POLG_LANVY
ID POLG_LANVY Reviewed; 776 AA.
AC P29838;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 02-JUN-2021, entry version 122.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein C;
DE AltName: Full=Core protein;
DE Contains:
DE RecName: Full=Protein prM;
DE Contains:
DE RecName: Full=Peptide pr;
DE Contains:
DE RecName: Full=Small envelope protein M;
DE AltName: Full=Matrix protein;
DE Contains:
DE RecName: Full=Envelope protein E;
DE Flags: Fragment;
OS Langat virus (strain Yelantsev).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=31639;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=6935; Ixodida (ticks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1720591; DOI=10.1016/0042-6822(91)90567-u;
RA Mandl C.W., Iacono-Connors L.C., Wallner G., Holzmann H., Kunz C.,
RA Heinz F.X.;
RT "Sequence of the genes encoding the structural proteins of the low-
RT virulence tick-borne flaviviruses Langat TP21 and Yelantsev.";
RL Virology 185:891-895(1991).
RN [2]
RP STRUCTURE BY NMR OF 580-675.
RX PubMed=16731969; DOI=10.1110/ps.051844006;
RA Mukherjee M., Dutta K., White M.A., Cowburn D., Fox R.O.;
RT "NMR solution structure and backbone dynamics of domain III of the E
RT protein of tick-borne Langat flavivirus suggests a potential site for
RT molecular recognition.";
RL Protein Sci. 15:1342-1355(2006).
CC -!- FUNCTION: Capsid protein C self-assembles to form an icosahedral capsid
CC about 30 nm in diameter. The capsid encapsulates the genomic RNA (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: prM acts as a chaperone for envelope protein E during
CC intracellular virion assembly by masking and inactivating envelope
CC protein E fusion peptide. prM is matured in the last step of virion
CC assembly, presumably to avoid catastrophic activation of the viral
CC fusion peptide induced by the acidic pH of the trans-Golgi network.
CC After cleavage by host furin, the pr peptide is released in the
CC extracellular medium and small envelope protein M and envelope protein
CC E homodimers are dissociated (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Envelope protein E binding to host cell surface receptor is
CC followed by virus internalization through clathrin-mediated
CC endocytosis. Envelope protein E is subsequently involved in membrane
CC fusion between virion and host late endosomes. Synthesized as a
CC homodimer with prM which acts as a chaperone for envelope protein E.
CC After cleavage of prM, envelope protein E dissociate from small
CC envelope protein M and homodimerizes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins Peptide
CC 2K acts as a signal sequence and is removed from the N-terminus of NS4B
CC by the host signal peptidase in the ER lumen. Signal cleavage at the
CC 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K
CC site (By similarity). {ECO:0000250}.
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DR EMBL; M73835; AAA02740.1; -; Unassigned_RNA.
DR PIR; A41704; A41704.
DR PDB; 1Z66; NMR; -; A=580-675.
DR PDBsum; 1Z66; -.
DR BMRB; P29838; -.
DR SMR; P29838; -.
DR EvolutionaryTrace; P29838; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd12149; Flavi_E_C; 1.
DR Gene3D; 1.10.8.970; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.60.260.50; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.98.10; -; 1.
DR Gene3D; 3.30.387.10; -; 1.
DR Gene3D; 3.30.67.10; -; 1.
DR InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR InterPro; IPR001122; Flavi_capsidC.
DR InterPro; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR Pfam; PF01004; Flavi_M; 1.
DR Pfam; PF01570; Flavi_propep; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; 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 membrane; Host-virus interaction;
KW Membrane; Secreted; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..>776
FT /note="Genome polyprotein"
FT /id="PRO_0000405133"
FT CHAIN 1..96
FT /note="Capsid protein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037699"
FT PROPEP 97..117
FT /note="ER anchor for the protein C, removed in mature form
FT by serine protease NS3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000405134"
FT CHAIN 118..280
FT /note="Protein prM"
FT /evidence="ECO:0000250"
FT /id="PRO_0000405135"
FT CHAIN 118..205
FT /note="Peptide pr"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037700"
FT CHAIN 206..280
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037701"
FT CHAIN 281..776
FT /note="Envelope protein E"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037702"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..727
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..755
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..68
FT /note="Hydrophobic; homodimerization of capsid protein C"
FT /evidence="ECO:0000250"
FT SITE 96..97
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 117..118
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 205..206
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT SITE 280..281
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 283..310
FT /evidence="ECO:0000250"
FT DISULFID 340..396
FT /evidence="ECO:0000250"
FT DISULFID 354..385
FT /evidence="ECO:0000250"
FT DISULFID 372..401
FT /evidence="ECO:0000250"
FT DISULFID 466..570
FT /evidence="ECO:0000250"
FT DISULFID 587..618
FT /evidence="ECO:0000250"
FT NON_TER 776
SQ SEQUENCE 776 AA; 84537 MW; 5F7557E55A33BE3B CRC64;
MAGKAVLKGK GGGPPRRASK VAPKKTRQLR VQMPNGLVLM RMLGVLWHAL TGTARSPVLK
AFWKVVPLKQ ATLALRKIKR TVSTLMVGLH RRGSRRTTID WMTPLLITVM LGMCLTATVR
RERDGSMVIR AEGRDAATQV RVENGTCVIL ATDMGSWCDD SLAYECVTID QGEEPVDVDC
FCRGVEKVTL EYGRCGRREG SRSRRSVLIP SHAQRDLTGR GHQWLEGEAV KAHLTRVEGW
VWKNKLFTLS LVMVAWLMVD GLLPRILIVV VALALVPAYA SRCTHLENRD FVTGVQGTTR
LTLVLELGGC VTVTADGKPS LDVWLDSIYQ ESPAQTREYC LHAKLTGTKV AARCPTMGPA
TLPEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKFT CEDKKKATGH VYDVNKITYT
IKVEPHTGEF VAANETHSGR KSASFTVSSE KTILTLGDYG DVSLLCRVAS GVDLAQTVVL
ALDKTHEHLP TAWQVHRDWF NDLALPWKHD GAEAWNEAGR LVEFGTPHAV KMDVFNLGDQ
TGVLLKSLAG VPVASIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTVCDKT KFTWKRAPTD
SGHDTVVMEV GFSGTRPCRI PVRAVAHGVP EVNVAMLITP NPTMENNGGG FIEMQLPPGD
NIIYVGDLNH QWFQKGSSIG RVLQKTRKGI ERLTVLGEHA WDFGSVGGVM TSIGRAMHTV
LGGAFNTLLG GVGFLPKILL GVAMAWLGLN MRNPTLSMGF LLSGGLVLAM TLGVGA
