VME1_MERS1
ID VME1_MERS1 Reviewed; 219 AA.
AC K9N7A1;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Membrane protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE Short=M protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=E1 glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=Matrix glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=Membrane glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
GN Name=M {ECO:0000255|HAMAP-Rule:MF_04202}; ORFNames=5;
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 SUBCELLULAR LOCATION.
RX PubMed=24318862; DOI=10.1007/s13238-013-3096-8;
RA Yang Y., Zhang L., Geng H., Deng Y., Huang B., Guo Y., Zhao Z., Tan W.;
RT "The structural and accessory proteins M, ORF 4a, ORF 4b, and ORF 5 of
RT Middle East respiratory syndrome coronavirus (MERS-CoV) are potent
RT interferon antagonists.";
RL Protein Cell 4:951-961(2013).
CC -!- FUNCTION: Component of the viral envelope that plays a central role in
CC virus morphogenesis and assembly via its interactions with other viral
CC proteins. {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000255|PROSITE-
CC ProRule:PRU01275}.
CC -!- SUBUNIT: Homomultimer. Interacts with envelope E protein in the budding
CC compartment of the host cell, which is located between endoplasmic
CC reticulum and the Golgi complex. Forms a complex with HE and S
CC proteins. Interacts with nucleocapsid N protein. This interaction
CC probably participates in RNA packaging into the virus.
CC {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000255|PROSITE-ProRule:PRU01275,
CC ECO:0000269|PubMed:24318862}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04202, ECO:0000269|PubMed:24318862}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_04202}. Note=Largely embedded in the
CC lipid bilayer. {ECO:0000255|HAMAP-Rule:MF_04202}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses M protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
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DR EMBL; KC164505; AFY13313.1; -; Genomic_RNA.
DR SMR; K9N7A1; -.
DR BioGRID; 4383876; 17.
DR IntAct; K9N7A1; 18.
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:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-UniRule.
DR GO; GO:0039501; P:suppression by virus of host type I interferon production; IDA:UniProtKB.
DR CDD; cd21567; MERS-like-CoV_M; 1.
DR HAMAP; MF_04202; BETA_CORONA_M; 1.
DR InterPro; IPR002574; M_CoV.
DR InterPro; IPR044363; M_MERS-like-CoV.
DR Pfam; PF01635; CoV_M; 1.
DR PROSITE; PS51927; COV_M; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Transmembrane; Transmembrane helix; Viral envelope protein;
KW Viral immunoevasion; Viral matrix protein; Virion.
FT CHAIN 1..219
FT /note="Membrane protein"
FT /id="PRO_0000422469"
FT TOPO_DOM 1..18
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 40..49
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 71..78
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 100..219
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
SQ SEQUENCE 219 AA; 24537 MW; 29E642389677638F CRC64;
MSNMTQLTEA QIIAIIKDWN FAWSLIFLLI TIVLQYGYPS RSMTVYVFKM FVLWLLWPSS
MALSIFSAVY PIDLASQIIS GIVAAVSAMM WISYFVQSIR LFMRTGSWWS FNPETNCLLN
VPFGGTTVVR PLVEDSTSVT AVVTNGHLKM AGMHFGACDY DRLPNEVTVA KPNVLIALKM
VKRQSYGTNS GVAIYHRYKA GNYRSPPITA DIELALLRA
