P16853 · GP_HANTL
- ProteinEnvelopment polyprotein
- GeneGP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1135 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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).
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 648-649 | Cleavage; by host signal peptidase | ||||
Sequence: AS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum membrane | |
Cellular Component | host cell Golgi membrane | |
Cellular Component | host cell mitochondrion | |
Cellular Component | host cell surface | |
Cellular Component | membrane | |
Cellular Component | viral envelope | |
Cellular Component | virion membrane | |
Molecular Function | metal ion binding | |
Biological Process | endocytosis involved in viral entry into host cell | |
Biological Process | fusion of virus membrane with host endosome membrane | |
Biological Process | signal transduction | |
Biological Process | symbiont-mediated suppression of host innate immune response | |
Biological Process | symbiont-mediated suppression of host TRAF-mediated signal transduction | |
Biological Process | virion attachment to host cell | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Biological process
- Ligand
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 > Hantaviridae > Mammantavirinae > Orthohantavirus > Orthohantavirus hantanense
- Virus hosts
Accessions
- Primary accessionP16853
Subcellular Location
UniProt Annotation
GO Annotation
Glycoprotein N
Virion membrane ; Multi-pass membrane protein
Host Golgi apparatus membrane ; Multi-pass membrane protein
Host endoplasmic reticulum membrane ; Multi-pass membrane protein
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 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-485 | Lumenal | ||||
Sequence: LRNVYDMKIECPHTVSFGENSVIGYVELPPMPLADTAQLVPESSCSMDNHQSLNTITKYTQVSWRGKADQSQSSQTSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHACNMMKSCLIALGPYRVQVVYERTYCMTGVLIEGKCFVPDQSVVSIIKHGIFDIASVHIVCFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEETATYSIVGPANAKVPHSASSDTLSLIAFSGIPSDSSLSILTSSTEAKHVFSPGLFPKLNHTNCDKGAIPLMWTGMIDLPGYYEAIHPCTVFCVLSGPGASCEAFSEGGIFNITYPMCLVSKQNRFRLTEQQVNFVCQRVDVDIVVYCNGQRKVILTKTLVIGQCIYTITSLFSLLPGVAHSIAVELCVPGFHGWATA | ||||||
Transmembrane | 486-506 | Helical | ||||
Sequence: ALLVTFCFGWVLIPAITFIIL | ||||||
Topological domain | 507-627 | Cytoplasmic | ||||
Sequence: TILKFIANIFHTSNQENRLKSVLRKIKEEFEKTKGSMVCDVCKYECETYKELKAHGVSCPQSQCPYCFTHCEPTEAAFQAHYKVCQVTHRFRDDLKKTVTPQNFTPGCYRTLNLFRYKSRC | ||||||
Transmembrane | 628-648 | Helical | ||||
Sequence: YIFTMWIFLLVLESILWAASA | ||||||
Topological domain | 649-1105 | Lumenal | ||||
Sequence: SETPLTPVWNDNAHGVGSVPMHTDLELDFSLTSSSKYTYRRKLTNPLEEAQSIDLHIEIEEQTIGVDVHALGHWFDGRLNLKTSFHCYGACTKYEYPWHTAKCHYERDYQYETSWGCNPSDCPGVGTGCTACGLYLDRLKPVGSAYKIITIRYSRRVCVQFGEENLCKIIDMNDCFVSRHVKVCIIGTVSKFSQGDTLLFFGPLEGGGLIFKHWCTSTCQFGDPGDIMSPRDKGFLCPEFPGSFRKKCNFATTPICEYDGNMVSGYKKVMATIDSFQSFNTSTMHFTDERIEWKDPDGMLRDHINILVTKDIDFDNLGENPCKIGLQTSSIEGAWGSGVGFTLTCLVSLTECPTFLTSIKACDKAICYGAESVTLTRGQNTVKVSGKGGHSGSTFKCCHGEDCSQIGLHAAAPHLDKVNGISEMENSKEYDDGAPQCGIKCWFVKSGEWISGIFSGN | ||||||
Transmembrane | 1106-1126 | Helical | ||||
Sequence: WIVLIVLCVFLLFSLVLLSIL | ||||||
Topological domain | 1127-1135 | Cytoplasmic | ||||
Sequence: CPVRKHKKS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MGIWKWLVMASLVWPVLT | ||||||
