ENV_FSVST
ID ENV_FSVST Reviewed; 534 AA.
AC P03392;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 109.
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 Flags: Precursor; Fragment;
GN Name=env;
OS Feline sarcoma virus (strain Snyder-Theilen).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11780;
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).
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}.
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 -!- 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}.
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DR EMBL; K01208; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P03392; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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; Membrane;
KW Signal; 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..>534
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239574"
FT CHAIN 35..465
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040729"
FT CHAIN 466..>534
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040730"
FT TOPO_DOM 35..>534
FT /note="Extracellular"
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 COILED 496..>534
FT /evidence="ECO:0000255"
FT MOTIF 332..335
FT /note="CXXC"
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 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 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 NON_TER 534
SQ SEQUENCE 534 AA; 58349 MW; D3A50B10B7F22BB3 CRC64;
MEGPTHPKPS KDKTFSWDLM ILVGVLLRLD VGMANPSPHQ IYNVTWTITN LVTGTKANAT
SMLGTLTDAF PTMYFDLCDI IGNTWNPSDQ EPFPGYGCDH PMRRWQQRNT PFYVCPGHAN
RKQCGGPQDG FCAVWGCETT GETYWRPTSS WDYITVKKGV TQGIYQCSGG GWCGPCYDKA
VHSSITGASE GGRCNPLILQ FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI
TPPQAMGPNL VLPDQKPPSR QSQIESRVTP HHSQGNGGTP GITLVNASIA PLSTPVTPAS
PKRIGTGNRL INLVQGTYLA LNVTNPNKTK DCWLCLVSRP PYYEGIAVLG NYSNQTNPPP
SCLSDPQHKL TISEVSGQGL CIGTVPKTHQ ALCKKTQKGH KGTHYLAAPS GTYWACNTGL
IPCISMAVLN WTSDFCVLIE LWPRVTYHQP EYVYTHFDKT VRLRREPISL TVALMLGGLT
VGGIAAGVGT GTKALLETAQ FRQLQMAMHT DIQALEESIS ALEKSLTSLS EVVL
