ENV_MLVF5
ID ENV_MLVF5 Reviewed; 675 AA.
AC P03390;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 70;
DE Short=gp70;
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 Friend murine leukemia virus (isolate 57) (FrMLV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11796;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Friedrich R.W., Koch W., von Maydell-Livonius U., Schrewe H.,
RA Zimmermann W.;
RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE.
RX PubMed=6321768; DOI=10.1128/jvi.49.3.828-840.1984;
RA Koch W., Zimmermann W., Oliff A., Friedrich R.W.;
RT "Molecular analysis of the envelope gene and long terminal repeat of Friend
RT mink cell focus-inducing virus: implications for the functions of these
RT sequences.";
RL J. Virol. 49:828-840(1984).
RN [3]
RP PALMITOYLATION AT CYS-640 OF THE TRANSMEMBRANE PROTEIN, AND MUTAGENESIS OF
RP CYS-640.
RX PubMed=8661417; DOI=10.1006/viro.1996.0355;
RA Yang C., Compans R.W.;
RT "Palmitoylation of the murine leukemia virus envelope glycoprotein
RT transmembrane subunits.";
RL Virology 221:87-97(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-270.
RX PubMed=9287219; DOI=10.1126/science.277.5332.1662;
RA Fass D., Davey R.A., Hamson C.A., Kim P.S., Cunningham J.M., Berger J.M.;
RT "Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0-
RT A resolution.";
RL Science 277:1662-1666(1997).
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.
CC {ECO:0000269|PubMed:8661417}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02794; CAA26561.1; -; Genomic_RNA.
DR PDB; 1AOL; X-ray; 2.00 A; A=43-270.
DR PDBsum; 1AOL; -.
DR SMR; P03390; -.
DR SwissPalm; P03390; -.
DR EvolutionaryTrace; P03390; -.
DR Proteomes; UP000007776; 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:0039588; P:suppression by virus of host antigen processing and presentation; 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 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Coiled coil;
KW Disulfide bond; 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;
KW Inhibition of host adaptive immune response by virus;
KW Inhibition of host proteasome antigen processing by virus; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell; Zinc.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..675
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239581"
FT CHAIN 35..479
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040751"
FT CHAIN 480..659
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040752"
FT PEPTIDE 660..675
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040753"
FT TOPO_DOM 35..620
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 35..270
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255"
FT REGION 276..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..502
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 548..564
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 513..547
FT /evidence="ECO:0000255"
FT MOTIF 346..349
FT /note="CXXC"
FT MOTIF 565..573
FT /note="CX6CC"
FT MOTIF 665..668
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT SITE 479..480
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 659..660
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT LIPID 640
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:8661417"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 80..132
FT DISULFID 106..121
FT DISULFID 107..117
FT DISULFID 155..175
FT DISULFID 167..180
FT DISULFID 212..218
FT DISULFID 346..573
FT /note="Interchain (between SU and TM chains, or C-349 with
FT C-573); in linked form"
FT DISULFID 346..349
FT DISULFID 376..430
FT /evidence="ECO:0000250"
FT DISULFID 395..407
FT /evidence="ECO:0000250"
FT DISULFID 437..450
FT /evidence="ECO:0000250"
FT DISULFID 565..572
FT /evidence="ECO:0000250"
FT MUTAGEN 640
FT /note="C->S: Complete loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:8661417"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:1AOL"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1AOL"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:1AOL"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1AOL"
SQ SEQUENCE 675 AA; 74025 MW; A097038E422BB3D3 CRC64;
MACSTLPKSP KDKIDPRDLL IPLILFLSLK GARSAAPGSS PHQVYNITWE VTNGDRETVW
AISGNHPLWT WWPVLTPDLC MLALSGPPHW GLEYQAPYSS PPGPPCCSGS SGSSAGCSRD
CDEPLTSLTP RCNTAWNRLK LDQVTHKSSE GFYVCPGSHR PREAKSCGGP DSFYCASWGC
ETTGRVYWKP SSSWDYITVD NNLTTSQAVQ VCKDNKWCNP LAIQFTNAGK QVTSWTTGHY
WGLRLYVSGR DPGLTFGIRL RYQNLGPRVP IGPNPVLADQ LSLPRPNPLP KPAKSPPASN
STPTLISPSP TPTQPPPAGT GDRLLNLVQG AYQALNLTNP DKTQECWLCL VSGPPYYEGV
AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GRGLCIGTVP KTHQALCNTT LKIDKGSYYL
VAPTGTTWAC NTGLTPCLSA TVLNRTTDYC VLVELWPRVT YHPPSYVYSQ FEKSYRHKRE
PVSLTLALLL GGLTMGGIAA GVGTGTTALV ATQQFQQLHA AVQDDLKEVE KSITNLEKSL
TSLSEVVLQN RRGLDLLFLK EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLTQRQKLF
ESSQGWFEGL FNRSPWFTTL ISTIMGPLII LLLILLFGPC ILNRLVQFVK DRISVVQALV
LTQQYHQLKP LEYEP
