Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Envelope glycoprotein gp95

Gene

env

Organism
Avian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).By similarity
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Protein family/group databases

TCDBi1.G.12.1.1. the avian leukosis virus gp95 fusion protein (alv-gp95) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein gp95
Alternative name(s):
Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 85
Short name:
gp85
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 37
Short name:
gp37
Gene namesi
Name:env
OrganismiAvian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A))
Taxonomic identifieri269446 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirus
Virus hostiGallus gallus (Chicken) [TaxID: 9031]
Proteomesi
  • UP000002238 Componenti: Genome

Subcellular locationi

Surface protein :
  • Virion membrane; Peripheral membrane protein
  • Host cell membrane By similarity; Peripheral membrane protein By similarity

  • Note: The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini63 – 552490ExtracellularSequence analysisAdd
BLAST
Transmembranei553 – 57321HelicalSequence analysisAdd
BLAST
Topological domaini574 – 60633CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 6262Sequence analysisAdd
BLAST
Chaini63 – 606544Envelope glycoprotein gp95PRO_0000239600Add
BLAST
Chaini63 – 401339Surface proteinBy similarityPRO_0000040799Add
BLAST
Chaini402 – 606205Transmembrane proteinBy similarityPRO_0000040800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi120 – 1201N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi141 – 1411N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi158 – 1581N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi178 – 1781N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi257 – 2571N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi291 – 2911N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi297 – 2971N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi307 – 3071N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi315 – 3151N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi391 – 3911N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi453 – 4531N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi501 – 5011N-linked (GlcNAc...); by hostSequence analysis
Lipidationi565 – 5651S-palmitoyl cysteine; by hostBy similarity
Lipidationi568 – 5681S-palmitoyl cysteine; by hostBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).By similarity
The transmembrane protein is palmitoylated. Palmitoylation is necessary for glycoprotein function and infectivity (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei401 – 4022Cleavage; by hostBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond.By similarity

Structurei

Secondary structure

1
606
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni419 – 4213Combined sources
Turni424 – 4263Combined sources
Beta strandi427 – 4293Combined sources
Turni430 – 4323Combined sources
Helixi433 – 44412Combined sources
Helixi452 – 48635Combined sources
Helixi491 – 4933Combined sources
Turni495 – 4984Combined sources
Helixi506 – 52116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNLNMR-A418-445[»]
4JPRX-ray2.00A452-522[»]
5H9CX-ray1.78A452-522[»]
ProteinModelPortaliP03397.
SMRiP03397. Positions 418-445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03397.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni418 – 43821Fusion peptideAdd
BLAST
Regioni474 – 49017ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili435 – 48551Sequence analysisAdd
BLAST
Coiled coili503 – 53331Sequence analysisAdd
BLAST

Domaini

The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR005166. RSV_p95_env.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PfamiPF03708. Avian_gp85. 1 hit.
PF00429. TLV_coat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAVIKAFLT GYPGKTSKKD SKEKPLATSK KDPEKTPLLP TRVNYILIIG
60 70 80 90 100
VLVLCEVTGV RADVHLLEQP GNLWITWANR TGQTDFCLST QSATSPFQTC
110 120 130 140 150
LIGIPSPISE GDFKGYVSDN CTTLGTDRLV SSADFTGGPD NSTTLTYRKV
160 170 180 190 200
SCLLLKLNVS MWDEPHELQL LGSQSLPNIT NIAQISGITG GCVGFRPQGV
210 220 230 240 250
PWYLGWSRQE ATRFLLRHPS FSKSTEPFTV VTADRHNLFM GSEYCGAYGY
260 270 280 290 300
RFWNMYNCSQ VGRQYRCGNA RSPRPGLPEI QCTRRGGKWV NQSQEINESE
310 320 330 340 350
PFSFTVNCTA SSLGNASGCC GKAGTILPGK WVDSTQGSFT KPKALPPAIF
360 370 380 390 400
LICGDRAWQG IPSRPVGGPC YLGKLTMLAP KHTDILKVLV NSSRTGIRRK
410 420 430 440 450
RSTSHLDDTC SDEVQLWGPT ARIFASILAP GVAAAQALRE IERLACWSVK
460 470 480 490 500
QANLTTSLLG DLLDDVTSIR HAVLQNRAAI DFLLLAHGHG CEDVAGMCCF
510 520 530 540 550
NLSDHSESIQ KKFQLMKEHV NKIGVDSDPI GSWLRGLFGG IGEWAVHLLK
560 570 580 590 600
GLLLGLVVIL LLVVCLPCLL QIVCGNIRKM INNSISYHTE YKKLQKACGQ

