ENV_AVIRE
ID ENV_AVIRE Reviewed; 582 AA.
AC P03399;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 73;
DE Short=gp73;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 22;
DE Short=gp22;
DE Flags: Precursor;
GN Name=env;
OS Avian reticuloendotheliosis virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11636;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A;
RX PubMed=6090694; DOI=10.1128/jvi.52.1.172-182.1984;
RA Wilhelmsen K.C., Eggleton K., Temin H.M.;
RT "Nucleic acid sequences of the oncogene v-rel in reticuloendotheliosis
RT virus strain T and its cellular homolog, the proto-oncogene c-rel.";
RL J. Virol. 52:172-182(1984).
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}. Note=It is probably concentrated at the site of budding
CC and incorporated into the virions possibly by contacts between the
CC cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Host cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The
CC surface protein is not anchored to the viral envelope, but associates
CC with the extravirion surface through its binding to TM. It is probably
CC concentrated at the site of budding and incorporated into the virions
CC possibly by contacts between the cytoplasmic tail of Env and the N-
CC terminus of Gag (By similarity). {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 (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 -!- MISCELLANEOUS: Strain A is a helper virus of the strain T.
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DR EMBL; X01455; CAA25686.1; -; Genomic_RNA.
DR PIR; A03999; VCVDAR.
DR SMR; P03399; -.
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 InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 2.
DR Pfam; PF00429; TLV_coat; 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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..582
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239546"
FT CHAIN 36..392
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040683"
FT CHAIN 393..582
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040684"
FT TOPO_DOM 36..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 396..416
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 456..472
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT REGION 562..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..467
FT /evidence="ECO:0000255"
FT COILED 477..513
FT /evidence="ECO:0000255"
FT MOTIF 251..254
FT /note="CXXC"
FT MOTIF 473..481
FT /note="CX6CC"
FT SITE 392..393
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 543
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 251..481
FT /note="Interchain (between SU and TM chains, or C-254 with
FT C-481); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 251..254
FT /evidence="ECO:0000250"
FT DISULFID 473..480
FT /evidence="ECO:0000250"
SQ SEQUENCE 582 AA; 64138 MW; CD2560ADFC026D32 CRC64;
MDCLTDLRST EGKVDQAGKT LILLVVWWGF GTTAEGHPLQ QLWELPCDCS GGYVSPDLPI
TPTPSIAVAS PLPDLRVWLQ GSWGWGGGFR QQWECVFKPK IIPSVQEQPG PCECLTIATQ
MHSTCYEKAQ ECTLLGKTYF TAILQKTKLG SYEDGPNKLL QASCTGIWET SMLGPRCPCV
CLDGGGPTDR FGRICAEGLE EIIRHSYPSV QYHPLALPRP RGVDLDPQTS DILEATHQVL
NATNPQLAEN CWLCMTLGTQ SPQPSRRMAM SLSMEIAVLA SLSGATHRVN RCQLLCREAD
NRTGIPVGYV HFTNCTSIQE SLTRRVIYEI LRDYVLHRVM YLCVEQHAYT ALPNKWIGLC
ILASIVPDMS IIPGEEPIPL PSIEYTAGRH KRAVQFIPLL VGLGITGATL AGGTGLGVSV
HTYHKLSNQL IEDVQALSGT INDLQDQIDS LAEVVLQNRR GLDLLTAEQG GICLALQEKC
CFYANKSGIV RDKIRKLQED LLARKRALYD NPLWNGLNGF LPYLLPSLGP LFGLILFLTL
GPCIRKTLTR IIHDKIQGSK NPRISPAVQA TPNRDGYPRS MV
