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

 GP_HANTB                Reviewed;        1133 AA.
P28728;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
07-JUN-2017, entry version 87.
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 B-1) (Korean hemorrhagic fever virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses; Bunyavirales;
Hantaviridae; Orthohantavirus.
NCBI_TaxID=31617;
NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2118626; DOI=10.1093/nar/18.16.4936;
Isegawa Y., Fujiwara Y., Ohshima A., Fukunaga R., Murakami H.,
Yamanishi K., Sokawa Y.;
"Nucleotide sequence of the M genome segment of hemorrhagic fever with
renal syndrome virus strain B-1.";
Nucleic Acids Res. 18:4936-4936(1990).
-!- FUNCTION: Glycoprotein Gn and glycoprotein Gc 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 interact 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 N and Glycoprotein C.
{ECO:0000250|UniProtKB:P08668}.
-!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein
family. {ECO:0000305}.
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EMBL; X53861; CAA37854.1; -; mRNA.
PIR; S12597; S12597.
SMR; P28728; -.
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.
2: Evidence at transcript level;
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 16 {ECO:0000255}.
CHAIN 17 1133 Envelopment polyprotein.
/FTId=PRO_0000036806.
CHAIN 17 646 Glycoprotein N. {ECO:0000250}.
/FTId=PRO_0000036807.
CHAIN 647 1133 Glycoprotein C. {ECO:0000250}.
/FTId=PRO_0000036808.
TOPO_DOM 17 485 Lumenal. {ECO:0000255}.
TRANSMEM 486 506 Helical. {ECO:0000255}.
TOPO_DOM 507 646 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 647 1103 Lumenal. {ECO:0000255}.
TRANSMEM 1104 1124 Helical. {ECO:0000255}.
TOPO_DOM 1125 1133 Cytoplasmic. {ECO:0000255}.
DOMAIN 609 632 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
SITE 646 647 Cleavage; by host signal peptidase.
{ECO:0000250}.
CARBOHYD 132 132 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
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


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