ENV_RSVSA
ID ENV_RSVSA Reviewed; 606 AA.
AC P03397; Q03803; Q85500;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 115.
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 Avian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain
OS Schmidt-Ruppin A)).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=269446;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6253794; DOI=10.1038/287198a0;
RA Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E.,
RA Goodman H.M.;
RT "Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed
RT amino acid sequence for gene product.";
RL Nature 287:198-203(1980).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=6298633; DOI=10.1038/301736b0;
RA Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E.,
RA Goodman H.;
RT "Corrections to the nucleotide sequence of the src gene of Rous sarcoma
RT virus.";
RL Nature 301:736-738(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate td mutant 1441;
RX PubMed=6292477; DOI=10.1128/jvi.44.1.1-11.1982;
RA Takeya T., Feldman R.A., Hanafusa H.;
RT "DNA sequence of the viral and cellular src gene of chickens. 1. Complete
RT nucleotide sequence of an EcoRI fragment of recovered avian sarcoma virus
RT which codes for gp37 and pp60src.";
RL J. Virol. 44:1-11(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1311072; DOI=10.1093/nar/20.2.367;
RA Bieth E., Darlix J.L.;
RT "Complete nucleotide sequence of a highly infectious avian leukosis
RT virus.";
RL Nucleic Acids Res. 20:367-367(1992).
RN [5]
RP CHARACTERIZATION OF THE FUSION PEPTIDE.
RX PubMed=15606759; DOI=10.1111/j.1432-1033.2004.04436.x;
RA Cheng S.F., Wu C.W., Kantchev E.A., Chang D.K.;
RT "Structure and membrane interaction of the internal fusion peptide of avian
RT sarcoma leukosis virus.";
RL Eur. J. Biochem. 271:4725-4736(2004).
RN [6]
RP FUNCTION IN FUSION.
RX PubMed=15731243; DOI=10.1128/jvi.79.6.3488-3499.2005;
RA Delos S.E., Godby J.A., White J.M.;
RT "Receptor-induced conformational changes in the SU subunit of the avian
RT sarcoma/leukosis virus A envelope protein: implications for fusion
RT activation.";
RL J. Virol. 79:3488-3499(2005).
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 (By similarity).
CC {ECO:0000250}.
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DR EMBL; V01169; CAA24494.1; -; Genomic_RNA.
DR EMBL; L29199; AAA42562.1; -; Genomic_DNA.
DR EMBL; K00928; AAA42564.1; -; Genomic_RNA.
DR EMBL; M37980; AAA91268.1; -; Genomic_RNA.
DR PIR; B38017; VCFV37.
DR PIR; S35427; S35427.
DR RefSeq; NP_040548.1; NC_001408.1.
DR PDB; 1XNL; NMR; -; A=418-445.
DR PDB; 4JPR; X-ray; 2.00 A; A=452-522.
DR PDB; 5H9C; X-ray; 1.78 A; A=452-522.
DR PDBsum; 1XNL; -.
DR PDBsum; 4JPR; -.
DR PDBsum; 5H9C; -.
DR SMR; P03397; -.
DR TCDB; 1.G.12.1.1; the avian leukosis virus gp95 fusion protein (alv-gp95) family.
DR PRIDE; P03397; -.
DR GeneID; 1491907; -.
DR KEGG; vg:1491907; -.
DR EvolutionaryTrace; P03397; -.
DR Proteomes; UP000002238; 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 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; 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..62
FT /evidence="ECO:0000255"
FT CHAIN 63..606
FT /note="Envelope glycoprotein gp95"
FT /id="PRO_0000239600"
FT CHAIN 63..401
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040799"
FT CHAIN 402..606
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040800"
FT TOPO_DOM 63..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 418..438
FT /note="Fusion peptide"
FT REGION 474..490
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 435..485
FT /evidence="ECO:0000255"
FT COILED 503..533
FT /evidence="ECO:0000255"
FT SITE 401..402
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 565
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 568
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 381
FT /note="K -> N (in Ref. 3; AAA42564)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="V -> I (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="V -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="T -> V (in Ref. 3; AAA42564)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="A -> R (in Ref. 4; AAA91268)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="R -> K (in Ref. 3; AAA42564)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="L -> F (in Ref. 4; AAA91268)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="H -> Q (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="P -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..573
FT /note="IV -> ML (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="I -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="C -> Y (in Ref. 3; AAA42564)"
FT /evidence="ECO:0000305"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:1XNL"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:1XNL"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1XNL"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:1XNL"
FT HELIX 433..444
FT /evidence="ECO:0007829|PDB:1XNL"
FT HELIX 452..486
FT /evidence="ECO:0007829|PDB:5H9C"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:5H9C"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:5H9C"
FT HELIX 506..521
FT /evidence="ECO:0007829|PDB:5H9C"
SQ SEQUENCE 606 AA; 66325 MW; 4A87F20967FFF6F3 CRC64;
MEAVIKAFLT GYPGKTSKKD SKEKPLATSK KDPEKTPLLP TRVNYILIIG VLVLCEVTGV
RADVHLLEQP GNLWITWANR TGQTDFCLST QSATSPFQTC LIGIPSPISE GDFKGYVSDN
CTTLGTDRLV SSADFTGGPD NSTTLTYRKV SCLLLKLNVS MWDEPHELQL LGSQSLPNIT
NIAQISGITG GCVGFRPQGV PWYLGWSRQE ATRFLLRHPS FSKSTEPFTV VTADRHNLFM
GSEYCGAYGY RFWNMYNCSQ VGRQYRCGNA RSPRPGLPEI QCTRRGGKWV NQSQEINESE
PFSFTVNCTA SSLGNASGCC GKAGTILPGK WVDSTQGSFT KPKALPPAIF LICGDRAWQG
IPSRPVGGPC YLGKLTMLAP KHTDILKVLV NSSRTGIRRK RSTSHLDDTC SDEVQLWGPT
ARIFASILAP GVAAAQALRE IERLACWSVK QANLTTSLLG DLLDDVTSIR HAVLQNRAAI
DFLLLAHGHG CEDVAGMCCF NLSDHSESIQ KKFQLMKEHV NKIGVDSDPI GSWLRGLFGG
IGEWAVHLLK GLLLGLVVIL LLVVCLPCLL QIVCGNIRKM INNSISYHTE YKKLQKACGQ
PESRIV
