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VEMP_MERS1
ID   VEMP_MERS1              Reviewed;          82 AA.
AC   K9N5R3;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   23-FEB-2022, entry version 42.
DE   RecName: Full=Envelope small membrane protein {ECO:0000255|HAMAP-Rule:MF_04204};
DE            Short=E protein {ECO:0000255|HAMAP-Rule:MF_04204};
DE            Short=sM protein {ECO:0000255|HAMAP-Rule:MF_04204};
GN   Name=E {ECO:0000255|HAMAP-Rule:MF_04204}; Synonyms=sM; ORFNames=4;
OS   Middle East respiratory syndrome-related coronavirus (isolate United
OS   Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Merbecovirus.
OX   NCBI_TaxID=1263720;
OH   NCBI_TaxID=9838; Camelus dromedarius (Dromedary) (Arabian camel).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=23078800;
RA   Bermingham A., Chand M.A., Brown C.S., Aarons E., Tong C., Langrish C.,
RA   Hoschler K., Brown K., Galiano M., Myers R., Pebody R.G., Green H.K.,
RA   Boddington N.L., Gopal R., Price N., Newsholme W., Drosten C.,
RA   Fouchier R.A., Zambon M.;
RT   "Severe respiratory illness caused by a novel coronavirus, in a patient
RT   transferred to the United Kingdom from the Middle East, September 2012.";
RL   Eurosurveillance 17:20290-20290(2012).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=25733052; DOI=10.1016/j.virusres.2015.02.023;
RA   Surya W., Li Y., Verdia-Baguena C., Aguilella V.M., Torres J.;
RT   "MERS coronavirus envelope protein has a single transmembrane domain that
RT   forms pentameric ion channels.";
RL   Virus Res. 201:61-66(2015).
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_04204,
CC       ECO:0000269|PubMed:25733052}.
CC   -!- SUBUNIT: Homopentamer. Interacts with membrane protein M in the budding
CC       compartment of the host cell, which is located between endoplasmic
CC       reticulum and the Golgi complex. Interacts with Nucleoprotein.
CC       {ECO:0000255|HAMAP-Rule:MF_04204, ECO:0000269|PubMed:25733052}.
CC   -!- INTERACTION:
CC       K9N5R3; Q8N448: LNX2; Xeno; NbExp=2; IntAct=EBI-26374535, EBI-2340947;
CC       K9N5R3; O95049: TJP3; Xeno; NbExp=2; IntAct=EBI-26374535, EBI-1171427;
CC   -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04204}; Single-pass type III membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04204}. Note=The cytoplasmic tail functions
CC       as a Golgi complex-targeting signal. {ECO:0000255|HAMAP-Rule:MF_04204}.
CC   -!- SIMILARITY: Belongs to the betacoronaviruses E protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04204}.
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DR   EMBL; KC164505; AFY13312.1; -; Genomic_RNA.
DR   BioGRID; 4383877; 39.
DR   IntAct; K9N5R3; 39.
DR   TCDB; 1.A.65.1.4; the coronavirus viroporin e protein (viroporin e) family.
DR   Proteomes; UP000139997; Genome.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IDA:UniProtKB.
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   CDD; cd21533; MERS-CoV-like_E; 1.
DR   HAMAP; MF_04204; BETA_CORONA_E; 1.
DR   InterPro; IPR044379; E_MERS-CoV-like.
DR   InterPro; IPR043506; E_protein_bCoV.
DR   InterPro; IPR003873; E_protein_CoV.
DR   Pfam; PF02723; CoV_E; 1.
DR   PROSITE; PS51926; COV_E; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Host Golgi apparatus; Host membrane; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..82
FT                   /note="Envelope small membrane protein"
FT                   /id="PRO_0000422468"
FT   TOPO_DOM        1..16
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04204"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04204"
FT   TOPO_DOM        38..78
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04204"
SQ   SEQUENCE   82 AA;  9354 MW;  3B135F09A5C7361F CRC64;
     MLPFVQERIG LFIVNFFIFT VVCAITLLVC MAFLTATRLC VQCMTGFNTL LVQPALYLYN
     TGRSVYVKFQ DSKPPLPPDE WV
 
 
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