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Protein

Envelope glycoprotein

Gene

env

Organism
Friend murine leukemia virus (isolate PVC-211) (FrMLV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi89ZincBy similarity1
Metal bindingi120ZincBy similarity1

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, Inhibition of host adaptive immune response by virus, Inhibition of host proteasome antigen processing by virus, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Virus entry into host cell

Keywords - Ligandi

Metal-binding, Zinc

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):
Envelope protein p15E
Alternative name(s):
p2E
Gene namesi
Name:env
OrganismiFriend murine leukemia virus (isolate PVC-211) (FrMLV)
Taxonomic identifieri11798 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000007777 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 domaini35 – 620ExtracellularSequence analysisAdd BLAST586
Transmembranei621 – 641HelicalSequence analysisAdd BLAST21
Topological domaini642 – 676CytoplasmicSequence analysisAdd BLAST35

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 – 34Sequence analysisAdd BLAST34
ChainiPRO_000023958335 – 676Envelope glycoproteinAdd BLAST642
ChainiPRO_000004075735 – 479Surface proteinBy similarityAdd BLAST445
ChainiPRO_0000040758480 – 659Transmembrane proteinBy similarityAdd BLAST180
PeptideiPRO_0000040759660 – 676R-peptideBy similarityAdd BLAST17

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi46N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi80 ↔ 132By similarity
Disulfide bondi106 ↔ 121By similarity
Disulfide bondi107 ↔ 117By similarity
Disulfide bondi155 ↔ 175By similarity
Disulfide bondi167 ↔ 180By similarity
Glycosylationi202N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi212 ↔ 218By similarity
Glycosylationi336N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi346 ↔ 573Interchain (between SU and TM chains, or C-349 with C-573); in linked form
Disulfide bondi346 ↔ 349
Glycosylationi368N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi375N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi376 ↔ 430By similarity
Disulfide bondi395 ↔ 407By similarity
Glycosylationi408N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi437 ↔ 450By similarity
Glycosylationi444N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi565 ↔ 572By similarity
Lipidationi640S-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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei479 – 480Cleavage; by hostBy similarity2
Sitei659 – 660Cleavage; 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.By similarity

Structurei

3D structure databases

ProteinModelPortaliP26803.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 270Receptor-binding domain (RBD)Sequence analysisAdd BLAST236
Regioni482 – 502Fusion peptideBy similarityAdd BLAST21
Regioni548 – 564ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili513 – 547Sequence analysisAdd BLAST35

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi346 – 349CXXC4
Motifi565 – 573CX6CC9
Motifi665 – 668YXXL motif; contains endocytosis signalBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi267 – 317Pro-richAdd BLAST51

Domaini

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).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. 2 hits.
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.

P26803-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACSTLSKSP KDKIDPRDLL IPLILFLSLK GARSAAPGSS PHQVYNITWE
60 70 80 90 100
VTNGDRETVW AISGNHPLWT WWPDLTPDLC MLALSGPPHW GLEYRAPYSS
110 120 130 140 150
PPGPPCCSGS SGNRAGCARD CDEPLTSLTP RCNTAWNRLK LDQVTHKSSG
160 170 180 190 200
GFYVCPGSHR PRKAKSCGGP DSFYCASWGC ETTGRAYWKP SSSWDYITVD
210 220 230 240 250
NNLTTNQAAQ VCKDNKWCNP LAIQFTNAGK QVTSWTIGHY WGLRLYVSGQ
260 270 280 290 300
DPGLTFGIRL KYQNLGPRVP IGPNPVLADQ LSFPLPNPLP KPAKSPSASN
310 320 330 340 350
STPTLISPSP APTQPPPAGT GDRLLNLVQG AYQALNLTNP DKTQECWLCL
360 370 380 390 400
VSAPPYYEGV AVLGTYSNHT SAPANCSAGS QHKLTLSEVT GQGLCIGTVP
410 420 430 440 450
KTHQALCNTT LKTGKGSYYL VAPAGTMWAC NTGLTPCLSA TVLNRTTDYC
460 470 480 490 500
VLVELWPRVT YHPPSYVYSQ FEKSYRHKRE PVSLTLALLL GGLTMGGIAA
510 520 530 540 550
GVGTGTTALV ATQQFQQLHA AVQDDLKEVE KSITNLEKSL TSLSEVVLQN
560 570 580 590 600
RRGLDLLFLK EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLTQRQKLF
610 620 630 640 650
ESSQGWFEGL FNRSPWFTTL ISTIMGPLII LLLILLFGPC ILNRLVQFVK
660 670
DRISVVQALV LTQQYHQLKP LEYEPQ
Length:676
Mass (Da):73,946
Last modified:August 1, 1992 - v1
Checksum:i18D8D8A7FE0A8FA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93134 Genomic RNA. Translation: AAA46478.1.
PIRiA38210. VCMVPV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93134 Genomic RNA. Translation: AAA46478.1.
PIRiA38210. VCMVPV.

3D structure databases

ProteinModelPortaliP26803.
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. 2 hits.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENV_MLVFP
AccessioniPrimary (citable) accession number: P26803
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 5, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The surface protein appears to be responsible for the neuropathogenicity of PVC-211 MuLV.

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.