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P03385

- ENV_MLVMS

UniProt

P03385 - ENV_MLVMS

Protein

Envelope glycoprotein

Gene

env

Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    The surface protein (SU) attaches the virus to the host cell by binding to its receptor. Interaction with HECT ubiquitin ligases activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane.1 Publication
    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 bindingi117 – 1171ZincBy similarity
    Sitei469 – 4702Cleavage; by host
    Sitei649 – 6502Cleavage; by viral protease p14Sequence Analysis

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. 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

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Envelope glycoprotein
    Short name:
    Pr80env
    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
    OrganismiMoloney murine leukemia virus (isolate Shinnick) (MoMLV)
    Taxonomic identifieri928306 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000006625: 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 1 Publication; Peripheral membrane protein 1 Publication
    Note: The R-peptide is membrane-associated through its palmitate.

    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 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 665632Envelope glycoproteinPRO_0000239588Add
    BLAST
    Chaini34 – 469436Surface proteinBy similarityPRO_0000040765Add
    BLAST
    Chaini470 – 649180Transmembrane proteinPRO_0000040766Add
    BLAST
    Peptidei650 – 66516R-peptidePRO_0000040767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi79 ↔ 129By similarity
    Disulfide bondi105 ↔ 118By similarity
    Disulfide bondi106 ↔ 114By similarity
    Disulfide bondi152 ↔ 172By similarity
    Disulfide bondi164 ↔ 177By similarity
    Glycosylationi199 – 1991N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi209 ↔ 215By similarity
    Glycosylationi326 – 3261N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi336 ↔ 563Interchain (between SU and TM chains, or C-339 with C-563); in linked form
    Disulfide bondi336 ↔ 339
    Glycosylationi358 – 3581N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi365 – 3651N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi366 ↔ 420By similarity
    Disulfide bondi385 ↔ 397By similarity
    Glycosylationi398 – 3981N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi427 ↔ 440By similarity
    Glycosylationi434 – 4341N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi555 ↔ 562By similarity
    Lipidationi630 – 6301S-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.1 Publication

    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. The activated Env consists of SU monomers and TM trimers.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-8074066,EBI-8074066

    Protein-protein interaction databases

    MINTiMINT-7304679.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi516 – 54732
    Helixi549 – 5513
    Helixi554 – 5585

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MOFX-ray1.70A514-567[»]
    ProteinModelPortaliP03385.
    SMRiP03385. Positions 42-266, 515-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03385.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 610577ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini632 – 66534CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei611 – 63121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni34 – 267234Receptor-binding domain (RBD)Sequence AnalysisAdd
    BLAST
    Regioni472 – 49221Fusion peptideBy similarityAdd
    BLAST
    Regioni538 – 55417ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili500 – 53738Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi336 – 3394CXXC
    Motifi555 – 5639CX6CC
    Motifi655 – 6584YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi264 – 30744Pro-richAdd
    BLAST

    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.

    P03385-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARSTLSKPL KNKVNPRGPL IPLILLMLRG VSTASPGSSP HQVYNITWEV    50
    TNGDRETVWA TSGNHPLWTW WPDLTPDLCM LAHHGPSYWG LEYQSPFSSP 100
    PGPPCCSGGS SPGCSRDCEE PLTSLTPRCN TAWNRLKLDQ TTHKSNEGFY 150
    VCPGPHRPRE SKSCGGPDSF YCAYWGCETT GRAYWKPSSS WDFITVNNNL 200
    TSDQAVQVCK DNKWCNPLVI RFTDAGRRVT SWTTGHYWGL RLYVSGQDPG 250
    LTFGIRLRYQ NLGPRVPIGP NPVLADQQPL SKPKPVKSPS VTKPPSGTPL 300
    SPTQLPPAGT ENRLLNLVDG AYQALNLTSP DKTQECWLCL VAGPPYYEGV 350
    AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GQGLCIGAVP KTHQALCNTT 400
    QTSSRGSYYL VAPTGTMWAC STGLTPCIST TILNLTTDYC VLVELWPRVT 450
    YHSPSYVYGL FERSNRHKRE PVSLTLALLL GGLTMGGIAA GIGTGTTALM 500
    ATQQFQQLQA AVQDDLREVE KSISNLEKSL TSLSEVVLQN RRGLDLLFLK 550
    EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLNQRQKLF ESTQGWFEGL 600
    FNRSPWFTTL ISTIMGPLIV LLMILLFGPC ILNRLVQFVK DRISVVQALV 650
    LTQQYHQLKP IEYEP 665
    Length:665
    Mass (Da):73,302
    Last modified:July 21, 1986 - v1
    Checksum:i12EBA09C8FB93FE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti655 – 6551Y → F(PubMed:6251454)Curated
    Sequence conflicti663 – 6631Y → C(PubMed:6251454)Curated
    Sequence conflicti663 – 6631Y → C(PubMed:6947213)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02255 Genomic RNA. Translation: AAB59943.1.
    AF033811 Genomic RNA. Translation: AAC82567.1.
    PIRiA93265. VCVWEM.
    RefSeqiNP_057935.1. NC_001501.1.

