ENV_FLVC6
ID ENV_FLVC6 Reviewed; 668 AA.
AC P21443;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 103.
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 (isolate CFE-6).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11922;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2539525; DOI=10.1128/jvi.63.5.2379-2384.1989;
RA Kumar D.V., Berry B.T., Roy-Burman P.;
RT "Nucleotide sequence and distinctive characteristics of the env gene of
RT endogenous feline leukemia provirus.";
RL J. Virol. 63:2379-2384(1989).
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 -!- 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; M25425; AAA30809.1; -; Genomic_DNA.
DR SMR; P21443; -.
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..668
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239561"
FT CHAIN 35..465
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040706"
FT CHAIN 466..644
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040707"
FT PEPTIDE 645..668
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239562"
FT TOPO_DOM 35..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..487
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 533..549
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 495..544
FT /evidence="ECO:0000255"
FT COILED 554..590
FT /evidence="ECO:0000255"
FT MOTIF 332..335
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 SITE 465..466
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 644..645
FT /note="Cleavage; by viral protease"
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:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
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 CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 115..132
FT /evidence="ECO:0000250"
FT DISULFID 124..137
FT /evidence="ECO:0000250"
FT DISULFID 332..558
FT /note="Interchain (between SU and TM chains, or C-335 with
FT C-558); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 332..335
FT /evidence="ECO:0000250"
FT DISULFID 550..557
FT /evidence="ECO:0000250"
SQ SEQUENCE 668 AA; 74298 MW; 4A6A06CF2EB8CE25 CRC64;
MEGPTHPKPS KDKTFSWDLI ILVGVLLRLD AGMANPSPHQ VYNITWTITN LVTGIKANAT
SMLGTLTDTF PTIYFDLCDI IGNTWNPSDQ EPFPGYGCDQ PMRRWQQRNT AFYVCPGHAN
RKQCGGPQDG FCAVWGCETT GETYWKPTSS WDYITVKKGV TQGIYQCNGG GWCGPCYDKA
VHSSTTGASE GGRCNPLILQ FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI
TPPQAMGPNP VLPDQKPPSR QSQIESRVIP HHPQGNGGTP GITLVNASIA PLSTPVTPAS
PKRIGTGNRL INLVQGTYLT LNVTNPNKTK DCWLCLVSRP PYYEGIAVLG NYSNQTNPPP
SCLSVPQHKL TISEVSGQGL CIATVPKTHQ ALCNKTQKGH RGTHYLVAPN GTYWACNTGL
TPCISMAVLN WTSDFCVLTE LWPRITYHEP EYIYSHFENK PRFKRDPISL TVALMLGGIT
VGGMARNRNR DCGLLETAQF RQLQMAMHTD IQALEESISA LEKSLTSLSE VVLQNRRGLD
ILFLQEGGLC TALKEECCFY ADHTGLVRDN MAKLRERLKQ RQQLFDSQQD GLEGWFNKSP
WFTTLISSIM GPLMILLLIL LFGPCILNRL VQFVKDRISV VQTLVLTQQY QRLGQWRLRP
TVSPQLNV
