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P06752

- ENV_FLVSA

UniProt

P06752 - ENV_FLVSA

Protein

Envelope glycoprotein

Gene

env

Organism
Feline leukemia virus (strain C/Sarma)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      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
    Sitei442 – 4432Cleavage; by hostBy similarity
    Sitei622 – 6232Cleavage; 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 C/Sarma)
    Taxonomic identifieri103919 [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 – 639605Envelope glycoproteinPRO_0000239568Add
    BLAST
    Chaini35 – 442408Surface proteinBy similarityPRO_0000040716Add
    BLAST
    Chaini443 – 622180Transmembrane proteinBy similarityPRO_0000040717Add
    BLAST
    Peptidei623 – 63917R-peptideBy similarityPRO_0000239569Add
    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
    Disulfide bondi122 ↔ 144By similarity
    Disulfide bondi136 ↔ 149By similarity
    Glycosylationi299 – 2991N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi304 – 3041N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi309 ↔ 536Interchain (between SU and TM chains, or C-312 with C-536); in linked formBy similarity
    Disulfide bondi309 ↔ 312By similarity
    Glycosylationi328 – 3281N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi331 – 3311N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi387 – 3871N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi407 – 4071N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi528 ↔ 535By similarity
    Lipidationi603 – 6031S-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

    ProteinModelPortaliP06752.
    SMRiP06752. Positions 38-230, 488-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 583549ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini605 – 63935CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei584 – 60421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni445 – 46521Fusion peptideSequence AnalysisAdd
    BLAST
    Regioni511 – 52717ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili473 – 52250Sequence AnalysisAdd
    BLAST
    Coiled coili532 – 56837Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi309 – 3124CXXC
    Motifi528 – 5369CX6CC

    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.

    P06752-1 [UniParc]FASTAAdd to Basket

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    MESPTHPKPS KDKTFPWNLV FLVGILFQID MGMANPSPHQ VYNVTWVITN    50
    VQTNSRANAT SMLGTLTDAY PTLYVDLCDL VGDTWEPIAP DPRSWARYSS 100
    STHGCKTTDR KKQQQTYPFY VCPGHAPSMG PKGTYCGGAQ DGFCAAWGCE 150
    TTGEAWWKPT SSWDYITVKR GSNQDNSCKG KCNPLVLQFT QKGRQASWDR 200
    PKMWGLRLYR SGYDPIALFS VSRQVMTITP PQAMGPNLVL PDQKPPSRQS 250
    QTKSKVTTQR PQITSSTPRS VASATMGPKR IGTGDRLINL VQGTYLALNA 300
    TDPNKTKDCW LCLVSRPPYY EGIAVLGNYS NQTNPPPSCL STPQHKLTIS 350
    EVSGQGLCIG TVPKTHQALC KKTQKGHKGT HYLAAPNGTY WACNTGLTPC 400
    ISMAVLNWTS DFCVLIELWP RVTYHQPEYI YTHFDKAVRF RREPISLTVA 450
    LMLGGLTVGG IAAGVGTGTK ALLETAQFRQ LQIAMHTDIQ ALEESISALE 500
    KSLTSLSEVV LQNRRGLDIL FLQEGGLCAA LKEECCFYAD HTGLVRDNMA 550
    KLRERLKQRQ QLFDSQQGWF EGWFNKSPWF TTLISSIMGP LLILLLILLL 600
    GPCILNRLVQ FVKDRISVVQ ALILTQQYQQ IQQYDSDRP 639
    Length:639
    Mass (Da):71,162
    Last modified:January 1, 1988 - v1
    Checksum:iA309B64AC8EC74E4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14331 Genomic DNA. Translation: AAA43049.1.
    PIRiA29013. VCMVSA.
    A46165.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14331 Genomic DNA. Translation: AAA43049.1 .
    PIRi A29013. VCMVSA.
    A46165.

    3D structure databases

    ProteinModelPortali P06752.
    SMRi P06752. Positions 38-230, 488-540.
    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. "Molecular analysis and pathogenesis of the feline aplastic anemia retrovirus, feline leukemia virus C-Sarma."
      Riedel N., Hoover E.A., Gasper P.W., Nicolson M.O., Mullins J.I.
      J. Virol. 60:242-250(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiENV_FLVSA
    AccessioniPrimary (citable) accession number: P06752
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program