ENV_FLVGL
ID ENV_FLVGL Reviewed; 642 AA.
AC P08359;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 104.
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 Feline leukemia virus (strain A/Glasgow-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11769;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3009890; DOI=10.1128/jvi.58.3.825-834.1986;
RA Stewart M.A., Warnock M., Wheeler A., Wilkie N., Mullins J.I., Onions D.E.,
RA Neil J.C.;
RT "Nucleotide sequences of a feline leukemia virus subgroup A envelope gene
RT and long terminal repeat and evidence for the recombinational origin of
RT subgroup B viruses.";
RL J. Virol. 58:825-834(1986).
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 extravirion 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 -!- 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; M12500; AAA43053.1; -; Genomic_RNA.
DR PIR; A24300; VCMVFG.
DR SMR; P08359; -.
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..34
FT /evidence="ECO:0000255"
FT CHAIN 35..642
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239564"
FT CHAIN 35..445
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040712"
FT CHAIN 446..625
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040713"
FT PEPTIDE 626..642
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239565"
FT TOPO_DOM 35..586
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 233..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..468
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 514..530
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 476..525
FT /evidence="ECO:0000255"
FT COILED 535..571
FT /evidence="ECO:0000255"
FT MOTIF 312..315
FT /note="CXXC"
FT MOTIF 531..539
FT /note="CX6CC"
FT COMPBIAS 246..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 445..446
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 625..626
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 606
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 267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 125..147
FT /evidence="ECO:0000250"
FT DISULFID 139..152
FT /evidence="ECO:0000250"
FT DISULFID 312..539
FT /note="Interchain (between SU and TM chains, or C-315 with
FT C-339); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 312..315
FT /evidence="ECO:0000250"
FT DISULFID 531..538
FT /evidence="ECO:0000250"
SQ SEQUENCE 642 AA; 71053 MW; 2DEF5A9EFFC245EC CRC64;
MESPTHPKPS KDKTLSWNLA FLVGILFTID IGMANPSPHQ IYNVTWVITN VQTNTQANAT
SMLGTLTDAY PTLHVDLCDL VGDTWEPIVL NPTNVKHGAR YSSSKYGCKT TDRKKQQQTY
PFYVCPGHAP SLGPKGTHCG GAQDGFCAAW GCETTGEAWW KPTSSWDYIT VKRGSSQDNS
CEGKCNPLVL QFTQKGRQAS WDGPKMWGLR LYRTGYDPIA LFTVSRQVST ITPPQAMGPN
LVLPDQKPPS RQSQTGSKVA TQRPQTNESA PRSVAPTTMG PKRIGTGDRL INLVQGTYLA
LNATDPNKTK DCWLCLVSRP PYYEGIAILG NYSNQTNPPP SCLSTPQHKL TISEVSGQGM
CIGTVPKTHQ ALCNKTQQGH TGAHYLAAPN GTYWACNTGL TPCISMAVLN WTSDFCVLIE
LWPRVTYHQP EYVYTHFAKA VRFRREPISL TVALMLGGLT VGGIAAGVGT GTKALLETAQ
FRQLQMAMHT DIQALEESIS ALEKSLTSLS EVVLQNRRGL DILFLQEGGL CAALKEECCF
YADHTGLVRD NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS PWFTTLISSI MGPLLILLLI
LLFGPCILNR LVQFVKDRIS VVQALILTQQ YQQIKQYDPD RP
