ID Q66034_9VIRU Unreviewed; 1684 AA. AC Q66034; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 2. DT 24-JUL-2024, entry version 68. DE RecName: Full=Envelopment polyprotein {ECO:0000256|PIRNR:PIRNR003962}; DE AltName: Full=M polyprotein {ECO:0000256|PIRNR:PIRNR003962}; DE Contains: DE RecName: Full=Mucin-like variable region {ECO:0000256|PIRNR:PIRNR003962}; DE Contains: DE RecName: Full=GP38 {ECO:0000256|PIRNR:PIRNR003962}; DE Contains: DE RecName: Full=Glycoprotein N {ECO:0000256|PIRNR:PIRNR003962}; DE Short=Gn {ECO:0000256|PIRNR:PIRNR003962}; DE Contains: DE RecName: Full=Non-Structural protein M {ECO:0000256|PIRNR:PIRNR003962}; DE Short=NSm {ECO:0000256|PIRNR:PIRNR003962}; DE Contains: DE RecName: Full=Glycoprotein C {ECO:0000256|PIRNR:PIRNR003962}; DE Short=Gc {ECO:0000256|PIRNR:PIRNR003962}; OS Orthonairovirus haemorrhagiae. OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Ellioviricetes; Bunyavirales; Nairoviridae; Orthonairovirus. OX NCBI_TaxID=3052518 {ECO:0000313|EMBL:AAA86616.2}; RN [1] {ECO:0000313|EMBL:AAA86616.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10200 {ECO:0000313|EMBL:AAA86616.2}; RA Parker M.D., Glass P.J., Jennings G.B., Lofts R., Smith J.F., Miller M.M., RA Spik K.W., Schoepp R.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: [Glycoprotein C]: Binds to host cell surface receptor LDLR CC and mediates fusion between viral and cellular membranes. Attachment to CC receptor induces virion internalization predominantly through clathrin- CC dependent endocytosis. Class II fusion protein that promotes fusion of CC viral membrane with host endosomal membrane after endocytosis of the CC virion. Exposure of the glycoprotein spikes to potassium is necessary CC for the conformational change leading to fusion. CC {ECO:0000256|PIRNR:PIRNR003962}. CC -!- FUNCTION: [Glycoprotein N]: Plays a role in virion attachment to host CC receptor. This attachment induces virion internalization predominantly CC through clathrin-dependent endocytosis. Glycoprotein N probably locks CC the Gn-Gc complex in a prefusion state. CC {ECO:0000256|PIRNR:PIRNR003962}. CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004244, ECO:0000256|PIRNR:PIRNR003962}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004244}. Virion CC membrane {ECO:0000256|PIRNR:PIRNR003962}; Multi-pass membrane protein CC {ECO:0000256|PIRNR:PIRNR003962}. Virion membrane CC {ECO:0000256|PIRNR:PIRNR003962}; Single-pass type I membrane protein CC {ECO:0000256|PIRNR:PIRNR003962}. Host endoplasmic reticulum membrane CC {ECO:0000256|PIRNR:PIRNR003962}; Single-pass type I membrane protein CC {ECO:0000256|PIRNR:PIRNR003962}. Note=Interaction between Glycoprotein CC C and Glycoprotein N is essential for proper targeting of Glycoprotein CC C to the Golgi complex, where virion budding occurs. CC {ECO:0000256|PIRNR:PIRNR003962}. CC -!- SIMILARITY: Belongs to the nairovirus envelope glycoprotein family. CC {ECO:0000256|PIRNR:PIRNR003962}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U39455; AAA86616.2; -; Genomic_RNA. DR TCDB; 1.G.20.2.1; the hantavirus gc envelope fusion glycoprotein (gc-efg) family. 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:0016020; C:membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:InterPro. DR CDD; cd22541; SP5_N; 1. DR Gene3D; 1.10.8.1320; -; 2. DR InterPro; IPR048791; Gc_C_bunya. DR InterPro; IPR048801; Gn_nairovirus. DR InterPro; IPR048529; GP38_nairovirus. DR InterPro; IPR002532; Hanta_Gc_N. DR InterPro; IPR049491; MLD_nairovirus. DR InterPro; IPR012487; Nairovirus_M. DR InterPro; IPR048796; NSm_dom_nairovirus. DR Pfam; PF20682; Hanta_Gc_C; 1. DR Pfam; PF01561; Hanta_Gc_N; 1. DR Pfam; PF20726; Nairovirus_Gn; 1. DR Pfam; PF07948; Nairovirus_GP38; 1. DR Pfam; PF20727; Nairovirus_MLD; 1. DR Pfam; PF20728; Nairovirus_NSm; 1. DR PIRSF; PIRSF003962; M_poly_NairoV; 1. PE 3: Inferred from