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P11261

- ENV_FLVLB

UniProt

P11261 - ENV_FLVLB

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Protein

Envelope glycoprotein

Gene

env

Organism
Feline leukemia virus (strain B/lambda-B1)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei465 – 4662Cleavage; by hostBy similarity
Sitei645 – 6462Cleavage; 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 B/lambda-B1)
Taxonomic identifieri103916 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]

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 – 662628Envelope glycoproteinPRO_0000239566Add
BLAST
Chaini35 – 465431Surface proteinBy similarityPRO_0000040714Add
BLAST
Chaini466 – 645180Transmembrane proteinBy similarityPRO_0000040715Add
BLAST
Peptidei646 – 66217R-peptideBy similarityPRO_0000239567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi115 ↔ 132By similarity
Disulfide bondi124 ↔ 137By similarity
Glycosylationi286 – 2861N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi327 – 3271N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi332 ↔ 559Interchain (between SU and TM chains, or C-335 with C-559); in linked formBy similarity
Disulfide bondi332 ↔ 335By similarity
Glycosylationi351 – 3511N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi354 – 3541N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi430 – 4301N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi551 ↔ 558By similarity
Lipidationi626 – 6261S-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

Secondary structure

1
662
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 509
Turni51 – 533
Beta strandi56 – 649
Turni66 – 683
Beta strandi73 – 764
Helixi77 – 793
Beta strandi98 – 1003
Helixi101 – 1088
Beta strandi112 – 1198
Helixi122 – 1243
Helixi127 – 1293
Beta strandi140 – 1434
Beta strandi150 – 1589
Beta strandi168 – 1747
Turni179 – 1813
Helixi190 – 1923
Beta strandi196 – 2016
Helixi203 – 2075
Beta strandi214 – 2207
Beta strandi228 – 23811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCSX-ray2.50A/B35-245[»]
ProteinModelPortaliP11261.
SMRiP11261. Positions 38-241, 511-563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11261.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 606572ExtracellularSequence AnalysisAdd
BLAST
Topological domaini628 – 66235CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei607 – 62721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni468 – 48821Fusion peptideSequence AnalysisAdd
BLAST
Regioni534 – 55017ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili496 – 54550Sequence AnalysisAdd
BLAST
Coiled coili555 – 59137Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi332 – 3354CXXC
Motifi551 – 5599CX6CC

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.

P11261 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGPTHPKPS KDKTFSWDLM ILVGVLLRLD VGMANPSPHQ IYNVTWTITN
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 VHSSITGASE GGRCNPLILQ
210 220 230 240 250
FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI TLPQAMGPNL
260 270 280 290 300
VLPDQKPPSR QSQIESRVTP HHSQGNGGTP GITLVNASIA PLSTPVTPAS
310 320 330 340 350
PKRIGTGNRL INLVQGTYLA LNVTNPNKTK DCWLCLVSRP PYYEGIAVLG
360 370 380 390 400
NYSNQTNPPP SCLSDPQHKL TISEVSGQGS CIGTVPKTHQ ALCKKTQKGH
410 420 430 440 450
KGTHYLAAPS GTYWACNTGL TPCISMAVLN WTSDFCVLIE LWPRVTYHQP
460 470 480 490 500
EYVYTHFDKT VRLRREPISL TVALMLGGLT VGGIAAGVGT GTKALLETAQ
510 520 530 540 550
FGQLQMAMHT 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 QP
Length:662
Mass (Da):73,132
Last modified:July 1, 1989 - v1
Checksum:iD4AC18E197230575
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03448 Genomic RNA. Translation: AAA43048.1.
PIRiA27172. VCMVLB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03448 Genomic RNA. Translation: AAA43048.1 .
PIRi A27172. VCMVLB.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LCS X-ray 2.50 A/B 35-245 [» ]
ProteinModelPortali P11261.
SMRi P11261. Positions 38-241, 511-563.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P11261.

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. "Natural feline leukemia virus variant escapes neutralization by a monoclonal antibody via an amino acid change outside the antibody-binding epitope."
    Nicolaisen-Strouss K., Kumar H.P.M., Fitting T., Grant C.K., Elder J.H.
    J. Virol. 61:3410-3415(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiENV_FLVLB
AccessioniPrimary (citable) accession number: P11261
Secondary accession number(s): Q85515, Q85516, Q85517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
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

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3