ENV_WMSV
ID ENV_WMSV Reviewed; 77 AA.
AC P03384;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE AltName: Full=Envelope protein p15E;
DE Contains:
DE RecName: Full=R-peptide;
DE AltName: Full=p2E;
DE Flags: Fragment;
GN Name=env;
OS Woolly monkey sarcoma virus (WMSV) (Smian sarcoma-associated virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11970;
OH NCBI_TaxID=9518; Lagothrix (woolly monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6298772; DOI=10.1073/pnas.80.3.731;
RA Devare S.G., Reddy E.P., Law J.D., Robbins K.C., Aaronson S.A.;
RT "Nucleotide sequence of the simian sarcoma virus genome: demonstration that
RT its acquired cellular sequences encode the transforming gene product
RT p28sis.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:731-735(1983).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to its receptor. This interaction triggers the refolding of
CC the transmembrane protein (TM) and is thought to activate its fusogenic
CC potential by unmasking its fusion peptide. Fusion occurs at the host
CC cell plasma membrane (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Membranes fusion leads to
CC delivery of the nucleocapsid into the cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached by noncovalent interactions or by a labile
CC interchain disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=The R-peptide is
CC membrane-associated through its palmitate. {ECO:0000250}.
CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC viral release at the surface of infected mononuclear cells and promotes
CC endocytosis. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC N-glycosylated and processed likely by host cell furin or by a furin-
CC like protease in the Golgi to yield the mature SU and TM proteins. The
CC cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC [KR]-R. The R-peptide is released from the C-terminus of the
CC cytoplasmic tail of the TM protein upon particle formation as a result
CC of proteolytic cleavage by the viral protease. Cleavage of this peptide
CC is required for TM to become fusogenic (By similarity). {ECO:0000250}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
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DR EMBL; V01201; CAA24517.1; -; Genomic_DNA.
DR PIR; A03982; A03982.
DR RefSeq; YP_003580186.1; NC_009424.4.
DR SMR; P03384; -.
DR Proteomes; UP000203831; Genome.
DR GO; GO:0020002; C:host cell plasma 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:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN <1..77
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239601"
FT CHAIN <1..62
FT /note="Transmembrane protein"
FT /id="PRO_0000125472"
FT PEPTIDE 63..77
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239602"
FT TOPO_DOM <1..24
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 68..71
FT /note="YXXL motif; contains endocytosis signal"
FT SITE 61..62
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 43
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 77 AA; 8985 MW; 91A54FCCE9B659BC CRC64;
LERQKNQNWY EGWFNSSPWF TTLLSTIAGP LLLLLLLLIL GPCIINRLVQ FINNRVSAVK
ILVLRQKYQT LDNEDNL
