Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Envelope glycoprotein

Gene

env

Organism
Feline leukemia virus (strain A/Glasgow-1)
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 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 - 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:
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
OrganismiFeline leukemia virus (strain A/Glasgow-1)
Taxonomic identifieri11769 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiFelidae (cat family) [TaxID: 9681]

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 extravirion 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 – 586ExtracellularSequence analysisAdd BLAST552
Transmembranei587 – 607HelicalSequence analysisAdd BLAST21
Topological domaini608 – 642CytoplasmicSequence 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_000023956435 – 642Envelope glycoproteinAdd BLAST608
ChainiPRO_000004071235 – 445Surface proteinBy similarityAdd BLAST411
ChainiPRO_0000040713446 – 625Transmembrane proteinBy similarityAdd BLAST180
PeptideiPRO_0000239565626 – 642R-peptideBy similarityAdd BLAST17

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi35N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi43N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi58N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi91N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi125 ↔ 147By similarity
Disulfide bondi139 ↔ 152By similarity
Glycosylationi267N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi302N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi307N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi312 ↔ 539Interchain (between SU and TM chains, or C-315 with C-339); in linked formBy similarity
Disulfide bondi312 ↔ 315By similarity
Glycosylationi334N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi374N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi390N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi410N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi531 ↔ 538By similarity
Lipidationi606S-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
Sitei445 – 446Cleavage; by hostBy similarity2
Sitei625 – 626Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiP08359.

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

ProteinModelPortaliP08359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni448 – 468Fusion peptideSequence analysisAdd BLAST21
Regioni514 – 530ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili476 – 525Sequence analysisAdd BLAST50
Coiled coili535 – 571Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi312 – 315CXXC4
Motifi531 – 539CX6CC9

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

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.

P08359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESPTHPKPS KDKTLSWNLA FLVGILFTID IGMANPSPHQ IYNVTWVITN
60 70 80 90 100
VQTNTQANAT SMLGTLTDAY PTLHVDLCDL VGDTWEPIVL NPTNVKHGAR
110 120 130 140 150
YSSSKYGCKT TDRKKQQQTY PFYVCPGHAP SLGPKGTHCG GAQDGFCAAW
160 170 180 190 200
GCETTGEAWW KPTSSWDYIT VKRGSSQDNS CEGKCNPLVL QFTQKGRQAS
210 220 230 240 250
WDGPKMWGLR LYRTGYDPIA LFTVSRQVST ITPPQAMGPN LVLPDQKPPS
260 270 280 290 300
RQSQTGSKVA TQRPQTNESA PRSVAPTTMG PKRIGTGDRL INLVQGTYLA
310 320 330 340 350
LNATDPNKTK DCWLCLVSRP PYYEGIAILG NYSNQTNPPP SCLSTPQHKL
360 370 380 390 400
TISEVSGQGM CIGTVPKTHQ ALCNKTQQGH TGAHYLAAPN GTYWACNTGL
410 420 430 440 450
TPCISMAVLN WTSDFCVLIE LWPRVTYHQP EYVYTHFAKA VRFRREPISL
460 470 480 490 500
TVALMLGGLT VGGIAAGVGT GTKALLETAQ FRQLQMAMHT DIQALEESIS
510 520 530 540 550
ALEKSLTSLS EVVLQNRRGL DILFLQEGGL CAALKEECCF YADHTGLVRD
560 570 580 590 600
NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS PWFTTLISSI MGPLLILLLI
610 620 630 640
LLFGPCILNR LVQFVKDRIS VVQALILTQQ YQQIKQYDPD RP
Length:642
Mass (Da):71,053
Last modified:August 1, 1988 - v1
Checksum:i2DEF5A9EFFC245EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12500 Genomic RNA. Translation: AAA43053.1.
PIRiA24300. VCMVFG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12500 Genomic RNA. Translation: AAA43053.1.
PIRiA24300. VCMVFG.

3D structure databases

ProteinModelPortaliP08359.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP08359.

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_FLVGL
AccessioniPrimary (citable) accession number: P08359
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 5, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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.