GP_DOBV
ID GP_DOBV Reviewed; 1135 AA.
AC Q806Y7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=Glycoprotein precursor {ECO:0000250|UniProtKB:P08668};
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P08668};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P08668};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Dobrava-Belgrade orthohantavirus (DOBV) (Dobrava virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980467;
OH NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
OH NCBI_TaxID=54292; Apodemus flavicollis (Yellow-necked field mouse).
OH NCBI_TaxID=134909; Apodemus ponticus (Caucasus field mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=DOBV/Ano-Poroia/Afl9/1999 {ECO:0000312|Proteomes:UP000202548};
RX PubMed=12457975; DOI=10.1016/s0168-1702(02)00179-x;
RA Nemirov K., Hentonnen H., Vaheri A., Plyusnin A.;
RT "Phylogenetic evidence for host switching in the evolution of hantaviruses
RT carried by Apodemus mice.";
RL Virus Res. 90:207-215(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=DOBV/Ano-Poroia/Afl9/1999 {ECO:0000312|EMBL:CAC85164.1,
RC ECO:0000312|Proteomes:UP000202548};
RX PubMed=12526053; DOI=10.1002/jmv.10304;
RA Nemirov K., Vapalahti O., Papa A., Plyusnina A., Lundkvist A.,
RA Antoniadis A., Plyusnin A.;
RT "Genetic characterization of new Dobrava hantavirus isolate from Greece.";
RL J. Med. Virol. 69:408-416(2003).
RN [3]
RP REVIEW.
RX PubMed=24755564; DOI=10.3390/v6041801;
RA Cifuentes-Munoz N., Salazar-Quiroz N., Tischler N.D.;
RT "Hantavirus Gn and Gc envelope glycoproteins: key structural units for
RT virus cell entry and virus assembly.";
RL Viruses 6:1801-1822(2014).
CC -!- FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at
CC the surface of the virion (By similarity). Attaches the virion to host
CC cell receptors including integrin ITGAV/ITGB3 (By similarity). This
CC attachment induces virion internalization predominantly through
CC clathrin-dependent endocytosis (By similarity). Mediates the assembly
CC and budding of infectious virus particles through its interaction with
CC the nucleocapsid protein and the viral genome (By similarity). May
CC dysregulate normal immune and endothelial cell responses through an
CC ITAM motif (By similarity). Translocates to mitochondria, binds to host
CC TUFM and recruits MAP1LC3B (By similarity). These interactions induce
CC mitochondrial autophagy and therefore destruction of host MAVS leading
CC to inhibition of type I interferon (IFN) responses (By similarity).
CC Concomitant breakdown of glycoprotein N is apparently prevented by the
CC nucleoprotein that may inhibit Gn-stimulated autophagosome-lysosome
CC fusion (By similarity). Interacts with the viral genomic RNA (By
CC similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312}.
CC -!- FUNCTION: [Glycoprotein C]: Forms homotetramers with glycoprotein N at
CC the surface of the virion. Attaches the virion to host cell receptors
CC including integrin ITGAV/ITGB3. This attachment induces virion
CC internalization predominantly through clathrin-dependent endocytosis.
CC Class II fusion protein that promotes fusion of viral membrane with
CC host endosomal membrane after endocytosis of the virion.
CC {ECO:0000250|UniProtKB:P08668}.
CC -!- SUBUNIT: [Glycoprotein N]: Homodimer (By similarity). Homotetramer;
CC forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By
CC similarity). Interacts (via C-terminus) with the nucleoprotein (By
CC similarity). Interacts with host TUFM; this interaction contributes to
CC the virus-induced degradation of mitochondria by autophagy, which leads
CC to degradation of host MAVS and inhibition of type I interferon (IFN)
CC responses (By similarity). Interacts with host MAP1LC3B; this
CC interaction contributes to the virus-induced degradation of
CC mitochondria by autophagy, which leads to degradation of host MAVS and
CC inhibition of type I interferon (IFN) responses (By similarity).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1}.
CC -!- SUBUNIT: [Glycoprotein C]: Homodimer. Homotetramer; forms
CC heterotetrameric Gn-Gc spikes in the pre-fusion conformation.
CC Homotrimer; forms homotrimer in the post-fusion conformation at acidic
CC pH (By similarity). Interacts (via C-terminus) with the nucleoprotein
CC (By similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein. Host cell
CC surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P08668}. Host mitochondrion
CC {ECO:0000250|UniProtKB:P08668}. Note=Interaction between glycoprotein N
CC and glycoprotein C is essential for proper targeting of glycoprotein N
CC to the host Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P27312}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane protein
CC {ECO:0000305}. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P08668}. Host
CC endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08668}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P08668}.
CC Note=Budding probably takes place at the host Golgi (Probable).
CC Glycoprotein C cytoplasmic tail is important for efficient Golgi
CC localization (By similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000305}.
CC -!- DOMAIN: [Glycoprotein N]: The YxxL motif at the C-terminus is
CC indispensable for the interaction with MAP1LC3B and for the Gn-mediated
CC induction of mitochondrial autophagy (By similarity). The cytoplasmic
CC tail is involved in the inhibition of the host innate immune response
CC (By similarity). The C-terminus of the cytoplasmic tail is involved in
CC binding to the viral genome and the nucleocapsid (By similarity).
