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P35253

- VGP_MABVM

UniProt

P35253 - VGP_MABVM

Protein

Envelope glycoprotein

Gene

GP

Organism
Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain Kenya/Musoke/1980))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection) By similarity.By similarity
    GP2 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. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei435 – 4362Cleavage; by host furinBy similarity

    GO - Biological processi

    1. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    2. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Fusion of virus membrane with host endosomal 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):
    GP1,2
    Short name:
    GP
    Virion spike glycoprotein
    Cleaved into the following 2 chains:
    Gene namesi
    Name:GP
    OrganismiLake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain Kenya/Musoke/1980))
    Taxonomic identifieri33727 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesFiloviridaeMarburgvirus
    Virus hostiChlorocebus aethiops (Green monkey) (Cercopithecus aethiops) [TaxID: 9534]
    Homo sapiens (Human) [TaxID: 9606]
    Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat) [TaxID: 9407]
    ProteomesiUP000007771: Genome

    Subcellular locationi

    Chain GP2 : Virion membrane By similarity; Single-pass type I membrane protein By similarity. Virion membrane By similarity; Lipid-anchor By similarity. Host cell membrane By similarity; Single-pass type I membrane protein By similarity. Host cell membrane By similarity; Lipid-anchor By similarity
    Note: In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site.By similarity
    Chain GP1 : Virion membrane By similarity; Peripheral membrane protein By similarity. Host cell membrane By similarity; Peripheral membrane protein By similarity
    Note: GP1 is not anchored to the viral envelope, but associates with the extravirion surface through its binding to GP2. In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site By similarity.By similarity

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral envelope Source: UniProtKB-KW
    4. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi434 – 4341K → M: Partial loss of cleavage between GP1 and GP2. 1 Publication
    Mutagenesisi435 – 4351R → L: Complete loss of cleavage between GP1 and GP2. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 681663Envelope glycoproteinPRO_0000037515Add
    BLAST
    Chaini33 – 435403GP1By similarityPRO_0000314979Add
    BLAST
    Chaini436 – 681246GP2By similarityPRO_0000314980Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi37 ↔ 610Interchain (between GP1 and GP2 chains)By similarity
    Disulfide bondi92 ↔ 119Sequence Analysis
    Glycosylationi94 – 941N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi171 – 1711N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi190 – 1901N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi202 – 2021N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi211 ↔ 226Sequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi223 – 2231N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi255 – 2551N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi310 – 3101N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi313 – 3131N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi325 – 3251N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi326 – 3261N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi337 – 3371N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi345 – 3451N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi350 – 3501N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi360 – 3601N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi408 – 4081N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi487 – 4871N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi512 ↔ 557Sequence Analysis
    Glycosylationi564 – 5641N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi602 ↔ 609By similarity
    Glycosylationi619 – 6191N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi671 – 6711S-palmitoyl cysteine; by host1 Publication
    Lipidationi673 – 6731S-palmitoyl cysteine; by host1 Publication

    Post-translational modificationi

    N-glycosylated.
    O-glycosylated in the mucin-like region.Curated
    Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into GP1 and GP2 by host cell furin in the trans Golgi, and maybe by other host proteases, to yield the mature GP1 and GP2 proteins. The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R.1 Publication
    GP1 is phosphorylated on serine residues between residues 260 and 273.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    PTM databases

    UniCarbKBiP35253.

    Interactioni

    Subunit structurei

    Homotrimer; each monomer consists of a GP1 and a GP2 subunit linked by disulfide bonds. The resulting peplomers (GP1,2) protrude from the virus surface as spikes. GP1,2 interacts with human CD209 and CLEC4M (collectively referred to as DC-SIGN(R)). Asialoglycoprotein receptor (ASGP-R) may be a liver-specific receptor for GP1,2. Members of the Tyro3 receptor tyrosine kinase family may be cell entry factors interacting with GP1,2.3 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliP35253.
    SMRiP35253. Positions 559-630.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 648630ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini670 – 68112CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei649 – 66921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni38 – 188151Receptor-bindingAdd
    BLAST
    Regioni277 – 455179Mucin-like regionBy similarityAdd
    BLAST
    Regioni529 – 54921Fusion peptideBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 424233Thr-richAdd
    BLAST
    Compositional biasi471 – 4744Poly-Ser

    Domaini

    The coiled coil regions play a role in oligomerization and fusion activity.By similarity
    The transmembrane domain is essential and sufficient for recruitment envelope glycoproteins into VP40-enriched multivesicular bodies.

    Sequence similaritiesi

    Belongs to the filoviruses glycoprotein family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR014625. GPC_FiloV.
    IPR002561. GPC_filovir-type_extra_dom.
    [Graphical view]
    PfamiPF01611. Filo_glycop. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036874. GPC_FiloV. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P35253-1 [UniParc]FASTAAdd to Basket

