ENV_SRV1
ID ENV_SRV1 Reviewed; 587 AA.
AC P04027;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 25-MAY-2022, entry version 101.
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 Flags: Precursor;
GN Name=env;
OS Simian retrovirus SRV-1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11942;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3006247; DOI=10.1126/science.3006247;
RA Power M.D., Marx P.A., Bryant M.L., Gardner M.B., Barr P.J., Luciw P.A.;
RT "Nucleotide sequence of SRV-1, a type D simian acquired immune deficiency
RT syndrome retrovirus.";
RL Science 231:1567-1572(1986).
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: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. 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; M11841; AAA47733.1; -; Genomic_RNA.
DR SMR; P04027; -.
DR Proteomes; UP000007228; 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 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; 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..587
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239603"
FT CHAIN 23..395
FT /note="Surface protein"
FT /id="PRO_0000040803"
FT CHAIN 396..569
FT /note="Transmembrane protein"
FT /id="PRO_0000040804"
FT PEPTIDE 570..587
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239604"
FT TOPO_DOM 23..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 399..419
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 459..475
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 420..470
FT /evidence="ECO:0000255"
FT COILED 480..516
FT /evidence="ECO:0000255"
FT MOTIF 248..251
FT /note="CXXC"
FT MOTIF 476..484
FT /note="CX6CC"
FT MOTIF 571..574
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT SITE 395..396
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 569..570
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
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 266
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 277
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 248..484
FT /note="Interchain (between SU and TM chains, or C-251 with
FT C-484); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 248..251
FT /evidence="ECO:0000250"
FT DISULFID 476..483
FT /evidence="ECO:0000250"
SQ SEQUENCE 587 AA; 64475 MW; 80939DD3BFB65A8D CRC64;
MNFNHHFTWS LVIISQIFQV QAGFGDPREA LLEIQQKHGK PCDCAGGYVS SPPTNSLTTV
SCSTYTAYSV TNSLKWQCVS TPTTASPTHI GSCPSQCNSQ SYDSVHATCY NHYQQCTIGN
KTYLTATMIR DKSPSSGDGN VPTILGNNQN LIIAGCPENK KGQVVCWNSQ PSVHMSDGGG
PQDKVREIIV NKKFEELHKS LFPELSYHPL ALPEARGKEK IDAHTFDLLA TVHSLLNVSS
QRQLAEDCWL CLRSGDPVPL ALPYDNTSCS NSTFFFNCSN CSCLITPPFL VQPFNFTHSV
CLYADYQNNS FDIDVGLAGF TNCSSYINIS KPSSPLCAPN SSVFVCGNNK AYTYLPTNWT
GSCVLATLLP DIDIIPGSEP VPIPAIDHFL GRPKRAIQFI PLVIGLGITT AVSTGTAGLG
VSLTQYTKLS HQLISDVQAI SSTIQDLQDQ VDSLAEVVLQ NRRGLDLLTA EQGGICLALQ
EKCCFYANKS GIVRDKIKNL QDDLEKRRKQ LIDNPFWTGF HGLLPYVMPL LGPLLCLLLV
LSFGPIIFNK LMTFIKHQIE SIQAKPIQVH YHRLEQEDHG GSYLNLT
