A0A0B5A886 · GP_SFTSV

Function

function

Glycoprotein N

Structural component of the virion that interacts with glycoprotein C (By similarity).
It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity).
The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity).
They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity).
Plays a role in the packaging of ribonucleoproteins and polymerase during virus assembly (PubMed:29467349).

Glycoprotein C

Structural component of the virion that interacts with glycoprotein N (By similarity).
Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity).
The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity).
They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity).

Features

Showing features for site.

TypeIDPosition(s)Description
Site562-563Cleavage; by host signal peptidase
Site1071Important for glycoprotein C and glycoprotein N subcellular location

GO annotations

AspectTerm
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell Golgi membrane
Cellular Componentmembrane
Cellular Componentvirion membrane
Biological Processentry receptor-mediated virion attachment to host cell
Biological Processfusion of virus membrane with host endosome membrane
Biological Processsymbiont entry into host cell

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
    A0A0B5A886
  • Secondary accessions
    • F1BA47

Proteomes

Subcellular Location

Glycoprotein N

Virion membrane
; Single-pass type I membrane protein
Host Golgi apparatus membrane
; Single-pass type I membrane protein
Host endoplasmic reticulum membrane
; Single-pass type I membrane protein
Note: Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs.

Glycoprotein C

Virion membrane
; Single-pass type I membrane protein
Host Golgi apparatus membrane
; Single-pass type I membrane protein
Host endoplasmic reticulum membrane
; Single-pass type I membrane protein
Note: Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain20-453Lumenal
Transmembrane454-474Helical
Topological domain475-535Cytoplasmic
Topological domain563-1036Lumenal
Transmembrane1037-1057Helical
Topological domain1058-1073Cytoplasmic

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000045555520-562Glycoprotein N
ChainPRO_000045555420-1073Envelopment polyprotein
Disulfide bond26↔49
Glycosylation33N-linked (GlcNAc...) asparagine; by host
Glycosylation63N-linked (GlcNAc...) asparagine; by host
Disulfide bond143↔156
Disulfide bond180↔327
Disulfide bond206↔216
Disulfide bond258↔305
Disulfide bond287↔292
Disulfide bond349↔352
Disulfide bond356↔424
Disulfide bond376↔381
Disulfide bond563↔604
ChainPRO_0000455556563-1073Glycoprotein C
Disulfide bond576↔586
Disulfide bond629↔725
Disulfide bond644↔841
Disulfide bond650↔698
Disulfide bond656↔705
Disulfide bond660↔687
Disulfide bond691↔696
Disulfide bond778↔793
Disulfide bond809↔823
Glycosylation853N-linked (GlcNAc...) asparagine; by host
Disulfide bond908↔978
Glycosylation914N-linked (GlcNAc...) asparagine; by host
Disulfide bond918↔921
Glycosylation936N-linked (GlcNAc...) asparagine; by host
Disulfide bond943↔974

Post-translational modification

Envelopment polyprotein

Specific enzymatic cleavages in vivo yield mature proteins including glycoprotein C and glycoprotein N.

Glycoprotein N

The cytoplasmic tail is Palmitoylated.

Glycoprotein N

Glycosylated.

Glycoprotein C

Palmitoylated.

Glycoprotein C

Glycosylated.

Keywords

PTM databases

Interaction

Subunit

Glycoprotein N

Homodimer. Heterodimer with glycoprotein C (By similarity).
Homotrimer (postfusion) (By similarity).

Glycoprotein C

Heterodimer with glycoprotein N.

Structure

3D structure databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region475-521Golgi retention signal
Region536-562Internal signal sequence for glycoprotein C
Region650-656Fusion loop
Region691-705Fusion loop

Domain

Glycoprotein N

Contains a Golgi retention signal on its C-terminus. The cytoplasmic tail specifically interacts with the ribonucleoproteins and is critical for genome packaging.

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,073
  • Mass (Da)
    116,636
  • Last updated
    2022-05-25 v2
  • Checksum
    612D80CA07722F4A
MMKVIWFSSLICLVIQCSGDSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKCYGFSRMMATLEVNPPEQRIGQCTGCHLECINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSCMFPDGCDAVDCTFCREFLKNPQCYPAKKWLFIIIVILLGYAGLMLLTNVLKAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEIGENGEGNQDDVRIEMARPRRVRHWMYSPVILTILAIGLAEGCDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEACLHFTAPGSPDSKCLKIKVKRINLKCKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVCYSKITSVEAVANYSAIPTTIGGLRFERSHDSQGKISGSPLDITAIRGSFSVNYRGLRLSLSEITATCTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNCGGHESQVTLKGNLIFLDVPKFVDGSYMQTYHSTVPTGANIPSPTDWLNALFGNGLSRWILGVIGVLLGGLALFFLIMFLLKLGTKQVFRSRTKLA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict321in Ref. 1; ADZ04471
Sequence conflict962in Ref. 1; ADZ04471

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HM745931
EMBL· GenBank· DDBJ
ADZ04471.1
EMBL· GenBank· DDBJ
Viral cRNA
KP202164
EMBL· GenBank· DDBJ
AJD86039.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

Disclaimer

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