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Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)]

 GP_HANTL                Reviewed;        1135 AA.
P16853;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
07-JUN-2017, entry version 89.
RecName: Full=Envelopment polyprotein;
AltName: Full=M polyprotein;
Contains:
RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P08668};
Short=Gn;
AltName: Full=Glycoprotein G1;
Contains:
RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P08668};
Short=Gc;
AltName: Full=Glycoprotein G2;
Flags: Precursor;
Name=GP;
Hantaan virus (strain Lee) (Lee virus) (Korean hemorrhagic fever
virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses; Bunyavirales;
Hantaviridae; Orthohantavirus.
NCBI_TaxID=11601;
NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2900289; DOI=10.1099/0022-1317-69-8-1949;
Schmaljohn C.S., Arikawa J., Hasty S.E., Rasmussen L., Lee H.W.,
Lee P.W., Dalrymple J.M.;
"Conservation of antigenic properties and sequences encoding the
envelope proteins of prototype Hantaan virus and two virus isolates
from Korean haemorrhagic fever patients.";
J. Gen. Virol. 69:1949-1955(1988).
-!- FUNCTION: Glycoprotein N and Glycoprotein C interact with each
other and are present at the surface of the virion. They are able
to attach the virion to host cell receptors. This attachment
induces virion internalization predominantly through clathrin-
dependent endocytosis. Also promote fusion of viral membrane with
host endosomal membrane after endocytosis of the virion. Gn
contains an ITAM motif which is likely to dysregulate normal
immune and endothelial cell responses and contribute to virus
pathogenesis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Glycoprotein N and Glycoprotein C interacts with each
other. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Glycoprotein N: Virion membrane
{ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane
{ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P08668}; Single-pass type I
membrane protein {ECO:0000250|UniProtKB:P08668}. Note=Interaction
between Glycoprotein N and Glycoprotein C is essential for proper
targeting of Glycoprotein N to the Golgi complex, where virion
budding occurs. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Glycoprotein C: Virion membrane
{ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane
{ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P08668}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
including glycoprotein Glycoprotein N and glycoprotein
Glycoprotein C. {ECO:0000250|UniProtKB:P08668}.
-!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein
family. {ECO:0000305}.
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EMBL; D00377; BAA00280.1; -; Genomic_RNA.
PIR; JS0605; JS0605.
SMR; P16853; -.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR016402; Envelope_glycoprot_Hantavirus.
InterPro; IPR002534; Hanta_G1.
InterPro; IPR002532; Hanta_G2.
InterPro; IPR012316; ITAM_motif_hantavir-typ.
Pfam; PF01567; Hanta_G1; 1.
Pfam; PF01561; Hanta_G2; 1.
Pfam; PF10538; ITAM_Cys-rich; 1.
PIRSF; PIRSF003945; M_poly_HantaV; 1.
ProDom; PD001813; Hanta_G2; 1.
PROSITE; PS51056; ITAM_2; 1.
3: Inferred from homology;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host TRAFs by virus; Membrane; Signal; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 1135 Envelopment polyprotein.
/FTId=PRO_0000036812.
CHAIN 19 648 Glycoprotein N. {ECO:0000250}.
/FTId=PRO_0000036813.
CHAIN 649 1135 Glycoprotein C. {ECO:0000250}.
/FTId=PRO_0000036814.
TOPO_DOM 19 485 Lumenal. {ECO:0000255}.
TRANSMEM 486 506 Helical. {ECO:0000255}.
TOPO_DOM 507 648 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 649 1105 Lumenal. {ECO:0000255}.
TRANSMEM 1106 1126 Helical. {ECO:0000255}.
TOPO_DOM 1127 1135 Cytoplasmic. {ECO:0000255}.
DOMAIN 611 634 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
SITE 648 649 Cleavage; by host signal peptidase.
{ECO:0000250}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 928 928 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
SEQUENCE 1135 AA; 126470 MW; B9C759ED6592265A CRC64;
MGIWKWLVMA SLVWPVLTLR NVYDMKIECP HTVSFGENSV IGYVELPPMP LADTAQLVPE
SSCSMDNHQS LNTITKYTQV SWRGKADQSQ SSQTSFETVS TEVDLKGTCV LKHKMVEESY
RSRKSITCYD LSCNSTYCKP TLYMIVPIHA CNMMKSCLIA LGPYRVQVVY ERTYCMTGVL
IEGKCFVPDQ SVVSIIKHGI FDIASVHIVC FFVAVKGNTY KIFEQVKKSF ESTCNDTENK
VQGYYICIVG GNSAPIYVPT LDDFRSMEAF TGIFRSPHGE DHDLAGEETA TYSIVGPANA
KVPHSASSDT LSLIAFSGIP SDSSLSILTS STEAKHVFSP GLFPKLNHTN CDKGAIPLMW
TGMIDLPGYY EAIHPCTVFC VLSGPGASCE AFSEGGIFNI TYPMCLVSKQ NRFRLTEQQV
NFVCQRVDVD IVVYCNGQRK VILTKTLVIG QCIYTITSLF SLLPGVAHSI AVELCVPGFH
GWATAALLVT FCFGWVLIPA ITFIILTILK FIANIFHTSN QENRLKSVLR KIKEEFEKTK
GSMVCDVCKY ECETYKELKA HGVSCPQSQC PYCFTHCEPT EAAFQAHYKV CQVTHRFRDD
LKKTVTPQNF TPGCYRTLNL FRYKSRCYIF TMWIFLLVLE SILWAASASE TPLTPVWNDN
AHGVGSVPMH TDLELDFSLT SSSKYTYRRK LTNPLEEAQS IDLHIEIEEQ TIGVDVHALG
HWFDGRLNLK TSFHCYGACT KYEYPWHTAK CHYERDYQYE TSWGCNPSDC PGVGTGCTAC
GLYLDRLKPV GSAYKIITIR YSRRVCVQFG EENLCKIIDM NDCFVSRHVK VCIIGTVSKF
SQGDTLLFFG PLEGGGLIFK HWCTSTCQFG DPGDIMSPRD KGFLCPEFPG SFRKKCNFAT
TPICEYDGNM VSGYKKVMAT IDSFQSFNTS TMHFTDERIE WKDPDGMLRD HINILVTKDI
DFDNLGENPC KIGLQTSSIE GAWGSGVGFT LTCLVSLTEC PTFLTSIKAC DKAICYGAES
VTLTRGQNTV KVSGKGGHSG STFKCCHGED CSQIGLHAAA PHLDKVNGIS EMENSKEYDD
GAPQCGIKCW FVKSGEWISG IFSGNWIVLI VLCVFLLFSL VLLSILCPVR KHKKS


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