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P11261

- ENV_FLVLB

UniProt

P11261 - ENV_FLVLB

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
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    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-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral capsid Source: InterPro
    4. viral envelope Source: UniProtKB-KW
    5. virion membrane Source: UniProtKB-SubCell

    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.

    P11261-1 [UniParc]FASTAAdd to Basket

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    MEGPTHPKPS KDKTFSWDLM ILVGVLLRLD VGMANPSPHQ IYNVTWTITN    50
    LVTGTKANAT SMLGTLTDAF PTMYFDLCDI IGNTWNPSDQ EPFPGYGCDQ 100
    PMRRWQQRNT PFYVCPGHAN RKQCGGPQDG FCAVWGCETT GETYWRPTSS 150
    WDYITVKKGV TQGIYQCSGG GWCGPCYDKA VHSSITGASE GGRCNPLILQ 200
    FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI TLPQAMGPNL 250
    VLPDQKPPSR QSQIESRVTP HHSQGNGGTP GITLVNASIA PLSTPVTPAS 300
    PKRIGTGNRL INLVQGTYLA LNVTNPNKTK DCWLCLVSRP PYYEGIAVLG 350
    NYSNQTNPPP SCLSDPQHKL TISEVSGQGS CIGTVPKTHQ ALCKKTQKGH 400
    KGTHYLAAPS GTYWACNTGL TPCISMAVLN WTSDFCVLIE LWPRVTYHQP 450
    EYVYTHFDKT VRLRREPISL TVALMLGGLT VGGIAAGVGT GTKALLETAQ 500
    FGQLQMAMHT DIQALEESIS ALEKSLTSLS EVVLQNRRGL DILFLQEGGL 550
    CAALKEECCF YADHTGLVRD NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS 600
    PWFTTLISSI MGPLLILLLI LLFGPCILNR LVQFVKDRIS VVQALILTQQ 650
    YQQIKQYDPD QP 662
    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 1, 2014
    This is version 100 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