ID   ENV_FLVC1               Reviewed;         273 AA.
AC   P21444;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 100.
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   Flags: Precursor; Fragment;
GN   Name=env;
OS   Feline leukemia virus (isolate CFE-16).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11921;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2539525; DOI=10.1128/jvi.63.5.2379-2384.1989;
RA   Kumar D.V., Berry B.T., Roy-Burman P.;
RT   "Nucleotide sequence and distinctive characteristics of the env gene of
RT   endogenous feline leukemia provirus.";
RL   J. Virol. 63:2379-2384(1989).
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   -!- 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: [Surface protein]: Virion membrane; Peripheral
CC       membrane protein. Host cell membrane; Peripheral membrane protein.
CC       Note=The surface protein is not anchored to the viral envelope, but
CC       associates with the extravirion surface through its binding to TM.
CC       {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 (By
CC       similarity). {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M25582; AAA30810.1; -; Genomic_DNA.
DR   PIR; B31479; B31479.
DR   SMR; P21444; -.
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   Disulfide bond; 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..>273
FT                   /note="Envelope glycoprotein"
FT                   /id="PRO_0000239560"
FT   CHAIN           35..>273
FT                   /note="Surface protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040705"
FT   TOPO_DOM        35..>273
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          242..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   DISULFID        115..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..137
FT                   /evidence="ECO:0000250"
FT   NON_TER         273
SQ   SEQUENCE   273 AA;  30008 MW;  6B605FCD582B325D CRC64;
     MEGPTHPKPS KDKTFSWDLI ILVGVLLRLD VGMANPSPHQ VYNITWTITN LVTGTKANAT
     SMLGTLTDAF PTLYFDLCDI IGNTWNPSGQ EPFPGYGCDQ PMRRWQQRNT AFYVCPGHAN
     RKQCGGPQDG FCAVWGCETT GETYWKPTSS WDYITVKKGV TQGIYQCSGG GWCGPCYDKA
     VHSSTTGASE GGRCNPLILQ FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI
     TPPQAMGPDP VLPDQKPPSR TVSPQLNVIP HPS