POLG_DEN23
ID POLG_DEN23 Reviewed; 495 AA.
AC P14339;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Envelope protein E;
DE Flags: Fragment;
OS Dengue virus type 2 (isolate Malaysia M3) (DENV-2).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=11063;
OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH NCBI_TaxID=299627; Aedes furcifer (Mosquito).
OH NCBI_TaxID=299628; Aedes taylori (Mosquito).
OH NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2587242; DOI=10.1093/nar/17.21.8887;
RA Samuel S., Koh C.L., Blok J., Pang T., Lam S.K.;
RT "Nucleotide sequence of the envelope protein gene of a Malaysian dengue-2
RT virus isolated from a patient with dengue fever.";
RL Nucleic Acids Res. 17:8887-8887(1989).
CC -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC mediates fusion between viral and cellular membranes. Envelope protein
CC is synthesized in the endoplasmic reticulum in the form of heterodimer
CC with protein prM. They play a role in virion budding in the ER, and the
CC newly formed immature particle is covered with 60 spikes composed of
CC heterodimer between precursor prM and envelope protein E. The virion is
CC transported to the Golgi apparatus where the low pH causes dissociation
CC of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC inefficient, and many virions are only partially matured. These
CC uncleaved prM would play a role in immune evasion.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi. Interacts with protein prM. Interacts with non-structural
CC protein 1. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC {ECO:0000255}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: [Envelope protein E]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC performed by host signal peptidase, wereas cleavages in the cytoplasmic
CC side are performed by serine protease NS3. Signal cleavage at the 2K-4B
CC site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- MISCELLANEOUS: Isolate M3 comes from a patient with dengue fever.
CC -!- WEB RESOURCE: Name=Virus Pathogen Resource;
CC URL="https://www.viprbrc.org/brc/home.spg?decorator=flavi_dengue";
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DR EMBL; X15214; CAA33284.1; -; Genomic_RNA.
DR PIR; S06740; S06740.
DR SMR; P14339; -.
DR PRIDE; P14339; -.
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:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; 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: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; 1.20.1280.260; -; 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; IPR013755; Flav_gly_cen_dom_subdom1.
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; 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; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PE 3: Inferred from homology;
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; Suppressor of RNA silencing; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Viral nucleoprotein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc.
FT CHAIN <1..>495
FT /note="Genome polyprotein"
FT /id="PRO_0000405209"
FT CHAIN 1..495
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000037916"
FT TOPO_DOM 1..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..>495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 98..111
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 3..30
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 60..121
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 74..105
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 92..116
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 185..285
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 302..333
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT NON_TER 1
FT NON_TER 495
SQ SEQUENCE 495 AA; 54120 MW; 009C7AB4EDCB9526 CRC64;
MRCIGISNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFEVIKTEA KQPATLRKSC
FEAKLTNTTT ESRCPTLGEP SLNEEQDKRL VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
CKKNMEGKFV HPENLEYTIV ITPHSGEEHA VGNDTGKHGK ELKITPQSSI TEAELTGYGT
VTMQCSPRTG LDFNEIVLLQ MEDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF
KNPHAKKQDV VVLGSQEGAM QTALTGAAEI QMSSGNLLFT GHLKCRLRMD KLQLKGISYS
MCTGKFKIVK EFAETQHGTI VIRVQYEGDG SPCKIPFEII DLEKRHVLGC LITVYPIVTE
KDSPVNIEAD PPFGDSYIII GIEPGQLKLH WLKKGSSIGQ MFETTMRGAK RMAILGDTAW
DFGSLGGVFT SIGKALNQVF GTIYGAAFSG VSWTMKILIG VIITCIGMNS RSTSLSVSLV
LVGVVTLYLG GMVHA