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    MKTTCFLISL ILIQGTKNLP ILEIASNNQP QNVDSVCSGT LQKTEDVHLM    50
    GFTLSGQKVA DSPLEASKRW AFRTGVPPKN VEYTEGEEAK TCYNISVTDP 100
    SGKSLLLDPP TNIRDYPKCK TIHHIQGQNP HAQGIALHLW GAFFLYDRIA 150
    STTMYRGKVF TEGNIAAMIV NKTVHKMIFS RQGQGYRHMN LTSTNKYWTS 200
    SNGTQTNDTG CFGALQEYNS TKNQTCAPSK IPPPLPTARP EIKLTSTPTD 250
    ATKLNTTDPS SDDEDLATSG SGSGEREPHT TSDAVTKQGL SSTMPPTPSP 300
    QPSTPQQGGN NTNHSQDAVT ELDKNNTTAQ PSMPPHNTTT ISTNNTSKHN 350
    FSTLSAPLQN TTNDNTQSTI TENEQTSAPS ITTLPPTGNP TTAKSTSSKK 400
    GPATTAPNTT NEHFTSPPPT PSSTAQHLVY FRRKRSILWR EGDMFPFLDG 450
    LINAPIDFDP VPNTKTIFDE SSSSGASAEE DQHASPNISL TLSYFPNINE 500
    NTAYSGENEN DCDAELRIWS VQEDDLAAGL SWIPFFGPGI EGLYTAVLIK 550
    NQNNLVCRLR RLANQTAKSL ELLLRVTTEE RTFSLINRHA IDFLLTRWGG 600
    TCKVLGPDCC IGIEDLSKNI SEQIDQIKKD EQKEGTGWGL GGKWWTSDWG 650
    VLTNLGILLL LSIAVLIALS CICRIFTKYI G 681
    Length:681
    Mass (Da):74,376
    Last modified:February 1, 1994 - v1
    Checksum:iCC89305C64D34B0B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti547 – 5471V → G in strain: pp3/guinea pig lethal and pp4/guinea pig nonlethal.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12132 mRNA. Translation: CAA78117.1.
    AY430365 Genomic RNA. Translation: AAR85463.1.
    AY430366 Genomic RNA. Translation: AAR85456.1.
    DQ217792 Genomic RNA. Translation: ABA87127.1.
    PIRiA45705.
    RefSeqiYP_001531156.1. NC_001608.3.

    Genome annotation databases

    GeneIDi920945.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12132 mRNA. Translation: CAA78117.1 .
    AY430365 Genomic RNA. Translation: AAR85463.1 .
    AY430366 Genomic RNA. Translation: AAR85456.1 .
    DQ217792 Genomic RNA. Translation: ABA87127.1 .
    PIRi A45705.
    RefSeqi YP_001531156.1. NC_001608.3.

    3D structure databases

    ProteinModelPortali P35253.
    SMRi P35253. Positions 559-630.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    UniCarbKBi P35253.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 920945.

    Family and domain databases

    InterProi IPR014625. GPC_FiloV.
    IPR002561. GPC_filovir-type_extra_dom.
    [Graphical view ]
    Pfami PF01611. Filo_glycop. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036874. GPC_FiloV. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein."
      Will C., Muehlberger E., Linder D., Slenczka W., Klenk H.-D., Feldmann H.
      J. Virol. 67:1203-1210(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-37.
    2. Chain P.S.G., Malfatti S.A., Hajjaj A., Vergez L.M., Do L.H., Smith K.L., McCready P.M.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: pp3/guinea pig lethal and pp4/guinea pig nonlethal.
    3. Ichou M.A., Paragas J., Jahrling P.B., Ibrahim M.S., Lofts L., Hevey M., Schmaljohn A.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: pp3/guinea pig lethal and pp4/guinea pig nonlethal.
    4. "Rescue of recombinant Marburg virus from cDNA is dependent on nucleocapsid protein VP30."
      Enterlein S., Volchkov V., Weik M., Kolesnikova L., Volchkova V., Klenk H.-D., Muehlberger E.
      J. Virol. 80:1038-1043(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    5. "Glycosylation and oligomerization of the spike protein of Marburg virus."
      Feldmann H., Will C., Schikore M., Slenczka W., Klenk H.-D.
      Virology 182:353-356(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, GLYCOSYLATION.
    6. Cited for: PALMITOYLATION.
    7. "Carbohydrate structure of Marburg virus glycoprotein."
      Geyer H., Will C., Feldmann H., Klenk H.-D., Geyer R.
      Glycobiology 2:299-312(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    8. "The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus."
      Becker S., Spiess M., Klenk H.-D.
      J. Gen. Virol. 76:393-399(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN ASIALOGLYCOPROTEIN RECEPTOR.
    9. Cited for: PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN, MUTAGENESIS OF LYS-434 AND ARG-435.
    10. "The Marburg virus surface protein GP is phosphorylated at its ectodomain."
      Saenger C., Muehlberger E., Loetfering B., Klenk H.-D., Becker S.
      Virology 295:20-29(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    11. "DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus."
      Marzi A., Gramberg T., Simmons G., Moeller P., Rennekamp A.J., Krumbiegel M., Geier M., Eisemann J., Turza N., Saunier B., Steinkasserer A., Becker S., Bates P., Hofmann H., Poehlmann S.
      J. Virol. 78:12090-12095(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN CD209 AND CLEC4M.
    12. Cited for: FUNCTION.
    13. "Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor."
      Kuhn J.H., Radoshitzky S.R., Guth A.C., Warfield K.L., Li W., Vincent M.J., Towner J.S., Nichol S.T., Bavari S., Choe H., Aman M.J., Farzan M.
      J. Biol. Chem. 281:15951-15958(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECEPTOR-BINDING REGION.
    14. "Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope."
      Mittler E., Kolesnikova L., Strecker T., Garten W., Becker S.
      J. Virol. 81:3942-3948(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSMEMBRANE DOMAIN.

    Entry informationi

    Entry nameiVGP_MABVM
    AccessioniPrimary (citable) accession number: P35253
    Secondary accession number(s): Q38L42, Q6T6U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Filoviruses entry requires functional lipid rafts at the host cell surface.By similarity
    Essential for infectivity, as it is the sole viral protein expressed at the virion surface.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3