VME1_CVPPU
ID VME1_CVPPU Reviewed; 262 AA.
AC P04135;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 23-FEB-2022, entry version 111.
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 Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=11151;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2841792; DOI=10.1016/0042-6822(88)90581-8;
RA Kapke P.A., Tung F.Y.T., Hogue B.G., Brian D.A., Woods R.D., Wesley R.;
RT "The amino-terminal signal peptide on the porcine transmissible
RT gastroenteritis coronavirus matrix protein is not an absolute requirement
RT for membrane translocation and glycosylation.";
RL Virology 165:367-376(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3035066; DOI=10.1099/0022-1317-68-6-1687;
RA Laude H., Rasschaert D., Huet J.-C.;
RT "Sequence and N-terminal processing of the transmembrane protein E1 of the
RT coronavirus transmissible gastroenteritis virus.";
RL J. Gen. Virol. 68:1687-1693(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2825819; DOI=10.1016/0300-9084(87)90178-7;
RA Rasschaert D., Gelfi J., Laude H.;
RT "Enteric coronavirus TGEV: partial sequence of the genomic RNA, its
RT organization and expression.";
RL Biochimie 69:591-600(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate PUR46-MAD;
RX PubMed=10805807; DOI=10.1073/pnas.97.10.5516;
RA Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E., Plana-Duran J.,
RA Enjuanes L.;
RT "Engineering the largest RNA virus genome as an infectious bacterial
RT artificial chromosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5516-5521(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 157-262.
RX PubMed=3008432; DOI=10.1016/0042-6822(86)90102-9;
RA Kapke P.A., Brian D.A.;
RT "Sequence analysis of the porcine transmissible gastroenteritis coronavirus
RT nucleocapsid protein gene.";
RL Virology 151:41-49(1986).
RN [6]
RP FUNCTION, AND INTERACTION WITH N PROTEIN.
RX PubMed=11152504; DOI=10.1128/jvi.75.3.1312-1324.2001;
RA Escors D., Ortego J., Laude H., Enjuanes L.;
RT "The membrane M protein carboxy terminus binds to transmissible
RT gastroenteritis coronavirus core and contributes to core stability.";
RL J. Virol. 75:1312-1324(2001).
RN [7]
RP MUTANTS DM49-4; H92 AND DM25-9/49-12.
RX PubMed=1309909; DOI=10.1128/jvi.66.2.743-749.1992;
RA Laude H., Gelfi J., Lavenant L., Charley B.;
RT "Single amino acid changes in the viral glycoprotein M affect induction of
RT alpha interferon by the coronavirus transmissible gastroenteritis virus.";
RL J. Virol. 66:743-749(1992).
RN [8]
RP TOPOLOGY.
RC STRAIN=Isolate PUR46-MAD;
RX PubMed=7636969; DOI=10.1128/jvi.69.9.5269-5277.1995;
RA Risco C., Anton I.M., Sune C., Pedregosa A.M., Martin-Alonso J.M.,
RA Parra F., Carrascosa J.L., Enjuanes L.;
RT "Membrane protein molecules of transmissible gastroenteritis coronavirus
RT also expose the carboxy-terminal region on the external surface of the
RT virion.";
RL J. Virol. 69:5269-5277(1995).
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, ECO:0000269|PubMed:11152504}.
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 -!- INTERACTION:
CC P04135; A6M930: EIF4A2; Xeno; NbExp=4; IntAct=EBI-25568430, EBI-25568629;
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}.
CC -!- CAUTION: The C-terminus of some M molecules seems to be exposed on the
CC external surface of the virion.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47912.1; Type=Erroneous initiation;
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DR EMBL; M21627; AAA47912.1; ALT_INIT; Genomic_RNA.
DR EMBL; X05598; CAA29091.1; -; Genomic_RNA.
DR EMBL; X06371; CAA29673.1; -; Genomic_RNA.
DR EMBL; AJ271965; CAB91149.2; -; Genomic_RNA.
DR EMBL; M14878; AAA47914.1; -; Genomic_RNA.
DR PIR; A26961; VGIHPC.
DR PIR; A29241; MFIHPC.
DR SMR; P04135; -.
DR IntAct; P04135; 5.
DR Proteomes; UP000001440; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; 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 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_0000037155"
FT TOPO_DOM 18..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"
FT MUTAGEN 33
FT /note="S->I: In DM49-3; reduces production of alpha-
FT interferon by the host organism."
FT MUTAGEN 33
FT /note="S->R: In DM25-3/49-12; does not affect production of
FT alpha-interferon by the host organism."
FT MUTAGEN 34
FT /note="T->I: In DM49-4; abolishes production of alpha-
FT interferon by the host organism."
FT CONFLICT 80
FT /note="V -> A (in Ref. 1; AAA47912)"
FT CONFLICT 144
FT /note="K -> N (in Ref. 2; CAA29091)"
FT CONFLICT 195
FT /note="G -> D (in Ref. 2 and 3)"
FT CONFLICT 197
FT /note="M -> V (in Ref. 3)"
SQ SEQUENCE 262 AA; 29569 MW; 56D6441D2ABBABF4 CRC64;
MKILLILACV IACACGERYC AMKSDTDLSC RNSTASDCES CFNGGDLIWH LANWNFSWSI
ILIVFITVLQ YGRPQFSWFV YGIKMLIMWL LWPVVLALTI FNAYSEYQVS RYVMFGFSIA
GAIVTFVLWI MYFVRSIQLY RRTKSWWSFN PETKAILCVS ALGRSYVLPL EGVPTGVTLT
LLSGNLYAEG FKIAGGMNID NLPKYVMVAL PSRTIVYTLV GKKLKASSAT GWAYYVKSKA
GDYSTEARTD NLSEQEKLLH MV
