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P35253

- VGP_MABVM

UniProt

P35253 - VGP_MABVM

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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

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
Complete GO annotation...

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-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MKTTCFLISL ILIQGTKNLP ILEIASNNQP QNVDSVCSGT LQKTEDVHLM
60 70 80 90 100
GFTLSGQKVA DSPLEASKRW AFRTGVPPKN VEYTEGEEAK TCYNISVTDP
110 120 130 140 150
SGKSLLLDPP TNIRDYPKCK TIHHIQGQNP HAQGIALHLW GAFFLYDRIA
160 170 180 190 200
STTMYRGKVF TEGNIAAMIV NKTVHKMIFS RQGQGYRHMN LTSTNKYWTS
210 220 230 240 250
SNGTQTNDTG CFGALQEYNS TKNQTCAPSK IPPPLPTARP EIKLTSTPTD
260 270 280 290 300
ATKLNTTDPS SDDEDLATSG SGSGEREPHT TSDAVTKQGL SSTMPPTPSP
310 320 330 340 350
QPSTPQQGGN NTNHSQDAVT ELDKNNTTAQ PSMPPHNTTT ISTNNTSKHN
360 370 380 390 400
FSTLSAPLQN TTNDNTQSTI TENEQTSAPS ITTLPPTGNP TTAKSTSSKK
410 420 430 440 450
GPATTAPNTT NEHFTSPPPT PSSTAQHLVY FRRKRSILWR EGDMFPFLDG
460 470 480 490 500
LINAPIDFDP VPNTKTIFDE SSSSGASAEE DQHASPNISL TLSYFPNINE
510 520 530 540 550
NTAYSGENEN DCDAELRIWS VQEDDLAAGL SWIPFFGPGI EGLYTAVLIK
560 570 580 590 600
NQNNLVCRLR RLANQTAKSL ELLLRVTTEE RTFSLINRHA IDFLLTRWGG
610 620 630 640 650
TCKVLGPDCC IGIEDLSKNI SEQIDQIKKD EQKEGTGWGL GGKWWTSDWG
660 670 680
VLTNLGILLL LSIAVLIALS CICRIFTKYI G
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 29, 2014
This is version 80 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