ENV_MLVRD
ID ENV_MLVRD Reviewed; 665 AA.
AC P11268;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 76;
DE Short=gp76;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Envelope protein p15E;
DE Contains:
DE RecName: Full=R-peptide;
DE AltName: Full=p2E;
DE Flags: Precursor;
GN Name=env;
OS Radiation murine leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11787;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3033897; DOI=10.1016/0042-6822(87)90241-8;
RA Merregaert J., Janowski M., Reddy E.P.;
RT "Nucleotide sequence of a radiation leukemia virus genome.";
RL Virology 158:88-102(1987).
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 a labile interchain disulfide bond.
CC {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: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the virion surface through its
CC binding to TM. Both proteins are thought to be concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC similarity). {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.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By similarity). {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 CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion (By
CC similarity). {ECO:0000250}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; K03363; AAA46519.1; ALT_INIT; Genomic_RNA.
DR PIR; C26183; VCMVVR.
DR SMR; P11268; -.
DR Proteomes; UP000007778; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.90.310.10; -; 1.
DR InterPro; IPR008981; FMuLV_rcpt-bd.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil; 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; Metal-binding; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell;
KW Zinc.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..665
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239590"
FT CHAIN 32..467
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040771"
FT CHAIN 468..644
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040772"
FT PEPTIDE 645..665
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040773"
FT TOPO_DOM 32..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..267
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255"
FT REGION 266..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..490
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 533..549
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 505..532
FT /evidence="ECO:0000255"
FT MOTIF 334..337
FT /note="CXXC"
FT MOTIF 550..558
FT /note="CX6CC"
FT MOTIF 650..653
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 273..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 467..468
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 644..645
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT LIPID 625
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 77..129
FT /evidence="ECO:0000250"
FT DISULFID 103..118
FT /evidence="ECO:0000250"
FT DISULFID 104..114
FT /evidence="ECO:0000250"
FT DISULFID 152..172
FT /evidence="ECO:0000250"
FT DISULFID 164..177
FT /evidence="ECO:0000250"
FT DISULFID 209..215
FT /evidence="ECO:0000250"
FT DISULFID 334..558
FT /note="Interchain (between SU and TM chains, or C-337 with
FT C-558); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 334..337
FT /evidence="ECO:0000250"
FT DISULFID 364..418
FT /evidence="ECO:0000250"
FT DISULFID 383..395
FT /evidence="ECO:0000250"
FT DISULFID 425..438
FT /evidence="ECO:0000250"
FT DISULFID 550..557
FT /evidence="ECO:0000250"
SQ SEQUENCE 665 AA; 73083 MW; 93B2BFECC9E45984 CRC64;
MESTTLSKPF KNQVNPWGPL IVLLILGRVN PVALGNSPHQ VFNLSWEVTN EDRETVWAIT
GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YQAPFSPPPG PPCCSGSSGS TPGCSRDCEE
PLTSYTPRCN TAWNRLKLSK VTHAHNEGFY VCPGPHRPRW ARSCGGPESF YCASWGCETT
GRASWKPSSS WDYITVSNNL TSGQATPVCK NNTWCNSLTI RFTSLGKQAT SWVTGHWWGL
RLYVSGHDPG LIFGIRLKIT DSGPRVPIGP NPVLSDQRPP SQPRSPPHSN STPTETPLTL
PEPPPAGVEN RLLNLVKGAY QALNLTSPDR TQECWLCLVS GPPYYEGVAV LGTYSNHTSA
PANCSVALQH KLTLSEVTGQ GLCVGAVPKT HQALCNTTQN TSGGSYYLAA PAGTIWACNT
GLTPCLSTTV LNLTTDYCVL VELWPRVTYH SPSYVYHQFE RRGKYKREPV SLTLALLLGG
LTMGGIAAGI GTGTTALVAT QQLQAAVHDD LKEVEKSITN LEKSLTSLSE VVLQNRRGLD
LLFLKEGGLC AALKEECCFY ADHTGVVRDS MAKLRERLNQ RQKLFESGQG WFERLFNGSP
WFTTLISTIM GPLIVLLLIL LLGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE
MESRE