Chain | PRO_0000036813 | 19-648 | Glycoprotein N | |||
Sequence: LRNVYDMKIECPHTVSFGENSVIGYVELPPMPLADTAQLVPESSCSMDNHQSLNTITKYTQVSWRGKADQSQSSQTSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHACNMMKSCLIALGPYRVQVVYERTYCMTGVLIEGKCFVPDQSVVSIIKHGIFDIASVHIVCFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEETATYSIVGPANAKVPHSASSDTLSLIAFSGIPSDSSLSILTSSTEAKHVFSPGLFPKLNHTNCDKGAIPLMWTGMIDLPGYYEAIHPCTVFCVLSGPGASCEAFSEGGIFNITYPMCLVSKQNRFRLTEQQVNFVCQRVDVDIVVYCNGQRKVILTKTLVIGQCIYTITSLFSLLPGVAHSIAVELCVPGFHGWATAALLVTFCFGWVLIPAITFIILTILKFIANIFHTSNQENRLKSVLRKIKEEFEKTKGSMVCDVCKYECETYKELKAHGVSCPQSQCPYCFTHCEPTEAAFQAHYKVCQVTHRFRDDLKKTVTPQNFTPGCYRTLNLFRYKSRCYIFTMWIFLLVLESILWAASA | ||||||
Chain | PRO_0000036812 | 19-1135 | Envelopment polyprotein | |||
Sequence: LRNVYDMKIECPHTVSFGENSVIGYVELPPMPLADTAQLVPESSCSMDNHQSLNTITKYTQVSWRGKADQSQSSQTSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHACNMMKSCLIALGPYRVQVVYERTYCMTGVLIEGKCFVPDQSVVSIIKHGIFDIASVHIVCFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEETATYSIVGPANAKVPHSASSDTLSLIAFSGIPSDSSLSILTSSTEAKHVFSPGLFPKLNHTNCDKGAIPLMWTGMIDLPGYYEAIHPCTVFCVLSGPGASCEAFSEGGIFNITYPMCLVSKQNRFRLTEQQVNFVCQRVDVDIVVYCNGQRKVILTKTLVIGQCIYTITSLFSLLPGVAHSIAVELCVPGFHGWATAALLVTFCFGWVLIPAITFIILTILKFIANIFHTSNQENRLKSVLRKIKEEFEKTKGSMVCDVCKYECETYKELKAHGVSCPQSQCPYCFTHCEPTEAAFQAHYKVCQVTHRFRDDLKKTVTPQNFTPGCYRTLNLFRYKSRCYIFTMWIFLLVLESILWAASASETPLTPVWNDNAHGVGSVPMHTDLELDFSLTSSSKYTYRRKLTNPLEEAQSIDLHIEIEEQTIGVDVHALGHWFDGRLNLKTSFHCYGACTKYEYPWHTAKCHYERDYQYETSWGCNPSDCPGVGTGCTACGLYLDRLKPVGSAYKIITIRYSRRVCVQFGEENLCKIIDMNDCFVSRHVKVCIIGTVSKFSQGDTLLFFGPLEGGGLIFKHWCTSTCQFGDPGDIMSPRDKGFLCPEFPGSFRKKCNFATTPICEYDGNMVSGYKKVMATIDSFQSFNTSTMHFTDERIEWKDPDGMLRDHINILVTKDIDFDNLGENPCKIGLQTSSIEGAWGSGVGFTLTCLVSLTECPTFLTSIKACDKAICYGAESVTLTRGQNTVKVSGKGGHSGSTFKCCHGEDCSQIGLHAAAPHLDKVNGISEMENSKEYDDGAPQCGIKCWFVKSGEWISGIFSGNWIVLIVLCVFLLFSLVLLSILCPVRKHKKS | ||||||
Disulfide bond | 29↔151 | |||||
Sequence: CPHTVSFGENSVIGYVELPPMPLADTAQLVPESSCSMDNHQSLNTITKYTQVSWRGKADQSQSSQTSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHAC | ||||||
Disulfide bond | 63↔157 | |||||
Sequence: CSMDNHQSLNTITKYTQVSWRGKADQSQSSQTSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHACNMMKSC | ||||||
Disulfide bond | 109↔128 | |||||
Sequence: CVLKHKMVEESYRSRKSITC | ||||||
Disulfide bond | 133↔138 | |||||
Sequence: CNSTYC | ||||||
Glycosylation | 134 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 175↔185 | |||||
Sequence: CMTGVLIEGKC | ||||||
Disulfide bond | 210↔247 | |||||
Sequence: CFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYIC | ||||||
Disulfide bond | 234↔351 | |||||
Sequence: CNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEETATYSIVGPANAKVPHSASSDTLSLIAFSGIPSDSSLSILTSSTEAKHVFSPGLFPKLNHTNC | ||||||
Glycosylation | 235 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 347 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 376↔435 | |||||
Sequence: CTVFCVLSGPGASCEAFSEGGIFNITYPMCLVSKQNRFRLTEQQVNFVCQRVDVDIVVYC | ||||||
Disulfide bond | 380↔389 | |||||
Sequence: CVLSGPGASC | ||||||
Glycosylation | 399 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 405↔424 | |||||
Sequence: CLVSKQNRFRLTEQQVNFVC | ||||||
Disulfide bond | 452↔475 | |||||
Sequence: CIYTITSLFSLLPGVAHSIAVELC | ||||||
Chain | PRO_0000036814 | 649-1135 | Glycoprotein C | |||
