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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)DescriptionActionsGraphical viewLength
Topological domaini63 – 552ExtracellularSequence analysisAdd BLAST490
Transmembranei553 – 573HelicalSequence analysisAdd BLAST21
Topological domaini574 – 606CytoplasmicSequence analysisAdd BLAST33

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 62Sequence analysisAdd BLAST62
ChainiPRO_000023960063 – 606Envelope glycoprotein gp95Add BLAST544
ChainiPRO_000004079963 – 401Surface proteinBy similarityAdd BLAST339
ChainiPRO_0000040800402 – 606Transmembrane proteinBy similarityAdd BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi120N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi141N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi158N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi178N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi257N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi291N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi297N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi307N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi315N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi391N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi453N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi501N-linked (GlcNAc...); by hostSequence analysis1
Lipidationi565S-palmitoyl cysteine; by hostBy similarity1
Lipidationi568S-palmitoyl cysteine; by hostBy similarity1

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)DescriptionActionsGraphical viewLength
Sitei401 – 402Cleavage; by hostBy similarity2

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

1606
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni419 – 421Combined sources3
Turni424 – 426Combined sources3
Beta strandi427 – 429Combined sources3
Turni430 – 432Combined sources3
Helixi433 – 444Combined sources12
Helixi452 – 486Combined sources35
Helixi491 – 493Combined sources3
Turni495 – 498Combined sources4
Helixi506 – 521Combined sources16

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP03397.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni418 – 438Fusion peptideAdd BLAST21
Regioni474 – 490ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili435 – 485Sequence analysisAdd BLAST51
Coiled coili503 – 533Sequence analysisAdd BLAST31

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)DescriptionActionsGraphical viewLength
Sequence conflicti381K → N in AAA42564 (PubMed:6292477).Curated1
Sequence conflicti388V → I (PubMed:6292477).Curated1
Sequence conflicti390V → A (PubMed:6292477).Curated1
Sequence conflicti403T → V in AAA42564 (PubMed:6292477).Curated1
Sequence conflicti434A → R in AAA91268 (PubMed:1311072).Curated1
Sequence conflicti439R → K in AAA42564 (PubMed:6292477).Curated1
Sequence conflicti458L → F in AAA91268 (PubMed:1311072).Curated1
Sequence conflicti505H → Q (PubMed:6253794).Curated1
Sequence conflicti505H → Q (PubMed:6298633).Curated1
Sequence conflicti529P → L (PubMed:6253794).Curated1
Sequence conflicti529P → L (PubMed:6298633).Curated1
Sequence conflicti572 – 573IV → ML (PubMed:6253794).Curated2
Sequence conflicti572 – 573IV → ML (PubMed:6298633).Curated2
Sequence conflicti577I → R (PubMed:6253794).Curated1
Sequence conflicti577I → R (PubMed:6298633).Curated1
Sequence conflicti598C → Y in AAA42564 (PubMed:6292477).Curated1

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.
RefSeqiNP_040548.1. NC_001408.1.

Genome annotation databases

GeneIDi1491907.

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.
RefSeqiNP_040548.1. NC_001408.1.

3D structure databases

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

Genome annotation databases

GeneIDi1491907.

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...

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: November 2, 2016
This is version 100 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.