VGP_MABVA
ID VGP_MABVA Reviewed; 681 AA.
AC Q1PD50;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=GP1,2;
DE Short=GP;
DE AltName: Full=Virion spike glycoprotein;
DE Contains:
DE RecName: Full=GP1;
DE Contains:
DE RecName: Full=GP2;
DE Flags: Precursor;
GN Name=GP;
OS Lake Victoria marburgvirus (strain Angola/2005) (MARV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=378830;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Ang0126, Isolate Ang0214, Isolate Ang0215, Isolate Ang0754,
RC Isolate Ang0998, Isolate Ang1379c, Isolate Ang1381, and Isolate Ang1386;
RX PubMed=16775337; DOI=10.1128/jvi.00069-06;
RA Towner J.S., Khristova M.L., Sealy T.K., Vincent M.J., Erickson B.R.,
RA Bawiec D.A., Hartman A.L., Comer J.A., Zaki S.R., Stroeher U.,
RA Gomes da Silva F., del Castillo F., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT "Marburgvirus genomics and association with a large hemorrhagic fever
RT outbreak in Angola.";
RL J. Virol. 80:6497-6516(2006).
CC -!- FUNCTION: GP1 is responsible for binding to the receptor(s) on target
CC cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as
CC cofactors for virus entry into the host cell. Binding to CD209 and
CC CLEC4M, which are respectively found on dendritic cells (DCs), and on
CC endothelial cells of liver sinusoids and lymph node sinuses, facilitate
CC infection of macrophages and endothelial cells. These interactions not
CC only facilitate virus cell entry, but also allow capture of viral
CC particles by DCs and subsequent transmission to susceptible cells
CC without DCs infection (trans infection) (By similarity). {ECO:0000250}.
CC -!- FUNCTION: GP2 acts as a class I viral fusion protein. Under the current
CC model, the protein has at least 3 conformational states: pre-fusion
CC native state, pre-hairpin intermediate state, and post-fusion hairpin
CC state. During viral and target cell membrane fusion, the coiled coil
CC regions (heptad repeats) assume a trimer-of-hairpins structure,
CC positioning the fusion peptide in close proximity to the C-terminal
CC region of the ectodomain. The formation of this structure appears to
CC drive apposition and subsequent fusion of viral and target cell
CC membranes. Responsible for penetration of the virus into the cell
CC cytoplasm by mediating the fusion of the membrane of the endocytosed
CC virus particle with the endosomal membrane. Low pH in endosomes induces
CC an irreversible conformational change in GP2, releasing the fusion
CC hydrophobic peptide (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; each monomer consists of a GP1 and a GP2 subunit
CC linked by disulfide bonds. The resulting peplomers (GP1,2) protrude
CC from the virus surface as spikes. GP1,2 interacts with human CD209 and
CC CLEC4M (collectively referred to as DC-SIGN(R)). Asialoglycoprotein
CC receptor (ASGP-R) may be a liver-specific receptor for GP1,2. Members
CC of the Tyro3 receptor tyrosine kinase family may be cell entry factors
CC interacting with GP1,2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [GP2]: Virion membrane
CC {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:Q05320};
CC Single-pass type I membrane protein {ECO:0000255}. Note=In the cell,
CC localizes to the plasma membrane lipid rafts, which probably represent
CC the assembly and budding site. {ECO:0000250|UniProtKB:Q05320}.
CC -!- SUBCELLULAR LOCATION: [GP1]: Virion membrane
CC {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q05320}. Host cell membrane
CC {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q05320}. Note=GP1 is not anchored to the viral
CC envelope, but forms a disulfid-linked complex with the extravirion
CC surface GP2. In the cell, both GP1 and GP2 localize to the plasma
CC membrane lipid rafts, which probably represent the assembly and budding
CC site. GP1 can also be shed after proteolytic processing.
CC {ECO:0000250|UniProtKB:Q05320}.
CC -!- DOMAIN: The coiled coil regions play a role in oligomerization and
CC fusion activity. {ECO:0000250}.
