A0A0B5A886 · GP_SFTSV
- ProteinEnvelopment polyprotein
- GeneGP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1073 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 562-563 | Cleavage; by host signal peptidase | ||||
Sequence: GC | ||||||
Site | 1071 | Important for glycoprotein C and glycoprotein N subcellular location | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum membrane | |
Cellular Component | host cell Golgi membrane | |
Cellular Component | membrane | |
Cellular Component | virion membrane | |
Biological Process | entry receptor-mediated virion attachment to host cell | |
Biological Process | fusion of virus membrane with host endosome membrane | |
Biological Process | symbiont entry into host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameEnvelopment polyprotein
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Ellioviricetes > Bunyavirales > Phenuiviridae > Bandavirus > Bandavirus dabieense
- Virus hosts
Accessions
- Primary accessionA0A0B5A886
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-453 | Lumenal | ||||
Sequence: DSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKCYGFSRMMATLEVNPPEQRIGQCTGCHLECINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSCMFPDGCDAVDCTFCREFLKNPQCYPAKKW | ||||||
Transmembrane | 454-474 | Helical | ||||
Sequence: LFIIIVILLGYAGLMLLTNVL | ||||||
Topological domain | 475-535 | Cytoplasmic | ||||
Sequence: KAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEIGENGEGNQDDVRIE | ||||||
Topological domain | 563-1036 | Lumenal | ||||
Sequence: CDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEACLHFTAPGSPDSKCLKIKVKRINLKCKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVCYSKITSVEAVANYSAIPTTIGGLRFERSHDSQGKISGSPLDITAIRGSFSVNYRGLRLSLSEITATCTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNCGGHESQVTLKGNLIFLDVPKFVDGSYMQTYHSTVPTGANIPSPTDWLNALFGNGLSRW | ||||||
Transmembrane | 1037-1057 | Helical | ||||
Sequence: ILGVIGVLLGGLALFFLIMFL | ||||||
Topological domain | 1058-1073 | Cytoplasmic | ||||
Sequence: LKLGTKQVFRSRTKLA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MMKVIWFSSLICLVIQCSG | ||||||
Chain | PRO_0000455555 | 20-562 | Glycoprotein N | |||
Sequence: DSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKCYGFSRMMATLEVNPPEQRIGQCTGCHLECINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSCMFPDGCDAVDCTFCREFLKNPQCYPAKKWLFIIIVILLGYAGLMLLTNVLKAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEIGENGEGNQDDVRIEMARPRRVRHWMYSPVILTILAIGLAEG | ||||||
Chain | PRO_0000455554 | 20-1073 | Envelopment polyprotein | |||
Sequence: DSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKCYGFSRMMATLEVNPPEQRIGQCTGCHLECINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSCMFPDGCDAVDCTFCREFLKNPQCYPAKKWLFIIIVILLGYAGLMLLTNVLKAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEIGENGEGNQDDVRIEMARPRRVRHWMYSPVILTILAIGLAEGCDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEACLHFTAPGSPDSKCLKIKVKRINLKCKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVCYSKITSVEAVANYSAIPTTIGGLRFERSHDSQGKISGSPLDITAIRGSFSVNYRGLRLSLSEITATCTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNCGGHESQVTLKGNLIFLDVPKFVDGSYMQTYHSTVPTGANIPSPTDWLNALFGNGLSRWILGVIGVLLGGLALFFLIMFLLKLGTKQVFRSRTKLA | ||||||
Disulfide bond | 26↔49 | |||||
Sequence: CAGPIHSNKSAGIPHLLGYSEKIC | ||||||
Glycosylation | 33 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 63 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 143↔156 | |||||
Sequence: CGSGKSRTESGELC | ||||||
Disulfide bond | 180↔327 | |||||
Sequence: CQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKC | ||||||
Disulfide bond | 206↔216 | |||||
Sequence: CKIDGIVFNQC | ||||||
Disulfide bond | 258↔305 | |||||
Sequence: CYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRC | ||||||
Disulfide bond | 287↔292 | |||||
Sequence: CKVAGC | ||||||
Disulfide bond | 349↔352 | |||||
Sequence: CTGC | ||||||
Disulfide bond | 356↔424 | |||||
Sequence: CINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSC | ||||||
Disulfide bond | 376↔381 | |||||
Sequence: CASHFC | ||||||
Disulfide bond | 563↔604 | |||||
Sequence: CDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEAC | ||||||
Chain | PRO_0000455556 | 563-1073 | Glycoprotein C | |||
Sequence: CDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEACLHFTAPGSPDSKCLKIKVKRINLKCKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVCYSKITSVEAVANYSAIPTTIGGLRFERSHDSQGKISGSPLDITAIRGSFSVNYRGLRLSLSEITATCTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNCGGHESQVTLKGNLIFLDVPKFVDGSYMQTYHSTVPTGANIPSPTDWLNALFGNGLSRWILGVIGVLLGGLALFFLIMFLLKLGTKQVFRSRTKLA | ||||||
Disulfide bond | 576↔586 | |||||
Sequence: CRQGSGNMKEC | ||||||
Disulfide bond | 629↔725 | |||||
Sequence: CKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPC | ||||||
Disulfide bond | 644↔841 | |||||
Sequence: CTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVC | ||||||
Disulfide bond | 650↔698 | |||||
Sequence: CRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGC | ||||||
Disulfide bond | 656↔705 | |||||
Sequence: CQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSC | ||||||
Disulfide bond | 660↔687 | |||||
Sequence: CPPHFTSNSFSDDWAGKMDRAGLGFSGC | ||||||
Disulfide bond | 691↔696 | |||||
Sequence: CGGAAC | ||||||
Disulfide bond | 778↔793 | |||||
Sequence: CEIEELKSKKLALAPC | ||||||
Disulfide bond | 809↔823 | |||||
Sequence: CSSEESARTIKKDGC | ||||||
Glycosylation | 853 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 908↔978 | |||||
Sequence: CTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNC | ||||||
Glycosylation | 914 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 918↔921 | |||||
Sequence: CYSC | ||||||
Glycosylation | 936 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 943↔974 | |||||
Sequence: CKGDETAFSVLEGVHSYIVSLSFDHAVVDEQC |
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
PTM databases
Interaction
Subunit
Glycoprotein N
Homodimer. Heterodimer with glycoprotein C (By similarity).
Homotrimer (postfusion) (By similarity).
Homotrimer (postfusion) (By similarity).
Glycoprotein C
Heterodimer with glycoprotein N.
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 475-521 | Golgi retention signal | ||||
Sequence: KAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEI | ||||||
Region | 536-562 | Internal signal sequence for glycoprotein C | ||||
Sequence: MARPRRVRHWMYSPVILTILAIGLAEG | ||||||
Region | 650-656 | Fusion loop | ||||
Sequence: CRWAGDC | ||||||
Region | 691-705 | Fusion loop | ||||
Sequence: CGGAACGCFNAAPSC |
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
Belongs to the phlebovirus envelope glycoprotein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,073
- Mass (Da)116,636
- Last updated2022-05-25 v2
- Checksum612D80CA07722F4A
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 321 | in Ref. 1; ADZ04471 | ||||
Sequence: M → T | ||||||
Sequence conflict | 962 | in Ref. 1; ADZ04471 | ||||
Sequence: S → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HM745931 EMBL· GenBank· DDBJ | ADZ04471.1 EMBL· GenBank· DDBJ | Viral cRNA | ||
KP202164 EMBL· GenBank· DDBJ | AJD86039.1 EMBL· GenBank· DDBJ | Genomic RNA |