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Protein

Envelope glycoprotein

Gene

env

Organism
Xenotropic MuLV-related virus (isolate VP62) (XMRV)
Status
Reviewed-Annotation score: Annotation score: 5 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 activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, 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 - Molecular functioni

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:
Gene namesi
Name:env
OrganismiXenotropic MuLV-related virus (isolate VP62) (XMRV)
Taxonomic identifieri373193 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000002240 Componenti: Genome

Subcellular locationi

Surface protein :
  • Virion membrane; Peripheral membrane protein
  • 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 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).By similarity
Peptide R-peptide :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 585ExtracellularSequence analysisAdd BLAST552
Transmembranei586 – 606HelicalSequence analysisAdd BLAST21
Topological domaini607 – 640CytoplasmicSequence analysisAdd BLAST34

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 – 33Sequence analysisAdd BLAST33
ChainiPRO_000039083134 – 645Envelope glycoproteinBy similarityAdd BLAST612
ChainiPRO_000039083234 – 444Surface proteinBy similarityAdd BLAST411
ChainiPRO_0000390833445 – 645Transmembrane proteinBy similarityAdd BLAST201
PeptideiPRO_0000390834625 – 645R-peptideBy similarityAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi43N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi58N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi113 ↔ 130By similarity
Disulfide bondi122 ↔ 135By similarity
Glycosylationi301N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi311 ↔ 538Interchain (between SU and TM chains, or C-314 with C-538); in linked formBy similarity
Disulfide bondi311 ↔ 314By similarity
Glycosylationi333N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi340N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi341 ↔ 395By similarity
Disulfide bondi360 ↔ 372By similarity
Glycosylationi373N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi402 ↔ 415By similarity
Glycosylationi409N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi530 ↔ 537By similarity
Lipidationi605S-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
The R-peptide is palmitoylated.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei444 – 445Cleavage; by hostBy similarity2
Sitei624 – 625Cleavage; by viral protease p14By 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. The activated Env consists of SU monomers and TM trimers (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ27ID8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 237Receptor-binding domain (RBD)Sequence analysisAdd BLAST206
Regioni447 – 467Fusion peptideBy similarityAdd BLAST21
Regioni513 – 529ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili490 – 510Sequence analysisAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi311 – 314CXXCBy similarity4
Motifi530 – 538CX6CCBy similarity9
Motifi630 – 633YXXL motif; contains endocytosis signalBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi234 – 283Pro-richAdd BLAST50

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.By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.310.10. 1 hit.
InterProiIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q27ID8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESPAFSKPL KDKINPWGPL IIMGILVRAG ASVQRDSPHQ VFNVTWKITN
60 70 80 90 100
LMTGQTANAT SLLGTMTDTF PKLYFDLCDL VGDNWDDPEP DIGDGCRSPG
110 120 130 140 150
GRKRTRLYDF YVCPGHTVLT GCGGPREGYC GKWGCETTGQ AYWKPSSSWD
160 170 180 190 200
LISLKRGNTP KGQGPCFDSS VGSGSIQGAT PGGRCNPLVL EFTDAGKRAS
210 220 230 240 250
WDAPKTWGLR LYRSTGADPV TLFSLTRQVL NVGPRVPIGP NPVITEQLPP
260 270 280 290 300
SQPVQIMLPR TPRPPPSGAA SMVPGAPPPS QQPGTGDRLL NLVEGAYLAL
310 320 330 340 350
NLTSPDKTQE CWLCLVSGPP YYEGVAVLGT YSNHTSAPAN CSVTSQHKLT
360 370 380 390 400
LSEVTGQGLC IGAVPKTHQA LCNTTQKTSD GSYYLASPAG TIWACSTGLT
410 420 430 440 450
PCLSTTVLNL TTDYCVLVEL WPKVTYHSPN YVYGQFEKKT KYKREPVSLT
460 470 480 490 500
LALLLGGLTM GGIAAGVGTG TTALVATKQF EQLQAAIHTD LGALEKSVSA
510 520 530 540 550
LEKSLTSLSE VVLQNRRGLD LLFLKEGGLC AALKEECCFY ADHTGVVRDS
560 570 580 590 600
MAKLRERLNQ RQKLFESGQG WFEGLFNRSP WFTTLISTIM GPLIVLLLIL
610 620 630 640
LFGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE VESRE
Length:645
Mass (Da):69,876
Last modified:April 4, 2006 - v1
Checksum:i19ACC5E3EAF9AEC3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti261T → P in ABM47429 (PubMed:16609730).Curated1
Sequence conflicti298L → Q in ABM47429 (PubMed:16609730).Curated1
Sequence conflicti568G → R in ABM47429 (PubMed:16609730).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ399707 Genomic RNA. Translation: ABD49688.1.
EF185282 Genomic RNA. Translation: ABM47429.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ399707 Genomic RNA. Translation: ABD49688.1.
EF185282 Genomic RNA. Translation: ABM47429.1.

3D structure databases

ProteinModelPortaliQ27ID8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.90.310.10. 1 hit.
InterProiIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENV_XMRV6
AccessioniPrimary (citable) accession number: Q27ID8
Secondary accession number(s): A1Z653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: April 4, 2006
Last modified: October 5, 2016
This is version 49 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, Reference 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.