ENV_MLVCB
ID ENV_MLVCB Reviewed; 661 AA.
AC P08360;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=Envelope protein p15E;
DE Contains:
DE RecName: Full=R-peptide;
DE AltName: Full=p2E;
DE Flags: Precursor;
GN Name=env;
OS Cas-Br-E murine leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11792;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023680; DOI=10.1128/jvi.60.3.910-919.1986;
RA Rassart E., Nelbach L., Jolicoeur P.;
RT "Cas-Br-E murine leukemia virus: sequencing of the paralytogenic region of
RT its genome and derivation of specific probes to study its origin and the
RT structure of its recombinant genomes in leukemic tissues.";
RL J. Virol. 60:910-919(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840655; DOI=10.1093/nar/19.7.1707;
RA Perryman S.M., McAtee F.J., Portis J.L.;
RT "Complete nucleotide sequence of the neurotropic murine retrovirus CAS-BR-
RT E.";
RL Nucleic Acids Res. 19:1707-1707(1991).
RN [3]
RP CLEAVAGE OF R-PEPTIDE.
RX PubMed=12185279; DOI=10.1099/0022-1317-83-9-2241;
RA Bobkova M., Stitz J., Engelstadter M., Cichutek K., Buchholz C.J.;
RT "Identification of R-peptides in envelope proteins of C-type
RT retroviruses.";
RL J. Gen. Virol. 83:2241-2246(2002).
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 virion 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 -!- SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=The R-peptide is
CC membrane-associated through its palmitate. {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.
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}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
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DR EMBL; M14702; AAA46512.1; -; Genomic_DNA.
DR EMBL; X57540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B26103; VCMVCB.
DR SMR; P08360; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.90.310.10; -; 1.
DR InterPro; IPR008981; FMuLV_rcpt-bd.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW 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; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell;
KW Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..661
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239580"
FT CHAIN 34..465
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040748"
FT CHAIN 466..645
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040749"
FT PEPTIDE 646..661
FT /note="R-peptide"
FT /id="PRO_0000040750"
FT TOPO_DOM 34..606
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..267
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255"
FT REGION 268..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..488
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 534..550
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 497..533
FT /evidence="ECO:0000255"
FT MOTIF 332..335
FT /note="CXXC"
FT MOTIF 551..559
FT /note="CX6CC"
FT MOTIF 651..654
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 273..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 465..466
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 645..646
FT /note="Cleavage; by viral protease p14"
FT LIPID 626
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 77..129
FT /evidence="ECO:0000250"
FT DISULFID 103..118
FT /evidence="ECO:0000250"
FT DISULFID 104..114
FT /evidence="ECO:0000250"
FT DISULFID 152..172
FT /evidence="ECO:0000250"
FT DISULFID 164..177
FT /evidence="ECO:0000250"
FT DISULFID 209..215
FT /evidence="ECO:0000250"
FT DISULFID 332..559
FT /note="Interchain (between SU and TM chains, or C-335 with
FT C-559); in linked form"
FT DISULFID 332..335
FT DISULFID 362..416
FT /evidence="ECO:0000250"
FT DISULFID 381..393
FT /evidence="ECO:0000250"
FT DISULFID 423..436
FT /evidence="ECO:0000250"
FT DISULFID 551..558
FT /evidence="ECO:0000250"
FT CONFLICT 476..477
FT /note="PE -> LG (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 72625 MW; 255BEE3AF62FB9FF CRC64;
MEGPAFSKSP KDKTIERAFL GVLGILFVTG GLASRDNPHQ VYNITWEVTN GEQDTVWAVT
GNHPLWTWWP DLTPDLCMLA LHGPTHWGLD NHPPYSSPPG PPCCSGDAGA VSGCARDCDE
PLTSYSPRCN TAWNRLKLAR VTHAPKEGFY ICPGSHRPRW ARSCGGLDAY YCASWGCETT
GRAAWNPTSS WDYITVSNNL TSSQATKACK NNGWCNPLVI RFTGPGKRAT SWTTGHFWGL
RLYISGHDPG LTFGIRLKVT DLGPRVPIGP NPVLSDQRPP SRPVPARPPP PSASPSTPTI
PPQQGTGDRL LNLVQGAYLT LNMTDPTRTQ ECWLCLVSEP PYYEGVAVLR EYTSHETAPA
NCSSGSQHKL TLSEVTGQGR CLGTVPKTHQ ALCNRTEPTV SGSNYLVAPE GTLWACSTGL
TPCLSTTVLN LTTDYCVLVE LWPKVTYHSP DYVYTQFEPG ARFRREPVSL TLALLPEGLT
MGGIAAGVGT GTTALVATQQ FQQLQAAMHN DLKEVEKSIT NLEKSLTSLS EVVLQNRRGL
DLLFLKEGGL CAALKEECCF YADHTGLVRD SMAKLRERLN QRQKLFESGQ GWFEGLFNRS
PWFTTLISTI MGPLIVLLLI LLFGPCILNR LVQFVKDRIS VVQALVLTQQ YHQLKPIEYE
P
