ENV_AVIR3
ID ENV_AVIR3 Reviewed; 257 AA.
AC P33498;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 85;
DE Short=gp85;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 37;
DE Short=gp37;
DE Flags: Precursor; Fragment;
GN Name=env;
OS Avian retrovirus RPL30.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=31671;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1527848; DOI=10.1128/jvi.66.10.5975-5987.1992;
RA Jia R., Mayer B.J., Hanafusa T., Hanafusa H.;
RT "A novel oncogene, v-ryk, encoding a truncated receptor tyrosine kinase is
RT transduced into the RPL30 virus without loss of viral sequences.";
RL J. Virol. 66:5975-5987(1992).
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 noncovalent interactions or by a labile
CC interchain disulfide bond. {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 transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein is synthesized as a Env-Ryk chimeric
CC protein and then cellular protease cleaves this precursor into gp85 and
CC the putative oncogene termed gp69 (gp37-Ryk). The sequence shown here
CC corresponds to the Env (gp85-gp37) homolog fragment of the chimera.
CC -!- CAUTION: The cleavage site does not match the consensus used by furin.
CC {ECO:0000305}.
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DR EMBL; M92847; AAA42673.1; ALT_TERM; mRNA.
DR PIR; A43362; A43362.
DR SMR; P33498; -.
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; IPR005166; RSV_p95_env.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF03708; Avian_gp85; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 2: Evidence at transcript level;
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..257
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239545"
FT CHAIN <1..78
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040681"
FT CHAIN 79..257
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040682"
FT TOPO_DOM <1..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 95..115
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 151..167
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 112..162
FT /evidence="ECO:0000255"
FT COILED 180..210
FT /evidence="ECO:0000255"
FT SITE 78..79
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 245
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
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 68
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 257 AA; 27916 MW; B46FC61B8F10E187 CRC64;
FPILPGVWVD STQGNFTKPK ALPPAIFLIC GDRAWQGIPS RPVGGPCYLG KLTMLAPNHT
DIHKILANSS QTGVRHFRSV SHLDDTCSDE VQLWGPTARI FASILAPGVA AAQALREIER
LACWSVKQAN LTTSLLGDLL DDVTSIRHAV LQNRAAIDFL LLAHGHGCKD IAGMCCFNLS
DHSEAIQKKF QLMKEHVNKI GVDSDPIGSW LRGLFGGIGE WAIHLLKGLL LGLVVILLLV
VCLPCLLQFV SSSTRKM
