ENV_AVISU
ID ENV_AVISU Reviewed; 174 AA.
AC P03398;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 37;
DE Short=gp37;
DE Flags: Fragment;
GN Name=env;
OS UR2 sarcoma virus (UR2SV) (Avian sarcoma virus (strain UR2)).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=354090;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2983097; DOI=10.1128/jvi.53.3.879-884.1985;
RA Neckameyer W.S., Wang L.-H.;
RT "Nucleotide sequence of avian sarcoma virus UR2 and comparison of its
RT transforming gene with other members of the tyrosine protein kinase
RT oncogene family.";
RL J. Virol. 53:879-884(1985).
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 noncovalent interactions or by a labile
CC interchain disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-
CC pass type I membrane protein. Host cell membrane {ECO:0000250}; Single-
CC pass type I membrane protein {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 transmembrane protein is palmitoylated. {ECO:0000250}.
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DR EMBL; M10455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03998; VCFVUR.
DR RefSeq; NP_597837.2; NC_001618.1.
DR SMR; P03398; -.
DR GeneID; 1491915; -.
DR KEGG; vg:1491915; -.
DR Proteomes; UP000143802; 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: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; 1.
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; 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 CHAIN <1..174
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239548"
FT CHAIN 1..174
FT /note="Transmembrane protein"
FT /id="PRO_0000125467"
FT TOPO_DOM <1..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 43..59
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 4..54
FT /evidence="ECO:0000255"
FT COILED 72..102
FT /evidence="ECO:0000255"
FT LIPID 137
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 174 AA; 19338 MW; 60ADDECFBB8500F5 CRC64;
VAAAQALREI ERLACWSVKQ ANLTTSLLGD LLDDVTSIRH AVLQNRAAID FLLLAHGHGC
EDIAGMCCFN LSDHSESIQK KFQLMKEHVN KIGVDSDPIG SWLRGLFGGI GEWAVHLLKG
LLLGLVVILL LVVCLPCLLQ FVSSSIRKMI DNSLGYREER KKFQEAYKQP ERVV
