ENV_FSVGA
ID ENV_FSVGA Reviewed; 662 AA.
AC P03391; P21446;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 114.
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 sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein
OS feline leukemia oncovirus B).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11774;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6319767; DOI=10.1128/jvi.49.2.629-632.1984;
RA Nunberg J.H., Williams M.E., Innis M.A.;
RT "Nucleotide sequences of the envelope genes of two isolates of feline
RT leukemia virus subgroup B.";
RL J. Virol. 49:629-632(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6304347; DOI=10.1128/jvi.46.3.871-880.1983;
RA Elder J.H., Mullins J.I.;
RT "Nucleotide sequence of the envelope gene of Gardner-Arnstein feline
RT leukemia virus B reveals unique sequence homologies with a murine mink cell
RT focus-forming virus.";
RL J. Virol. 46:871-880(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6321156; DOI=10.1002/j.1460-2075.1983.tb01729.x;
RA Wunsch M., Schulz A.S., Koch W., Friedrich R., Hunsmann G.;
RT "Sequence analysis of Gardner-Arnstein feline leukaemia virus envelope gene
RT reveals common structural properties of mammalian retroviral envelope
RT genes.";
RL EMBO J. 2:2239-2246(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2823466; DOI=10.1016/0042-6822(87)90194-2;
RA Guilhot S., Hampe A., D'Auriol L., Galibert F.;
RT "Nucleotide sequence analysis of the LTRs and env genes of SM-FeSV and GA-
RT FeSV.";
RL Virology 161:252-258(1987).
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; K01209; AAA43052.1; -; Genomic_RNA.
DR EMBL; V01172; CAA24497.1; -; Genomic_DNA.
DR EMBL; X00188; CAA25008.1; -; Genomic_DNA.
DR EMBL; M23026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03991; VCVWGF.
DR SMR; P03391; -.
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..662
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239570"
FT CHAIN 35..465
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040724"
FT CHAIN 466..645
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040725"
FT PEPTIDE 646..662
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239571"
FT TOPO_DOM 35..606
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 244..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..488
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 534..550
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 496..545
FT /evidence="ECO:0000255"
FT COILED 555..591
FT /evidence="ECO:0000255"
FT MOTIF 332..335
FT /note="CXXC"
FT MOTIF 551..559
FT /note="CX6CC"
FT COMPBIAS 255..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 465..466
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 645..646
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 626
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..559
FT /note="Interchain (between SU and TM chains, or C-335 with
FT C-559); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 332..335
FT /evidence="ECO:0000250"
FT DISULFID 551..558
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="Missing (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="V -> I (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="T -> V (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..56
FT /note="LVTGTK -> VQTNTQ (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..75
FT /note="FPTMYF -> YPTLHV (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..95
FT /note="IIGNTWNPSDQEPFPG -> LVGDSWEPIVLDPNNVKHGARYSSSK (in
FT Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..110
FT /note="DQPMRRWQQRNT -> KTTDRKKQQQTY (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..123
FT /note="NRKQ -> PSLGPKGTH (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="P -> A (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> A (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..148
FT /note="TYWRPT -> AWWKPS (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..193
FT /note="KGVTQGIYQCSGGGWCGPCYDKAVHSSTTGASEGGR -> RGSSQDTNSCEG
FT K (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="T -> A (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> M (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> T (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="S -> T (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="M -> S (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..300
FT /note="IESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPAS -> TGSKVATQRPQ
FT TNESAPRSVAPTTMG (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 73150 MW; 1482088D547CFF47 CRC64;
MESPTHPKPS KDKTLSWNLV FLVGILFTID IGMANPSPHQ VYNVTWTITN LVTGTKANAT
SMLGTLTDAF PTMYFDLCDI IGNTWNPSDQ EPFPGYGCDQ PMRRWQQRNT PFYVCPGHAN
RKQCGGPQDG FCAVWGCETT GETYWRPTSS WDYITVKKGV TQGIYQCSGG GWCGPCYDKA
VHSSTTGASE GGRCNPLILQ FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI
TPPQAMGPNL VLPDQKPPSR QSQIESRVTP HHSQGNGGTP GITLVNASIA PLSTPVTPAS
PKRIGTGDRL INLVQGTYLA LNATDPNRTK DCWLCLVSRP PYYEGIAILG NYSNQTNPPP
SCLSIPQHKL TISEVSGQGL CIGTVPKTHQ ALCNETQQGH TGAHYLAAPN GTYWACNTGL
TPCISMAVLN WTSDFCVLIE LWPRVTYHQP EYVYTHFAKA ARFRREPISL TVALMLGGLT
VGGIAAGVGT GTKALIETAQ FRQLQMAMHT DIQALEESIS ALEKSLTSLS EVVLQNRRGL
DILFLQEGGL CAALKEECCF YADHTGLVRD NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS
PWFTTLISSI MGPLLILLLI LLFGPCILNR LVQFVKDRIS VVQALILTQQ YQQIKQYDPD
RP
