GP_SINV
ID GP_SINV Reviewed; 1140 AA.
AC Q89905; A0A059WG88;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Sin Nombre orthohantavirus (SNV) (Sin Nombre virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980491;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10042; Peromyscus maniculatus (North American deer mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=NM H10 {ECO:0000312|EMBL:AAA75530.1};
RX PubMed=8178455; DOI=10.1006/viro.1994.1235;
RA Spiropoulou C.F., Morzunov S., Feldmann H., Sanchez A., Peters C.J.,
RA Nichol S.T.;
RT "Genome structure and variability of a virus causing hantavirus pulmonary
RT syndrome.";
RL Virology 200:715-723(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7494336; DOI=10.1128/jvi.69.12.8132-8136.1995;
RA Chizhikov V.E., Spiropoulou C.F., Morzunov S.P., Monroe M.C., Peters C.J.,
RA Nichol S.T.;
RT "Complete genetic characterization and analysis of isolation of Sin Nombre
RT virus.";
RL J. Virol. 69:8132-8136(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=77734 {ECO:0000312|EMBL:AIA08876.1};
RX PubMed=24778254; DOI=10.1073/pnas.1401998111;
RA Safronetz D., Prescott J., Feldmann F., Haddock E., Rosenke R., Okumura A.,
RA Brining D., Dahlstrom E., Porcella S.F., Ebihara H., Scott D.P., Hjelle B.,
RA Feldmann H.;
RT "Pathophysiology of hantavirus pulmonary syndrome in rhesus macaques.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7114-7119(2014).
RN [4]
RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=15919886; DOI=10.1128/jvi.79.12.7319-7326.2005;
RA Larson R.S., Brown D.C., Ye C., Hjelle B.;
RT "Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry
RT through the beta3-integrin receptor.";
RL J. Virol. 79:7319-7326(2005).
RN [5]
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 (Probable). 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, ECO:0000305|PubMed:15919886}.
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 (Probable). This
CC attachment induces virion internalization predominantly through
CC clathrin-dependent endocytosis (By similarity). Class II fusion protein
CC that promotes fusion of viral membrane with host endosomal membrane
CC after endocytosis of the virion (By similarity).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000305|PubMed:15919886}.
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 plasma membrane complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P08668}.
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 plasma membrane (Probable). Glycoprotein C
CC cytoplasmic tail is important for efficient Golgi localization (By
CC similarity). {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; L25783; AAA75530.1; -; Viral_cRNA.
DR EMBL; L37903; AAC42202.1; -; Genomic_RNA.
DR EMBL; KF537002; AIA08876.1; -; Viral_cRNA.
DR EMBL; KF537005; AIA08879.1; -; Viral_cRNA.
DR RefSeq; NP_941974.1; NC_005215.1.
DR SMR; Q89905; -.
DR GeneID; 2654026; -.
DR KEGG; vg:2654026; -.
DR Proteomes; UP000113911; Genome.
DR Proteomes; UP000167429; Genome.
