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Protein

Envelope glycoprotein

Gene

env

Organism
Baboon endogenous virus (strain M7)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

Complete GO annotation...

Keywords - Biological processi

Fusion 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 3 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 70
Short name:
gp70
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein p20E
Alternative name(s):
p2E
Gene namesi
Name:env
OrganismiBaboon endogenous virus (strain M7)
Taxonomic identifieri11764 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostiPapio (baboons) [TaxID: 9554]
Theropithecus gelada (Gelada baboon) [TaxID: 9565]
Proteomesi
  • UP000007443 Componenti: Genome

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
Peptide R-peptide :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 503ExtracellularSequence analysisAdd BLAST485
Transmembranei504 – 524HelicalSequence analysisAdd BLAST21
Topological domaini525 – 563CytoplasmicSequence analysisAdd BLAST39

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000023954919 – 563Envelope glycoproteinAdd BLAST545
ChainiPRO_000004068719 – 376Surface proteinBy similarityAdd BLAST358
ChainiPRO_0000040688377 – 546Transmembrane proteinBy similarityAdd BLAST170
PeptideiPRO_0000239550547 – 563R-peptideBy similarityAdd BLAST17

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi113N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi219N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi229N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi236 ↔ 465Interchain (between SU and TM chains, or C-239 with C-465); in linked formBy similarity
Disulfide bondi236 ↔ 239By similarity
Glycosylationi264N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi282N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi292N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi306N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi312N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi321N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi339N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi457 ↔ 464By similarity
Glycosylationi469N-linked (GlcNAc...); by hostSequence analysis1
Lipidationi527S-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. 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).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).By similarity
The transmembrane protein is palmitoylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei376 – 377Cleavage; by hostBy similarity2
Sitei546 – 547Cleavage; by viral proteaseBy 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.By similarity

Structurei

3D structure databases

ProteinModelPortaliP10269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni380 – 400Fusion peptideSequence analysisAdd BLAST21
Regioni440 – 456ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili401 – 451Sequence analysisAdd BLAST51
Coiled coili461 – 497Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi236 – 239CXXC4
Motifi457 – 465CX6CC9
Motifi552 – 555YXXL motif; contains endocytosis signalBy similarity4

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

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10269-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFTTKIIFL YNLVLVYAGF DDPRKAIELV QKRYGRPCDC SGGQVSEPPS
60 70 80 90 100
DRVSQVTCSG KTAYLMPDQR WKCKSIPKDT SPSGPLQECP CNSYQSSVHS
110 120 130 140 150
SCYTSYQQCR SGNKTYYTAT LLKTQTGGTS DVQVLGSTNK LIQSPCNGIK
160 170 180 190 200
GQSICWSTTA PIHVSDGGGP LDTTRIKSVQ RKLEEIHKAL YPELQYHPLA
210 220 230 240 250
IPKVRDNLMV DAQTLNILNA TYNLLLMSNT SLVDDCWLCL KLGPPTPLAI
260 270 280 290 300
PNFLLSYVTR SSDNISCLII PPLLVQPMQF SNSSCLFSPS YNSTEEIDLG
310 320 330 340 350
HVAFSNCTSI TNVTGPICAV NGSVFLCGNN MAYTYLPTNW TGLCVLATLL
360 370 380 390 400
PDIDIIPGDE PVPIPAIDHF IYRPKRAIQF IPLLAGLGIT AAFTTGATGL
410 420 430 440 450
GVSVTQYTKL SNQLISDVQI LSSTIQDLQD QVDSLAEVVL QNRRGLDLLT
460 470 480 490 500
AEQGGICLAL QEKCCFYVNK SGIVRDKIKT LQEELERRRK DLASNPLWTG
510 520 530 540 550
LQGLLPYLLP FLGPLLTLLL LLTIGPCIFN RLTAFINDKL NIIHAMVLTQ
560
QYQVLRTDEE AQD
Length:563
Mass (Da):61,879
Last modified:July 1, 1989 - v1
Checksum:i9573137DC4620BB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10032 Genomic DNA. Translation: BAA00924.1.
X05470 Genomic DNA. Translation: CAA29028.1.
PIRiJT0262. VCMVM7.
RefSeqiYP_009109691.1. NC_022517.1.

Genome annotation databases

GeneIDi22318530.
KEGGivg:22318530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10032 Genomic DNA. Translation: BAA00924.1.
X05470 Genomic DNA. Translation: CAA29028.1.
PIRiJT0262. VCMVM7.
RefSeqiYP_009109691.1. NC_022517.1.

3D structure databases

ProteinModelPortaliP10269.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi22318530.
KEGGivg:22318530.

Family and domain databases

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENV_BAEVM
AccessioniPrimary (citable) accession number: P10269
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 5, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.