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P31796 (ENV_AVISN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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 spleen necrosis virus
Taxonomic identifier11899 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostGalliformes [TaxID: 8976]

Protein attributes

Sequence length567 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 567532Envelope glycoprotein
PRO_0000239547
Chain36 – 398363Surface protein By similarity
PRO_0000040685
Chain399 – 567169Transmembrane protein By similarity
PRO_0000040686

Regions

Topological domain36 – 525490Extracellular Potential
Transmembrane526 – 54621Helical; Potential
Topological domain547 – 56721Cytoplasmic Potential
Region402 – 42221Fusion peptide Potential
Region462 – 47817Immunosuppression By similarity
Coiled coil423 – 47351 Potential
Coiled coil483 – 51937 Potential
Motif255 – 2584CXXC
Motif479 – 4879CX6CC

Sites

Site398 – 3992Cleavage; by host By similarity

Amino acid modifications

Lipidation5491S-palmitoyl cysteine; by host By similarity
Glycosylation2451N-linked (GlcNAc...); by host Potential
Glycosylation2741N-linked (GlcNAc...); by host Potential
Glycosylation2801N-linked (GlcNAc...); by host Potential
Glycosylation3061N-linked (GlcNAc...); by host Potential
Glycosylation3191N-linked (GlcNAc...); by host Potential
Glycosylation3281N-linked (GlcNAc...); by host Potential
Glycosylation3351N-linked (GlcNAc...); by host Potential
Glycosylation4911N-linked (GlcNAc...); by host Potential
Disulfide bond255 ↔ 487Interchain (between SU and TM chains, or C-258 with C-487); alternate By similarity
Disulfide bond255 ↔ 258Alternate By similarity
Disulfide bond479 ↔ 486 By similarity

Sequences

Sequence LengthMass (Da)Tools
P31796 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 204EA57C32159175

FASTA56761,597
        10         20         30         40         50         60 
MDCLTNLRSA EGKVDQASKI LILLVAWWGF GTTAEGYPLQ QLWELPCDCS GGYVSSIPTY 

        70         80         90        100        110        120 
YTYSLDCGGS TAYLTYGSGT GSWSWGGGFK QQWECVFKPK IIPSVQGQPG PCPSECLQIA 

       130        140        150        160        170        180 
TQMHSTCYEK TQECTLLGKT YFTAILQKTK LGSYEDGPNK LIQASCTGTV GKPVCWDPVA 

       190        200        210        220        230        240 
PVYVSDGGGP TDMIREESVR ERLEEIIRHS YPSVQYHPLA LPRSRGVDLD PQTSDILEAT 

       250        260        270        280        290        300 
HQVLNATNPK LAENCWLCMT LGTPIPAAIP TNGNVTLDGN CSLSLPFGCN PPGSIDVSCY 

       310        320        330        340        350        360 
AGEADNRTGI PVGYVHFTNC TSIQEVTNET SQMGNLTRLC PPPGHVFVCG NNMAYTALPN 

       370        380        390        400        410        420 
KWIGLCILAS IVPDISIISG EEPIPLPSIE YTARRHKRAV QFIPLLVGLG ISGATLAGGT 

       430        440        450        460        470        480 
GLGVSVHTYH KLSNQLIEDV QALSGTINDL QDQIDSLAEV VLQNRRGLDL LTAEQGGICL 

       490        500        510        520        530        540 
ALQEKCCFYA NKSGIVRDKI RKLQEDLIER KRALYDNPLW SGLNGFLPYL LPLLGPLFGL 

       550        560 
ILFLTLGPCI MKTLTRIIHD KIQAVKS 

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References

[1]"Spleen necrosis virus, an avian immunosuppressive retrovirus, shares a receptor with the type D simian retroviruses."
Kewalramani V.N., Panganiban A.T., Emerman M.
J. Virol. 66:3026-3031(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Clone PPB101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87666 Genomic DNA. No translation available.
PIRVCFVAS. A38212.

3D structure databases

ProteinModelPortalP31796.
SMRP31796. Positions 439-491.
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_AVISN
AccessionPrimary (citable) accession number: P31796
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program