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Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU) (Glycoprotein 70) (gp70); Transmembrane protein (TM) (Envelope protein p15E); R-peptide (p2E)]

 ENV_FLVC6               Reviewed;         668 AA.
P21443;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
10-MAY-2017, entry version 93.
RecName: Full=Envelope glycoprotein;
AltName: Full=Env polyprotein;
Contains:
RecName: Full=Surface protein;
Short=SU;
AltName: Full=Glycoprotein 70;
Short=gp70;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
AltName: Full=Envelope protein p15E;
Contains:
RecName: Full=R-peptide;
AltName: Full=p2E;
Flags: Precursor;
Name=env;
Feline leukemia virus (isolate CFE-6).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Gammaretrovirus.
NCBI_TaxID=11922;
NCBI_TaxID=9681; Felidae (cat family).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2539525;
Kumar D.V., Berry B.T., Roy-Burman P.;
"Nucleotide sequence and distinctive characteristics of the env gene
of endogenous feline leukemia provirus.";
J. Virol. 63:2379-2384(1989).
-!- FUNCTION: The surface protein (SU) attaches the virus to the host
cell by binding to its receptor. This interaction triggers the
refolding of the transmembrane protein (TM) and is thought to
activate its fusogenic potential by unmasking its fusion peptide.
Fusion occurs at the host cell plasma membrane (By similarity).
{ECO:0000250}.
-!- FUNCTION: The transmembrane protein (TM) acts as a class I viral
fusion protein. Under the current model, the protein has at least
3 conformational states: pre-fusion native state, pre-hairpin
intermediate state, and post-fusion hairpin state. During viral
and target cell membrane fusion, the coiled coil regions (heptad
repeats) assume a trimer-of-hairpins structure, positioning the
fusion peptide in close proximity to the C-terminal region of the
ectodomain. The formation of this structure appears to drive
apposition and subsequent fusion of viral and target cell
membranes. Membranes fusion leads to delivery of the nucleocapsid
into the cytoplasm (By similarity). {ECO:0000250}.
-!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of
SU-TM heterodimers attached by a labile interchain disulfide bond.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Surface protein: Virion membrane; Peripheral
membrane protein. Host cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}. Note=The surface protein is not
anchored to the viral envelope, but associates with the
extravirion surface through its binding to TM. Both proteins are
thought to be concentrated at the site of budding and incorporated
into the virions possibly by contacts between the cytoplasmic tail
of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: R-peptide: Host cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Note=The R-peptide is
membrane-associated through its palmitate. {ECO:0000250}.
-!- DOMAIN: The 17 amino acids long immunosuppressive region is
present in many retroviral envelope proteins. Synthetic peptides
derived from this relatively conserved sequence inhibit immune
function in vitro and in vivo (By similarity). {ECO:0000250}.
-!- DOMAIN: The YXXL motif is involved in determining the exact site
of viral release at the surface of infected mononuclear cells and
promotes endocytosis.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Envelope glycoproteins are synthesized as a inactive precursor
that is N-glycosylated and processed likely by host cell furin or
by a furin-like protease in the Golgi to yield the mature SU and
TM proteins. The cleavage site between SU and TM requires the
minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the
C-terminus of the cytoplasmic tail of the TM protein upon particle
formation as a result of proteolytic cleavage by the viral
protease. Cleavage of this peptide is required for TM to become
fusogenic (By similarity). {ECO:0000250}.
-!- PTM: The CXXC motif is highly conserved across a broad range of
retroviral envelope proteins. It is thought to participate in the
formation of a labile disulfide bond possibly with the CX6CC motif
present in the transmembrane protein. Isomerization of the
intersubunit disulfide bond to an SU intrachain disulfide bond is
thought to occur upon receptor recognition in order to allow
membrane fusion (By similarity). {ECO:0000250}.
-!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
-!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M25425; AAA30809.1; -; Genomic_DNA.
ProteinModelPortal; P21443; -.
SMR; P21443; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:InterPro.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 3.90.310.10; -; 2.
InterPro; IPR008981; FMuLV_rcpt-bd.
InterPro; IPR018154; TLV/ENV_coat_polyprotein.
PANTHER; PTHR10424; PTHR10424; 1.
Pfam; PF00429; TLV_coat; 1.
SUPFAM; SSF49830; SSF49830; 1.
3: Inferred from homology;
Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Host-virus interaction;
Lipoprotein; Membrane; Palmitate; Signal; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 668 Envelope glycoprotein.
/FTId=PRO_0000239561.
CHAIN 35 465 Surface protein. {ECO:0000250}.
/FTId=PRO_0000040706.
CHAIN 466 644 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000040707.
PEPTIDE 645 668 R-peptide. {ECO:0000250}.
/FTId=PRO_0000239562.
TOPO_DOM 35 605 Extracellular. {ECO:0000255}.
TRANSMEM 606 626 Helical. {ECO:0000255}.
TOPO_DOM 627 668 Cytoplasmic. {ECO:0000255}.
REGION 467 487 Fusion peptide. {ECO:0000255}.
REGION 533 549 Immunosuppression. {ECO:0000250}.
COILED 495 544 {ECO:0000255}.
COILED 554 590 {ECO:0000255}.
MOTIF 332 335 CXXC.
MOTIF 550 558 CX6CC.
MOTIF 650 653 YXXL motif; contains endocytosis signal.
{ECO:0000250}.
SITE 465 466 Cleavage; by host. {ECO:0000250}.
SITE 644 645 Cleavage; by viral protease.
{ECO:0000250}.
LIPID 625 625 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 115 132 {ECO:0000250}.
DISULFID 124 137 {ECO:0000250}.
DISULFID 332 558 Interchain (between SU and TM chains, or
C-335 with C-558); in linked form.
{ECO:0000250}.
DISULFID 332 335 {ECO:0000250}.
DISULFID 550 557 {ECO:0000250}.
SEQUENCE 668 AA; 74298 MW; 4A6A06CF2EB8CE25 CRC64;
MEGPTHPKPS KDKTFSWDLI ILVGVLLRLD AGMANPSPHQ VYNITWTITN LVTGIKANAT
SMLGTLTDTF PTIYFDLCDI IGNTWNPSDQ EPFPGYGCDQ PMRRWQQRNT AFYVCPGHAN
RKQCGGPQDG FCAVWGCETT GETYWKPTSS WDYITVKKGV TQGIYQCNGG GWCGPCYDKA
VHSSTTGASE GGRCNPLILQ FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI
TPPQAMGPNP VLPDQKPPSR QSQIESRVIP HHPQGNGGTP GITLVNASIA PLSTPVTPAS
PKRIGTGNRL INLVQGTYLT LNVTNPNKTK DCWLCLVSRP PYYEGIAVLG NYSNQTNPPP
SCLSVPQHKL TISEVSGQGL CIATVPKTHQ ALCNKTQKGH RGTHYLVAPN GTYWACNTGL
TPCISMAVLN WTSDFCVLTE LWPRITYHEP EYIYSHFENK PRFKRDPISL TVALMLGGIT
VGGMARNRNR DCGLLETAQF RQLQMAMHTD IQALEESISA LEKSLTSLSE VVLQNRRGLD
ILFLQEGGLC TALKEECCFY ADHTGLVRDN MAKLRERLKQ RQQLFDSQQD GLEGWFNKSP
WFTTLISSIM GPLMILLLIL LFGPCILNRL VQFVKDRISV VQTLVLTQQY QRLGQWRLRP
TVSPQLNV


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