GP_HANTH
ID GP_HANTH Reviewed; 1134 AA.
AC P16493;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Hojo) (Hojo virus) (Korean hemorrhagic fever virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=11583;
OH NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2900289; DOI=10.1099/0022-1317-69-8-1949;
RA Schmaljohn C.S., Arikawa J., Hasty S.E., Rasmussen L., Lee H.W., Lee P.W.,
RA Dalrymple J.M.;
RT "Conservation of antigenic properties and sequences encoding the envelope
RT proteins of prototype Hantaan virus and two virus isolates from Korean
RT haemorrhagic fever patients.";
RL J. Gen. Virol. 69:1949-1955(1988).
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; D00376; BAA00279.1; -; Genomic_RNA.
DR SMR; P16493; -.
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 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; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1134
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036809"
FT CHAIN 19..648
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036810"
FT CHAIN 649..1134
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036811"
FT TOPO_DOM 19..487
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..1104
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1126..1134
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 756..776
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P41266"
FT REGION 1121..1134
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 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 927
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 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 734..769
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 738..776
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 750..884
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 764..895
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 779..903
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 805..814
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 822..831
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 969..999
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 992..1044
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1009..1014
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1045..1050
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1084..1088
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
SQ SEQUENCE 1134 AA; 126405 MW; 01E59250FC267D23 CRC64;
MGIWKWLVMA SLVWPVLTLR NVYDMKIECP HTVSFGENSV IGYVELPPMP LADTAQLVPE
SSCSMDNHQS LNTITKYTQV SWRGKADQSQ SSQNSFETVS TEVDLKGTCV LKHKMVEESY
RSRKSITCYD LSCNSTYCKP TLYMIVPIHA CNMMKSCLIA LGPYRVQVVY ERTYCMTGVL
IEGKCFVPDQ SVVSIIKHGI FDIASVHIVC FFVAVKGNTY KIFEQVKKSF ESTCNDTENK
VQGYYICIVG GNSAPIYVPT LDDFRSMEAF TGIFRSPHGE DHDLAGEETA TYSIVGPANA
KVPHSASSDT LSLIAFSGIP SYSSLSILTS STEAKHVFSP GLFPKLNHTN CDKGAIPLMW
TGMIDVPRYY DGIHPFTVFC VLSGPGASCE AFSEGGIFNI TSPMCLVSKQ NRFRLTEQQV
NFVCQRVDVD IVVYCNGQRK VILTKTLVIG QCIYTITSLF SLLPGVAHSI AVELCVPGFH
GWATAALLVT FCFGWVLIPA VTFIILAILK FIANIFHTSN QENRLKSVLR KIKEEFEKTK
GSMVCDVCKY ECETYKELKA HGVSCPQSQC PYCFTHCEPT EAAFQAHYKV CQVTHRFRDD
LKKTVTPQNF TPGCYRTLNL FRYKSRCYIF TMWIFLLVLE SILWAASASE TPLTPVWNDN
AHGVGSIPMH TDLELDFSLT SSSKYTYRRK LTNPLEAQSI DLHIEIEEQT IGVDVHALGH
WFDGRLNLKT SFHCYGACTK YEYPWHTAKC HYERDYQYET SWGCNPSDCP GCGTGCTACG
LYLDRLKPVG SAYKIITIRY SRRVCVQFGE ENLCKIIDMN DCFVSRHVKV CIIGTVSKFS
QGDTLLFFGP LEGGGLIFKH WRTSTCQFGD PGDIMSPRDK GFLCPEFPGS FRKKCNFATT
PICEYDGNMV SGYKKVMATI DSFQSFNTST MHFTDERIEW KDPDGMLRDH INILVTKDID
FDNLGENPCK IGLQTSSIEG AWGSGVGFTL TCLVSLTECP TFLTSIKACD KAICYGAESV
TLTRGQNTVK VSGKGGHSGS TFKCCHGEDC SPNGLHAAAP HLDKVNGISE IENSKEYDDG
APQCGIKCWF VKSGEWISGI FSGNWIVLIV LCVFLLFSLV LLSILCPVRK HKKS
