P16853 · GP_HANTL

Function

function

Glycoprotein N

Forms homotetramers with glycoprotein C at the surface of the virion (By similarity).
Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (By similarity).
This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity).
May also bind to host C1QBP for virus entry into the host cell (By similarity).
Mediates the assembly and budding of infectious virus particles through its interaction with the nucleocapsid protein and the viral genome (By similarity).
May dysregulate normal immune and endothelial cell responses through an ITAM motif (By similarity).
Translocates to mitochondria, binds to host TUFM and recruits MAP1LC3B (By similarity).
These interactions induce mitochondrial autophagy and therefore destruction of host MAVS leading to inhibition of type I interferon (IFN) responses (By similarity).
Concomitant breakdown of glycoprotein N is apparently prevented by the nucleoprotein that may inhibit Gn-stimulated autophagosome-lysosome fusion (By similarity).
Interacts with the viral genomic RNA (By similarity).

Glycoprotein C

Forms homotetramers with glycoprotein N at the surface of the virion (By similarity).
Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (By similarity).
This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity).
May also bind to host C1QBP for virus entry into the host cell (By similarity).
Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (By similarity).

Features

Showing features for site.

TypeIDPosition(s)Description
Site648-649Cleavage; by host signal peptidase

GO annotations

AspectTerm
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell Golgi membrane
Cellular Componenthost cell mitochondrion
Cellular Componenthost cell surface
Cellular Componentmembrane
Cellular Componentviral envelope
Cellular Componentvirion membrane
Molecular Functionmetal ion binding
Biological Processendocytosis involved in viral entry into host cell
Biological Processfusion of virus membrane with host endosome membrane
Biological Processsignal transduction
Biological Processsymbiont-mediated suppression of host innate immune response
Biological Processsymbiont-mediated suppression of host TRAF-mediated signal transduction
Biological Processvirion attachment to host cell
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Envelopment polyprotein
  • Alternative names
    • M polyprotein
  • Cleaved into 2 chains

Gene names

    • Name
      GP

Organism names

Accessions

  • Primary accession
    P16853

Subcellular Location

Glycoprotein N

Virion membrane
; Multi-pass membrane protein
Host cell surface
Host Golgi apparatus membrane
; Multi-pass membrane protein
Host endoplasmic reticulum membrane
; Multi-pass membrane protein
Host mitochondrion
Note: Interaction between glycoprotein N and glycoprotein C is essential for proper targeting of glycoprotein N to the host Golgi complex, where virion budding occurs.

Glycoprotein C

Virion membrane
; Single-pass type I membrane protein
Host cell surface
Host Golgi apparatus membrane
; Single-pass type I membrane protein
Host endoplasmic reticulum membrane
; Single-pass type I membrane protein
Note: Budding probably takes place at the host Golgi (Probable). Glycoprotein C cytoplasmic tail is important for efficient Golgi localization (By similarity).

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain19-485Lumenal
Transmembrane486-506Helical
Topological domain507-627Cytoplasmic
Transmembrane628-648Helical
Topological domain649-1105Lumenal
Transmembrane1106-1126Helical
Topological domain1127-1135Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000003681319-648Glycoprotein N
ChainPRO_000003681219-1135Envelopment polyprotein
Disulfide bond29↔151
Disulfide bond63↔157
Disulfide bond109↔128
Disulfide bond133↔138
Glycosylation134N-linked (GlcNAc...) asparagine; by host
Disulfide bond175↔185
Disulfide bond210↔247
Disulfide bond234↔351
Glycosylation235N-linked (GlcNAc...) asparagine; by host
Glycosylation347N-linked (GlcNAc...) asparagine; by host
Disulfide bond376↔435
Disulfide bond380↔389
Glycosylation399N-linked (GlcNAc...) asparagine; by host
Disulfide bond405↔424
Disulfide bond452↔475
ChainPRO_0000036814649-1135Glycoprotein C
Disulfide bond735↔770
Disulfide bond739↔777
Disulfide bond751↔885
Disulfide bond765↔896
Disulfide bond780↔904
Disulfide bond806↔815
Disulfide bond823↔832
Disulfide bond863↔867
Glycosylation928N-linked (GlcNAc...) asparagine; by host
Disulfide bond970↔1000
Disulfide bond993↔1045
Disulfide bond1010↔1015
Disulfide bond1046↔1051
Disulfide bond1085↔1089

Post-translational modification

Envelopment polyprotein

Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase.

