ENV_RMCFV
ID ENV_RMCFV Reviewed; 640 AA.
AC P06445; Q85628; Q85629; Q89529;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 111.
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 Rauscher mink cell focus-inducing virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11784;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=4009793; DOI=10.1128/jvi.55.1.184-192.1985;
RA Vogt M., Haggblom C., Swift S., Haas M.;
RT "Envelope gene and long terminal repeat determine the different biological
RT properties of Rauscher, Friend, and Moloney mink cell focus-inducing
RT viruses.";
RL J. Virol. 55:184-192(1985).
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 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 -!- 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 -!- 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}.
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DR EMBL; M10100; AAA46528.1; -; Genomic_RNA.
DR PIR; A03990; VCMVRV.
DR SMR; P06445; -.
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 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; Palmitate; Signal; 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 SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..640
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239598"
FT CHAIN 33..443
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040792"
FT CHAIN 444..623
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040793"
FT PEPTIDE 624..640
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040794"
FT TOPO_DOM 33..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..236
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255"
FT REGION 259..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..466
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 512..528
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 477..511
FT /evidence="ECO:0000255"
FT MOTIF 310..313
FT /note="CXXC"
FT MOTIF 529..537
FT /note="CX6CC"
FT MOTIF 629..632
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT SITE 443..444
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 623..624
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT LIPID 604
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:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
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 DISULFID 113..130
FT /evidence="ECO:0000250"
FT DISULFID 122..135
FT /evidence="ECO:0000250"
FT DISULFID 310..537
FT /note="Interchain (between SU and TM chains, or C-310 with
FT C-535); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 310..313
FT /evidence="ECO:0000250"
FT DISULFID 529..536
FT /evidence="ECO:0000250"
SQ SEQUENCE 640 AA; 70072 MW; 1E4450343643D799 CRC64;
MACSTFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHK VFNVTWRVTN LMTGQTANAT
SLLGTMTDAF PKLYFDLCDL VGDYWDDPEP DIGDGCRTPG GRRRTRLYDF YVCPGHTVPI
GCGGPGEGYC GKWGCETTGQ AYWKPSSSWD LISLKRGNTP KDQGPCYDSS VSSDIKGATP
GGRCNPLVLE FTDAGKKASW DGPKVWGLRL YRSTGTDPVT RFSLTRRVLN IGPRVPIGPN
PVIIDQLPPS RPVQIMLPRP PQPPPPGAAS IVPETAPPSQ QPGTGDRLLN LVDGAYQALN
LTSPDKTQEC WLCLVAEPPY YEGVAVLGTY SNHTSAPTNC SVASQHKLTL SEVTGQGLCI
GTVPKTHQAL CNTTLKTNKG SYYLVAPAGT TWACNTGLTP CLSATVLNRT TDYCVLVELW
PRVTYHPPSY VYSQFEKSYR HKREPVSLTL ALLLGGLTMG GIAAGVGTGT TALVATQQFQ
QLHAAVQDDL KEVEKSITNL EKSLTSLSEV VLQNRRGLDL LFLKEGGLCA ALKEECCFYA
DHTGLVRDSM AKLRERLTQR QKLFESSQGW FEGLFNRSPW FTTLISTIMG PLIILLLILL
FGPCILNRLV QFVKDRISVV QALVLTQQYH QLKPLEYEPQ
