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P03399 (ENV_AVIRE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein

Cleaved into the following 2 chains:

  1. Surface protein
    Short name=SU
    Alternative name(s):
    Glycoprotein 73
    Short name=gp73
  2. Transmembrane protein
    Short name=TM
    Alternative name(s):
    Glycoprotein 22
    Short name=gp22
Gene names
Name:env
OrganismAvian reticuloendotheliosis virus
Taxonomic identifier11636 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostGalliformes [TaxID: 8976]

Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

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.

Subunit structure

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

Subcellular location

Transmembrane protein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity. Note: 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.

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

Domain

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.

Post-translational modification

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.

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.

The transmembrane protein is palmitoylated By similarity.

Miscellaneous

Strain A is a helper virus of the strain T.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 582547Envelope glycoprotein
PRO_0000239546
Chain36 – 392357Surface protein By similarity
PRO_0000040683
Chain393 – 582190Transmembrane protein By similarity
PRO_0000040684

Regions

Topological domain36 – 519484Extracellular Potential
Transmembrane520 – 54021Helical; Potential
Topological domain541 – 58242Cytoplasmic Potential
Region396 – 41621Fusion peptide Potential
Region456 – 47217Immunosuppression By similarity
Coiled coil417 – 46751 Potential
Coiled coil477 – 51337 Potential
Motif251 – 2544CXXC
Motif473 – 4819CX6CC

Sites

Site392 – 3932Cleavage; by host By similarity

Amino acid modifications

Lipidation5431S-palmitoyl cysteine; by host By similarity
Glycosylation2411N-linked (GlcNAc...); by host Potential
Glycosylation3011N-linked (GlcNAc...); by host Potential
Glycosylation3141N-linked (GlcNAc...); by host Potential
Glycosylation4851N-linked (GlcNAc...); by host Potential
Disulfide bond251 ↔ 481Interchain (between SU and TM chains, or C-254 with C-481); alternate By similarity
Disulfide bond251 ↔ 254Alternate By similarity
Disulfide bond473 ↔ 480 By similarity

Sequences

Sequence LengthMass (Da)Tools
P03399 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: CD2560ADFC026D32

FASTA58264,138
        10         20         30         40         50         60 
MDCLTDLRST EGKVDQAGKT LILLVVWWGF GTTAEGHPLQ QLWELPCDCS GGYVSPDLPI 

        70         80         90        100        110        120 
TPTPSIAVAS PLPDLRVWLQ GSWGWGGGFR QQWECVFKPK IIPSVQEQPG PCECLTIATQ 

       130        140        150        160        170        180 
MHSTCYEKAQ ECTLLGKTYF TAILQKTKLG SYEDGPNKLL QASCTGIWET SMLGPRCPCV 

       190        200        210        220        230        240 
CLDGGGPTDR FGRICAEGLE EIIRHSYPSV QYHPLALPRP RGVDLDPQTS DILEATHQVL 

       250        260        270        280        290        300 
NATNPQLAEN CWLCMTLGTQ SPQPSRRMAM SLSMEIAVLA SLSGATHRVN RCQLLCREAD 

       310        320        330        340        350        360 
NRTGIPVGYV HFTNCTSIQE SLTRRVIYEI LRDYVLHRVM YLCVEQHAYT ALPNKWIGLC 

       370        380        390        400        410        420 
ILASIVPDMS IIPGEEPIPL PSIEYTAGRH KRAVQFIPLL VGLGITGATL AGGTGLGVSV 

       430        440        450        460        470        480 
HTYHKLSNQL IEDVQALSGT INDLQDQIDS LAEVVLQNRR GLDLLTAEQG GICLALQEKC 

       490        500        510        520        530        540 
CFYANKSGIV RDKIRKLQED LLARKRALYD NPLWNGLNGF LPYLLPSLGP LFGLILFLTL 

       550        560        570        580 
GPCIRKTLTR IIHDKIQGSK NPRISPAVQA TPNRDGYPRS MV 

« Hide

References

[1]"Nucleic acid sequences of the oncogene v-rel in reticuloendotheliosis virus strain T and its cellular homolog, the proto-oncogene c-rel."
Wilhelmsen K.C., Eggleton K., Temin H.M.
J. Virol. 52:172-182(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01455 Genomic RNA. Translation: CAA25686.1.
PIRVCVDAR. A03999.

3D structure databases

ProteinModelPortalP03399.
SMRP03399. Positions 433-485.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERPTHR10424. PTHR10424. 1 hit.
PfamPF00429. TLV_coat. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENV_AVIRE
AccessionPrimary (citable) accession number: P03399
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program