POLG_DEN22
ID POLG_DEN22 Reviewed; 495 AA.
AC P14338;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 07-OCT-2020, entry version 121.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Envelope protein E;
DE Flags: Fragment;
OS Dengue virus type 2 (isolate Malaysia M2) (DENV-2).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=11062;
OH NCBI_TaxID=53540; Aedimorphus.
OH NCBI_TaxID=53539; Diceromyia.
OH NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=53541; Stegomyia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2587243; DOI=10.1093/nar/17.21.8888;
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 shock syndrome.";
RL Nucleic Acids Res. 17:8888-8888(1989).
RN [2]
RP FUNCTION (ENVELOPE PROTEIN E).
RX PubMed=19295646; DOI=10.1139/w08-107;
RA Peng T., Wang J.L., Chen W., Zhang J.L., Gao N., Chen Z.T., Xu X.F.,
RA Fan D.Y., An J.;
RT "Entry of dengue virus serotype 2 into ECV304 cells depends on clathrin-
RT dependent endocytosis, but not on caveolae-dependent endocytosis.";
RL Can. J. Microbiol. 55:139-145(2009).
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, ECO:0000269|PubMed:19295646}.
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, ECO:0000255|PROSITE-ProRule:PRU00860};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC envelope protein E contain an endoplasmic reticulum retention signal.
CC {ECO:0000250|UniProtKB:P17763}.
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 -!- PTM: Non-structural protein 1: N-glycosylated. The excreted form is
CC glycosylated and this is required for efficient secretion of the
CC protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC -!- MISCELLANEOUS: Isolate M2 comes from a patient with dengue shock
CC syndrome.
CC -!- WEB RESOURCE: Name=Virus Pathogen Resource;
CC URL="https://www.viprbrc.org/brc/home.spg?decorator=flavi_dengue";
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; X15433; CAA33474.1; -; Genomic_RNA.
DR PIR; S06741; S06741.
DR SMR; P14338; -.
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_0000405208"
FT CHAIN 1..495
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000037915"
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; 54326 MW; 02FCBACC8CB6721E CRC64;
MRCIGISNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC
IEAKLTNTTT ESRCPTQGEP SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
CQKNMEGKIV QPENLEYTIV VTPHSGEEHA VGNDTGKHGK EIKITPQSSI TEAELTGYGT
VTMDCSPRTG LDFNEMVLLQ MENKAWLVHR QWFLDLPLPW LPGADTQGSK LDQKETLVTF
KNPHAKKQDV VVLGSQEGAM HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS
MCTGKFKVVE EIAETQHGTI VIRVQYEGDG SPCKIPLEIM DLDNRHVLGR LITVNPIVTE
KDSPVNVEAE PPLGDSYIII GVEPGQLKLN WFKKGSSIGQ MFETTMIRAK RMAILGDTAW
DFRSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV
LVGIVTLYLG VMVQA