DR Proteomes; UP000204632; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1140
FT /note="Envelopment polyprotein"
FT /id="PRO_0000455197"
FT CHAIN 18..652
FT /note="Glycoprotein N"
FT /id="PRO_0000455198"
FT CHAIN 653..1140
FT /note="Glycoprotein C"
FT /id="PRO_0000455199"
FT TOPO_DOM 18..480
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..1108
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1130..1140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 615..638
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT ZN_FING 549..569
FT /note="CCHC-type 1"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT ZN_FING 574..595
FT /note="CCHC-type 2"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 520..537
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 592..609
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 596..607
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 615..629
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 761..781
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P41266"
FT REGION 1125..1140
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT MOTIF 619..622
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT SITE 652..653
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT MOD_RES 619
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 632
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 30..155
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 64..161
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 113..132
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 137..142
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 179..189
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 214..251
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 380..439
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 384..393
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 409..428
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 456..479
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 739..774
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 743..781
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 755..888
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 769..899
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 784..907
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 810..819
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 827..836
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 867..871
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 973..1003
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 996..1048
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1013..1018
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1049..1054
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1088..1092
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT VARIANT 47
FT /note="I -> T (in strain:77734)"
FT /evidence="ECO:0000269|PubMed:24778254"
FT VARIANT 107
FT /note="I -> V (in strain:77734)"
FT /evidence="ECO:0000269|PubMed:24778254"
FT VARIANT 302
FT /note="V -> I (in strain:77734)"
FT /evidence="ECO:0000269|PubMed:24778254"
FT VARIANT 472
FT /note="H -> R (in strain:77734)"
FT /evidence="ECO:0000269|PubMed:24778254"
FT VARIANT 504
FT /note="A -> T (in strain:77734)"
FT /evidence="ECO:0000269|PubMed:24778254"
FT VARIANT 1120
FT /note="I -> V (in strain:77734)"
FT /evidence="ECO:0000269|PubMed:24778254"
FT CONFLICT 1140
FT /note="N -> KKKY (in Ref. 3; AIA08876/AIA08879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1140 AA; 125735 MW; 4678FD536AB7DBC0 CRC64;
MVGWVCIFLV VLTTATAGLT RNLYELKIEC PHTVGLGQGY VTGSVEITPI LLTQVADLKI
ESSCNFDLHV PATTTQKYNQ VDWTKKSSTT ESTNAGATTF EAKTKEINLK GTCNIPPTTF
EAAYKSRKTV ICYDLACNQT HCLPTVHLIA PVQTCMSVRS CMIGLLSSRI QVIYEKTYCV
TGQLIEGLCF IPTHTIALTQ PGHTYDTMTL PVTCFLVAKK LGTQLKLAVE LEKLITGVSC
TENSFQGYYI CFIGKHSEPL FVPTMEDYRS AELFTRMVLN PRGEDHDPDQ NGQGLMRIAG
PVTAKVPSTE TTETMQGIAF AGAPMYSSFS TLVRKADPEY VFSPGIIAES NHSVCDKKTV
PLTWTGFLAV SGEIEKITGC TVFCTLAGPG ASCEAYSETG IFNISSPTCL VNKVQKFRGS
EQRINFMCQR VDQDVVVYCN GQKKVILTKT LVIGQCIYTF TSLFSLIPGV AHSLAVELCV
PGLHGWATTA LLITFCFGWL LIPAVTLIIL KILRLLTFSC SHYSTESKFK VILERVKVEY
QKTMGSMVCD ICHHECETAK ELETHKKSCP EGQCPYCMTI TESTESALQA HFAICKLTNR
FQENLKKSLK RPEVRKGCYR TLGVFRYKSR CYVGLVWGIL LTTELIIWAA SADTPLMESG
WSDTAHGVGI IPMKTDLELD FALASSSSYS YRRKLVNPAN QEETLPFHFQ LDKQVVHAEI
QNLGHWMDGT FNIKTAFHCY GECKKYAYPW QTAKCFFEKD YQYETSWGCN PPDCPGVGTG
CTACGVYLDK LRSVGKAYKI VSLKYTRKVC IQLGTEQTCK HIDVNDCLVT PSVKVCMIGT
ISKLQPGDTL LFLGPLEQGG IILKQWCTTS CVFGDPGDIM STTSGMRCPE HTGSFRKICG
FATTPTCEYQ GNTVSGFQRM MATRDSFQSF NVTEPHITSN RLEWIDPDSS IKDHINMVLN
RDVSFQDLSD NPCKVDLHTQ SIDGAWGSGV GFTLVCTVGL TECANFITSI KACDSAMCYG
ATVTNLLRGS NTVKVVGKGG HSGSLFKCCH DTDCTEEGLA ASPPHLDRVT GYNQIDSDKV
YDDGAPPCTI KCWFTKSGEW LLGILNGNWV VVAVLIVILI LSILLFSFFC PVRSRKNKAN
