ENV_MLVHO
ID ENV_MLVHO Reviewed; 666 AA.
AC P21436;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 76;
DE Short=gp76;
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 Hortulanus murine leukemia virus (HoMuLV) (Mus hortulanus virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11799;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2554579; DOI=10.1016/0042-6822(89)90221-3;
RA Voytek P., Kozak C.A.;
RT "Nucleotide sequence and mode of transmission of the wild mouse ecotropic
RT virus, HoMuLV.";
RL Virology 173:58-67(1989).
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; M26527; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; B32594; VCMVHL.
DR SMR; P21436; -.
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..666
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239585"
FT CHAIN 34..466
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040760"
FT CHAIN 467..646
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040761"
FT PEPTIDE 647..666
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239586"
FT TOPO_DOM 34..607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 31..264
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255"
FT REGION 265..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..489
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 535..551
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 500..534
FT /evidence="ECO:0000255"
FT MOTIF 334..337
FT /note="CXXC"
FT MOTIF 552..560
FT /note="CX6CC"
FT MOTIF 652..655
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 270..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 466..467
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 646..647
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT LIPID 627
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
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:0000250"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 76..127
FT /evidence="ECO:0000250"
FT DISULFID 102..116
FT /evidence="ECO:0000250"
FT DISULFID 103..112
FT /evidence="ECO:0000250"
FT DISULFID 150..170
FT /evidence="ECO:0000250"
FT DISULFID 162..175
FT /evidence="ECO:0000250"
FT DISULFID 207..213
FT /evidence="ECO:0000250"
FT DISULFID 334..560
FT /note="Interchain (between SU and TM chains, or C-337 with
FT C-560); in linked form"
FT DISULFID 334..337
FT DISULFID 364..417
FT /evidence="ECO:0000250"
FT DISULFID 424..437
FT /evidence="ECO:0000250"
FT DISULFID 552..560
FT /evidence="ECO:0000250"
SQ SEQUENCE 666 AA; 73035 MW; FDC77956E4B213D1 CRC64;
MDRPALPKSI KDKTNPWGPI ILGILIMLGG ALGKGSPHKV FNLTWEVYNQ EYETVWATSG
SHPLWTWWPT LTPDLCMLAQ LAKPSWGLSD YPPYSKPPGP PCCTTDNNPP GCSRDCNGPL
TYLTPRCSTA WNRLKLVLTT HHLNQGFYVC PGPHRPRHAR NCGGPDDFYC AHWGCETTGQ
AYWKPSSSWD YIRVSNNASS SDATTACKNN NWCSPLAISF TDPGKRATSW TSGFTWGLRL
YISGHPGLIF GVRLKISDLG PRVPIGPNPV LSEQRPPSQP EPARLPPSSN LTQGGTPSAP
TGPPQEGTGD RLLDLVQGAY QALNATSPDK TQECWLCLVS SPPYYEGVAV VGPYSNHTTA
PANCSADSQH KLTLSEVTGK PLPRKGSQDP PGPVQYHSGA RQKYSLSGGS RGTMWACNTG
LTPCLSTAVL NLTTDYCVLV ELWPRVTYHS LDFVYRQVEG RTRYQREPVS LTLALLLGGL
TMGGIAAGVG TGTSALVKTQ QFEQLHAAIQ ADLKEVESSI TNLEKSLTSL SEVVLQNRRG
LDLLFLEKGG LCAALKEECC FYADHTGLVR DSMAKLRERL NQRQKLFEAG QGWFEGLFNR
SPWLTTLIST IMGPLIILLL ILMFGPCILN RLVQFVKDRI SVVQALVLTQ QYHQLKPLEH
GRAIVK
