Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21443

- ENV_FLVC6

UniProt

P21443 - ENV_FLVC6

Protein

Envelope glycoprotein

Gene

env

Organism
Feline leukemia virus (isolate CFE-6)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    Sitei644 – 6452Cleavage; 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 (isolate CFE-6)
    Taxonomic identifieri11922 [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-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 – 668634Envelope glycoproteinPRO_0000239561Add
    BLAST
    Chaini35 – 465431Surface proteinBy similarityPRO_0000040706Add
    BLAST
    Chaini466 – 644179Transmembrane proteinBy similarityPRO_0000040707Add
    BLAST
    Peptidei645 – 66824R-peptideBy similarityPRO_0000239562Add
    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 ↔ 558Interchain (between SU and TM chains, or C-335 with C-558); in linked formBy similarity
    Disulfide bondi332 ↔ 335By similarity
    Glycosylationi351 – 3511N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi394 – 3941N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi410 – 4101N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi430 – 4301N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi550 ↔ 557By similarity
    Lipidationi625 – 6251S-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

    ProteinModelPortaliP21443.
    SMRiP21443. Positions 38-242, 510-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 605571ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini627 – 66842CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei606 – 62621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni467 – 48721Fusion peptideSequence AnalysisAdd
    BLAST
    Regioni533 – 54917ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili495 – 54450Sequence AnalysisAdd
    BLAST
    Coiled coili554 – 59037Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi332 – 3354CXXC
    Motifi550 – 5589CX6CC
    Motifi650 – 6534YXXL motif; contains endocytosis signalBy similarity

    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
    The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.

    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.

    P21443-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGPTHPKPS KDKTFSWDLI ILVGVLLRLD AGMANPSPHQ VYNITWTITN    50
    LVTGIKANAT SMLGTLTDTF PTIYFDLCDI IGNTWNPSDQ EPFPGYGCDQ 100
    PMRRWQQRNT AFYVCPGHAN RKQCGGPQDG FCAVWGCETT GETYWKPTSS 150
    WDYITVKKGV TQGIYQCNGG GWCGPCYDKA VHSSTTGASE GGRCNPLILQ 200
    FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI TPPQAMGPNP 250
    VLPDQKPPSR QSQIESRVIP HHPQGNGGTP GITLVNASIA PLSTPVTPAS 300
    PKRIGTGNRL INLVQGTYLT LNVTNPNKTK DCWLCLVSRP PYYEGIAVLG 350
    NYSNQTNPPP SCLSVPQHKL TISEVSGQGL CIATVPKTHQ ALCNKTQKGH 400
    RGTHYLVAPN GTYWACNTGL TPCISMAVLN WTSDFCVLTE LWPRITYHEP 450
    EYIYSHFENK PRFKRDPISL TVALMLGGIT VGGMARNRNR DCGLLETAQF 500
    RQLQMAMHTD IQALEESISA LEKSLTSLSE VVLQNRRGLD ILFLQEGGLC 550
    TALKEECCFY ADHTGLVRDN MAKLRERLKQ RQQLFDSQQD GLEGWFNKSP 600
    WFTTLISSIM GPLMILLLIL LFGPCILNRL VQFVKDRISV VQTLVLTQQY 650
    QRLGQWRLRP TVSPQLNV 668
    Length:668
    Mass (Da):74,298
    Last modified:May 1, 1991 - v1
    Checksum:i4A6A06CF2EB8CE25
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25425 Genomic DNA. Translation: AAA30809.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25425 Genomic DNA. Translation: AAA30809.1 .

    3D structure databases

    ProteinModelPortali P21443.
    SMRi P21443. Positions 38-242, 510-562.
    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 sequence and distinctive characteristics of the env gene of endogenous feline leukemia provirus."
      Kumar D.V., Berry B.T., Roy-Burman P.
      J. Virol. 63:2379-2384(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiENV_FLVC6
    AccessioniPrimary (citable) accession number: P21443
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program