CC       ion secretion through a calcium ion-dependent signaling pathway,
CC       inducing age-dependent diarrhea. To perform this enterotoxigenic role
CC       in vivo, NSP4 is released from infected enterocytes in a soluble form
CC       capable of diffusing within the intestinal lumen and interacting with
CC       host plasma membrane receptors on neighboring epithelial cells such as
CC       integrins ITGA1/ITGB1 and ITGA2/ITGB1. {ECO:0000255|HAMAP-
CC       Rule:MF_04091}.
CC   -!- SUBUNIT: Homotetramer. Interacts with the immature particle in the
CC       viroplasm. Interacts with host CAV1, early and late in infection.
CC       Interacts with host integrin ITGA1/ITGB1 heterodimer. Interacts with
CC       host integrin ITGA2/ITGB1 heterodimer. Interaction with microtubules
CC       blocks trafficking to the Golgi apparatus. {ECO:0000255|HAMAP-
CC       Rule:MF_04091}.
CC   -!- SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola
CC       {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-
CC       Rule:MF_04091}. Note=NSP4 localizes also in vesicular structures which
CC       contain autophagosomal markers and associate with viroplasms in virus-
CC       infected cells. Additionally, a soluble form of glycosylated NSP4 is
CC       secreted despite retention of its transmembrane domain.
CC       {ECO:0000255|HAMAP-Rule:MF_04091}.
CC   -!- SIMILARITY: Belongs to the rotavirus NSP4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04091}.
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DR   EMBL; AY548957; AAT36306.1; -; Genomic_RNA.
DR   SMR; Q5QGZ2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044155; C:host caveola; IEA:UniProtKB-SubCell.
DR   GO; GO:0044169; C:host cell rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   HAMAP; MF_04091; ROTA_NSP4; 1.
DR   InterPro; IPR002107; Rotavirus_NSP4.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus; Enterotoxin; Glycoprotein;
KW   Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW   Ion channel; Ion transport; Membrane; Secreted; Signal-anchor; Toxin;
KW   Transmembrane; Transmembrane helix; Transport; Viral ion channel;
KW   Virulence.
FT   CHAIN           1..219
FT                   /note="Non-structural glycoprotein 4"
FT                   /id="PRO_0000369864"
FT   TOPO_DOM        1..47
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
FT   TRANSMEM        48..74
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
FT   TOPO_DOM        75..219
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
SQ   SEQUENCE   219 AA;  25347 MW;  9569C7E9763005BD CRC64;
     MAESSDMQEL FVQATYEEIL KLASSVNHEQ IRETISSSSP QKILTGTMLT LGALLTTLIV
     KKKGTKFLTT KVQSNVAYLA EMVVWKANQT VKTICDEVLH QRKVIEKLQC LDKMCSEIEK
     LRYDMEHFQG MDVTKELIQM CEQKMIDIDS KVKEVERSCD RRIRDYDWKI ATLTAHPTQQ
     LPAHIDIINQ HIEDDAETQI IQQHMNKQAR VKLNSRNRL
 
 
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