ID VME1_SARS2 Reviewed; 222 AA.
AC P0DTC5;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 10-FEB-2021, entry version 6.
DE RecName: Full=Membrane protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE Short=M;
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 ORFNames=M;
OS Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=2697049;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT "A new coronavirus associated with human respiratory disease in China.";
RL Nature 579:265-269(2020).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=33060197; DOI=10.1126/science.abe9403;
RG QCRG Structural Biology Consortium;
RG Zoonomia Consortium;
RA Gordon D.E., Hiatt J., Bouhaddou M., Rezelj V.V., Ulferts S., Braberg H.,
RA Jureka A.S., Obernier K., Guo J.Z., Batra J., Kaake R.M., Weckstein A.R.,
RA Owens T.W., Gupta M., Pourmal S., Titus E.W., Cakir M., Soucheray M.,
RA McGregor M., Cakir Z., Jang G., O'Meara M.J., Tummino T.A., Zhang Z.,
RA Foussard H., Rojc A., Zhou Y., Kuchenov D., Huettenhain R., Xu J.,
RA Eckhardt M., Swaney D.L., Fabius J.M., Ummadi M., Tutuncuoglu B.,
RA Rathore U., Modak M., Haas P., Haas K.M., Naing Z.Z.C., Pulido E.H.,
RA Shi Y., Barrio-Hernandez I., Memon D., Petsalaki E., Dunham A.,
RA Marrero M.C., Burke D., Koh C., Vallet T., Silvas J.A., Azumaya C.M.,
RA Billesboelle C., Brilot A.F., Campbell M.G., Diallo A., Dickinson M.S.,
RA Diwanji D., Herrera N., Hoppe N., Kratochvil H.T., Liu Y., Merz G.E.,
RA Moritz M., Nguyen H.C., Nowotny C., Puchades C., Rizo A.N.,
RA Schulze-Gahmen U., Smith A.M., Sun M., Young I.D., Zhao J., Asarnow D.,
RA Biel J., Bowen A., Braxton J.R., Chen J., Chio C.M., Chio U.S.,
RA Deshpande I., Doan L., Faust B., Flores S., Jin M., Kim K., Lam V.L.,
RA Li F., Li J., Li Y.L., Li Y., Liu X., Lo M., Lopez K.E., Melo A.A.,
RA Moss F.R. III, Nguyen P., Paulino J., Pawar K.I., Peters J.K.,
RA Pospiech T.H. Jr., Safari M., Sangwan S., Schaefer K., Thomas P.V.,
RA Thwin A.C., Trenker R., Tse E., Tsui T.K.M., Wang F., Whitis N., Yu Z.,
RA Zhang K., Zhang Y., Zhou F., Saltzberg D., Hodder A.J., Shun-Shion A.S.,
RA Williams D.M., White K.M., Rosales R., Kehrer T., Miorin L., Moreno E.,
RA Patel A.H., Rihn S., Khalid M.M., Vallejo-Gracia A., Fozouni P.,
RA Simoneau C.R., Roth T.L., Wu D., Karim M.A., Ghoussaini M., Dunham I.,
RA Berardi F., Weigang S., Chazal M., Park J., Logue J., McGrath M.,
RA Weston S., Haupt R., Hastie C.J., Elliott M., Brown F., Burness K.A.,
RA Reid E., Dorward M., Johnson C., Wilkinson S.G., Geyer A., Giesel D.M.,
RA Baillie C., Raggett S., Leech H., Toth R., Goodman N., Keough K.C.,
RA Lind A.L., Klesh R.J., Hemphill K.R., Carlson-Stevermer J., Oki J.,
RA Holden K., Maures T., Pollard K.S., Sali A., Agard D.A., Cheng Y.,
RA Fraser J.S., Frost A., Jura N., Kortemme T., Manglik A., Southworth D.R.,
RA Stroud R.M., Alessi D.R., Davies P., Frieman M.B., Ideker T., Abate C.,
RA Jouvenet N., Kochs G., Shoichet B., Ott M., Palmarini M., Shokat K.M.,
RA Garcia-Sastre A., Rassen J.A., Grosse R., Rosenberg O.S., Verba K.A.,
RA Basler C.F., Vignuzzi M., Peden A.A., Beltrao P., Krogan N.J.;
RT "Comparative host-coronavirus protein interaction networks reveal pan-viral
RT disease mechanisms.";
RL Science 0:0-0(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: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 (By similarity).
CC Interacts with the accessory proteins 3a and 7a (By similarity).
CC {ECO:0000250|UniProtKB:P59596, ECO:0000255|HAMAP-Rule:MF_04202}.
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, ECO:0000269|PubMed:33060197}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_04202}. Host membrane
CC {ECO:0000269|PubMed:33060197}; Multi-pass membrane protein.
CC Note=Largely embedded in the lipid bilayer. {ECO:0000255|HAMAP-
CC Rule:MF_04202}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses M protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
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DR EMBL; MN908947; QHD43419.1; -; Genomic_RNA.
DR RefSeq; YP_009724393.1; NC_045512.2.
DR BioGRID; 4383846; 1605.
DR IntAct; P0DTC5; 216.
DR ABCD; P0DTC5; 10 sequenced antibodies.
DR GeneID; 43740571; -.
DR KEGG; vg:43740571; -.
DR Reactome; R-HSA-9694322; Virion Assembly and Release.
DR Reactome; R-HSA-9694594; Maturation of protein M.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-9694635; Translation of structural proteins.
DR PRO; PR:P0DTC5; -.
DR Proteomes; UP000464024; 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:0030683; P:mitigation of host immune response by virus; IEA:UniProtKB-KW.
DR HAMAP; MF_04202; BETA_CORONA_M; 1.
DR InterPro; IPR002574; M_CoV.
DR Pfam; PF01635; CoV_M; 1.
DR PROSITE; PS51927; COV_M; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral immunoevasion; Viral matrix protein; Virion.
FT CHAIN 1..222
FT /note="Membrane protein"
FT /id="PRO_0000449652"
FT TOPO_DOM 2..19
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 41..50
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 72..79
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 101..222
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
SQ SEQUENCE 222 AA; 25147 MW; ED44D84C3BB9A6DB CRC64;
MADSNGTITV EELKKLLEQW NLVIGFLFLT WICLLQFAYA NRNRFLYIIK LIFLWLLWPV
TLACFVLAAV YRINWITGGI AIAMACLVGL MWLSYFIASF RLFARTRSMW SFNPETNILL
NVPLHGTILT RPLLESELVI GAVILRGHLR IAGHHLGRCD IKDLPKEITV ATSRTLSYYK
LGASQRVAGD SGFAAYSRYR IGNYKLNTDH SSSSDNIALL VQ
//