P03517 · GP_PTPV
- ProteinEnvelopment polyprotein
- GeneGP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1313 (go to sequence)
- Protein existenceInferred from homology
- 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 endocytosis of the virion (PubMed:21767814).
Plays a role in the packaging of ribonucleoproteins and polymerase during virus assembly (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 endocytosis of the virion (PubMed:21767814).
Plays a role in the packaging of ribonucleoproteins and polymerase during virus assembly (By similarity).
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. 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 endocytosis of the virion (PubMed:21767814).
Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N. 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 endocytosis of the virion (PubMed:21767814).
NSm-Gn protein
Plays a role for virus dissemination in mosquitoes.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 271-272 | Cleavage; by host signal peptidase | ||||
Sequence: AP | ||||||
Site | 809-810 | Cleavage; by host signal peptidase | ||||
Sequence: AC | ||||||
Site | 1311 | 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 3 chains
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Ellioviricetes > Bunyavirales > Phenuiviridae > Phlebovirus > Phlebovirus toroense
- Virus hosts
Accessions
- Primary accessionP03517
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
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 | 18-712 | Lumenal | ||||
Sequence: MYSLTTWDSTSRNDMCFSNDSPLEGLVYYWETHSKRHDYKKQESQRCRVGDSDKKMITNVTIISLISEIQKSISELSLSCVNDDNSTGQVLTFNGLEDTIRGDYIVDCVTGLYQSDIGVGVGLGRTHHGHQQMKNKAVVIDEKERMISLLETQQSENDIKMQVLMSEIEQLKNQLSKKRNERGQEKRDAEKVMSDLMARNSDLRKHNDILTAEISQMKNKNTIQRNKNTVSTTVVPAILSVALLSSSVAPIIAAPPDSPMINPWPHAKNRVGTGMYKYDENDDSGCRPIRYGVSCIGFDFMLKMDKYPFFNAFIGHKTPLESFADKIIEKEEETCEIGTNKEFKCFEERAYIKGTCPTNINAVHYIDNKGKLRYVKCKENLEMTEDCAFCRKIKKKAGQSVQVQKTSVPLQDAICQENSDTYSGPKIPFKGVCKIGLIKYKECKFKTSSYETVSFITLKEKGKIYIEHLMLKNIEVVTNVSFVCYEHVGQDEQEVEHRALKRVSVNDCKIVDNSKQKICTGDHVFCEKYDCSTSYPDVTCIHAPGSGPLYINLMGSWIKPQCVGYERVLVDREVKQPLLAPEQNCDTCVSECLDEGVHIKSTGFEITSAVACSHGSCISAHQEPSTSVIVPYPGLLASVGGRIGIHLSHTSDSASVHMVVVCPPRDSCAAHNCLLCYHGILNYQCHSTLSAILTS | ||||||
Transmembrane | 713-733 | Helical | ||||
Sequence: FLLILFIYTVFSVTTNILYVL | ||||||
Topological domain | 734-791 | Cytoplasmic | ||||
Sequence: RLIPKQLKSPVGWLKLFINWLLTALRIKTRNVMRRINQRIGWVDHHDVERPRHREPMR | ||||||
Topological domain | 810-1278 | Lumenal | ||||
Sequence: CSNTVVANSKQTRCVQEGSNTKCSITATITLRAGVIGAESCFIIKGPMENQQKTISIKTISSETVCREGSSFWTSLYIPSCLSSRRCHLVGDCVGNKCQSWRDDQLSREFSGVKDNHIMNENKCFEQCGAIGCGCFNINPSCLYVHAYLKSARNEAVRVFSCSDWVHRVSFEVKGPDGETELVTLGSPGTKFLNWGTLSLSLDAEGISGTNSISFLESSKGGFALYDEGYNEIPREGFLGEIRCSSESAAISAHKSCIRAPGLIKYKPMTDQIECTASLVDPFAIFLKGSLPQTRNGQTFTSTKDKKTVQAFTNGAIKALLSINLDDHEIVFINKVKNCDATFLNVSGCYSCDYGAHVCVKVKSSESADFFAESEDKTTVLSFPIQSGTHDYCQVLHFQKPLVDERLSYSCGSEPKLIVIKGTLVCMGVYDFRNKTGGSSTVVNPSEGAWSISNWFSGLLDWLGGPMKA | ||||||
