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

 ENV_XMRV6               Reviewed;         645 AA.
Q27ID8; A1Z653;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 1.
20-JUN-2018, entry version 55.
RecName: Full=Envelope glycoprotein;
AltName: Full=Env polyprotein;
Contains:
RecName: Full=Surface protein;
Short=SU;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
Contains:
RecName: Full=R-peptide;
Flags: Precursor;
Name=env;
Xenotropic MuLV-related virus (isolate VP62) (XMRV).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Gammaretrovirus; unclassified Gammaretrovirus.
NCBI_TaxID=373193;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16609730; DOI=10.1371/journal.ppat.0020025;
Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G.,
Klein E.A., Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D.,
Silverman R.H., DeRisi J.L.;
"Identification of a novel Gammaretrovirus in prostate tumors of
patients homozygous for R462Q RNASEL variant.";
PLoS Pathog. 2:E25-E25(2006).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=17234809; DOI=10.1073/pnas.0610291104;
Dong B., Kim S., Hong S., Das Gupta J., Malathi K., Klein E.A.,
Ganem D., Derisi J.L., Chow S.A., Silverman R.H.;
"An infectious retrovirus susceptible to an IFN antiviral pathway from
human prostate tumors.";
Proc. Natl. Acad. Sci. U.S.A. 104:1655-1660(2007).
-!- FUNCTION: The surface protein (SU) attaches the virus to the host
cell by binding to its receptor. This interaction activates a
thiol in a CXXC motif of the C-terminal domain, where the other
Cys residue participates in the formation of the intersubunit
disulfide. The activated thiol will attack the disulfide and cause
its isomerization into a disulfide isomer within the motif. This
leads to SU displacement and TM refolding, 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.
The activated Env consists of SU monomers and TM trimers (By
similarity). {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; Peripheral
membrane protein. 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. {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.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; DQ399707; ABD49688.1; -; Genomic_RNA.
EMBL; EF185282; ABM47429.1; -; Genomic_RNA.
ProteinModelPortal; Q27ID8; -.
SMR; Q27ID8; -.
OrthoDB; VOG0900004N; -.
Proteomes; UP000002240; Genome.
Proteomes; UP000180675; Genome.
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: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.
3: Inferred from homology;
Cleavage on pair of basic residues; Coiled coil; Complete proteome;
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; Reference proteome; 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 33 {ECO:0000255}.
CHAIN 34 645 Envelope glycoprotein. {ECO:0000250}.
/FTId=PRO_0000390831.
CHAIN 34 444 Surface protein. {ECO:0000250}.
/FTId=PRO_0000390832.
CHAIN 445 645 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000390833.
PEPTIDE 625 645 R-peptide. {ECO:0000250}.
/FTId=PRO_0000390834.
TOPO_DOM 34 585 Extracellular. {ECO:0000255}.
TRANSMEM 586 606 Helical. {ECO:0000255}.
TOPO_DOM 607 640 Cytoplasmic. {ECO:0000255}.
REGION 32 237 Receptor-binding domain (RBD).
{ECO:0000255}.
REGION 447 467 Fusion peptide. {ECO:0000250}.
REGION 513 529 Immunosuppression. {ECO:0000250}.
COILED 490 510 {ECO:0000255}.
MOTIF 311 314 CXXC. {ECO:0000250}.
MOTIF 530 538 CX6CC. {ECO:0000250}.
MOTIF 630 633 YXXL motif; contains endocytosis signal.
{ECO:0000250}.
COMPBIAS 234 283 Pro-rich.
SITE 444 445 Cleavage; by host. {ECO:0000250}.
SITE 624 625 Cleavage; by viral protease p14.
{ECO:0000250}.
LIPID 605 605 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 301 301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 373 373 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 113 130 {ECO:0000250}.
DISULFID 122 135 {ECO:0000250}.
DISULFID 311 538 Interchain (between SU and TM chains, or
C-314 with C-538); in linked form.
{ECO:0000250}.
DISULFID 311 314 {ECO:0000250}.
DISULFID 341 395 {ECO:0000250}.
DISULFID 360 372 {ECO:0000250}.
DISULFID 402 415 {ECO:0000250}.
DISULFID 530 537 {ECO:0000250}.
CONFLICT 261 261 T -> P (in Ref. 1; ABM47429).
{ECO:0000305}.
CONFLICT 298 298 L -> Q (in Ref. 1; ABM47429).
{ECO:0000305}.
CONFLICT 568 568 G -> R (in Ref. 1; ABM47429).
{ECO:0000305}.
SEQUENCE 645 AA; 69876 MW; 19ACC5E3EAF9AEC3 CRC64;
MESPAFSKPL KDKINPWGPL IIMGILVRAG ASVQRDSPHQ VFNVTWKITN LMTGQTANAT
SLLGTMTDTF PKLYFDLCDL VGDNWDDPEP DIGDGCRSPG GRKRTRLYDF YVCPGHTVLT
GCGGPREGYC GKWGCETTGQ AYWKPSSSWD LISLKRGNTP KGQGPCFDSS VGSGSIQGAT
PGGRCNPLVL EFTDAGKRAS WDAPKTWGLR LYRSTGADPV TLFSLTRQVL NVGPRVPIGP
NPVITEQLPP SQPVQIMLPR TPRPPPSGAA SMVPGAPPPS QQPGTGDRLL NLVEGAYLAL
NLTSPDKTQE CWLCLVSGPP YYEGVAVLGT YSNHTSAPAN CSVTSQHKLT LSEVTGQGLC
IGAVPKTHQA LCNTTQKTSD GSYYLASPAG TIWACSTGLT PCLSTTVLNL TTDYCVLVEL
WPKVTYHSPN YVYGQFEKKT KYKREPVSLT LALLLGGLTM GGIAAGVGTG TTALVATKQF
EQLQAAIHTD LGALEKSVSA LEKSLTSLSE VVLQNRRGLD LLFLKEGGLC AALKEECCFY
ADHTGVVRDS MAKLRERLNQ RQKLFESGQG WFEGLFNRSP WFTTLISTIM GPLIVLLLIL
LFGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE VESRE


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