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Protein

Envelope glycoprotein

Gene

env

Organism
Feline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B)
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 sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B)
Taxonomic identifieri11774 [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 – 606ExtracellularSequence analysisAdd BLAST572
Transmembranei607 – 627HelicalSequence analysisAdd BLAST21
Topological domaini628 – 662CytoplasmicSequence 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_000023957035 – 662Envelope glycoproteinAdd BLAST628
ChainiPRO_000004072435 – 465Surface proteinBy similarityAdd BLAST431
ChainiPRO_0000040725466 – 645Transmembrane proteinBy similarityAdd BLAST180
PeptideiPRO_0000239571646 – 662R-peptideBy similarityAdd BLAST17

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi43N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi58N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi115 ↔ 132By similarity
Disulfide bondi124 ↔ 137By similarity
Glycosylationi286N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi322N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi327N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi332 ↔ 559Interchain (between SU and TM chains, or C-335 with C-559); in linked formBy similarity
Disulfide bondi332 ↔ 335By similarity
Glycosylationi351N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi354N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi394N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi410N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi430N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi551 ↔ 558By similarity
Lipidationi626S-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
Sitei465 – 466Cleavage; by hostBy similarity2
Sitei645 – 646Cleavage; 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

ProteinModelPortaliP03391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni468 – 488Fusion peptideSequence analysisAdd BLAST21
Regioni534 – 550ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili496 – 545Sequence analysisAdd BLAST50
Coiled coili555 – 591Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi332 – 335CXXC4
Motifi551 – 559CX6CC9

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.

P03391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESPTHPKPS KDKTLSWNLV FLVGILFTID IGMANPSPHQ VYNVTWTITN
60 70 80 90 100
LVTGTKANAT SMLGTLTDAF PTMYFDLCDI IGNTWNPSDQ EPFPGYGCDQ
110 120 130 140 150
PMRRWQQRNT PFYVCPGHAN RKQCGGPQDG FCAVWGCETT GETYWRPTSS
160 170 180 190 200
WDYITVKKGV TQGIYQCSGG GWCGPCYDKA VHSSTTGASE GGRCNPLILQ
210 220 230 240 250
FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI TPPQAMGPNL
260 270 280 290 300
VLPDQKPPSR QSQIESRVTP HHSQGNGGTP GITLVNASIA PLSTPVTPAS
310 320 330 340 350
PKRIGTGDRL INLVQGTYLA LNATDPNRTK DCWLCLVSRP PYYEGIAILG
360 370 380 390 400
NYSNQTNPPP SCLSIPQHKL TISEVSGQGL CIGTVPKTHQ ALCNETQQGH
410 420 430 440 450
TGAHYLAAPN GTYWACNTGL TPCISMAVLN WTSDFCVLIE LWPRVTYHQP
460 470 480 490 500
EYVYTHFAKA ARFRREPISL TVALMLGGLT VGGIAAGVGT GTKALIETAQ
510 520 530 540 550
FRQLQMAMHT DIQALEESIS ALEKSLTSLS EVVLQNRRGL DILFLQEGGL
560 570 580 590 600
CAALKEECCF YADHTGLVRD NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS
610 620 630 640 650
PWFTTLISSI MGPLLILLLI LLFGPCILNR LVQFVKDRIS VVQALILTQQ
660
YQQIKQYDPD RP
Length:662
Mass (Da):73,150
Last modified:July 21, 1986 - v1
Checksum:i1482088D547CFF47
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15Missing (PubMed:2823466).Curated1
Sequence conflicti41V → I (PubMed:2823466).Curated1
Sequence conflicti47T → V (PubMed:2823466).Curated1
Sequence conflicti51 – 56LVTGTK → VQTNTQ (PubMed:2823466).Curated6
Sequence conflicti70 – 75FPTMYF → YPTLHV (PubMed:2823466).Curated6
Sequence conflicti80 – 95IIGNT…EPFPG → LVGDSWEPIVLDPNNVKHGA RYSSSK (PubMed:2823466).CuratedAdd BLAST16
Sequence conflicti99 – 110DQPMR…QQRNT → KTTDRKKQQQTY (PubMed:2823466).CuratedAdd BLAST12
Sequence conflicti120 – 123NRKQ → PSLGPKGTH (PubMed:2823466).Curated4
Sequence conflicti127P → A (PubMed:2823466).Curated1
Sequence conflicti134V → A (PubMed:2823466).Curated1
Sequence conflicti143 – 148TYWRPT → AWWKPS (PubMed:2823466).Curated6
Sequence conflicti158 – 193KGVTQ…SEGGR → RGSSQDTNSCEGK (PubMed:2823466).CuratedAdd BLAST36
Sequence conflicti208T → A (PubMed:2823466).Curated1
Sequence conflicti215S → M (PubMed:2823466).Curated1
Sequence conflicti223S → T (PubMed:2823466).Curated1
Sequence conflicti232S → T (PubMed:2823466).Curated1
Sequence conflicti238M → S (PubMed:2823466).Curated1
Sequence conflicti264 – 300IESRV…VTPAS → TGSKVATQRPQTNESAPRSV APTTMG (PubMed:2823466).CuratedAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01209 Genomic RNA. Translation: AAA43052.1.
V01172 Genomic DNA. Translation: CAA24497.1.
X00188 Genomic DNA. Translation: CAA25008.1.
M23026 Genomic DNA. No translation available.
PIRiA03991. VCVWGF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01209 Genomic RNA. Translation: AAA43052.1.
V01172 Genomic DNA. Translation: CAA24497.1.
X00188 Genomic DNA. Translation: CAA25008.1.
M23026 Genomic DNA. No translation available.
PIRiA03991. VCVWGF.

3D structure databases

ProteinModelPortaliP03391.
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_FSVGA
AccessioniPrimary (citable) accession number: P03391
Secondary accession number(s): P21446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 5, 2016
This is version 101 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.