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P08360 (ENV_MLVCB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. 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 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
OrganismCas-Br-E murine leukemia virus
Taxonomic identifier11792 [NCBI]
Taxonomic lineageViruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › Murine leukemia virus ›
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length661 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 – 3333 Potential
Chain34 – 661628Envelope glycoprotein
PRO_0000239580
Chain34 – 465432Surface protein By similarity
PRO_0000040748
Chain466 – 645180Transmembrane protein By similarity
PRO_0000040749
Peptide646 – 66116R-peptide
PRO_0000040750

Regions

Topological domain34 – 606573Extracellular Potential
Transmembrane607 – 62721Helical; Potential
Topological domain628 – 66134Cytoplasmic Potential
Region32 – 267236Receptor-binding domain (RBD) Potential
Region468 – 48821Fusion peptide By similarity
Region534 – 55017Immunosuppression By similarity
Coiled coil497 – 53337 Potential
Motif332 – 3354CXXC
Motif551 – 5599CX6CC
Motif651 – 6544YXXL motif; contains endocytosis signal By similarity
Compositional bias264 – 30239Pro-rich

Sites

Metal binding861Zinc By similarity
Metal binding1171Zinc By similarity
Site465 – 4662Cleavage; by host By similarity
Site645 – 6462Cleavage; by viral protease p14

Amino acid modifications

Lipidation6261S-palmitoyl cysteine; by host By similarity
Glycosylation431N-linked (GlcNAc...); by host By similarity
Glycosylation1991N-linked (GlcNAc...); by host By similarity
Glycosylation3221N-linked (GlcNAc...); by host By similarity
Glycosylation3611N-linked (GlcNAc...); by host Potential
Glycosylation3941N-linked (GlcNAc...); by host Potential
Glycosylation4301N-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 bond332 ↔ 559Interchain (between SU and TM chains, or C-335 with C-559); alternate
Disulfide bond332 ↔ 335Alternate
Disulfide bond362 ↔ 416 By similarity
Disulfide bond381 ↔ 393 By similarity
Disulfide bond423 ↔ 436 By similarity
Disulfide bond551 ↔ 558 By similarity

Experimental info

Sequence conflict476 – 4772PE → LG Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08360 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 255BEE3AF62FB9FF

FASTA66172,625
        10         20         30         40         50         60 
MEGPAFSKSP KDKTIERAFL GVLGILFVTG GLASRDNPHQ VYNITWEVTN GEQDTVWAVT 

        70         80         90        100        110        120 
GNHPLWTWWP DLTPDLCMLA LHGPTHWGLD NHPPYSSPPG PPCCSGDAGA VSGCARDCDE 

       130        140        150        160        170        180 
PLTSYSPRCN TAWNRLKLAR VTHAPKEGFY ICPGSHRPRW ARSCGGLDAY YCASWGCETT 

       190        200        210        220        230        240 
GRAAWNPTSS WDYITVSNNL TSSQATKACK NNGWCNPLVI RFTGPGKRAT SWTTGHFWGL 

       250        260        270        280        290        300 
RLYISGHDPG LTFGIRLKVT DLGPRVPIGP NPVLSDQRPP SRPVPARPPP PSASPSTPTI 

       310        320        330        340        350        360 
PPQQGTGDRL LNLVQGAYLT LNMTDPTRTQ ECWLCLVSEP PYYEGVAVLR EYTSHETAPA 

       370        380        390        400        410        420 
NCSSGSQHKL TLSEVTGQGR CLGTVPKTHQ ALCNRTEPTV SGSNYLVAPE GTLWACSTGL 

       430        440        450        460        470        480 
TPCLSTTVLN LTTDYCVLVE LWPKVTYHSP DYVYTQFEPG ARFRREPVSL TLALLPEGLT 

       490        500        510        520        530        540 
MGGIAAGVGT GTTALVATQQ FQQLQAAMHN DLKEVEKSIT NLEKSLTSLS EVVLQNRRGL 

       550        560        570        580        590        600 
DLLFLKEGGL CAALKEECCF YADHTGLVRD SMAKLRERLN QRQKLFESGQ GWFEGLFNRS 

       610        620        630        640        650        660 
PWFTTLISTI MGPLIVLLLI LLFGPCILNR LVQFVKDRIS VVQALVLTQQ YHQLKPIEYE 


P

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References

[1]"Cas-Br-E murine leukemia virus: sequencing of the paralytogenic region of its genome and derivation of specific probes to study its origin and the structure of its recombinant genomes in leukemic tissues."
Rassart E., Nelbach L., Jolicoeur P.
J. Virol. 60:910-919(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of the neurotropic murine retrovirus CAS-BR-E."
Perryman S.M., McAtee F.J., Portis J.L.
Nucleic Acids Res. 19:1707-1707(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Identification of R-peptides in envelope proteins of C-type retroviruses."
Bobkova M., Stitz J., Engelstadter M., Cichutek K., Buchholz C.J.
J. Gen. Virol. 83:2241-2246(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE OF R-PEPTIDE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M14702 Genomic DNA. Translation: AAA46512.1.
X57540 Genomic DNA. No translation available.
PIRVCMVCB. B26103.

3D structure databases

ProteinModelPortalP08360.
SMRP08360. Positions 40-266, 511-563.
ModBaseSearch...

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. FMuLVrecept-bind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameENV_MLVCB
AccessionPrimary (citable) accession number: P08360
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info