ID VME1_CVP67 Reviewed; 230 AA. AC Q8BB24; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JUN-2015, entry version 63. DE RecName: Full=Membrane protein; DE Short=M protein; DE AltName: Full=E1 glycoprotein; DE AltName: Full=Matrix glycoprotein; DE AltName: Full=Membrane glycoprotein; GN Name=M; OS Porcine hemagglutinating encephalomyelitis virus (strain 67N) OS (HEV-67N). OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus. OX NCBI_TaxID=230237; OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=12237422; RA Sasseville A.M.-J., Boutin M., Gelinas A.-M., Dea S.; RT "Sequence of the 3'-terminal end (8.1 kb) of the genome of porcine RT haemagglutinating encephalomyelitis virus: comparison with other RT haemagglutinating coronaviruses."; RL J. Gen. Virol. 83:2411-2416(2002). CC -!- FUNCTION: Component of the viral envelope that plays a central CC role in virus morphogenesis and assembly via its interactions with CC other viral proteins. {ECO:0000250}. CC -!- SUBUNIT: Homomultimer. Interacts with envelope E protein in the CC budding compartment of the host cell, which is located between CC endoplasmic reticulum and the Golgi complex. Forms a complex with CC HE and S proteins. Interacts with nucleocapsid N protein. This CC interaction probably participates in RNA packaging into the virus CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. Host Golgi apparatus membrane CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. CC Note=Largely embedded in the lipid bilayer. {ECO:0000250}. CC -!- PTM: O-linked glycans consist of Gal-GalNAc disaccharides which CC are modified with up to 2 sialic acid residues. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the coronaviruses M protein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY078417; AAL80035.1; -; Genomic_RNA. DR RefSeq; YP_459956.1; NC_007732.1. DR GeneID; 3882093; -. DR KEGG; vg:3882093; -. DR Proteomes; UP000007546; Genome. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW. DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW. DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW. DR GO; GO:0019058; P:viral life cycle; IEA:InterPro. DR InterPro; IPR002574; Corona_M. DR Pfam; PF01635; Corona_M; 1. PE 3: Inferred from homology; KW Complete proteome; Glycoprotein; Host Golgi apparatus; Host membrane; KW Host-virus interaction; KW Inhibition of host innate immune response by virus; KW Inhibition of host RLR pathway by virus; KW Inhibition of host TRAFs by virus; Membrane; Transmembrane; KW Transmembrane helix; Viral envelope protein; Viral immunoevasion; KW Viral matrix protein; Virion. FT CHAIN 1 230 Membrane protein. FT /FTId=PRO_0000106041. FT TOPO_DOM 1 28 Virion surface. {ECO:0000255}. FT TRANSMEM 29 45 Helical. {ECO:0000255}. FT TOPO_DOM 46 48 Intravirion. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TOPO_DOM 70 80 Virion surface. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TOPO_DOM 102 230 Intravirion. {ECO:0000255}. FT CARBOHYD 2 2 O-linked (GalNAc...); by host. FT {ECO:0000250}. FT CARBOHYD 3 3 O-linked (GalNAc...); by host. FT {ECO:0000250}. FT CARBOHYD 5 5 O-linked (GalNAc...); by host. FT {ECO:0000250}. FT CARBOHYD 6 6 O-linked (GalNAc...); by host. FT {ECO:0000250}. FT CARBOHYD 14 14 O-linked (GalNAc...); by host. FT {ECO:0000250}. FT CARBOHYD 28 28 O-linked (GalNAc...); by host. FT {ECO:0000250}. SQ SEQUENCE 230 AA; 26287 MW; 1820EFAE161F26C4 CRC64; MSSPTTPVPV ISWTADEAIK FLKEWNFSLG IIVLFITIIL QFGYTSRSMF VYVIKMVILW LMWPLTIILT IFNCVYALNN VYLGFSIVFT IVAIIMWVVY FVNSIRLFIR TGSWWSFNPE TNNLMCIDMK GRMYVRPIIE DYHTLTATII RGHLYIQGIK LGTGYSLSDL PAYVTVAKVT HLCTYKRGFL DRIGDTSGFA VYVKSKVGNY RLPSTHKGSG MDTALLRNNI //