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P08359

- ENV_FLVGL

UniProt

P08359 - ENV_FLVGL

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Protein

Envelope glycoprotein

Gene

env

Organism
Feline leukemia virus (strain A/Glasgow-1)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei445 – 4462Cleavage; by hostBy similarity
Sitei625 – 6262Cleavage; by viral proteaseBy similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
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

Chain 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
R-peptide : Host cell membrane By similarity; Peripheral membrane protein By similarity
Note: The R-peptide is membrane-associated through its palmitate.By similarity

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral capsid Source: InterPro
  4. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Chaini35 – 642608Envelope glycoproteinPRO_0000239564Add
BLAST
Chaini35 – 445411Surface proteinBy similarityPRO_0000040712Add
BLAST
Chaini446 – 625180Transmembrane proteinBy similarityPRO_0000040713Add
BLAST
Peptidei626 – 64217R-peptideBy similarityPRO_0000239565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi91 – 911N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi125 ↔ 147By similarity
Disulfide bondi139 ↔ 152By similarity
Glycosylationi267 – 2671N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi302 – 3021N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi307 – 3071N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi312 ↔ 539Interchain (between SU and TM chains, or C-315 with C-339); in linked formBy similarity
Disulfide bondi312 ↔ 315By similarity
Glycosylationi334 – 3341N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi374 – 3741N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi390 – 3901N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi410 – 4101N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi531 ↔ 538By similarity
Lipidationi606 – 6061S-palmitoyl cysteine; by hostBy similarity

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

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

ProteinModelPortaliP08359.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 586552ExtracellularSequence AnalysisAdd
BLAST
Topological domaini608 – 64235CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei587 – 60721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni448 – 46821Fusion peptideSequence AnalysisAdd
BLAST
Regioni514 – 53017ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili476 – 52550Sequence AnalysisAdd
BLAST
Coiled coili535 – 57137Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi312 – 3154CXXC
Motifi531 – 5399CX6CC

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. 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.

P08359-1 [UniParc]FASTAAdd to Basket

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        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:
EMBL
GenBank
DDBJ
Links Updated
M12500 Genomic RNA. Translation: AAA43053.1.
PIRiA24300. VCMVFG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12500 Genomic RNA. Translation: AAA43053.1 .
PIRi A24300. VCMVFG.

3D structure databases

ProteinModelPortali P08359.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.90.310.10. 1 hit.
InterProi IPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view ]
PANTHERi PTHR10424. PTHR10424. 1 hit.
Pfami PF00429. TLV_coat. 1 hit.
[Graphical view ]
SUPFAMi SSF49830. SSF49830. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequences of a feline leukemia virus subgroup A envelope gene and long terminal repeat and evidence for the recombinational origin of subgroup B viruses."
    Stewart M.A., Warnock M., Wheeler A., Wilkie N., Mullins J.I., Onions D.E., Neil J.C.
    J. Virol. 58:825-834(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

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 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program