PESRIV
Length:606
Mass (Da):66,325
Last modified:September 27, 2004 - v2
Checksum:i4A87F20967FFF6F3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811K → N in AAA42564 (PubMed:6292477).Curated
Sequence conflicti388 – 3881V → I (PubMed:6292477).Curated
Sequence conflicti390 – 3901V → A (PubMed:6292477).Curated
Sequence conflicti403 – 4031T → V in AAA42564 (PubMed:6292477).Curated
Sequence conflicti434 – 4341A → R in AAA91268 (PubMed:1311072).Curated
Sequence conflicti439 – 4391R → K in AAA42564 (PubMed:6292477).Curated
Sequence conflicti458 – 4581L → F in AAA91268 (PubMed:1311072).Curated
Sequence conflicti505 – 5051H → Q (PubMed:6253794).Curated
Sequence conflicti505 – 5051H → Q (PubMed:6298633).Curated
Sequence conflicti529 – 5291P → L (PubMed:6253794).Curated
Sequence conflicti529 – 5291P → L (PubMed:6298633).Curated
Sequence conflicti572 – 5732IV → ML (PubMed:6253794).Curated
Sequence conflicti572 – 5732IV → ML (PubMed:6298633).Curated
Sequence conflicti577 – 5771I → R (PubMed:6253794).Curated
Sequence conflicti577 – 5771I → R (PubMed:6298633).Curated
Sequence conflicti598 – 5981C → Y in AAA42564 (PubMed:6292477).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01169 Genomic RNA. Translation: CAA24494.1.
L29199 Genomic DNA. Translation: AAA42562.1.
K00928 Genomic RNA. Translation: AAA42564.1.
M37980 Genomic RNA. Translation: AAA91268.1.
PIRiB38017. VCFV37.
S35427.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01169 Genomic RNA. Translation: CAA24494.1.
L29199 Genomic DNA. Translation: AAA42562.1.
K00928 Genomic RNA. Translation: AAA42564.1.
M37980 Genomic RNA. Translation: AAA91268.1.
PIRiB38017. VCFV37.
S35427.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNLNMR-A418-445[»]
4JPRX-ray2.00A452-522[»]
5H9CX-ray1.78A452-522[»]
ProteinModelPortaliP03397.
SMRiP03397. Positions 418-445.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.G.12.1.1. the avian leukosis virus gp95 fusion protein (alv-gp95) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03397.

Family and domain databases

InterProiIPR005166. RSV_p95_env.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PfamiPF03708. Avian_gp85. 1 hit.
PF00429. TLV_coat. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product."
    Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E., Goodman H.M.
    Nature 287:198-203(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Corrections to the nucleotide sequence of the src gene of Rous sarcoma virus."
    Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E., Goodman H.
    Nature 301:736-738(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "DNA sequence of the viral and cellular src gene of chickens. 1. Complete nucleotide sequence of an EcoRI fragment of recovered avian sarcoma virus which codes for gp37 and pp60src."
    Takeya T., Feldman R.A., Hanafusa H.
    J. Virol. 44:1-11(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate td mutant 1441.
  4. "Complete nucleotide sequence of a highly infectious avian leukosis virus."
    Bieth E., Darlix J.L.
    Nucleic Acids Res. 20:367-367(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  5. "Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus."
    Cheng S.F., Wu C.W., Kantchev E.A., Chang D.K.
    Eur. J. Biochem. 271:4725-4736(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE FUSION PEPTIDE.
  6. "Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation."
    Delos S.E., Godby J.A., White J.M.
    J. Virol. 79:3488-3499(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FUSION.

Entry informationi

Entry nameiENV_RSVSA
AccessioniPrimary (citable) accession number: P03397
Secondary accession number(s): Q03803, Q85500
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 27, 2004
Last modified: April 13, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.