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Protein

Envelope glycoprotein

Gene

env

Organism
Avian reticuloendotheliosis virus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 73
Short name:
gp73
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 22
Short name:
gp22
Gene namesi
Name:env
OrganismiAvian reticuloendotheliosis virus
Taxonomic identifieri11636 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiGalliformes [TaxID: 8976]

Subcellular locationi

Transmembrane protein :
Surface protein :
  • Virion membrane By similarity; Peripheral membrane protein By similarity
  • 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. It is probably 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 domaini36 – 519ExtracellularSequence analysisAdd BLAST484
Transmembranei520 – 540HelicalSequence analysisAdd BLAST21
Topological domaini541 – 582CytoplasmicSequence analysisAdd BLAST42

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 – 35Sequence analysisAdd BLAST35
ChainiPRO_000023954636 – 582Envelope glycoproteinAdd BLAST547
ChainiPRO_000004068336 – 392Surface proteinBy similarityAdd BLAST357
ChainiPRO_0000040684393 – 582Transmembrane proteinBy similarityAdd BLAST190

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi241N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi251 ↔ 481Interchain (between SU and TM chains, or C-254 with C-481); in linked formBy similarity
Disulfide bondi251 ↔ 254By similarity
Glycosylationi301N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi314N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi473 ↔ 480By similarity
Glycosylationi485N-linked (GlcNAc...); by hostSequence analysis1
Lipidationi543S-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 CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity).By similarity
The transmembrane protein is palmitoylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei392 – 393Cleavage; 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

3D structure databases

ProteinModelPortaliP03399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni396 – 416Fusion peptideSequence analysisAdd BLAST21
Regioni456 – 472ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili417 – 467Sequence analysisAdd BLAST51
Coiled coili477 – 513Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi251 – 254CXXC4
Motifi473 – 481CX6CC9

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

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P03399-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDCLTDLRST EGKVDQAGKT LILLVVWWGF GTTAEGHPLQ QLWELPCDCS
60 70 80 90 100
GGYVSPDLPI TPTPSIAVAS PLPDLRVWLQ GSWGWGGGFR QQWECVFKPK
110 120 130 140 150
IIPSVQEQPG PCECLTIATQ MHSTCYEKAQ ECTLLGKTYF TAILQKTKLG
160 170 180 190 200
SYEDGPNKLL QASCTGIWET SMLGPRCPCV CLDGGGPTDR FGRICAEGLE
210 220 230 240 250
EIIRHSYPSV QYHPLALPRP RGVDLDPQTS DILEATHQVL NATNPQLAEN
260 270 280 290 300
CWLCMTLGTQ SPQPSRRMAM SLSMEIAVLA SLSGATHRVN RCQLLCREAD
310 320 330 340 350
NRTGIPVGYV HFTNCTSIQE SLTRRVIYEI LRDYVLHRVM YLCVEQHAYT
360 370 380 390 400
ALPNKWIGLC ILASIVPDMS IIPGEEPIPL PSIEYTAGRH KRAVQFIPLL
410 420 430 440 450
VGLGITGATL AGGTGLGVSV HTYHKLSNQL IEDVQALSGT INDLQDQIDS
460 470 480 490 500
LAEVVLQNRR GLDLLTAEQG GICLALQEKC CFYANKSGIV RDKIRKLQED
510 520 530 540 550
LLARKRALYD NPLWNGLNGF LPYLLPSLGP LFGLILFLTL GPCIRKTLTR
560 570 580
IIHDKIQGSK NPRISPAVQA TPNRDGYPRS MV
Length:582
Mass (Da):64,138
Last modified:July 21, 1986 - v1
Checksum:iCD2560ADFC026D32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01455 Genomic RNA. Translation: CAA25686.1.
PIRiA03999. VCVDAR.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01455 Genomic RNA. Translation: CAA25686.1.
PIRiA03999. VCVDAR.

3D structure databases

ProteinModelPortaliP03399.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENV_AVIRE
AccessioniPrimary (citable) accession number: P03399
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 5, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Strain A is a helper virus of the strain T.

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.