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VME1_CVBM
ID   VME1_CVBM               Reviewed;         230 AA.
AC   P69704; P10526; P36359;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Membrane protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE            Short=M protein {ECO:0000255|HAMAP-Rule:MF_04202};
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   Name=M {ECO:0000255|HAMAP-Rule:MF_04202}; ORFNames=6;
OS   Bovine coronavirus (strain Mebus) (BCoV) (BCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
OX   NCBI_TaxID=11132;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3029965; DOI=10.1016/0042-6822(87)90312-6;
RA   Lapps W.E., Hogue B.G., Brian D.A.;
RT   "Sequence analysis of the bovine coronavirus nucleocapsid and matrix
RT   protein genes.";
RL   Virology 157:47-57(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3434434; DOI=10.1007/978-1-4684-1280-2_14;
RA   Lapps W.E., Hogue B.G., Brian D.A.;
RT   "Deduced amino acid sequence and potential O-glycosylation sites for the
RT   bovine coronavirus matrix protein.";
RL   Adv. Exp. Med. Biol. 218:123-129(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7966615; DOI=10.1128/jvi.68.12.8223-8231.1994;
RA   Chang R.Y., Hofmann M.A., Sethna P.B., Brian D.A.;
RT   "A cis-acting function for the coronavirus leader in defective interfering
RT   RNA replication.";
RL   J. Virol. 68:8223-8231(1994).
RN   [4]
RP   INTERACTION WITH HE AND S.
RX   PubMed=9371586; DOI=10.1128/jvi.71.12.9278-9284.1997;
RA   Nguyen V.-P., Hogue B.G.;
RT   "Protein interactions during coronavirus assembly.";
RL   J. Virol. 71:9278-9284(1997).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000255|PROSITE-ProRule:PRU01275,
CC       ECO:0000269|PubMed:9371586}.
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}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04202}. Note=Largely embedded in the lipid bilayer.
CC       {ECO:0000255|HAMAP-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; M27474; AAA79959.1; -; Genomic_RNA.
DR   EMBL; U00735; AAK29779.2; -; Genomic_RNA.
DR   PIR; A26347; VGIHBC.
DR   SMR; P69704; -.
DR   Proteomes; UP000007554; 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; 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   1: Evidence at protein level;
KW   Glycoprotein; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW   Membrane; Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral immunoevasion; Viral matrix protein; Virion.
FT   CHAIN           1..230
FT                   /note="Membrane protein"
FT                   /id="PRO_0000106030"
FT   TOPO_DOM        1..24
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT   TOPO_DOM        46..55
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT   TOPO_DOM        77..84
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT   TOPO_DOM        106..228
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
SQ   SEQUENCE   230 AA;  26372 MW;  6A7EA77313E01730 CRC64;
     MSSVTTPAPV YTWTADEAIK FLKEWNFSLG IILLFITIIL QFGYTSRSMF VYVIKMIILW
     LMWPLTIILT IFNCVYALNN VYLGFSIVFT IVAIIMWIVY FVNSIRLFIR TGSWWSFNPE
     TNNLMCIDMK GRMYVRPIIE DYHTLTVTII RGHLYMQGIK LGTGYSLSDL PAYVTVAKVS
     HLLTYKRGFL DKIGDTSGFA VYVKSKVGNY RLPSTQKGSG MDTALLRNNI
 
 
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