CC -!- DOMAIN: The transmembrane domain is essential and sufficient for
CC recruitment envelope glycoproteins into VP40-enriched multivesicular
CC bodies. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: O-glycosylated in the mucin-like region. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into GP1 and GP2 by host cell furin in the trans
CC Golgi, and maybe by other host proteases, to yield the mature GP1 and
CC GP2 proteins. The cleavage site corresponds to the furin optimal
CC cleavage sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.
CC -!- PTM: GP1 is phosphorylated on serine residues between residues 260 and
CC 273. {ECO:0000250}.
CC -!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts at the
CC host cell surface. {ECO:0000250}.
CC -!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
CC protein expressed at the virion surface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; DQ447653; ABE27015.1; -; Genomic_RNA.
DR EMBL; DQ447654; ABE27022.1; -; Genomic_RNA.
DR EMBL; DQ447655; ABE27029.1; -; Genomic_RNA.
DR EMBL; DQ447656; ABE27036.1; -; Genomic_RNA.
DR EMBL; DQ447657; ABE27043.1; -; Genomic_RNA.
DR EMBL; DQ447658; ABE27050.1; -; Genomic_RNA.
DR EMBL; DQ447659; ABE27057.1; -; Genomic_RNA.
DR EMBL; DQ447660; ABE27064.1; -; Genomic_RNA.
DR SMR; Q1PD50; -.
DR Proteomes; UP000008242; Genome.
DR Proteomes; UP000097432; Genome.
DR Proteomes; UP000102513; Genome.
DR Proteomes; UP000109618; Genome.
DR Proteomes; UP000115353; Genome.
DR Proteomes; UP000130744; Genome.
DR Proteomes; UP000168007; Genome.
DR Proteomes; UP000171838; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR014625; GPC_FiloV.
DR InterPro; IPR002561; GPC_filovir-type_extra_dom.
DR Pfam; PF01611; Filo_glycop; 1.
DR PIRSF; PIRSF036874; GPC_FiloV; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..681
FT /note="Envelope glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000314976"
FT CHAIN 33..435
FT /note="GP1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000314977"
FT CHAIN 436..681
FT /note="GP2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000314978"
FT TOPO_DOM 19..648
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 38..188
FT /note="Receptor-binding"
FT /evidence="ECO:0000250"
FT REGION 222..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..455
FT /note="Mucin-like region"
FT /evidence="ECO:0000250"
FT REGION 529..549
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COMPBIAS 241..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 435..436
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT LIPID 671
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250|UniProtKB:P35253"
FT LIPID 673
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250|UniProtKB:P35253"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 681 AA; 74304 MW; 05DDE25436A55B50 CRC64;
MKTTCLLISL ILIQGVKTLP ILEIASNIQP QNVDSVCSGT LQKTEDVHLM GFTLSGQKVA
DSPLEASKRW AFRAGVPPKN VEYTEGEEAK TCYNISVTDP SGKSLLLDPP TNIRDYPKCK
TIHHIQGQNP HAQGIALHLW GAFFLYDRIA STTMYRGKVF TEGNIAAMIV NKTVHKMIFS
RQGQGYRHMN LTSTNKYWTS SNGTQTNDTG CFGTLQEYNS TKNQTCAPSK KPLPLPTAHP
EVKLTSTSTD ATKLNTTDPN SDDEDLTTSG SGSGEQEPYT TSDAATKQGL SSTMPPTPSP
QPSTPQQGGN NTNHSQGVVT EPGKTNTTAQ PSMPPHNTTT ISTNNTSKHN LSTPSVPIQN
ATNYNTQSTA PENEQTSAPS KTTLLPTENP TTAKSTNSTK SPTTTVPNTT NKYSTSPSPT
PNSTAQHLVY FRRKRNILWR EGDMFPFLDG LINAPIDFDP VPNTKTIFDE SSSSGASAEE
DQHASPNISL TLSYFPKVNE NTAHSGENEN DCDAELRIWS VQEDDLAAGL SWIPFFGPGI
EGLYTAGLIK NQNNLVCRLR RLANQTAKSL ELLLRVTTEE RTFSLINRHA IDFLLARWGG
TCKVLGPDCC IGIEDLSRNI SEQIDQIKKD EQKEGTGWGL GGKWWTSDWG VLTNLGILLL
LSIAVLIALS CICRIFTKYI G
