ENV_HTL32
ID ENV_HTL32 Reviewed; 491 AA.
AC Q0R5Q9;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Envelope glycoprotein gp63;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 46;
DE Short=gp46;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 21;
DE Short=gp21;
DE Flags: Precursor;
GN Name=env;
OS Human T-cell leukemia virus 3 (strain 2026ND) (HTLV-3).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=402036;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16840323; DOI=10.1128/jvi.00690-06;
RA Switzer W.M., Qari S.H., Wolfe N.D., Burke D.S., Folks T.M., Heneine W.;
RT "Ancient origin and molecular features of the novel human T-lymphotropic
RT virus type 3 revealed by complete genome analysis.";
RL J. Virol. 80:7427-7438(2006).
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}. 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 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
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DR EMBL; DQ093792; AAZ77656.1; -; Genomic_DNA.
DR SMR; Q0R5Q9; -.
DR PRIDE; Q0R5Q9; -.
DR Proteomes; UP000008029; 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; 2.
PE 3: Inferred from homology;
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; Palmitate; Reference proteome; 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.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..491
FT /note="Envelope glycoprotein gp63"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259825"
FT CHAIN 21..313
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259826"
FT CHAIN 314..491
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259827"
FT TOPO_DOM 21..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 314..334
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 377..393
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 342..388
FT /evidence="ECO:0000255"
FT COILED 398..430
FT /evidence="ECO:0000255"
FT MOTIF 223..226
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 394..402
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT SITE 313..314
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT LIPID 463
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
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 305
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 223..402
FT /note="Interchain (between SU and TM chains, or C-226 with
FT C-402); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 223..226
FT /evidence="ECO:0000250"
FT DISULFID 394..401
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 54673 MW; 7CE74DAF6826F8FB CRC64;
MGKFCLYFCL IYILFSASSG NPSRCTLFIG ASSYHSDPCG SDHPRCTWRL DLFSLTRDQS
LSPPCPDLVT YSQYHRPYSL YVFPHWITKP NRRGLGYYSA SYSDPCAIQC PYLGCQSWTC
PYTGPVSSPH WKYSSDLNFT QEVSSISLHL HFSKCGSSFS FLLDAPGYDP VWFLSSQATQ
APPTPAPLIQ DSDLQHILEP SIPWSSKILN LILLTLKSSN YSCMVCVDRS SLSSWHVLYD
PLKAPNPPDP KAQSILRPSL AIPASNVTPP FPWTHCYRPL LQAISSEHCN NSVVLPPFSL
SPLPNVSRPR KRRAVPIAIW LVSALAAGTG IAGGVTGSLS LASSKSLLRE VDQDIDHLTQ
AIVKNHDNIL RVAQYAAQNR RGLDLLFWEQ GGLCKAIQEQ CCFLNISNTH VSVLQERPPL
EKRVITGWGL NWDLGLSQWA REALQTGITL LALFLLLIVV GPCVIRQLQA LPSRLQHRSQ
PYSLLNYETN L
