GP_HANTB
ID GP_HANTB Reviewed; 1133 AA.
AC P28728;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Hantaan virus (strain B-1) (Korean hemorrhagic fever virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=31617;
OH NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2118626; DOI=10.1093/nar/18.16.4936;
RA Isegawa Y., Fujiwara Y., Ohshima A., Fukunaga R., Murakami H.,
RA Yamanishi K., Sokawa Y.;
RT "Nucleotide sequence of the M genome segment of hemorrhagic fever with
RT renal syndrome virus strain B-1.";
RL Nucleic Acids Res. 18:4936-4936(1990).
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). May also bind to host
CC C1QBP for virus entry into the host cell (By similarity). Mediates the
CC assembly and budding of infectious virus particles through its
CC interaction with the nucleocapsid protein and the viral genome (By
CC similarity). May dysregulate normal immune and endothelial cell
CC responses through an ITAM motif (By similarity). Translocates to
CC mitochondria, binds to host TUFM and recruits MAP1LC3B (By similarity).
CC These interactions induce mitochondrial autophagy and therefore
CC destruction of host MAVS leading to inhibition of type I interferon
CC (IFN) responses (By similarity). Concomitant breakdown of glycoprotein
CC N is apparently prevented by the nucleoprotein that may inhibit Gn-
CC stimulated autophagosome-lysosome fusion (By similarity). Interacts
CC with the viral genomic RNA (By similarity).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P27312}.
CC -!- FUNCTION: [Glycoprotein C]: Forms homotetramers with glycoprotein N 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). May also bind to host
CC C1QBP for virus entry into the host cell (By similarity). Class II
CC fusion protein that promotes fusion of viral membrane with host
CC endosomal membrane after endocytosis of the virion (By similarity).
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 Host cell surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:P08668}. Note=Budding probably takes
CC place at the host Golgi (Probable). Glycoprotein C cytoplasmic tail is
CC important for efficient Golgi localization (By similarity).
CC {ECO:0000250|UniProtKB:P08668, 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; X53861; CAA37854.1; -; mRNA.
DR PIR; S12597; S12597.
DR SMR; P28728; -.
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:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039547; P:suppression by virus of host TRAF 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 2: Evidence at transcript level;
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; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW Virus endocytosis by host; Virus entry into host cell; Zinc; Zinc-finger.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1133
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036806"
FT CHAIN 17..646
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036807"
FT CHAIN 647..1133
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036808"
FT TOPO_DOM 17..485
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..1103
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1104..1124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1125..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 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; 125909 MW; 0A25160A32862FD6 CRC64;
MWSLLLLAAL VGQGFALKNV FDMRIQCPHS VNFGETSVSG YTELPPLSLQ EAEQLVPESS
CNMDNHQSLS TINKLTKVIW RKKANQESAN QNSFEVVESE VSFKGLCMLK HRMVEESYRN
RRSVIYYDLA GNSTFCKPTV YMIVPIHACN MMKSCLIGLG PYRIQVVYER TYCTTGILTE
GKCFVPDKAV VSALKRGMYA IASIETICFF IHQKWNKYKI VTAITSAMGS KCNNTDTKVQ
GYYICIIGGN SAPVYAPAGE DFRAMEVFSG IITSPHGEDH DLPGEEIATY HISGQIEAKI
PHTVSSKNLR LAAFAGIPSY SSTSILAASE DGRFIFSPGL FPNLNQSVCD NNALPLIWRG
LIDLTGYYEA VHPCNVFCVL SGPGASCEAF SEGGIFNITS PMCLVSKQNR FRAAEQQISF
VCQRVDMDII VYCNGQKKTI LTKTLVIGQC IYTITSLFSL LPGVAHSIAI ELCVPGFHGW
ATAALLITFC FGWVLIPACT LAILLVLKFF ANILHTSNQE NRFKAILRKI KEEFEKRKGS
MVCEICKYEC ETLKELKAHN LSCVQGECPY CFTHCEPTET AIQAHYKVCQ ATHRFREDLK
KTVTPQNIGP GCYRTLNLFR YKSRCYILTM WTLLLIIESI LWAASAAEIP LVPLWTDNAH
GVGSVPMHTD LELDFSLPSS SKYTYKRHLT NPVNDQQSVS LHIEIESQGI GADVHHLGHW
YDARLNLKTS FHCYGACTKY QYPWHTAKCH FEKDYEYENS WACNPPDCPG VGTGCTACGL
YLDQLKPVGT AFKIISVRYS RKVCVQFGEE HLCKTIDMND CFVTRHAKIC IIGTVSKFSQ
GDTLLFLGPM EGGGIIFKHW CTSTCHFGDP RDVMGPKDKP FICPEFPGQF RKKCNFATTP
VCEYDGNIIS GYKKVLATID SFQSFNTSNI HFTDERIEWR DPDGMLRDHI NIVISKDIDF
ENLAENPCKV GLQAANIEGA WGSGVGFTLT CQVSLTECPT FLTSIKACDM AICYGAESVT
LSRGQNTVKI TGKGGHSGSS FKCCHGKECS STGLQASAPH LDKVNGISEL ENEKVYDDGA
PECGVTCWFK KSGEWVMGII NGNWVVLIVL CVLLLFSLIL LSILCPVRKH KKS
