ID A0A679E1U2_9BETC Unreviewed; 230 AA. AC A0A679E1U2; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 14-DEC-2022, entry version 8. DE RecName: Full=Membrane protein {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; DE Short=M protein {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; DE AltName: Full=E1 glycoprotein {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; DE AltName: Full=Matrix glycoprotein {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; DE AltName: Full=Membrane glycoprotein {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; GN Name=M {ECO:0000256|HAMAP-Rule:MF_04202, GN ECO:0000256|RuleBase:RU363118, ECO:0000313|EMBL:BBM61122.1}; OS Bovine coronavirus. OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Betacoronavirus; Embecovirus. OX NCBI_TaxID=11128 {ECO:0000313|EMBL:BBM61122.1}; RN [1] {ECO:0000313|EMBL:BBM61122.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IWT-15 {ECO:0000313|EMBL:BBM61072.1}, IWT-16 RC {ECO:0000313|EMBL:BBM61122.1}, and IWT-21 RC {ECO:0000313|EMBL:BBM61112.1}; RA Suzuki T., Otake Y., Uchimoto S., Hasebe A., Goto Y.; RT "Genomic characterization and phylogenetic classification of bovine RT coronaviruses through whole genome sequence analysis."; RL Viruses 12:0-183(2020). 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:0000256|HAMAP-Rule:MF_04202, CC ECO:0000256|RuleBase:RU363118}. 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:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}. CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000256|HAMAP- CC Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; Multi-pass membrane CC protein {ECO:0000256|HAMAP-Rule:MF_04202, CC ECO:0000256|RuleBase:RU363118}. Virion membrane {ECO:0000256|HAMAP- CC Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; Multi-pass membrane CC protein {ECO:0000256|HAMAP-Rule:MF_04202, CC ECO:0000256|RuleBase:RU363118}. Note=Largely embedded in the lipid CC bilayer. {ECO:0000256|HAMAP-Rule:MF_04202}. CC -!- SIMILARITY: Belongs to the betacoronaviruses M protein family. CC {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04202}. 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; LC494141; BBM61072.1; -; Genomic_RNA. DR EMBL; LC494145; BBM61112.1; -; Genomic_RNA. DR EMBL; LC494146; BBM61122.1; -; Genomic_RNA. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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:0019049; P:mitigation of host antiviral defense response; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04202}; KW Host Golgi apparatus {ECO:0000256|HAMAP-Rule:MF_04202, KW ECO:0000256|RuleBase:RU363118}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04202, KW ECO:0000256|RuleBase:RU363118}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04202}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04202, KW ECO:0000256|RuleBase:RU363118}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04202, KW ECO:0000256|RuleBase:RU363118}; KW Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04202, KW ECO:0000256|RuleBase:RU363118}; KW Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04202}; KW Viral matrix protein {ECO:0000256|HAMAP-Rule:MF_04202, KW ECO:0000256|RuleBase:RU363118}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04202, ECO:0000256|RuleBase:RU363118}. FT TRANSMEM 25..45 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363118" FT TOPO_DOM 46..55 FT /note="Intravirion" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04202" FT TRANSMEM 57..78 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363118" FT TOPO_DOM 77..84 FT /note="Virion surface" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04202" FT TRANSMEM 84..102 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363118" SQ SEQUENCE 230 AA; 26290 MW; A1FE51BE75E8634D CRC64; MSSVTTPAPV YTWTADEAIK FLKEWNFSLG IILLFITVIL QFGYTSRSMF VYVIKMIILW LMWPLTIILT IFNCVYALNN VYLGFSIVFT IVAIIMWIVY FVNSIRLFIR TGSWWSFNPE TNNLMAIDMK GRMYVRPIIE DYHTLTVTII RGHLYLQGIK LGTGYSLSDL PAYVTVAKVS HLLTYKRGFL DKIGDTSGFA VYVKSKVGNY RLPSTQKGSG LDTALLRNNI //