Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08359 (ENV_FLVGL) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

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

Cleaved into the following 3 chains:

  1. Surface protein
    Short name=SU
    Alternative name(s):
    Glycoprotein 70
    Short name=gp70
  2. Transmembrane protein
    Short name=TM
    Alternative name(s):
    Envelope protein p15E
  3. R-peptide
    Alternative name(s):
    p2E
Gene names
Name:env
OrganismFeline leukemia virus (strain A/Glasgow-1)
Taxonomic identifier11769 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length642 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.

Surface protein: Virion membrane; Peripheral membrane protein. 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. 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.

R-peptide: Host cell membrane; Peripheral membrane protein By similarity. Note: The R-peptide is membrane-associated through its palmitate 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. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic 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.

The R-peptide is palmitoylated By similarity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 642608Envelope glycoprotein
PRO_0000239564
Chain35 – 445411Surface protein By similarity
PRO_0000040712
Chain446 – 625180Transmembrane protein By similarity
PRO_0000040713
Peptide626 – 64217R-peptide By similarity
PRO_0000239565

Regions

Topological domain35 – 586552Extracellular Potential
Transmembrane587 – 60721Helical; Potential
Topological domain608 – 64235Cytoplasmic Potential
Region448 – 46821Fusion peptide Potential
Region514 – 53017Immunosuppression By similarity
Coiled coil476 – 52550 Potential
Coiled coil535 – 57137 Potential
Motif312 – 3154CXXC
Motif531 – 5399CX6CC

Sites

Site445 – 4462Cleavage; by host By similarity
Site625 – 6262Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation6061S-palmitoyl cysteine; by host By similarity
Glycosylation351N-linked (GlcNAc...); by host Potential
Glycosylation431N-linked (GlcNAc...); by host Potential
Glycosylation581N-linked (GlcNAc...); by host Potential
Glycosylation911N-linked (GlcNAc...); by host Potential
Glycosylation2671N-linked (GlcNAc...); by host Potential
Glycosylation3021N-linked (GlcNAc...); by host Potential
Glycosylation3071N-linked (GlcNAc...); by host Potential
Glycosylation3341N-linked (GlcNAc...); by host Potential
Glycosylation3741N-linked (GlcNAc...); by host Potential
Glycosylation3901N-linked (GlcNAc...); by host Potential
Glycosylation4101N-linked (GlcNAc...); by host Potential
Disulfide bond125 ↔ 147 By similarity
Disulfide bond139 ↔ 152 By similarity
Disulfide bond312 ↔ 539Interchain (between SU and TM chains, or C-315 with C-339); alternate By similarity
Disulfide bond312 ↔ 315Alternate By similarity
Disulfide bond531 ↔ 538 By similarity

Sequences

Sequence LengthMass (Da)Tools
P08359 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 2DEF5A9EFFC245EC

FASTA64271,053
        10         20         30         40         50         60 
MESPTHPKPS KDKTLSWNLA FLVGILFTID IGMANPSPHQ IYNVTWVITN VQTNTQANAT 

        70         80         90        100        110        120 
SMLGTLTDAY PTLHVDLCDL VGDTWEPIVL NPTNVKHGAR YSSSKYGCKT TDRKKQQQTY 

       130        140        150        160        170        180 
PFYVCPGHAP SLGPKGTHCG GAQDGFCAAW GCETTGEAWW KPTSSWDYIT VKRGSSQDNS 

       190        200        210        220        230        240 
CEGKCNPLVL QFTQKGRQAS WDGPKMWGLR LYRTGYDPIA LFTVSRQVST ITPPQAMGPN 

       250        260        270        280        290        300 
LVLPDQKPPS RQSQTGSKVA TQRPQTNESA PRSVAPTTMG PKRIGTGDRL INLVQGTYLA 

       310        320        330        340        350        360 
LNATDPNKTK DCWLCLVSRP PYYEGIAILG NYSNQTNPPP SCLSTPQHKL TISEVSGQGM 

       370        380        390        400        410        420 
CIGTVPKTHQ ALCNKTQQGH TGAHYLAAPN GTYWACNTGL TPCISMAVLN WTSDFCVLIE 

       430        440        450        460        470        480 
LWPRVTYHQP EYVYTHFAKA VRFRREPISL TVALMLGGLT VGGIAAGVGT GTKALLETAQ 

       490        500        510        520        530        540 
FRQLQMAMHT DIQALEESIS ALEKSLTSLS EVVLQNRRGL DILFLQEGGL CAALKEECCF 

       550        560        570        580        590        600 
YADHTGLVRD NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS PWFTTLISSI MGPLLILLLI 

       610        620        630        640 
LLFGPCILNR LVQFVKDRIS VVQALILTQQ YQQIKQYDPD RP 

« Hide

References

[1]"Nucleotide sequences of a feline leukemia virus subgroup A envelope gene and long terminal repeat and evidence for the recombinational origin of subgroup B viruses."
Stewart M.A., Warnock M., Wheeler A., Wilkie N., Mullins J.I., Onions D.E., Neil J.C.
J. Virol. 58:825-834(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12500 Genomic RNA. Translation: AAA43053.1.
PIRVCMVFG. A24300.

3D structure databases

ProteinModelPortalP08359.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.310.10. 1 hit.
InterProIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERPTHR10424. PTHR10424. 1 hit.
PfamPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMSSF49830. SSF49830. 1 hit.
ProtoNetSearch...

Entry information

Entry nameENV_FLVGL
AccessionPrimary (citable) accession number: P08359
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
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