Transmembrane | 1279-1299 | Helical | ||||
Sequence: ILKILGFIAIGIVCFVLFMIL | ||||||
Topological domain | 1300-1313 | Cytoplasmic | ||||
Sequence: IRIAVNSINIKKKN |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MIFTILNVLTRAMLVMS | ||||||
Chain | PRO_0000036844 | 18-270 | NSm-Gn protein | |||
Sequence: MYSLTTWDSTSRNDMCFSNDSPLEGLVYYWETHSKRHDYKKQESQRCRVGDSDKKMITNVTIISLISEIQKSISELSLSCVNDDNSTGQVLTFNGLEDTIRGDYIVDCVTGLYQSDIGVGVGLGRTHHGHQQMKNKAVVIDEKERMISLLETQQSENDIKMQVLMSEIEQLKNQLSKKRNERGQEKRDAEKVMSDLMARNSDLRKHNDILTAEISQMKNKNTIQRNKNTVSTTVVPAILSVALLSSSVAPIIA | ||||||
Chain | PRO_0000247008 | 18-1313 | Envelopment polyprotein | |||
Sequence: MYSLTTWDSTSRNDMCFSNDSPLEGLVYYWETHSKRHDYKKQESQRCRVGDSDKKMITNVTIISLISEIQKSISELSLSCVNDDNSTGQVLTFNGLEDTIRGDYIVDCVTGLYQSDIGVGVGLGRTHHGHQQMKNKAVVIDEKERMISLLETQQSENDIKMQVLMSEIEQLKNQLSKKRNERGQEKRDAEKVMSDLMARNSDLRKHNDILTAEISQMKNKNTIQRNKNTVSTTVVPAILSVALLSSSVAPIIAAPPDSPMINPWPHAKNRVGTGMYKYDENDDSGCRPIRYGVSCIGFDFMLKMDKYPFFNAFIGHKTPLESFADKIIEKEEETCEIGTNKEFKCFEERAYIKGTCPTNINAVHYIDNKGKLRYVKCKENLEMTEDCAFCRKIKKKAGQSVQVQKTSVPLQDAICQENSDTYSGPKIPFKGVCKIGLIKYKECKFKTSSYETVSFITLKEKGKIYIEHLMLKNIEVVTNVSFVCYEHVGQDEQEVEHRALKRVSVNDCKIVDNSKQKICTGDHVFCEKYDCSTSYPDVTCIHAPGSGPLYINLMGSWIKPQCVGYERVLVDREVKQPLLAPEQNCDTCVSECLDEGVHIKSTGFEITSAVACSHGSCISAHQEPSTSVIVPYPGLLASVGGRIGIHLSHTSDSASVHMVVVCPPRDSCAAHNCLLCYHGILNYQCHSTLSAILTSFLLILFIYTVFSVTTNILYVLRLIPKQLKSPVGWLKLFINWLLTALRIKTRNVMRRINQRIGWVDHHDVERPRHREPMRRFKTTLLLTLIMMTGGNACSNTVVANSKQTRCVQEGSNTKCSITATITLRAGVIGAESCFIIKGPMENQQKTISIKTISSETVCREGSSFWTSLYIPSCLSSRRCHLVGDCVGNKCQSWRDDQLSREFSGVKDNHIMNENKCFEQCGAIGCGCFNINPSCLYVHAYLKSARNEAVRVFSCSDWVHRVSFEVKGPDGETELVTLGSPGTKFLNWGTLSLSLDAEGISGTNSISFLESSKGGFALYDEGYNEIPREGFLGEIRCSSESAAISAHKSCIRAPGLIKYKPMTDQIECTASLVDPFAIFLKGSLPQTRNGQTFTSTKDKKTVQAFTNGAIKALLSINLDDHEIVFINKVKNCDATFLNVSGCYSCDYGAHVCVKVKSSESADFFAESEDKTTVLSFPIQSGTHDYCQVLHFQKPLVDERLSYSCGSEPKLIVIKGTLVCMGVYDFRNKTGGSSTVVNPSEGAWSISNWFSGLLDWLGGPMKAILKILGFIAIGIVCFVLFMILIRIAVNSINIKKKN | ||||||
Glycosylation | 76 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 102 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000036845 | 271-809 | Glycoprotein N | |||
Sequence: APPDSPMINPWPHAKNRVGTGMYKYDENDDSGCRPIRYGVSCIGFDFMLKMDKYPFFNAFIGHKTPLESFADKIIEKEEETCEIGTNKEFKCFEERAYIKGTCPTNINAVHYIDNKGKLRYVKCKENLEMTEDCAFCRKIKKKAGQSVQVQKTSVPLQDAICQENSDTYSGPKIPFKGVCKIGLIKYKECKFKTSSYETVSFITLKEKGKIYIEHLMLKNIEVVTNVSFVCYEHVGQDEQEVEHRALKRVSVNDCKIVDNSKQKICTGDHVFCEKYDCSTSYPDVTCIHAPGSGPLYINLMGSWIKPQCVGYERVLVDREVKQPLLAPEQNCDTCVSECLDEGVHIKSTGFEITSAVACSHGSCISAHQEPSTSVIVPYPGLLASVGGRIGIHLSHTSDSASVHMVVVCPPRDSCAAHNCLLCYHGILNYQCHSTLSAILTSFLLILFIYTVFSVTTNILYVLRLIPKQLKSPVGWLKLFINWLLTALRIKTRNVMRRINQRIGWVDHHDVERPRHREPMRRFKTTLLLTLIMMTGGNA | ||||||