Sequence: SETPLTPVWNDNAHGVGSVPMHTDLELDFSLTSSSKYTYRRKLTNPLEEAQSIDLHIEIEEQTIGVDVHALGHWFDGRLNLKTSFHCYGACTKYEYPWHTAKCHYERDYQYETSWGCNPSDCPGVGTGCTACGLYLDRLKPVGSAYKIITIRYSRRVCVQFGEENLCKIIDMNDCFVSRHVKVCIIGTVSKFSQGDTLLFFGPLEGGGLIFKHWCTSTCQFGDPGDIMSPRDKGFLCPEFPGSFRKKCNFATTPICEYDGNMVSGYKKVMATIDSFQSFNTSTMHFTDERIEWKDPDGMLRDHINILVTKDIDFDNLGENPCKIGLQTSSIEGAWGSGVGFTLTCLVSLTECPTFLTSIKACDKAICYGAESVTLTRGQNTVKVSGKGGHSGSTFKCCHGEDCSQIGLHAAAPHLDKVNGISEMENSKEYDDGAPQCGIKCWFVKSGEWISGIFSGNWIVLIVLCVFLLFSLVLLSILCPVRKHKKS | ||||||
Disulfide bond | 735↔770 | |||||
Sequence: CYGACTKYEYPWHTAKCHYERDYQYETSWGCNPSDC | ||||||
Disulfide bond | 739↔777 | |||||
Sequence: CTKYEYPWHTAKCHYERDYQYETSWGCNPSDCPGVGTGC | ||||||
Disulfide bond | 751↔885 | |||||
Sequence: CHYERDYQYETSWGCNPSDCPGVGTGCTACGLYLDRLKPVGSAYKIITIRYSRRVCVQFGEENLCKIIDMNDCFVSRHVKVCIIGTVSKFSQGDTLLFFGPLEGGGLIFKHWCTSTCQFGDPGDIMSPRDKGFLC | ||||||
Disulfide bond | 765↔896 | |||||
Sequence: CNPSDCPGVGTGCTACGLYLDRLKPVGSAYKIITIRYSRRVCVQFGEENLCKIIDMNDCFVSRHVKVCIIGTVSKFSQGDTLLFFGPLEGGGLIFKHWCTSTCQFGDPGDIMSPRDKGFLCPEFPGSFRKKC | ||||||
Disulfide bond | 780↔904 | |||||
Sequence: CGLYLDRLKPVGSAYKIITIRYSRRVCVQFGEENLCKIIDMNDCFVSRHVKVCIIGTVSKFSQGDTLLFFGPLEGGGLIFKHWCTSTCQFGDPGDIMSPRDKGFLCPEFPGSFRKKCNFATTPIC | ||||||
Disulfide bond | 806↔815 | |||||
Sequence: CVQFGEENLC | ||||||
Disulfide bond | 823↔832 | |||||
Sequence: CFVSRHVKVC | ||||||
Disulfide bond | 863↔867 | |||||
Sequence: CTSTC | ||||||
Glycosylation | 928 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 970↔1000 | |||||
Sequence: CKIGLQTSSIEGAWGSGVGFTLTCLVSLTEC | ||||||
Disulfide bond | 993↔1045 | |||||
Sequence: CLVSLTECPTFLTSIKACDKAICYGAESVTLTRGQNTVKVSGKGGHSGSTFKC | ||||||
Disulfide bond | 1010↔1015 | |||||
Sequence: CDKAIC | ||||||
Disulfide bond | 1046↔1051 | |||||
Sequence: CHGEDC | ||||||
Disulfide bond | 1085↔1089 | |||||
Sequence: CGIKC |
Post-translational modification
Envelopment polyprotein
Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase.
Keywords
- PTM
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).
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).
Interacts (via C-terminus) with the nucleoprotein (By similarity).
Family & Domains
Features
Showing features for region, zinc finger, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 516-533 | Binding to the ribonucleoprotein | ||||
Sequence: FHTSNQENRLKSVLRKIK | ||||||
Zinc finger | 545-565 | CCHC-type 1 | ||||
Sequence: CDVCKYECETYKELKAHGVSC | ||||||
Zinc finger | 570-591 | CCHC-type 2 | ||||
Sequence: CPYCFTHCEPTEAAFQAHYKVC | ||||||
Region | 588-605 | Binding to the ribonucleoprotein | ||||
Sequence: YKVCQVTHRFRDDLKKTV | ||||||
Region | 592-603 | Binding to the ribonucleoprotein | ||||
Sequence: QVTHRFRDDLKK | ||||||
Region | 611-625 | Binding to the ribonucleoprotein | ||||
Sequence: TPGCYRTLNLFRYKS | ||||||
Domain | 611-634 | ITAM | ||||
Sequence: TPGCYRTLNLFRYKSRCYIFTMWI | ||||||
Motif | 615-618 | YxxL | ||||
Sequence: YRTL | ||||||
Region | 757-777 | Fusion loop | ||||
Sequence: YQYETSWGCNPSDCPGVGTGC | ||||||
Region | 1122-1135 | Binding to the ribonucleoprotein | ||||
Sequence: LLSILCPVRKHKKS |
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).
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).
The cytoplasmic tail is involved in binding to the nucleocapsid (By similarity).
Sequence similarities
Belongs to the hantavirus envelope glycoprotein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,135
- Mass (Da)126,470
- Last updated1990-08-01 v1
- ChecksumB9C759ED6592265A