    Genome annotation databases

    GeneIDi2193424.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02255 Genomic RNA. Translation: AAB59943.1 .
    AF033811 Genomic RNA. Translation: AAC82567.1 .
    PIRi A93265. VCVWEM.
    RefSeqi NP_057935.1. NC_001501.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MOF X-ray 1.70 A 514-567 [» ]
    ProteinModelPortali P03385.
    SMRi P03385. Positions 42-266, 515-567.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-7304679.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2193424.

    Miscellaneous databases

    EvolutionaryTracei P03385.

    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 of Moloney murine leukaemia virus."
      Shinnick T.M., Lerner R.A., Sutcliffe J.G.
      Nature 293:543-548(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Clone pMLV-1.
    2. Chappey C.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Chemical synthesis of a polypeptide predicted from nucleotide sequence allows detection of a new retroviral gene product."
      Sutcliffe J.G., Shinnick T.M., Green N., Liu F.-T., Niman H.L., Lerner R.A.
      Nature 287:801-805(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 496-665.
    4. "Nucleotide sequence of Moloney leukemia virus: 3' end reveals details of replications, analogy to bacterial transposons, and an unexpected gene."
      Sutcliffe J.G., Shinnick T.M., Verma I.M., Lerner R.A.
      Proc. Natl. Acad. Sci. U.S.A. 77:3302-3306(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 484-665.
      Strain: Clone pMLV-201.
    5. "Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope polyprotein involves removal of a COOH-terminal peptide."
      Green N., Shinnick T.M., Witte O., Ponticelli A., Sutcliffe J.G., Lerner R.A.
      Proc. Natl. Acad. Sci. U.S.A. 78:6023-6027(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 470-489 AND 598-665.
    6. "Inhibition of lymphocyte proliferation by a synthetic peptide homologous to retroviral envelope proteins."
      Cianciolo G.J., Copeland T.D., Oroszlan S., Snyderman R.
      Science 230:453-455(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: IMMUNOSUPPRESSIVE REGION.
    7. "Palmitoylation of the intracytoplasmic R peptide of the transmembrane envelope protein in Moloney murine leukemia virus."
      Olsen K.E., Andersen K.B.
      J. Virol. 73:8975-8981(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION OF THE R-PEPTIDE, PALMITOYLATION OF THE R-PEPTIDE.
    8. "Mutational analysis of the R peptide cleavage site of Moloney murine leukaemia virus envelope protein."
      Kubo Y., Amanuma H.
      J. Gen. Virol. 84:2253-2257(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF THE R-PEPTIDE.
    9. "Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion."
      Wallin M., Ekstroem M., Garoff H.
      EMBO J. 23:54-65(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERCHAIN DISULFIDE BOND.
    10. "Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion."
      Wu S.-R., Sjoeberg M., Wallin M., Lindqvist B., Ekstroem M., Hebert H., Koeck P.J., Garoff H.
      EMBO J. 27:2799-2808(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Stabilization of TM trimer interactions during activation of moloney murine leukemia virus Env."
      Sjoberg M., Lindqvist B., Garoff H.
      J. Virol. 82:2358-2366(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    12. "Retrovirus envelope domain at 1.7-A resolution."
      Fass D., Harrison S.C., Kim P.S.
      Nat. Struct. Biol. 3:465-469(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 514-567.

    Entry informationi

    Entry nameiENV_MLVMS
    AccessioniPrimary (citable) accession number: P03385
    Secondary accession number(s): Q77YG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 116 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3