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Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU) (Glycoprotein 70) (gp70); Transmembrane protein (TM) (Glycoprotein 20) (gp20); R-peptide (p2E)]

 ENV_MPMV                Reviewed;         586 AA.
P07575;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
20-JUN-2018, entry version 104.
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=Glycoprotein 20;
Short=gp20;
Contains:
RecName: Full=R-peptide;
AltName: Full=p2E;
Flags: Precursor;
Name=env;
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Betaretrovirus.
NCBI_TaxID=11855;
NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE 6A).
PubMed=2421920; DOI=10.1016/0092-8674(86)90323-5;
Sonigo P., Barker C., Hunter E., Wain-Hobson S.;
"Nucleotide sequence of Mason-Pfizer monkey virus: an
immunosuppressive D-type retrovirus.";
Cell 45:375-385(1986).
[2]
CLEAVAGE OF R-PEPTIDE, DOMAIN YXXL MOTIF, AND MUTAGENESIS OF VAL-568
AND HIS-569.
PubMed=16140733; DOI=10.1128/JVI.79.18.11559-11568.2005;
Song C., Micoli K., Bauerova H., Pichova I., Hunter E.;
"Amino acid residues in the cytoplasmic domain of the Mason-Pfizer
monkey virus glycoprotein critical for its incorporation into
virions.";
J. Virol. 79:11559-11568(2005).
-!- 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}.
-!- 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:0000269|PubMed:16140733}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; M12349; AAA47712.1; -; Genomic_RNA.
PIR; D25839; VCLJMP.
RefSeq; NP_056894.1; NC_001550.1.
PDB; 4JF3; X-ray; 1.70 A; A/B=412-513.
PDBsum; 4JF3; -.
ProteinModelPortal; P07575; -.
SMR; P07575; -.
PRIDE; P07575; -.
GeneID; 2746973; -.
OrthoDB; VOG09000077; -.
Proteomes; UP000008870; 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.
InterPro; IPR018154; TLV/ENV_coat_polyprotein.
PANTHER; PTHR10424; PTHR10424; 1.
Pfam; PF00429; TLV_coat; 1.
1: Evidence at protein level;
3D-structure; 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; Membrane;
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 22 {ECO:0000255}.
CHAIN 23 586 Envelope glycoprotein.
/FTId=PRO_0000239595.
CHAIN 23 394 Surface protein. {ECO:0000250}.
/FTId=PRO_0000040787.
CHAIN 395 568 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000040788.
PEPTIDE 569 586 R-peptide.
/FTId=PRO_0000239596.
TOPO_DOM 23 526 Extracellular. {ECO:0000255}.
TRANSMEM 527 547 Helical. {ECO:0000255}.
TOPO_DOM 548 586 Cytoplasmic. {ECO:0000255}.
REGION 398 418 Fusion peptide. {ECO:0000250}.
REGION 458 474 Immunosuppression. {ECO:0000250}.
COILED 419 469 {ECO:0000255}.
COILED 479 515 {ECO:0000255}.
MOTIF 247 250 CXXC.
MOTIF 475 483 CX6CC.
MOTIF 570 573 YXXL motif; contains endocytosis signal.
COMPBIAS 505 508 Poly-Arg.
SITE 394 395 Cleavage; by host. {ECO:0000250}.
SITE 568 569 Cleavage; by viral protease.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 247 483 Interchain (between SU and TM chains, or
C-250 with C-483); in linked form.
{ECO:0000250}.
DISULFID 247 250 {ECO:0000250}.
DISULFID 475 482 {ECO:0000250}.
MUTAGEN 568 568 V->A: Complete loss of R-peptide
cleavage. {ECO:0000269|PubMed:16140733}.
MUTAGEN 569 569 H->A: Complete loss of R-peptide
cleavage. {ECO:0000269|PubMed:16140733}.
MUTAGEN 570 570 Y->A: Reduced endocytosis of TM and
incorporation into virions.
MUTAGEN 573 573 L->A: Reduced endocytosis of TM and
incorporation into virions.
HELIX 424 467 {ECO:0000244|PDB:4JF3}.
HELIX 469 471 {ECO:0000244|PDB:4JF3}.
HELIX 474 478 {ECO:0000244|PDB:4JF3}.
HELIX 489 511 {ECO:0000244|PDB:4JF3}.
SEQUENCE 586 AA; 63883 MW; 3CE7A399D9E2F450 CRC64;
MNFNYHFIWS LVILSQISQV QAGFGDPREA LAEIQQKHGK PCDCAGGYVS SPPINSLTTV
SCSTHTAYSV TNSLKWQCVS TPTTPSNTHI GSCPGECNTI SYDSVHASCY NHYQQCNIGN
KTYLTATITG DRTPAIGDGN VPTVLGTSHN LITAGCPNGK KGQVVCWNSR PSVHISDGGG
PQDKARDIIV NKKFEELHRS LFPELSYHPL ALPEARGKEK IDAHTLDLLA TVHSLLNASQ
PSLAEDCWLC LQSGDPVPLA LPYNDTLCSN FACLSNHSCP LTPPFLVQPF NFTDSNCLYA
HYQNNSFDID VGLASFTNCS SYYNVSTASK PSNSLCAPNS SVFVCGNNKA YTYLPTNWTG
SCVLATLLPD IDIIPGSEPV PIPAIDHFLG KAKRAIQLIP LFVGLGITTA VSTGAAGLGV
SITQYTKLSH QLISDVQAIS STIQDLQDQV DSLAEVVLQN RRGLDLLTAE QGGICLALQE
KCCFYANKSG IVRDKIKNLQ DDLERRRRQL IDNPFWTSFH GFLPYVMPLL GPLLCLLLVL
SFGPIIFNKL MTFIKHQIES IQAKPIQVHY HRLEQEDSGG SYLTLT


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