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P31791

- ENV_FENV1

UniProt

P31791 - ENV_FENV1

Protein

Envelope glycoprotein

Gene

env

Organism
Feline endogenous virus ECE1
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      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
    Sitei470 – 4712Cleavage; by hostBy similarity
    Sitei650 – 6512Cleavage; 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 endogenous virus ECE1
    Taxonomic identifieri11766 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
    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 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 671649Envelope glycoproteinPRO_0000239558Add
    BLAST
    Chaini23 – 470448Surface proteinBy similarityPRO_0000040703Add
    BLAST
    Chaini471 – 650180Transmembrane proteinBy similarityPRO_0000040704Add
    BLAST
    Peptidei651 – 67121R-peptideBy similarityPRO_0000239559Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi121 ↔ 142By similarity
    Disulfide bondi134 ↔ 147By similarity
    Glycosylationi169 – 1691N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi281 – 2811N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi326 – 3261N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi331 – 3311N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi358 – 3581N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi415 – 4151N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi435 – 4351N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi631 – 6311S-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 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 noncovalent interactions or by a labile interchain disulfide bond.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP31791.
    SMRiP31791. Positions 516-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 611589ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini633 – 67139CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei612 – 63221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni473 – 49321Fusion peptideSequence AnalysisAdd
    BLAST
    Regioni539 – 55517ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili501 – 55050Sequence AnalysisAdd
    BLAST
    Coiled coili560 – 59637Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi336 – 3394CXXC
    Motifi556 – 5649CX6CC
    Motifi656 – 6594YXXL 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

    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.

    P31791-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPPAGMVFL WVLTSLGAGI GAKIVKEGNP HQVYTLTWQI YSQSGEVVWE    50
    VQGNHALNTW WPALTPDFCQ LAAGLDTWDI PDRSPKNLET SMEGTSQQLT 100
    PQGCSKPWKR CALTERDFYV CPRDNRDRAT AHRCGGYEEY FCSAWGCETT 150
    GDAYWQPTST WDLITITRNY TKPDSCDDRV ERERKTSRHW RDPLSLPLKI 200
    TFTDSGKRAL GWQTGYTWGL RWYLPGKDRG IILKIKLKID TITQTVGPNL 250
    VLADQKTPVQ LAIPVQPPRA PTQTPRVNPV NSTLSPSLGY PAPAPGPRPP 300
    YPTSPSRPGT GDRLLNLVQG VYLTLNLTAP NQTQDCWLCL TAKPPYYQGV 350
    AIIGNFTNHT NAPLRCSTTP RHGLTLTEVT GYGLCIGKIP PSHQNLCSQT 400
    VPSVGQGPYY LTAPNGTYWV CNTGLTPCIS LQILNDTADY CILIELWPKI 450
    FYHDSEYIYG HYEPGGRFRR DPVSLTVALL LGGLTMGSLA AGIGTGTAAL 500
    IETNQFKQLQ IAMHSDIQAL EESISALERS LISLSEVVLQ NRRGLDLLFL 550
    QEGGLCAALK EECCFYADHT GIVRDSMAKL RERFKQRQKL FESQQGWFEG 600
    WYNKSPWFTT LVSSLMVPLI LLLLILMFGP CILNHLLQFI RERLSVIQAL 650
    VLTQQYHQLR QFDAERPDAI E 671
    Length:671
    Mass (Da):75,152
    Last modified:July 1, 1993 - v1
    Checksum:iEA9847024EF794A0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51929 Genomic DNA. Translation: CAB38567.1.
    PIRiS12815. VCMVCE.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51929 Genomic DNA. Translation: CAB38567.1 .
    PIRi S12815. VCMVCE.

    3D structure databases

    ProteinModelPortali P31791.
    SMRi P31791. Positions 516-568.
    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. "The exogenous RD-114 and the related endogenous proviral element ECE1 of domestic cat differ in their env genes."
      Moehring R., Drescher B., Riedel H., Bauer D., Rohde K., Beyer W., Rosenthal S.
      Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiENV_FENV1
    AccessioniPrimary (citable) accession number: P31791
    Secondary accession number(s): Q28416
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program