VEMP_IBVK
ID VEMP_IBVK Reviewed; 109 AA.
AC P19744;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=Envelope small membrane protein {ECO:0000255|HAMAP-Rule:MF_04206};
DE Short=E protein {ECO:0000255|HAMAP-Rule:MF_04206};
DE Short=sM protein {ECO:0000255|HAMAP-Rule:MF_04206};
GN Name=E {ECO:0000255|HAMAP-Rule:MF_04206}; Synonyms=sM; ORFNames=3c;
OS Avian infectious bronchitis virus (strain KB8523) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11126;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2841803; DOI=10.1016/0042-6822(88)90603-4;
RA Sutou S., Sato S., Okabe T., Nakai M., Sasaki N.;
RT "Cloning and sequencing of genes encoding structural proteins of avian
RT infectious bronchitis virus.";
RL Virology 165:589-595(1988).
CC -!- FUNCTION: Plays a central role in virus morphogenesis and assembly.
CC Acts as a viroporin and self-assembles in host membranes forming
CC pentameric protein-lipid pores that allow ion transport. Also plays a
CC role in the induction of apoptosis. {ECO:0000255|HAMAP-Rule:MF_04206}.
CC -!- SUBUNIT: Homooligomer. Interacts with the M membrane protein in the
CC budding compartment of the host cell, which is located between
CC endoplasmic reticulum and the Golgi complex. The cytoplasmic tails of
CC both proteins are important for this function. Interacts with
CC Nucleoprotein. {ECO:0000255|HAMAP-Rule:MF_04206}.
CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04206}; Single-pass type III membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04206}. Note=The cytoplasmic tail functions
CC as a Golgi complex-targeting signal. {ECO:0000255|HAMAP-Rule:MF_04206}.
CC -!- SIMILARITY: Belongs to the gammacoronaviruses E protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04206}.
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DR EMBL; M21515; AAA66580.1; -; Genomic_RNA.
DR PIR; E29249; QQIHI1.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0044662; P:disruption by virus of host cell membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:InterPro.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04206; GAMMA_CORONA_E; 1.
DR InterPro; IPR003873; E_protein_CoV.
DR InterPro; IPR005296; IBV_3C.
DR Pfam; PF03620; IBV_3C; 1.
DR PROSITE; PS51926; COV_E; 1.
PE 3: Inferred from homology;
KW Apoptosis; Host Golgi apparatus; Host membrane; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..109
FT /note="Envelope small membrane protein"
FT /id="PRO_0000106079"
FT TOPO_DOM 1..11
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04206"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04206"
FT TOPO_DOM 33..109
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04206"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 109 AA; 12300 MW; 6BC6F8559754A553 CRC64;
MTNLLNKSLE ENGSFLTAVY IFVGFVALYL LGRALQAFVQ AADACCLFWY TWVVVPGAKG
TAFVYNHTYG KKLNKPELEA VVVNEFPKNG WNNKNPANFQ DVQRNKLYS