Disulfide bond | 303↔312 | |||||
Sequence: CRPIRYGVSC | ||||||
Disulfide bond | 352↔362 | |||||
Sequence: CEIGTNKEFKC | ||||||
Disulfide bond | 373↔404 | |||||
Sequence: CPTNINAVHYIDNKGKLRYVKCKENLEMTEDC | ||||||
Disulfide bond | 394↔407 | |||||
Sequence: CKENLEMTEDCAFC | ||||||
Disulfide bond | 432↔579 | |||||
Sequence: CQENSDTYSGPKIPFKGVCKIGLIKYKECKFKTSSYETVSFITLKEKGKIYIEHLMLKNIEVVTNVSFVCYEHVGQDEQEVEHRALKRVSVNDCKIVDNSKQKICTGDHVFCEKYDCSTSYPDVTCIHAPGSGPLYINLMGSWIKPQC | ||||||
Disulfide bond | 450↔460 | |||||
Sequence: CKIGLIKYKEC | ||||||
Glycosylation | 496 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 501↔557 | |||||
Sequence: CYEHVGQDEQEVEHRALKRVSVNDCKIVDNSKQKICTGDHVFCEKYDCSTSYPDVTC | ||||||
Disulfide bond | 525↔536 | |||||
Sequence: CKIVDNSKQKIC | ||||||
Disulfide bond | 543↔548 | |||||
Sequence: CEKYDC | ||||||
Disulfide bond | 602↔605 | |||||
Sequence: CDTC | ||||||
Disulfide bond | 609↔679 | |||||
Sequence: CLDEGVHIKSTGFEITSAVACSHGSCISAHQEPSTSVIVPYPGLLASVGGRIGIHLSHTSDSASVHMVVVC | ||||||
Disulfide bond | 629↔634 | |||||
Sequence: CSHGSC | ||||||
Disulfide bond | 810↔850 | |||||
Sequence: CSNTVVANSKQTRCVQEGSNTKCSITATITLRAGVIGAESC | ||||||
Chain | PRO_0000036846 | 810-1313 | Glycoprotein C | |||
Sequence: CSNTVVANSKQTRCVQEGSNTKCSITATITLRAGVIGAESCFIIKGPMENQQKTISIKTISSETVCREGSSFWTSLYIPSCLSSRRCHLVGDCVGNKCQSWRDDQLSREFSGVKDNHIMNENKCFEQCGAIGCGCFNINPSCLYVHAYLKSARNEAVRVFSCSDWVHRVSFEVKGPDGETELVTLGSPGTKFLNWGTLSLSLDAEGISGTNSISFLESSKGGFALYDEGYNEIPREGFLGEIRCSSESAAISAHKSCIRAPGLIKYKPMTDQIECTASLVDPFAIFLKGSLPQTRNGQTFTSTKDKKTVQAFTNGAIKALLSINLDDHEIVFINKVKNCDATFLNVSGCYSCDYGAHVCVKVKSSESADFFAESEDKTTVLSFPIQSGTHDYCQVLHFQKPLVDERLSYSCGSEPKLIVIKGTLVCMGVYDFRNKTGGSSTVVNPSEGAWSISNWFSGLLDWLGGPMKAILKILGFIAIGIVCFVLFMILIRIAVNSINIKKKN | ||||||
Disulfide bond | 823↔832 | |||||
Sequence: CVQEGSNTKC | ||||||
Disulfide bond | 875↔971 | |||||
Sequence: CREGSSFWTSLYIPSCLSSRRCHLVGDCVGNKCQSWRDDQLSREFSGVKDNHIMNENKCFEQCGAIGCGCFNINPSCLYVHAYLKSARNEAVRVFSC | ||||||
Disulfide bond | 890↔1084 | |||||
Sequence: CLSSRRCHLVGDCVGNKCQSWRDDQLSREFSGVKDNHIMNENKCFEQCGAIGCGCFNINPSCLYVHAYLKSARNEAVRVFSCSDWVHRVSFEVKGPDGETELVTLGSPGTKFLNWGTLSLSLDAEGISGTNSISFLESSKGGFALYDEGYNEIPREGFLGEIRCSSESAAISAHKSCIRAPGLIKYKPMTDQIEC | ||||||
Disulfide bond | 896↔944 | |||||
Sequence: CHLVGDCVGNKCQSWRDDQLSREFSGVKDNHIMNENKCFEQCGAIGCGC | ||||||
Disulfide bond | 902↔951 | |||||
Sequence: CVGNKCQSWRDDQLSREFSGVKDNHIMNENKCFEQCGAIGCGCFNINPSC | ||||||
Disulfide bond | 907↔933 | |||||
Sequence: CQSWRDDQLSREFSGVKDNHIMNENKC | ||||||
Disulfide bond | 937↔942 | |||||
Sequence: CGAIGC | ||||||
Disulfide bond | 1053↔1066 | |||||
Sequence: CSSESAAISAHKSC | ||||||