CC Contains 2 contiguous zinc-fingers (By similarity).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1,
CC ECO:0000250|UniProtKB:P27312, ECO:0000250|UniProtKB:Q9E006}.
CC -!- DOMAIN: [Glycoprotein C]: The C-terminus is necessary for proper
CC localization in the Golgi (By similarity). The cytoplasmic tail is
CC involved in binding to the nucleocapsid (By similarity).
CC {ECO:0000250|UniProtKB:P27312}.
CC -!- PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is
CC quickly cleaved in vivo just after synthesis, presumably by host signal
CC peptidase. {ECO:0000250|UniProtKB:P08668}.
CC -!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AJ410616; CAC85164.1; -; Genomic_RNA.
DR RefSeq; NP_942554.1; NC_005234.1.
DR GeneID; 2656264; -.
DR KEGG; vg:2656264; -.
DR Proteomes; UP000202548; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR016402; Envelope_glycoprot_Hantavirus.
DR InterPro; IPR002532; Hanta_Gc.
DR InterPro; IPR002534; Hanta_Gn.
DR InterPro; IPR012316; ITAM_motif_hantavir-typ.
DR Pfam; PF01567; Hanta_G1; 1.
DR Pfam; PF01561; Hanta_G2; 1.
DR Pfam; PF10538; ITAM_Cys-rich; 1.
DR PIRSF; PIRSF003945; M_poly_HantaV; 1.
DR PROSITE; PS51056; ITAM_2; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host mitochondrion; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host TRAFs by virus; Membrane; Metal-binding; Phosphoprotein;
KW Repeat; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1135
FT /note="Envelopment polyprotein"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT /id="PRO_0000455200"
FT CHAIN 19..648
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT /id="PRO_0000455201"
FT CHAIN 649..1135
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT /id="PRO_0000455202"
FT TOPO_DOM 19..495
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..1105
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 611..634
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT ZN_FING 545..565
FT /note="CCHC-type 1"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT ZN_FING 570..591
FT /note="CCHC-type 2"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 516..533
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 588..605
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 592..603
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 611..625
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 757..777
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P41266"
FT REGION 1122..1135
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT MOTIF 615..618
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT SITE 648..649
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT MOD_RES 615
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 628
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 29..151
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 63..157
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 109..128
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 133..138
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 175..185
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 210..247
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 234..351
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 376..435
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 380..389
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 405..424
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 452..475
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 735..770
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 739..777
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 751..885
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 765..896
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 780..904
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 806..815
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 823..832
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 863..867
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 970..1000
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 993..1045
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1010..1015
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1046..1051
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1085..1089
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
SQ SEQUENCE 1135 AA; 125716 MW; D5B48BAC30939E82 CRC64;
MIMWGLLLTM ILIDFGASLR NVYDMKIECP HSINFGESSV TGKVELPPLL LTDAEALVPE
SSCNMDNHQS MSIIQKVTKV SWRKKADKAQ AAKDSFETTS SEVNLKGTCA LSHRMVEESY
RNRRSVICYD LSCNSTHCKP TMHMIVPVHS CNMMKSCLVG LGPYRIQIVY ERTYCTTGIL
TEGKCFVPDQ SIVNVIKNGV FDIASVSIVC FFIRVKGTNY KIMASIKTAT ANNCNDTDNK
VQGYYLCIVG GNSSPVYAPS TTDFRSMEAL ASLLRAPHGE DHDLSGEEVA TYSIAGQIEG
KIPHTANAAN MLFTAFSGIP SYSSLSVFIG SQDGPVIYSP GLFPRLNQSS CDKIALPLIW
EGYIDLPGYY ETVHPCNVFC VLSGPGASCE AFSEGGIFNI TSPTCLVSKQ NRFRAAEQQV
NFVCQRVDQD IVIYCNGQKK TILTKTLVIG QCIYSVTSLF SIMPGVAHSI AIELCVPGFH
GWATAALLTT FCFGWILILS ITLAVLVVLK FFAAILHNSS QENRFKIILR KIKEEFEKTK
GSMVCEVCKY ECETGKELKA HNLSCPQSQC PYCFTHCEPT ESAFQAHYKV CQATHRFRDD
LKKTITPQST SPGCYRTLNL FRYKSRCYIF TVWVTLLIIE SIMWAASASE TVLEPSWNDN
AHGVGVVPMH TDLELDFSLP SSSKYTYKRK LTSPLNQEQS VDLHIEIESQ GISTSVHALG
HWFDGRLNLK TSFHCYGACT KYEYPWHTAK CHFERDFEYE NNWGCNPADC PGIGTGCTAC
GLYIDQLKPV GSAYKLITVR YSRKVCVQFG EENLCKTIDM NDCFVTRHVK VCIIGTVSKF
SQGDTLVFLG PMEGGGLIFK DWCTSTCQFG DPGDIMSPKD KGFSCPDFTG HFRKKCNFAT
TPVCEYDGNM VSGYKKVMAT IDSFQSFNTS SIHYTDERIE WKDPDGMLKD HLNILVTKDI
DFENLGENPC KVGLQTSSIE GAWGSGVGFT LTCQISLTEC SRFLTSIKAC DMAICYGAQS
VTLIRGQNTV KVSGKGGHSG SSFKCCHGTD CSQQGLQASA PHLDKVNGIV EQESEKVYDD
GAPQCGISCW FVKSGEWITG IFNGNWIVIV VLVFFFILSL ILLSLLCPIR KHKRS
