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Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU) (Glycoprotein 76) (gp76); Transmembrane protein (TM) (Envelope protein p15E); R-peptide (p2E)]

 ENV_MLVRK               Reviewed;         665 AA.
P31794;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
28-MAR-2018, entry version 100.
RecName: Full=Envelope glycoprotein;
AltName: Full=Env polyprotein;
Contains:
RecName: Full=Surface protein;
Short=SU;
AltName: Full=Glycoprotein 76;
Short=gp76;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
AltName: Full=Envelope protein p15E;
Contains:
RecName: Full=R-peptide;
AltName: Full=p2E;
Flags: Precursor;
Name=env;
Radiation murine leukemia virus (strain Kaplan).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Gammaretrovirus; Murine leukemia virus.
NCBI_TaxID=31689;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1629969;
Poliquin L., Bergeron D., Fortier J.L., Paquette Y., Bergeron R.,
Rassart E.;
"Determinants of thymotropism in Kaplan radiation leukemia virus and
nucleotide sequence of its envelope region.";
J. Virol. 66:5141-5146(1992).
-!- 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 virion
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 YXXL motif is involved in determining the exact site
of viral release at the surface of infected mononuclear cells and
promotes endocytosis.
-!- 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}.
-!- 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; M93052; AAA46526.1; -; Genomic_DNA.
PIR; B42743; VCMVKA.
ProteinModelPortal; P31794; -.
SMR; P31794; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 1.
InterPro; IPR008981; FMuLV_rcpt-bd.
InterPro; IPR018154; TLV/ENV_coat_polyprotein.
PANTHER; PTHR10424; PTHR10424; 1.
Pfam; PF00429; TLV_coat; 1.
SUPFAM; SSF49830; SSF49830; 1.
1: Evidence at protein level;
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; Metal-binding; Palmitate; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus entry into host cell; Zinc.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 665 Envelope glycoprotein.
/FTId=PRO_0000239589.
CHAIN 32 467 Surface protein. {ECO:0000250}.
/FTId=PRO_0000040768.
CHAIN 468 644 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000040769.
PEPTIDE 645 665 R-peptide. {ECO:0000250}.
/FTId=PRO_0000040770.
TOPO_DOM 32 605 Extracellular. {ECO:0000255}.
TRANSMEM 606 626 Helical. {ECO:0000255}.
TOPO_DOM 627 665 Cytoplasmic. {ECO:0000255}.
REGION 32 267 Receptor-binding domain (RBD).
{ECO:0000255}.
REGION 470 490 Fusion peptide. {ECO:0000250}.
REGION 533 549 Immunosuppression. {ECO:0000250}.
COILED 505 532 {ECO:0000255}.
MOTIF 334 337 CXXC.
MOTIF 550 558 CX6CC.
MOTIF 650 653 YXXL motif; contains endocytosis signal.
{ECO:0000250}.
COMPBIAS 264 305 Pro-rich.
METAL 117 117 Zinc. {ECO:0000250}.
SITE 467 468 Cleavage; by host. {ECO:0000250}.
SITE 644 645 Cleavage; by viral protease p14.
{ECO:0000250}.
LIPID 625 625 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 77 129 {ECO:0000250}.
DISULFID 103 118 {ECO:0000250}.
DISULFID 104 114 {ECO:0000250}.
DISULFID 152 172 {ECO:0000250}.
DISULFID 164 177 {ECO:0000250}.
DISULFID 209 215 {ECO:0000250}.
DISULFID 334 558 Interchain (between SU and TM chains, or
C-337 with C-558); in linked form.
DISULFID 334 337
DISULFID 364 418 {ECO:0000250}.
DISULFID 383 395 {ECO:0000250}.
DISULFID 425 438 {ECO:0000250}.
DISULFID 550 557 {ECO:0000250}.
SEQUENCE 665 AA; 73085 MW; FA15AB6B0C63F0AA CRC64;
MESTTLSKPF KNQVNPWGPL IVLLILGRVN PVALGNSPHQ VFNLSWEVTN EDRETVWAIT
GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YQAPFSPPPG PPCCSRSSGS TPGCSRDCEE
PLTSYTPRCN TAWNRLKLSK VTHAHNEGFY VCPGPHRPRW ARSCGGPESF YCASWGCETT
GRASWKPSSS WDYITVSNNL TSGQATPVCK NNTWCNSLTI RFTSLGKQAT SWVTGHWWGL
RLYVSGHDPG LIFGIRLKIT DSGPRVPIGP NPVLSDQRPP SQPRSPPHSN STPTETPLTL
PEPPPAGVEN RLLNLVKGAY QALNLTSPDR TQECWLCLVS GPPYYEGVAV LGTYSNHTSA
PANCSVASQH KLTLSEVTGR GLCVGAVPKT HQALCNTTQN TSGGSYYLAA PAGTIWACNT
GLTPCLSTTV LNLTTDYCVL VELWPRVTYH SPSYVYHQFE GRAKYKREPV SLTLALLLGG
LTMGGIAAGV GTGTTALVAT QQLQAAVHDD LKEVEKSITN LEKSLTSLSE VVLQNRRGLD
LLFLKEGGLC AALKEECCFY ADHTGVVRDS MAKLRERLNQ RQKLFESGQG WFERLFNGSP
WFTTLISTIM GPLIVLLLIL LLGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE
MESRE


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