Keywords

PTM databases

Interaction

Subunit

Glycoprotein N

Homodimer (By similarity).
Homotetramer; forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By similarity).
Interacts (via C-terminus) with the nucleoprotein (By similarity).
Interacts with host TUFM; this interaction contributes to the virus-induced degradation of mitochondria by autophagy, which leads to degradation of host MAVS and inhibition of type I interferon (IFN) responses (By similarity).
Interacts with host MAP1LC3B; this interaction contributes to the virus-induced degradation of mitochondria by autophagy, which leads to degradation of host MAVS and inhibition of type I interferon (IFN) responses (By similarity).

Glycoprotein C

Homodimer. Homotetramer; forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation. Homotrimer; forms homotrimer in the post-fusion conformation at acidic pH (By similarity).
Interacts (via C-terminus) with the nucleoprotein (By similarity).

Structure

3D structure databases

Family & Domains

Features

Showing features for region, zinc finger, domain, motif.

TypeIDPosition(s)Description
Region516-533Binding to the ribonucleoprotein
Zinc finger545-565CCHC-type 1
Zinc finger570-591CCHC-type 2
Region588-605Binding to the ribonucleoprotein
Region592-603Binding to the ribonucleoprotein
Region611-625Binding to the ribonucleoprotein
Domain611-634ITAM
Motif615-618YxxL
Region757-777Fusion loop
Region1122-1135Binding to the ribonucleoprotein

Domain

Glycoprotein N

The YxxL motif at the C-terminus is indispensable for the interaction with MAP1LC3B and for the Gn-mediated induction of mitochondrial autophagy (By similarity).
The cytoplasmic tail is involved in the inhibition of the host innate immune response (By similarity).
The C-terminus of the cytoplasmic tail is involved in binding to the viral genome and the nucleocapsid (By similarity).
Contains 2 contiguous zinc-fingers (By similarity).

Glycoprotein C

The C-terminus is necessary for proper localization in the Golgi (By similarity).
The cytoplasmic tail is involved in binding to the nucleocapsid (By similarity).

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,135
  • Mass (Da)
    126,470
  • Last updated
    1990-08-01 v1
  • Checksum
    B9C759ED6592265A
MGIWKWLVMASLVWPVLTLRNVYDMKIECPHTVSFGENSVIGYVELPPMPLADTAQLVPESSCSMDNHQSLNTITKYTQVSWRGKADQSQSSQTSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHACNMMKSCLIALGPYRVQVVYERTYCMTGVLIEGKCFVPDQSVVSIIKHGIFDIASVHIVCFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEETATYSIVGPANAKVPHSASSDTLSLIAFSGIPSDSSLSILTSSTEAKHVFSPGLFPKLNHTNCDKGAIPLMWTGMIDLPGYYEAIHPCTVFCVLSGPGASCEAFSEGGIFNITYPMCLVSKQNRFRLTEQQVNFVCQRVDVDIVVYCNGQRKVILTKTLVIGQCIYTITSLFSLLPGVAHSIAVELCVPGFHGWATAALLVTFCFGWVLIPAITFIILTILKFIANIFHTSNQENRLKSVLRKIKEEFEKTKGSMVCDVCKYECETYKELKAHGVSCPQSQCPYCFTHCEPTEAAFQAHYKVCQVTHRFRDDLKKTVTPQNFTPGCYRTLNLFRYKSRCYIFTMWIFLLVLESILWAASASETPLTPVWNDNAHGVGSVPMHTDLELDFSLTSSSKYTYRRKLTNPLEEAQSIDLHIEIEEQTIGVDVHALGHWFDGRLNLKTSFHCYGACTKYEYPWHTAKCHYERDYQYETSWGCNPSDCPGVGTGCTACGLYLDRLKPVGSAYKIITIRYSRRVCVQFGEENLCKIIDMNDCFVSRHVKVCIIGTVSKFSQGDTLLFFGPLEGGGLIFKHWCTSTCQFGDPGDIMSPRDKGFLCPEFPGSFRKKCNFATTPICEYDGNMVSGYKKVMATIDSFQSFNTSTMHFTDERIEWKDPDGMLRDHINILVTKDIDFDNLGENPCKIGLQTSSIEGAWGSGVGFTLTCLVSLTECPTFLTSIKACDKAICYGAESVTLTRGQNTVKVSGKGGHSGSTFKCCHGEDCSQIGLHAAAPHLDKVNGISEMENSKEYDDGAPQCGIKCWFVKSGEWISGIFSGNWIVLIVLCVFLLFSLVLLSILCPVRKHKKS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D00377
EMBL· GenBank· DDBJ
BAA00280.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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