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Protein

Envelope glycoprotein

Gene

env

Organism
Bovine leukemia virus (BLV)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).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).By similarity

GO - Biological processi

Keywordsi

Biological processFusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 51
Short name:
gp51
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 30
Short name:
gp30
Gene namesi
Name:env
OrganismiBovine leukemia virus (BLV)
Taxonomic identifieri11901 [NCBI]
Taxonomic lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeDeltaretrovirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]

Subcellular locationi

Transmembrane protein :
Surface protein :
  • Virion membrane By similarity; Peripheral membrane protein By similarity
  • Host cell membrane By similarity; 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).By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 436ExtracellularSequence analysisAdd BLAST403
Transmembranei437 – 457HelicalSequence analysisAdd BLAST21
Topological domaini458 – 515CytoplasmicSequence analysisAdd BLAST58

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000023955634 – 515Envelope glycoproteinAdd BLAST482
ChainiPRO_000004069934 – 301Surface proteinBy similarityAdd BLAST268
ChainiPRO_0000040700302 – 515Transmembrane proteinBy similarityAdd BLAST214

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi129N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi203N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi212 ↔ 392Interchain (between SU and TM chains, or C-215 with C-392); in linked formBy similarity
Disulfide bondi212 ↔ 215By similarity
Glycosylationi230N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi251N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi256N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi271N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi287N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi351N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi384 ↔ 391By similarity
Glycosylationi398N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Lipidationi455S-palmitoyl cysteine; by hostBy similarity1

Post-translational modificationi

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 (By similarity).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.
The transmembrane protein is palmitoylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei301 – 302Cleavage; by hostBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond.

Protein-protein interaction databases

ELMiP51519

Structurei

Secondary structure

1515
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP51519
SMRiP51519
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni304 – 324Fusion peptideSequence analysisAdd BLAST21
Regioni365 – 381ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili330 – 376Sequence analysisAdd BLAST47
Coiled coili388 – 420Sequence analysisAdd BLAST33

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi212 – 215CXXC4
Motifi384 – 392CX6CC9

Domaini

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).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiView protein in InterPro
IPR018154 TLV/ENV_coat_polyprotein
PANTHERiPTHR10424 PTHR10424, 1 hit
PfamiView protein in Pfam
PF00429 TLV_coat, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51519-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKERRSRRR PQPIIRWVSL TLTLLALCQP IQTWRCSLSL GNQQWMTTYN
60 70 80 90 100
QEAKFSISID QILEAHNQSP FCPRSPRYTL DFVNGYPKIY WPPPQGRRRF
110 120 130 140 150
GARAMVTYDC EPRCPYVGAD HFDCPHWDNA SQADQGSFYV NHQILFLHLK
160 170 180 190 200
QCHGIFTLTW EIWGYDPLIT FSLHKIPDPP QPDFPQLNSD WVPSVRSWAL
210 220 230 240 250
LLNQTARAFP DCAICWEPSP PWAPEILVYN KTISGSGPGL ALPDAQIFWV
260 270 280 290 300
NTSLFNTTQG WHHPSQRLLF NVSQGNALLL PPISLVNLST VSSAPPTRVR
310 320 330 340 350
RSPVAALTLG LALSVGLTGI NVAVSALSHQ RLTSLIHVLE QDQQRLITAI
360 370 380 390 400
NQTHYNLLNV ASVVAQNRRG LDWLYIRLGF QSLCPTINEP CCFLRIQNDS
410 420 430 440 450
IIRLGDLQPL SQRVSTDWQW PWNWDLGLTA WVRETIHSVL SLFLLALFLL
460 470 480 490 500
FLAPCLIKCL TSRLLKLLRQ APHFPEISFP PKPDSDYQAL LPSAPEIYSH
510
LSPTKPDYIN LRPCP
Length:515
Mass (Da):58,640
Last modified:October 1, 1996 - v1
Checksum:i69B028B4586AC1A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02251 Genomic RNA Translation: AAA42788.1
RefSeqiNP_056899.1, NC_001414.1

Genome annotation databases

GeneIDi2760848
KEGGivg:2760849

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02251 Genomic RNA Translation: AAA42788.1
RefSeqiNP_056899.1, NC_001414.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XZ3X-ray1.95A326-418[»]
ProteinModelPortaliP51519
SMRiP51519
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ELMiP51519

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2760848
KEGGivg:2760849

Family and domain databases

InterProiView protein in InterPro
IPR018154 TLV/ENV_coat_polyprotein
PANTHERiPTHR10424 PTHR10424, 1 hit
PfamiView protein in Pfam
PF00429 TLV_coat, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiENV_BLV
AccessioniPrimary (citable) accession number: P51519
Secondary accession number(s): Q85488, Q85489
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 18, 2018
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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