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)

P26803

- ENV_MLVFP

UniProt

P26803 - ENV_MLVFP

Protein

Envelope glycoprotein

Gene

env

Organism
Friend murine leukemia virus (isolate PVC-211) (FrMLV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      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
    Metal bindingi89 – 891ZincBy similarity
    Metal bindingi120 – 1201ZincBy similarity
    Sitei479 – 4802Cleavage; by hostBy similarity
    Sitei659 – 6602Cleavage; by viral protease p14By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
    2. suppression by virus of host adaptive immune response Source: UniProtKB-KW
    3. suppression by virus of host antigen processing and presentation Source: UniProtKB-KW
    4. 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, Inhibition of host adaptive immune response by virus, Inhibition of host proteasome antigen processing by virus, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Virus entry into host cell

    Keywords - Ligandi

    Metal-binding, Zinc

    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
    OrganismiFriend murine leukemia virus (isolate PVC-211) (FrMLV)
    Taxonomic identifieri11798 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000007777: Genome

    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 virion 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 – 676642Envelope glycoproteinPRO_0000239583Add
    BLAST
    Chaini35 – 479445Surface proteinBy similarityPRO_0000040757Add
    BLAST
    Chaini480 – 659180Transmembrane proteinBy similarityPRO_0000040758Add
    BLAST
    Peptidei660 – 67617R-peptideBy similarityPRO_0000040759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi46 – 461N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi80 ↔ 132By similarity
    Disulfide bondi106 ↔ 121By similarity
    Disulfide bondi107 ↔ 117By similarity
    Disulfide bondi155 ↔ 175By similarity
    Disulfide bondi167 ↔ 180By similarity
    Glycosylationi202 – 2021N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi212 ↔ 218By similarity
    Glycosylationi336 – 3361N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi346 ↔ 573Interchain (between SU and TM chains, or C-349 with C-573); in linked form
    Disulfide bondi346 ↔ 349
    Glycosylationi368 – 3681N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi375 – 3751N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi376 ↔ 430By similarity
    Disulfide bondi395 ↔ 407By similarity
    Glycosylationi408 – 4081N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi437 ↔ 450By similarity
    Glycosylationi444 – 4441N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi565 ↔ 572By similarity
    Lipidationi640 – 6401S-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

    ProteinModelPortaliP26803.
    SMRiP26803. Positions 43-269, 525-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 620586ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini642 – 67635CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei621 – 64121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 270236Receptor-binding domain (RBD)Sequence AnalysisAdd
    BLAST
    Regioni482 – 50221Fusion peptideBy similarityAdd
    BLAST
    Regioni548 – 56417ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili513 – 54735Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi346 – 3494CXXC
    Motifi565 – 5739CX6CC
    Motifi665 – 6684YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi267 – 31751Pro-richAdd
    BLAST

    Domaini

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

    P26803-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACSTLSKSP KDKIDPRDLL IPLILFLSLK GARSAAPGSS PHQVYNITWE    50
    VTNGDRETVW AISGNHPLWT WWPDLTPDLC MLALSGPPHW GLEYRAPYSS 100
    PPGPPCCSGS SGNRAGCARD CDEPLTSLTP RCNTAWNRLK LDQVTHKSSG 150
    GFYVCPGSHR PRKAKSCGGP DSFYCASWGC ETTGRAYWKP SSSWDYITVD 200
    NNLTTNQAAQ VCKDNKWCNP LAIQFTNAGK QVTSWTIGHY WGLRLYVSGQ 250
    DPGLTFGIRL KYQNLGPRVP IGPNPVLADQ LSFPLPNPLP KPAKSPSASN 300
    STPTLISPSP APTQPPPAGT GDRLLNLVQG AYQALNLTNP DKTQECWLCL 350
    VSAPPYYEGV AVLGTYSNHT SAPANCSAGS QHKLTLSEVT GQGLCIGTVP 400
    KTHQALCNTT LKTGKGSYYL VAPAGTMWAC NTGLTPCLSA TVLNRTTDYC 450
    VLVELWPRVT YHPPSYVYSQ FEKSYRHKRE PVSLTLALLL GGLTMGGIAA 500
    GVGTGTTALV ATQQFQQLHA AVQDDLKEVE KSITNLEKSL TSLSEVVLQN 550
    RRGLDLLFLK EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLTQRQKLF 600
    ESSQGWFEGL FNRSPWFTTL ISTIMGPLII LLLILLFGPC ILNRLVQFVK 650
    DRISVVQALV LTQQYHQLKP LEYEPQ 676
    Length:676
    Mass (Da):73,946
    Last modified:August 1, 1992 - v1
    Checksum:i18D8D8A7FE0A8FA4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93134 Genomic RNA. Translation: AAA46478.1.
    PIRiA38210. VCMVPV.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93134 Genomic RNA. Translation: AAA46478.1 .
    PIRi A38210. VCMVPV.

    3D structure databases

    ProteinModelPortali P26803.
    SMRi P26803. Positions 43-269, 525-577.
    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 characterization of a neuropathogenic and nonerythroleukemogenic variant of Friend murine leukemia virus PVC-211."
      Masuda M., Remington M.P., Hoffman P.M., Ruscetti S.K.
      J. Virol. 66:2798-2806(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Complete nucleotide sequence of a neuropathogenic variant of Friend murine leukemia virus PVC-211."
      Remington M.P., Hoffman P.M., Ruscetti S.K., Masuda M.
      Nucleic Acids Res. 20:3249-3249(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiENV_MLVFP
    AccessioniPrimary (citable) accession number: P26803
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The surface protein appears to be responsible for the neuropathogenicity of PVC-211 MuLV.

    Keywords - Technical termi

    Complete proteome

    External Data

    Dasty 3