ENV_MPMV
ID ENV_MPMV Reviewed; 586 AA.
AC P07575;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 114.
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 Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 20;
DE Short=gp20;
DE Contains:
DE RecName: Full=R-peptide;
DE AltName: Full=p2E;
DE Flags: Precursor;
GN Name=env;
OS Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11855;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE 6A).
RX PubMed=2421920; DOI=10.1016/0092-8674(86)90323-5;
RA Sonigo P., Barker C., Hunter E., Wain-Hobson S.;
RT "Nucleotide sequence of Mason-Pfizer monkey virus: an immunosuppressive D-
RT type retrovirus.";
RL Cell 45:375-385(1986).
RN [2]
RP CLEAVAGE OF R-PEPTIDE, DOMAIN YXXL MOTIF, AND MUTAGENESIS OF VAL-568 AND
RP HIS-569.
RX PubMed=16140733; DOI=10.1128/jvi.79.18.11559-11568.2005;
RA Song C., Micoli K., Bauerova H., Pichova I., Hunter E.;
RT "Amino acid residues in the cytoplasmic domain of the Mason-Pfizer monkey
RT virus glycoprotein critical for its incorporation into virions.";
RL J. Virol. 79:11559-11568(2005).
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 -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Membranes fusion leads to
CC delivery of the nucleocapsid into the cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached by a labile interchain disulfide bond.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the extravirion surface through its
CC binding to TM. Both proteins are thought to be concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC viral release at the surface of infected mononuclear cells and promotes
CC endocytosis. {ECO:0000269|PubMed:16140733}.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By similarity). {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. The
CC cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC [KR]-R. The R-peptide is released from the C-terminus of the
CC cytoplasmic tail of the TM protein upon particle formation as a result
CC of proteolytic cleavage by the viral protease. Cleavage of this peptide
CC is required for TM to become fusogenic (By similarity). {ECO:0000250}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion (By
CC similarity). {ECO:0000250}.
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DR EMBL; M12349; AAA47712.1; -; Genomic_RNA.
DR PIR; D25839; VCLJMP.
DR RefSeq; NP_056894.1; NC_001550.1.
DR PDB; 4JF3; X-ray; 1.70 A; A/B=412-513.
DR PDBsum; 4JF3; -.
DR SMR; P07575; -.
DR GeneID; 2746973; -.
DR Proteomes; UP000008870; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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 InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Coiled coil;
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; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..586
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239595"
FT CHAIN 23..394
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040787"
FT CHAIN 395..568
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040788"
FT PEPTIDE 569..586
FT /note="R-peptide"
FT /id="PRO_0000239596"
FT TOPO_DOM 23..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 398..418
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 458..474
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 419..469
FT /evidence="ECO:0000255"
FT COILED 479..515
FT /evidence="ECO:0000255"
FT MOTIF 247..250
FT /note="CXXC"
FT MOTIF 475..483
FT /note="CX6CC"
FT MOTIF 570..573
FT /note="YXXL motif; contains endocytosis signal"
FT SITE 394..395
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 568..569
FT /note="Cleavage; by viral protease"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 247..483
FT /note="Interchain (between SU and TM chains, or C-250 with
FT C-483); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 247..250
FT /evidence="ECO:0000250"
FT DISULFID 475..482
FT /evidence="ECO:0000250"
FT MUTAGEN 568
FT /note="V->A: Complete loss of R-peptide cleavage."
FT /evidence="ECO:0000269|PubMed:16140733"
FT MUTAGEN 569
FT /note="H->A: Complete loss of R-peptide cleavage."
FT /evidence="ECO:0000269|PubMed:16140733"
FT MUTAGEN 570
FT /note="Y->A: Reduced endocytosis of TM and incorporation
FT into virions."
FT MUTAGEN 573
FT /note="L->A: Reduced endocytosis of TM and incorporation
FT into virions."
FT HELIX 424..467
FT /evidence="ECO:0007829|PDB:4JF3"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:4JF3"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:4JF3"
FT HELIX 489..511
FT /evidence="ECO:0007829|PDB:4JF3"
SQ 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
