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P03390 (ENV_MLVF5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize 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
OrganismFriend murine leukemia virus (isolate 57) (FrMLV) [Complete proteome]
Taxonomic identifier11796 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length675 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. Ref.3

The R-peptide is palmitoylated By similarity. Ref.3

Ontologies

Keywords
   Biological processFusion of virus membrane with host cell membrane
Fusion of virus membrane with host membrane
Host-virus interaction
Inhibition of host adaptive immune response by virus
Inhibition of host proteasome antigen processing by virus
Viral attachment to host cell
Viral immunoevasion
Viral penetration into host cytoplasm
Virus entry into host cell
   Cellular componentHost cell membrane
Host membrane
Membrane
Viral envelope protein
Virion
   DomainCoiled coil
Signal
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processfusion of virus membrane with host plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host adaptive immune response

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host antigen processing and presentation

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: InterPro

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 675641Envelope glycoprotein
PRO_0000239581
Chain35 – 479445Surface protein By similarity
PRO_0000040751
Chain480 – 659180Transmembrane protein By similarity
PRO_0000040752
Peptide660 – 67516R-peptide By similarity
PRO_0000040753

Regions

Topological domain35 – 620586Extracellular Potential
Transmembrane621 – 64121Helical; Potential
Topological domain642 – 67534Cytoplasmic Potential
Region35 – 270236Receptor-binding domain (RBD) Potential
Region482 – 50221Fusion peptide By similarity
Region548 – 56417Immunosuppression By similarity
Coiled coil513 – 54735 Potential
Motif346 – 3494CXXC
Motif565 – 5739CX6CC
Motif665 – 6684YXXL motif; contains endocytosis signal By similarity
Compositional bias267 – 31751Pro-rich

Sites

Metal binding891Zinc
Metal binding1201Zinc
Site479 – 4802Cleavage; by host By similarity
Site659 – 6602Cleavage; by viral protease p14 By similarity

Amino acid modifications

Lipidation6401S-palmitoyl cysteine; by host Ref.3
Glycosylation461N-linked (GlcNAc...); by host
Glycosylation2021N-linked (GlcNAc...); by host
Glycosylation3361N-linked (GlcNAc...); by host By similarity
Glycosylation3681N-linked (GlcNAc...); by host Potential
Glycosylation3751N-linked (GlcNAc...); by host Potential
Glycosylation4081N-linked (GlcNAc...); by host Potential
Glycosylation4441N-linked (GlcNAc...); by host Potential
Disulfide bond80 ↔ 132
Disulfide bond106 ↔ 121
Disulfide bond107 ↔ 117
Disulfide bond155 ↔ 175
Disulfide bond167 ↔ 180
Disulfide bond212 ↔ 218
Disulfide bond346 ↔ 573Interchain (between SU and TM chains, or C-349 with C-573); alternate
Disulfide bond346 ↔ 349Alternate
Disulfide bond376 ↔ 430 By similarity
Disulfide bond395 ↔ 407 By similarity
Disulfide bond437 ↔ 450 By similarity
Disulfide bond565 ↔ 572 By similarity

Experimental info

Mutagenesis6401C → S: Complete loss of palmitoylation. Ref.3

Secondary structure

........................................ 675
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03390 [UniParc].

Last modified August 1, 1992. Version 3.
Checksum: A097038E422BB3D3

FASTA67574,025
        10         20         30         40         50         60 
MACSTLPKSP KDKIDPRDLL IPLILFLSLK GARSAAPGSS PHQVYNITWE VTNGDRETVW 

        70         80         90        100        110        120 
AISGNHPLWT WWPVLTPDLC MLALSGPPHW GLEYQAPYSS PPGPPCCSGS SGSSAGCSRD 

       130        140        150        160        170        180 
CDEPLTSLTP RCNTAWNRLK LDQVTHKSSE GFYVCPGSHR PREAKSCGGP DSFYCASWGC 

       190        200        210        220        230        240 
ETTGRVYWKP SSSWDYITVD NNLTTSQAVQ VCKDNKWCNP LAIQFTNAGK QVTSWTTGHY 

       250        260        270        280        290        300 
WGLRLYVSGR DPGLTFGIRL RYQNLGPRVP IGPNPVLADQ LSLPRPNPLP KPAKSPPASN 

       310        320        330        340        350        360 
STPTLISPSP TPTQPPPAGT GDRLLNLVQG AYQALNLTNP DKTQECWLCL VSGPPYYEGV 

       370        380        390        400        410        420 
AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GRGLCIGTVP KTHQALCNTT LKIDKGSYYL 

       430        440        450        460        470        480 
VAPTGTTWAC NTGLTPCLSA TVLNRTTDYC VLVELWPRVT YHPPSYVYSQ FEKSYRHKRE 

       490        500        510        520        530        540 
PVSLTLALLL GGLTMGGIAA GVGTGTTALV ATQQFQQLHA AVQDDLKEVE KSITNLEKSL 

       550        560        570        580        590        600 
TSLSEVVLQN RRGLDLLFLK EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLTQRQKLF 

       610        620        630        640        650        660 
ESSQGWFEGL FNRSPWFTTL ISTIMGPLII LLLILLFGPC ILNRLVQFVK DRISVVQALV 

       670 
LTQQYHQLKP LEYEP 

« Hide

References

[1]Friedrich R.W., Koch W., von Maydell-Livonius U., Schrewe H., Zimmermann W.
Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Molecular analysis of the envelope gene and long terminal repeat of Friend mink cell focus-inducing virus: implications for the functions of these sequences."
Koch W., Zimmermann W., Oliff A., Friedrich R.W.
J. Virol. 49:828-840(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE.
[3]"Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits."
Yang C., Compans R.W.
Virology 221:87-97(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION OF THE TRANSMEMBRANE PROTEIN, MUTAGENESIS OF CYS-640.
[4]"Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0-A resolution."
Fass D., Davey R.A., Hamson C.A., Kim P.S., Cunningham J.M., Berger J.M.
Science 277:1662-1666(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-270.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02794 Genomic RNA. Translation: CAA26561.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOLX-ray2.00A43-270[»]
ProteinModelPortalP03390.
SMRP03390. Positions 43-269, 525-577.
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...

Other

EvolutionaryTraceP03390.

Entry information

Entry nameENV_MLVF5
AccessionPrimary (citable) accession number: P03390
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references