ID   GP_SEOU8                Reviewed;        1133 AA.
AC   P33455;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   04-NOV-2026, entry version 116.
DE   RecName: Full=Envelopment polyprotein;
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   Seoul virus (strain 80-39).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Bunyaviricetes; Elliovirales; Hantaviridae; Mammantavirinae;
OC   Orthohantavirus; Orthohantavirus seoulense.
OX   NCBI_TaxID=12557;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
OH   NCBI_TaxID=10117; Rattus rattus (Black rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1867009; DOI=10.1016/0168-1702(91)90093-b;
RA   Antic D., Lim B.U., Kang C.Y.;
RT   "Molecular characterization of the M genomic segment of the Seoul 80-39
RT   virus; nucleotide and amino acid sequence comparisons with other
RT   hantaviruses reveal the evolutionary pathway.";
RL   Virus Res. 19:47-58(1991).
RN   [2]
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
CC       {ECO:0000305}. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host
CC       Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane
CC       protein {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S47716; AAB19434.1; -; Genomic_RNA.
DR   PIR; A43964; A43964.
DR   AlphaFoldDB; P33455; -.
DR   SMR; P33455; -.
DR   GlyCosmos; P33455; 5 sites, No reported glycans.
DR   KEGG; vg:3648453; -.
DR   Proteomes; UP000207620; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0044178; C:host cell Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0033650; C:host cell mitochondrion; ISS:UniProtKB.
DR   GO; GO:0044228; C:host cell surface; ISS:UniProtKB.
DR   GO; GO:0055036; C:virion membrane; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0140476; P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TRAF activity; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.1320; -; 1.
DR   InterPro; IPR016402; Envelope_glycoprot_Hantavirus.
DR   InterPro; IPR048791; Gc_C_bunya.
DR   InterPro; IPR048790; Gn-B_hanta.
DR   InterPro; IPR002532; Hanta_Gc_N.
DR   InterPro; IPR002534; Hanta_Gn-H.
DR   InterPro; IPR012316; ITAM_motif_hantavir-typ.
DR   Pfam; PF20682; Hanta_Gc_C; 1.
DR   Pfam; PF01561; Hanta_Gc_N; 1.
DR   Pfam; PF20679; Hanta_Gn-B; 1.
DR   Pfam; PF01567; Hanta_Gn-H; 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   Disulfide bond; 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 RLR pathway by virus; Inhibition of host TRAFs by virus;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..1133
FT                   /note="Envelopment polyprotein"
FT                   /id="PRO_0000036838"
FT   CHAIN           18..646
FT                   /note="Glycoprotein N"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036839"
FT   CHAIN           647..1133
FT                   /note="Glycoprotein C"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036840"
FT   TOPO_DOM        18..484
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..626
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        627..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        648..1104
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1105..1125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1126..1133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          609..632
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   ZN_FING         543..563
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   ZN_FING         568..589
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   REGION          514..531
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   REGION          586..603
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P27312"
FT   REGION          590..601
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   REGION          609..623
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P27312"
FT   REGION          755..775
FT                   /note="Fusion loop"
FT                   /evidence="ECO:0000250|UniProtKB:P41266"
FT   REGION          1120..1133
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P27312"
FT   MOTIF           613..616
FT                   /note="YxxL"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   SITE            646..647
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        926
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        27..149
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        61..155
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        107..126
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        131..136
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        173..183
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        208..245
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        232..349
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        374..433
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        378..387
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        403..422
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        450..473
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        733..768
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        737..775
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        749..883
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        763..894
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        778..902
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        804..813
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        821..830
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        861..865
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        968..998
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        991..1043
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1008..1013
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1044..1049
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1083..1087
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
SQ   SEQUENCE   1133 AA;  125776 MW;  3FD0695189E75DA9 CRC64;
     MWSLLLLAAL VGQGFALKNV FDMRIQCPHS VKFGETSVSG YTELPPLSLQ EAEQLVPESS
     CNMDNHQSLS TINKLTKVIW RKKANQESAN QNSFELMESE VSFKGLCMLK HRMVEESYRN
     RRSVICYDLA CNSTFCKPTV YMIVPIHACN MMKSCLIGLG PYRVQVVYER TYCTTGILTE
     GKCFVPDKAV VSALKRGMYA IASIETICFF IHQKGNTYKI VTAITSAMGS KCNNTDTKVQ
     GYYICIIGGN SAPVYAPAGE DFRAMEVFSG IITSPHGEDH DLPGEEIATY QISGQIEAKI
     PHTVSSKNLK LTAFAGIPSY SSTSILTASE DGRFIFSPGL FPNLNQSVCD NNALPLIWRG
     LIDLTGYYEA VHPCNVFCVL SGPGASCEAF SEGGIFNITS PMCLVSKQNR FRAAEQQISF
     VCQRVDMDII VYCNGQKKTI LTKTLVIGQC IYTITSLFSL LPGVAHSIAI ELCVPGFHGW
     ATAALLITFC FGWVLIPACT LAILLVLKFF ANILHTSNQE NRFKAILRKI KEEFEKTKGS
     MVCEICKYEC ETLKELKAHN LSCVQGECPY CFTHCEPTET AIQAHYKVCQ ATHRFREDLK
     KTVTPQNIGP GCYRTLNLFR YKSRCYILTM WTLLLIIESI LWAASAAEIP LVPLWTDNAH
     GVGSVPMHTD LELDFSLPSS SRYTYKRHLT NPVNDQQSVS LHIEIESQGI GADVHHLGHW
     YDARLNLKTS FHCYGACTKY QYPWHTAKCH FEKDYEYENS WACNPPDCPG VGTGCTACGL
     YLDQLKPVGT AFKIISVRYS RKVCVQFGEE YLCKTIDMND CFVTRHAKIC IIGTVSKFSQ
     GDTLLFLGPM EGGGIIFKHW CTSTCHFGDP GDVMGPKDKP FICPEFPGQF RKKCNFATTP
     VCEYDGNIIS GYKKVLATID SFQSFNTSNI HFTDERIEWR DPDGMLRDHI NIVISKDIDF
     ENLAENPCKV GLQAANIEGA WGSGVGFTLT CQVSLTECPT FLTSIRACDM AICYGAESVT
     LSRGQNTVKI TGKGGHSGSS FKCCHGKECS LTGLQASAPH LDKVNGISEL ENEKVYDDGA
     PECGITCWFK KSGEWVMGII NGNWVVLIVL CVLLLFSLIL LSILCPVRKH KKS
//