VME1_FIPV
ID VME1_FIPV Reviewed; 262 AA.
AC P25878; Q4U5F8; Q52PA8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 23-FEB-2022, entry version 94.
DE RecName: Full=Membrane protein {ECO:0000255|HAMAP-Rule:MF_04201};
DE Short=M protein {ECO:0000255|HAMAP-Rule:MF_04201};
DE AltName: Full=E1 glycoprotein {ECO:0000255|HAMAP-Rule:MF_04201};
DE AltName: Full=Matrix glycoprotein {ECO:0000255|HAMAP-Rule:MF_04201};
DE AltName: Full=Membrane glycoprotein {ECO:0000255|HAMAP-Rule:MF_04201};
GN Name=M {ECO:0000255|HAMAP-Rule:MF_04201}; ORFNames=5;
OS Feline coronavirus (strain FIPV WSU-79/1146) (FCoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33734;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1847259; DOI=10.1016/0042-6822(91)90499-2;
RA Vennema H., de Groot R.J., Harbour D.A., Horzinek M.C., Spaan W.J.M.;
RT "Primary structure of the membrane and nucleocapsid protein genes of feline
RT infectious peritonitis virus and immunogenicity of recombinant vaccinia
RT viruses in kittens.";
RL Virology 181:327-335(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16033972; DOI=10.1099/vir.0.80985-0;
RA Dye C., Siddell S.G.;
RT "Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146.";
RL J. Gen. Virol. 86:2249-2253(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J.,
RA Rottier P.J.M., de Groot R.J.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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_04201, 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_04201, ECO:0000255|PROSITE-
CC ProRule:PRU01275}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04201}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04201}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04201}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04201}. Note=Largely embedded in the lipid bilayer.
CC {ECO:0000255|HAMAP-Rule:MF_04201}.
CC -!- SIMILARITY: Belongs to the alphacoronaviruses M protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04201}.
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DR EMBL; X56496; CAA39850.1; -; Genomic_RNA.
DR EMBL; DQ010921; AAY32598.1; -; Genomic_RNA.
DR EMBL; AY994055; AAY16379.1; -; Genomic_RNA.
DR PIR; A38498; MFIH79.
DR RefSeq; YP_004070198.1; NC_002306.3.
DR SMR; P25878; -.
DR GeneID; 10040185; -.
DR KEGG; vg:10040185; -.
DR Proteomes; UP000000835; Genome.
DR Proteomes; UP000140386; 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; cd21564; alphaCoV_M; 1.
DR HAMAP; MF_04201; ALPHA_CORONA_M; 1.
DR InterPro; IPR042551; ALPHA_CORONA_M.
DR InterPro; IPR002574; M_CoV.
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; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral matrix protein; Virion.
FT CHAIN 1..262
FT /note="Membrane protein"
FT /id="PRO_0000037158"
FT TOPO_DOM 19..47
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT TOPO_DOM 69..77
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT TOPO_DOM 99..112
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT TOPO_DOM 134..262
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT REGION 237..252
FT /note="Interaction with N protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04201"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine; by host"
SQ SEQUENCE 262 AA; 29832 MW; 9D983B8C47A32CDA CRC64;
MKYILLILAC IIACVYGERY CAMQDSGLQC INGTNSRCQT CFERGDLIWH LANWNFSWSV
ILIVFITVLQ YGRPQFSWLV YGIKMLIMWL LWPIVLALTI FNAYSEYQVS RYVMFGFSVA
GAVVTFALWM MYFVRSVQLY RRTKSWWSFN PETNAILCVN ALGRSYVLPL DGTPTGVTLT
LLSGNLYAEG FKMAGGLTIE HLPKYVMIAT PSRTIVYTLV GKQLKATTAT GWAYYVKSKA
GDYSTEARTD NLSEHEKLLH MV