homology; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|PIRNR:PIRNR003962}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|PIRNR:PIRNR003962}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|PIRNR:PIRNR003962}; KW Host endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR003962}; KW Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812, KW ECO:0000256|PIRNR:PIRNR003962}; KW Host membrane {ECO:0000256|PIRNR:PIRNR003962}; KW Host-virus interaction {ECO:0000256|PIRNR:PIRNR003962}; KW Membrane {ECO:0000256|PIRNR:PIRNR003962, ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|PIRNR:PIRNR003962}; KW Viral envelope protein {ECO:0000256|PIRNR:PIRNR003962, KW ECO:0000313|EMBL:AAA86616.2}; KW Viral penetration into host cytoplasm {ECO:0000256|PIRNR:PIRNR003962}; KW Virion {ECO:0000256|PIRNR:PIRNR003962}; KW Virus endocytosis by host {ECO:0000256|PIRNR:PIRNR003962}; KW Virus entry into host cell {ECO:0000256|PIRNR:PIRNR003962}. FT TRANSMEM 693..722 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 820..837 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 857..876 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 969..993 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1595..1620 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 29..247 FT /note="Mucin-like" FT /evidence="ECO:0000259|Pfam:PF20727" FT DOMAIN 267..508 FT /note="GP38 nairovirus" FT /evidence="ECO:0000259|Pfam:PF07948" FT DOMAIN 521..842 FT /note="Structural glycoprotein Gn nairovirus" FT /evidence="ECO:0000259|Pfam:PF20726" FT DOMAIN 853..954 FT /note="Non-Structural protein M" FT /evidence="ECO:0000259|Pfam:PF20728" FT DOMAIN 1082..1409 FT /note="Hantavirus glycoprotein Gc N-terminal" FT /evidence="ECO:0000259|Pfam:PF01561" FT DOMAIN 1410..1631 FT /note="Glycoprotein Gc C-terminal bunyavirales" FT /evidence="ECO:0000259|Pfam:PF20682" FT REGION 23..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..178 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..222 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1684 AA; 186679 MW; C6DD80EBAD8CC3BE CRC64; MHISLMYAIL CLQLCGLGET HGSHNETRHN KTDTMTTHGD NPSSEPPVST ALSITLDPST VTPTTPASGL EGSGEVYTSP PITTGSLPLS ETTPELPVTT GTDTLSAGDV DPSTQTAGGT SAPTVRTSLP NSPSTPSTPQ DTHHPVRNLL SVTSPGPDET STPSGTGKES SATSSPHPVS NRPPTPPATA QGPTENDSHN ATEHPESLTQ SATPGLMTSP TQIVHPQSAT PITVQDTHPS PTNRSKRNLK MEIILTLSQG LKKYYGKILR LLQLTLEEDT EGLLEWCKRN LGLDCDDTFF QKRIEEFFIT GEGHFNEVLQ FRTPGTLSTT ESTPAGLPTA EPFKSYFAKG FLSIDSGYYS AKCYSGTSNS GLQLINITRH STRIVDTPGP KITNLKTINC INLKASIFKE HREVEINVLL PQVAVNLSNC HVVIKSHVCD YSLDIDGAVR LPHIYHEGVF IPGTYKIVID KKNKLNDRCT LFTDCVIKGR EVRKGQSVLR QYKTEIRIGK ASTGFRRLLS EEPSDDCVSR TQLLRTETAE IHGDNYGGPG DKITICNGST IVDQRLGSEL GCYTINRVRS FKLCENSATG KNCEIDSVPV KCRQGYCLRI TQEGRGHVKL SRGSEVVLDA CDTSCEIMIP KGTGDILVDC SGGQQHFLKD NLIDLGCPKI PLLGKMAIYI CRMSNHPKTT MAFLFWFSFG YVITCILCKA IFYLLIIVGT LGRRLKQYRE LKPQTCTICE TTPVNAIDAE MHDLNCSYNI CPYCASRLTS DGLARHVIQC PKRKEKVEET ELYLNLERIP WVVRKLLQVS ESTGVALKRS SWLIVLLVLF TVSLSPVQSA PIGQGKTIEA YRAREGYTSI CLFVLGSILF IVSCLMKGLV DSVGNSFFPG LSICKTCSIS SINGFEIESH KCYCSLFCCP YCRHCSTDKE IHKLHLSICK KRKTGSNVML AVCKLMCFRA TMEVSNRALF IRSIINTTFV LCILILAVCV VSTSAVEMEN LPAGTWEREE DLTNFCHQEC QVTETECLCP YEALVLRKPL FLDSTAKGMK NLLNSTSLET SLSIEAPWGA INVQSTYKPT VSTANIALSW SSVEHRGNKI LVSGRSESIM KLEERTGISW DLGVEDASES KLLTVSVMDL SQMYSPVFEY LSGDRQVEEW PKATCTGDCP ERCGCTSSTC LHKEWPHSRN WRCNPTWCWG VGTGCTCCGL DVKDLFTDYM FVKWKVEYIK TEAIVCVELT SQERQCSLIE AGTRFNLGPV TITLSEPRNI QQKLPPEIIT LHPRIEEGFF DLMHVQKVLS ASTVCKLQSC THGVPGDLQV YHIGNLLKGD KVNGHLIHKI EPHFNTSWMS WDGCDLDYYC NMGDWPSCTY TGVTQHNHAS FVNLLNIETD YTKNFHFHSK RVTAHGDTPQ LDLKARPTYG AGEITVLVEV ADMELHTKKI EISGLKFASL ACTGCYACSS SISCKVRIHV DEPDELTVHV KSDDPDVVAA SSSLMARKLE FGTDSTFKAF SAMPKTSLCF YIVEREHCKS CSEEDTKKCV NTKLEQPQSI LIEHKGTIIG KQNSTCTAKA SCWLESVKSF FYGLKNMLSG IFGNVFMGIF LFLAPFILLI LFFMFGWRIL FCFKCCRRTR GLFKYRHLKD DEETGYRRII EKLNNKKGKN KLLDGERLAD GRIAELFSTK THIG //