ENV_RSVP
ID ENV_RSVP Reviewed; 603 AA.
AC P03396; Q64984; Q86355;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Envelope glycoprotein gp95;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 85;
DE Short=gp85;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 37;
DE Short=gp37;
DE Flags: Precursor;
GN Name=env;
OS Rous sarcoma virus (strain Prague C) (RSV-PrC).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11888;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-17; SER-134; SER-158;
RP THR-334; THR-383; VAL-392; GLU-522; LEU-541 AND VAL-567.
RX PubMed=6299578; DOI=10.1016/0092-8674(83)90071-5;
RA Schwartz D., Tizard R., Gilbert W.;
RT "Nucleotide sequence of Rous sarcoma virus.";
RL Cell 32:853-869(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2982497; DOI=10.1016/0092-8674(85)90202-8;
RA Broome S., Gilbert W.;
RT "Rous sarcoma virus encodes a transcriptional activator.";
RL Cell 40:537-546(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-603, AND VARIANT VAL-567.
RX PubMed=2538803; DOI=10.1093/nar/17.5.2120;
RA Kashuba V.I., Zubak S.V., Lazurkevitch Z.V., Rynditch A.V., Kavsan V.M.,
RA Svoboda S.;
RT "The nucleotide sequence of the region of src gene deletion in
RT transformation-defective Rous sarcoma virus adapted to semi-permissive host
RT cells.";
RL Nucleic Acids Res. 17:2120-2120(1989).
RN [4]
RP PALMITOYLATION AT CYS-569 AND CYS-572 OF THE TRANSMEMBRANE PROTEIN, AND
RP MUTAGENESIS OF CYS-569 AND CYS-572.
RX PubMed=11689636; DOI=10.1128/jvi.75.23.11544-11554.2001;
RA Ochsenbauer-Jambor C., Miller D.C., Roberts C.R., Rhee S.S., Hunter E.;
RT "Palmitoylation of the Rous sarcoma virus transmembrane glycoprotein is
RT required for protein stability and virus infectivity.";
RL J. Virol. 75:11544-11554(2001).
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 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 transmembrane protein is palmitoylated. Palmitoylation is
CC necessary for glycoprotein function and infectivity.
CC {ECO:0000269|PubMed:11689636}.
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DR EMBL; V01197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J02342; AAB59934.1; -; Genomic_RNA.
DR EMBL; X13818; CAA32051.1; -; Genomic_DNA.
DR PIR; A03996; VCFVER.
DR SMR; P03396; -.
DR SwissPalm; P03396; -.
DR Proteomes; UP000007183; 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; IPR005166; RSV_p95_env.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF03708; Avian_gp85; 1.
DR Pfam; PF00429; TLV_coat; 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; 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..64
FT /evidence="ECO:0000255"
FT CHAIN 65..603
FT /note="Envelope glycoprotein gp95"
FT /id="PRO_0000239599"
FT CHAIN 65..405
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040797"
FT CHAIN 406..603
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040798"
FT TOPO_DOM 65..556
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 422..442
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 478..494
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 439..489
FT /evidence="ECO:0000255"
FT COILED 507..537
FT /evidence="ECO:0000255"
FT SITE 405..406
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 569
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:11689636"
FT LIPID 572
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:11689636"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 17
FT /note="K -> E"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 134
FT /note="L -> S"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 158
FT /note="L -> S"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 334
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 383
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 392
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 522
FT /note="K -> E"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 541
FT /note="I -> L"
FT /evidence="ECO:0000269|PubMed:6299578"
FT VARIANT 567
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:2538803,
FT ECO:0000269|PubMed:6299578"
FT MUTAGEN 569
FT /note="C->G: Reduced palmitoylation level. Slightly reduced
FT cell surface expression."
FT /evidence="ECO:0000269|PubMed:11689636"
FT MUTAGEN 572
FT /note="C->G: Reduced palmitoylation level. Reduced cell
FT surface expression. This mutant is degraded faster."
FT /evidence="ECO:0000269|PubMed:11689636"
FT CONFLICT 1..8
FT /note="MRRALFLQ -> MEAVIK (in Ref. 2; AAB59934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 65661 MW; D44EC2AA62282C94 CRC64;
MRRALFLQAF LTGYPGKTSK KDSKEKPLAT SKKDPEKTPL LPTRVNYILI IGVLVLCEVT
GVRADVHLLE QPGNLWITWA NRTGQTDFCL STQSATSPFQ TCLIGIPSPI SEGDFKGYVS
DTNCSTVGTD RLVLSASITG GPDNSTTLTY RKVSCLLLKL NVSMWDEPPE LQLLGSQSLP
NVTNITQVSG VAGGCVYFAP RATGLFLGWS KQGLSRFLLR HPFTSTSNST EPFTVVTADR
HNLFMGSEYC GAYGYRFWEI YNCSQTRNTY RCGDVGGTGL PETWCRGKGG IWVNQSKEIN
ETEPFSFTAN CTGSNLGNVS GCCGEPITIL PLGAWIDSTQ GSFTKPKALP PAIFLICGDR
AWQGIPSRPV GGPCYLGKLT MLAPNHTDIL KILANSSRTG IRRKRSVSHL DDTCSDEVQL
WGPTARIFAS ILAPGVAAAQ ALREIERLAC WSVKQANLTT SLLGDLLDDV TSIRHAVLQN
RAAIDFLLLA HGHGCEDVAG MCCFNLSDHS ESIQKKFQLM KKHVNKIGVD SDPIGSWLRG
IFGGIGEWAV HLLKGLLLGL VVILLLLVCL PCLLQFVSSS IRKMINSSIN YHTEYRKMQG
GAV
