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P31794 (ENV_MLVRK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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 3 chains:

  1. Surface protein
    Short name=SU
    Alternative name(s):
    Glycoprotein 76
    Short name=gp76
  2. Transmembrane protein
    Short name=TM
    Alternative name(s):
    Envelope protein p15E
  3. R-peptide
    Alternative name(s):
    p2E
Gene names
Name:env
OrganismRadiation murine leukemia virus (strain Kaplan)
Taxonomic identifier31689 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 virion 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 YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.

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 – 3131 Potential
Chain32 – 665634Envelope glycoprotein
PRO_0000239589
Chain32 – 467436Surface protein By similarity
PRO_0000040768
Chain468 – 644177Transmembrane protein By similarity
PRO_0000040769
Peptide645 – 66521R-peptide By similarity
PRO_0000040770

Regions

Topological domain32 – 605574Extracellular Potential
Transmembrane606 – 62621Helical; Potential
Topological domain627 – 66539Cytoplasmic Potential
Region32 – 267236Receptor-binding domain (RBD) Potential
Region470 – 49021Fusion peptide By similarity
Region533 – 54917Immunosuppression By similarity
Coiled coil505 – 53228 Potential
Motif334 – 3374CXXC
Motif550 – 5589CX6CC
Motif650 – 6534YXXL motif; contains endocytosis signal By similarity
Compositional bias264 – 30542Pro-rich

Sites

Metal binding1171Zinc By similarity
Site467 – 4682Cleavage; by host By similarity
Site644 – 6452Cleavage; by viral protease p14 By similarity

Amino acid modifications

Lipidation6251S-palmitoyl cysteine; by host By similarity
Glycosylation431N-linked (GlcNAc...); by host By similarity
Glycosylation1991N-linked (GlcNAc...); by host By similarity
Glycosylation2111N-linked (GlcNAc...); by host Potential
Glycosylation3241N-linked (GlcNAc...); by host By similarity
Glycosylation3561N-linked (GlcNAc...); by host Potential
Glycosylation3631N-linked (GlcNAc...); by host Potential
Glycosylation3961N-linked (GlcNAc...); by host Potential
Glycosylation4001N-linked (GlcNAc...); by host Potential
Glycosylation4321N-linked (GlcNAc...); by host Potential
Disulfide bond77 ↔ 129 By similarity
Disulfide bond103 ↔ 118 By similarity
Disulfide bond104 ↔ 114 By similarity
Disulfide bond152 ↔ 172 By similarity
Disulfide bond164 ↔ 177 By similarity
Disulfide bond209 ↔ 215 By similarity
Disulfide bond334 ↔ 558Interchain (between SU and TM chains, or C-337 with C-558); alternate
Disulfide bond334 ↔ 337Alternate
Disulfide bond364 ↔ 418 By similarity
Disulfide bond383 ↔ 395 By similarity
Disulfide bond425 ↔ 438 By similarity
Disulfide bond550 ↔ 557 By similarity

Sequences

Sequence LengthMass (Da)Tools
P31794 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: FA15AB6B0C63F0AA

FASTA66573,085
        10         20         30         40         50         60 
MESTTLSKPF KNQVNPWGPL IVLLILGRVN PVALGNSPHQ VFNLSWEVTN EDRETVWAIT 

        70         80         90        100        110        120 
GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YQAPFSPPPG PPCCSRSSGS TPGCSRDCEE 

       130        140        150        160        170        180 
PLTSYTPRCN TAWNRLKLSK VTHAHNEGFY VCPGPHRPRW ARSCGGPESF YCASWGCETT 

       190        200        210        220        230        240 
GRASWKPSSS WDYITVSNNL TSGQATPVCK NNTWCNSLTI RFTSLGKQAT SWVTGHWWGL 

       250        260        270        280        290        300 
RLYVSGHDPG LIFGIRLKIT DSGPRVPIGP NPVLSDQRPP SQPRSPPHSN STPTETPLTL 

       310        320        330        340        350        360 
PEPPPAGVEN RLLNLVKGAY QALNLTSPDR TQECWLCLVS GPPYYEGVAV LGTYSNHTSA 

       370        380        390        400        410        420 
PANCSVASQH KLTLSEVTGR GLCVGAVPKT HQALCNTTQN TSGGSYYLAA PAGTIWACNT 

       430        440        450        460        470        480 
GLTPCLSTTV LNLTTDYCVL VELWPRVTYH SPSYVYHQFE GRAKYKREPV SLTLALLLGG 

       490        500        510        520        530        540 
LTMGGIAAGV GTGTTALVAT QQLQAAVHDD LKEVEKSITN LEKSLTSLSE VVLQNRRGLD 

       550        560        570        580        590        600 
LLFLKEGGLC AALKEECCFY ADHTGVVRDS MAKLRERLNQ RQKLFESGQG WFERLFNGSP 

       610        620        630        640        650        660 
WFTTLISTIM GPLIVLLLIL LLGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE 


MESRE 

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References

[1]"Determinants of thymotropism in Kaplan radiation leukemia virus and nucleotide sequence of its envelope region."
Poliquin L., Bergeron D., Fortier J.L., Paquette Y., Bergeron R., Rassart E.
J. Virol. 66:5141-5146(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93052 Genomic DNA. Translation: AAA46526.1.
PIRVCMVKA. B42743.

3D structure databases

ProteinModelPortalP31794.
SMRP31794. Positions 40-266, 510-562.
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_MLVRK
AccessionPrimary (citable) accession number: P31794
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program