VME1_CVHOC
ID VME1_CVHOC Reviewed; 230 AA.
AC Q01455; Q6TNF6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=6;
OS Human coronavirus OC43 (HCoV-OC43).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=31631;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND GLYCOSYLATION AT SER-2; SER-3;
RP THR-5; THR-6; THR-14 AND SER-28.
RX PubMed=1402806; DOI=10.1099/0022-1317-73-10-2731;
RA Mounir S., Talbot P.J.;
RT "Sequence analysis of the membrane protein gene of human coronavirus OC43
RT and evidence for O-glycosylation.";
RL J. Gen. Virol. 73:2731-2736(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759, and Isolate clinical OC43-Paris;
RX PubMed=15280490; DOI=10.1128/jvi.78.16.8824-8834.2004;
RA St Jean J.R., Jacomy H., Desforges M., Vabret A., Freymuth F., Talbot P.J.;
RT "Human respiratory coronavirus OC43: genetic stability and neuroinvasion.";
RL J. Virol. 78:8824-8834(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759;
RX PubMed=15650185; DOI=10.1128/jvi.79.3.1595-1604.2005;
RA Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P.,
RA Vandamme A.M., Van Ranst M.;
RT "Complete genomic sequence of human coronavirus OC43: molecular clock
RT analysis suggests a relatively recent zoonotic coronavirus transmission
RT event.";
RL J. Virol. 79:1595-1604(2005).
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-
CC ProRule:PRU01275}.
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}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04202}. Note=Largely embedded in the lipid bilayer.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
CC -!- PTM: O-linked glycans consist of Gal-GalNAc disaccharides which are
CC modified with up to 2 sialic acid residues.
CC {ECO:0000269|PubMed:1402806}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses M protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
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DR EMBL; M93390; AAA45462.1; -; Genomic_RNA.
DR EMBL; AY585229; AAT84365.1; -; Genomic_RNA.
DR EMBL; AY585228; AAT84357.1; -; Genomic_RNA.
DR EMBL; AY391777; AAR01018.1; -; Genomic_RNA.
DR PIR; JQ1749; JQ1749.
DR iPTMnet; Q01455; -.
DR Proteomes; UP000007552; Genome.
DR Proteomes; UP000100580; Genome.
DR Proteomes; UP000180344; Genome.
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 CDD; cd21568; HCoV-like_M; 1.
DR HAMAP; MF_04202; BETA_CORONA_M; 1.
DR InterPro; IPR002574; M_CoV.
DR InterPro; IPR044362; M_HCoV-like.
DR Pfam; PF01635; CoV_M; 1.
DR PROSITE; PS51927; COV_M; 1.
PE 1: Evidence at protein level;
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..230
FT /note="Membrane protein"
FT /id="PRO_0000106033"
FT TOPO_DOM 1..24
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 46..55
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 77..84
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 106..228
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT CARBOHYD 2
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000269|PubMed:1402806"
FT CARBOHYD 3
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000269|PubMed:1402806"
FT CARBOHYD 5
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:1402806"
FT CARBOHYD 6
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:1402806"
FT CARBOHYD 14
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:1402806"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000269|PubMed:1402806"
FT VARIANT 167
FT /note="W -> L (in strain: Isolate ATCC VR-759 and Isolate
FT clinical OC43-Paris)"
SQ SEQUENCE 230 AA; 26418 MW; 4E5C6E9400FB7C18 CRC64;
MSSKTTPAPV YIWTADEAIK FLKEWNFSLG IILLFITIIL QFGYTSRSMF VYVIKMIILW
LMWPLTIILT IFNCVYALNN VYLGLSIVFT IVAIIMWIVY FVNSIRLFIR TGSFWSFNPE
TNNLMCIDMK GTMYVRPIIE DYHTLTVTII RGHLYIQGIK LGTGYSWADL PAYMTVAKVT
HLCTYKRGFL DRISDTSGFA VYVKSKVGNY RLPSTQKGSG MDTALLRNNI
