ENV_BLV
ID ENV_BLV Reviewed; 515 AA.
AC P51519; Q85488; Q85489;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 51;
DE Short=gp51;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 30;
DE Short=gp30;
DE Flags: Precursor;
GN Name=env;
OS Bovine leukemia virus (BLV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11901;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6093363; DOI=10.1016/0042-6822(84)90149-1;
RA Rice N.R., Stephens R.M., Couez D., Deschamps J., Kettmann R., Burny A.,
RA Gilden R.V.;
RT "The nucleotide sequence of the env gene and post-env region of bovine
RT leukemia virus.";
RL Virology 138:82-93(1984).
RN [2]
RP INTERCHAIN DISULFIDE BOND.
RX PubMed=10684314; DOI=10.1128/jvi.74.6.2930-2935.2000;
RA Johnston E.R., Radke K.;
RT "The SU and TM envelope protein subunits of bovine leukemia virus are
RT linked by disulfide bonds, both in cells and in virions.";
RL J. Virol. 74:2930-2935(2000).
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 -!- 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}. Note=It is probably concentrated at the site of budding
CC and incorporated into the virions possibly by contacts between the
CC cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Host cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The
CC surface protein is not anchored to the viral envelope, but associates
CC with the extravirion surface through its binding to TM. It is probably
CC concentrated at the site of budding and incorporated into the virions
CC possibly by contacts between the cytoplasmic tail of Env and the N-
CC terminus of Gag (By similarity). {ECO:0000250}.
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 (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.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
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DR EMBL; K02251; AAA42788.1; -; Genomic_RNA.
DR RefSeq; NP_056899.1; NC_001414.1.
DR PDB; 2XZ3; X-ray; 1.95 A; A=326-418.
DR PDBsum; 2XZ3; -.
DR SMR; P51519; -.
DR ELM; P51519; -.
DR GeneID; 2760848; -.
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; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..515
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239556"
FT CHAIN 34..301
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040699"
FT CHAIN 302..515
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040700"
FT TOPO_DOM 34..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 304..324
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 365..381
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 330..376
FT /evidence="ECO:0000255"
FT COILED 388..420
FT /evidence="ECO:0000255"
FT MOTIF 212..215
FT /note="CXXC"
FT MOTIF 384..392
FT /note="CX6CC"
FT SITE 301..302
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 455
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 212..392
FT /note="Interchain (between SU and TM chains, or C-215 with
FT C-392); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 212..215
FT /evidence="ECO:0000250"
FT DISULFID 384..391
FT /evidence="ECO:0000250"
SQ SEQUENCE 515 AA; 58640 MW; 69B028B4586AC1A5 CRC64;
MPKERRSRRR PQPIIRWVSL TLTLLALCQP IQTWRCSLSL GNQQWMTTYN QEAKFSISID
QILEAHNQSP FCPRSPRYTL DFVNGYPKIY WPPPQGRRRF GARAMVTYDC EPRCPYVGAD
HFDCPHWDNA SQADQGSFYV NHQILFLHLK QCHGIFTLTW EIWGYDPLIT FSLHKIPDPP
QPDFPQLNSD WVPSVRSWAL LLNQTARAFP DCAICWEPSP PWAPEILVYN KTISGSGPGL
ALPDAQIFWV NTSLFNTTQG WHHPSQRLLF NVSQGNALLL PPISLVNLST VSSAPPTRVR
RSPVAALTLG LALSVGLTGI NVAVSALSHQ RLTSLIHVLE QDQQRLITAI NQTHYNLLNV
ASVVAQNRRG LDWLYIRLGF QSLCPTINEP CCFLRIQNDS IIRLGDLQPL SQRVSTDWQW
PWNWDLGLTA WVRETIHSVL SLFLLALFLL FLAPCLIKCL TSRLLKLLRQ APHFPEISFP
PKPDSDYQAL LPSAPEIYSH LSPTKPDYIN LRPCP
