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VME1_BEV
ID   VME1_BEV                Reviewed;         233 AA.
AC   P27904;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Membrane protein;
DE            Short=M protein;
DE   AltName: Full=E1 glycoprotein;
DE   AltName: Full=Matrix glycoprotein;
DE   AltName: Full=Membrane glycoprotein;
GN   Name=M;
OS   Berne virus (BEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC   Renitovirus; Equine torovirus.
OX   NCBI_TaxID=11156;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate P138/72;
RX   PubMed=2024492; DOI=10.1016/0042-6822(91)90606-c;
RA   den Boon J.A., Snijder E.J., Locker J.K., Horzinek M.C., Rottier P.J.M.;
RT   "Another triple-spanning envelope protein among intracellularly budding RNA
RT   viruses: the torovirus E protein.";
RL   Virology 182:655-663(1991).
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:0000250}.
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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}. Host Golgi apparatus membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Largely
CC       embedded in the lipid bilayer. {ECO:0000250}.
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DR   EMBL; X52505; CAA36747.1; -; mRNA.
DR   PIR; A39989; VMWJBV.
DR   Proteomes; UP000006571; 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   InterPro; IPR024251; M_Torovirus.
DR   Pfam; PF10943; DUF2632; 1.
PE   2: Evidence at transcript level;
KW   Host Golgi apparatus; Host membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral matrix protein; Virion.
FT   CHAIN           1..233
FT                   /note="Membrane protein"
FT                   /id="PRO_0000106129"
FT   TOPO_DOM        1..31
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..69
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..93
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..233
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   233 AA;  26548 MW;  A07A34DC539104BE CRC64;
     MFETNYWPFP DQAPNPFTAQ IEQLTATENV YIFLTTLFGI LQLVYVMFKL LCTMFPSLHF
     SPIWRGLENF WLFLSLASLA IAYWWLPSMT FTGYWALTII ATILVFILLI MMFVKFVNFV
     KLFYRTGSFA IAIRGPIVLV ALDVTIKLHC TPFAILVKEI GNIFYLSEYC NKPLTAAQIA
     ALRICVNGQW FAYTRSSTTS AARVAAANST AKYHLFVLQG VAEYTQLSSV KFE
 
 
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