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P10269 (ENV_BAEVM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. 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):
    Glycoprotein p20E
  3. R-peptide
    Alternative name(s):
    p2E
Gene names
Name:env
OrganismBaboon endogenous virus (strain M7) [Complete proteome]
Taxonomic identifier11764 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostPapio (baboons) [TaxID: 9554]
Theropithecus gelada (Gelada baboon) [TaxID: 9565]

Protein attributes

Sequence length563 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.

R-peptide: Host cell membrane; Peripheral membrane protein. 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.

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 563545Envelope glycoprotein
PRO_0000239549
Chain19 – 376358Surface protein By similarity
PRO_0000040687
Chain377 – 546170Transmembrane protein By similarity
PRO_0000040688
Peptide547 – 56317R-peptide By similarity
PRO_0000239550

Regions

Topological domain19 – 503485Extracellular Potential
Transmembrane504 – 52421Helical; Potential
Topological domain525 – 56339Cytoplasmic Potential
Region380 – 40021Fusion peptide Potential
Region440 – 45617Immunosuppression By similarity
Coiled coil401 – 45151 Potential
Coiled coil461 – 49737 Potential
Motif236 – 2394CXXC
Motif457 – 4659CX6CC
Motif552 – 5554YXXL motif; contains endocytosis signal By similarity

Sites

Site376 – 3772Cleavage; by host By similarity
Site546 – 5472Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation5271S-palmitoyl cysteine; by host By similarity
Glycosylation1131N-linked (GlcNAc...); by host Potential
Glycosylation2191N-linked (GlcNAc...); by host Potential
Glycosylation2291N-linked (GlcNAc...); by host Potential
Glycosylation2641N-linked (GlcNAc...); by host Potential
Glycosylation2821N-linked (GlcNAc...); by host Potential
Glycosylation2921N-linked (GlcNAc...); by host Potential
Glycosylation3061N-linked (GlcNAc...); by host Potential
Glycosylation3121N-linked (GlcNAc...); by host Potential
Glycosylation3211N-linked (GlcNAc...); by host Potential
Glycosylation3391N-linked (GlcNAc...); by host Potential
Glycosylation4691N-linked (GlcNAc...); by host Potential
Disulfide bond236 ↔ 465Interchain (between SU and TM chains, or C-239 with C-465); alternate By similarity
Disulfide bond236 ↔ 239Alternate By similarity
Disulfide bond457 ↔ 464 By similarity

Sequences

Sequence LengthMass (Da)Tools
P10269 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 9573137DC4620BB7

FASTA56361,879
        10         20         30         40         50         60 
MGFTTKIIFL YNLVLVYAGF DDPRKAIELV QKRYGRPCDC SGGQVSEPPS DRVSQVTCSG 

        70         80         90        100        110        120 
KTAYLMPDQR WKCKSIPKDT SPSGPLQECP CNSYQSSVHS SCYTSYQQCR SGNKTYYTAT 

       130        140        150        160        170        180 
LLKTQTGGTS DVQVLGSTNK LIQSPCNGIK GQSICWSTTA PIHVSDGGGP LDTTRIKSVQ 

       190        200        210        220        230        240 
RKLEEIHKAL YPELQYHPLA IPKVRDNLMV DAQTLNILNA TYNLLLMSNT SLVDDCWLCL 

       250        260        270        280        290        300 
KLGPPTPLAI PNFLLSYVTR SSDNISCLII PPLLVQPMQF SNSSCLFSPS YNSTEEIDLG 

       310        320        330        340        350        360 
HVAFSNCTSI TNVTGPICAV NGSVFLCGNN MAYTYLPTNW TGLCVLATLL PDIDIIPGDE 

       370        380        390        400        410        420 
PVPIPAIDHF IYRPKRAIQF IPLLAGLGIT AAFTTGATGL GVSVTQYTKL SNQLISDVQI 

       430        440        450        460        470        480 
LSSTIQDLQD QVDSLAEVVL QNRRGLDLLT AEQGGICLAL QEKCCFYVNK SGIVRDKIKT 

       490        500        510        520        530        540 
LQEELERRRK DLASNPLWTG LQGLLPYLLP FLGPLLTLLL LLTIGPCIFN RLTAFINDKL 

       550        560 
NIIHAMVLTQ QYQVLRTDEE AQD 

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References

[1]"The entire nucleotide sequence of baboon endogenous virus DNA: a chimeric genome structure of murine type C and simian type D retroviruses."
Kato S., Matsuo K., Nishimura N., Takahashi N., Takano T.
Jpn. J. Genet. 62:127-137(1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10032 Genomic DNA. Translation: BAA00924.1.
X05470 Genomic DNA. Translation: CAA29028.1.
PIRVCMVM7. JT0262.

3D structure databases

ProteinModelPortalP10269.
SMRP10269. Positions 417-469.
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_BAEVM
AccessionPrimary (citable) accession number: P10269
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 19, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program