Disulfide bond | 1148↔1220 | |||||
Sequence: CDATFLNVSGCYSCDYGAHVCVKVKSSESADFFAESEDKTTVLSFPIQSGTHDYCQVLHFQKPLVDERLSYSC | ||||||
Glycosylation | 1154 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 1158↔1161 | |||||
Sequence: CYSC | ||||||
Disulfide bond | 1168↔1202 | |||||
Sequence: CVKVKSSESADFFAESEDKTTVLSFPIQSGTHDYC | ||||||
Glycosylation | 1243 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N |
Post-translational modification
Envelopment polyprotein
Specific enzymatic cleavages in vivo yield mature proteins including NSm protein, Glycoprotein C, and Glycoprotein N.
Glycoprotein N
Glycosylated. The glycans can attach to host CD209/DC-SIGN, and may play a role in virus entry into dendritic cells.
Glycoprotein C
Glycosylated. The glycans can attach to host CD209/DC-SIGN, and may play a role in virus entry into dendritic cells.
Glycoprotein C
Palmitoylated.
Keywords
- PTM
PTM databases
Interaction
Subunit
Glycoprotein N
Heterodimer with glycoprotein C (By similarity).
Interacts with nucleocapsid protein N and with the polymerase L in order to package them into virus particles (By similarity).
Interacts with nucleocapsid protein N and with the polymerase L in order to package them into virus particles (By similarity).
Glycoprotein C
Heterodimer with glycoprotein C. Homotrimer (postfusion) (By similarity).
Interacts with nucleocapsid protein N and with the polymerase L in order to package them into virus particles. Interacts with host E3 ubiquitin-protein ligase UBR4; this interaction is important for viral RNA production (By similarity).
Interacts with nucleocapsid protein N and with the polymerase L in order to package them into virus particles. Interacts with host E3 ubiquitin-protein ligase UBR4; this interaction is important for viral RNA production (By similarity).
Family & Domains
Features
Showing features for coiled coil, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 178-237 | |||||
Sequence: MQVLMSEIEQLKNQLSKKRNERGQEKRDAEKVMSDLMARNSDLRKHNDILTAEISQMKNK | ||||||
Region | 250-270 | Internal signal sequence for glycoprotein N | ||||
Sequence: TVVPAILSVALLSSSVAPIIA | ||||||
Region | 731-773 | Golgi retention signal | ||||
Sequence: YVLRLIPKQLKSPVGWLKLFINWLLTALRIKTRNVMRRINQRI | ||||||
Region | 769-773 | Important for correct targeting of the glycoproteins to the Golgi complex but not for heterodimerization | ||||
Sequence: INQRI | ||||||
Region | 793-809 | Internal signal sequence for glycoprotein C | ||||
Sequence: FKTTLLLTLIMMTGGNA | ||||||
Region | 896-902 | Fusion loop | ||||
Sequence: CHLVGDC | ||||||
Region | 938-949 | Fusion loop | ||||
Sequence: GAIGCGCFNINP |
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.
- Length1,313
- Mass (Da)146,375
- Last updated1986-07-21 v1
- Checksum72072F27735A74A2