GP_BHAV
ID GP_BHAV Reviewed; 1070 AA.
AC L7V0S7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P21401};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P21401};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Bhanja virus (BHAV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Bandavirus; Bhanja bandavirus.
OX NCBI_TaxID=1213620;
OH NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH NCBI_TaxID=9368; Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog).
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9858; Capreolus capreolus (European roe deer).
OH NCBI_TaxID=49202; Dermacentor marginatus (Ornate sheep tick) (Acarus marginatus).
OH NCBI_TaxID=1027255; Haemaphysalis intermedia.
OH NCBI_TaxID=49204; Haemaphysalis punctata.
OH NCBI_TaxID=490559; Haemaphysalis sulcata.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=572043; Hyalomma detritum.
OH NCBI_TaxID=34626; Hyalomma dromedarii (Camel tick).
OH NCBI_TaxID=34627; Hyalomma marginatum.
OH NCBI_TaxID=72855; Hyalomma truncatum.
OH NCBI_TaxID=34613; Ixodes ricinus (Common tick) (Acarus ricinus).
OH NCBI_TaxID=59656; Ixodes vespertilionis.
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=34611; Rhipicephalus annulatus.
OH NCBI_TaxID=34631; Rhipicephalus appendiculatus (Brown ear tick).
OH NCBI_TaxID=67831; Rhipicephalus bursa (Tick).
OH NCBI_TaxID=60189; Rhipicephalus decoloratus (African blue tick) (Boophilus decoloratus).
OH NCBI_TaxID=136141; Rhipicephalus geigyi.
OH NCBI_TaxID=34632; Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
OH NCBI_TaxID=327507; Xerus erythropus (Striped ground squirrel).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=Isolate Rhipicephalus decoloratus/Nigeria/ibAr2709/1968
RC {ECO:0000305};
RX PubMed=23325688; DOI=10.1128/jvi.02845-12;
RA Matsuno K., Weisend C., Travassos da Rosa A.P., Anzick S.L., Dahlstrom E.,
RA Porcella S.F., Dorward D.W., Yu X.J., Tesh R.B., Ebihara H.;
RT "Characterization of the Bhanja serogroup viruses (Bunyaviridae): a novel
RT species of the genus Phlebovirus and its relationship with other emerging
RT tick-borne phleboviruses.";
RL J. Virol. 87:3719-3728(2013).
CC -!- FUNCTION: [Glycoprotein N]: Structural component of the virion that
CC interacts with glycoprotein C (By similarity). It shields the
CC hydrophobic fusion loops of the glycoprotein C, preventing premature
CC fusion (By similarity). The glycoprotein protrusions are arranged on an
CC icosahedral lattice, with T=12 triangulation (By similarity). They are
CC able to attach the virion to the host cell receptor CD209/DC-SIGN and
CC to promote fusion of membranes with the late endosome after endocytosis
CC of the virion (By similarity). Plays a role in the packaging of
CC ribonucleoproteins during virus assembly (By similarity).
CC {ECO:0000250|UniProtKB:J3WAX0, ECO:0000250|UniProtKB:P03518,
CC ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401}.
CC -!- FUNCTION: [Glycoprotein C]: Structural component of the virion that
CC interacts with glycoprotein N (By similarity). Acts as a class II
CC fusion protein that is activated upon acidification and subsequent
CC repositioning of the glycoprotein N (By similarity). The glycoprotein
CC protrusions are arranged on an icosahedral lattice, with T=12
CC triangulation (By similarity). They are able to attach the virion to
CC the host cell receptor CD209/DC-SIGN and to promote fusion of membranes
CC with the late endosome after endocytosis of the virion (By similarity).
CC {ECO:0000250|UniProtKB:J3WAX0, ECO:0000250|UniProtKB:P03518,
CC ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401}.
CC -!- SUBUNIT: [Glycoprotein N]: Heterodimer with glycoprotein C.
CC {ECO:0000250|UniProtKB:P03518}.
CC -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein N (By
CC similarity). Homotrimer (postfusion) (By similarity).
CC {ECO:0000250|UniProtKB:J3WAX0, ECO:0000250|UniProtKB:P03518}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P03518}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N
CC and Glycoprotein C is essential for proper targeting of Glycoprotein C
CC to the Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P03518}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N
CC and Glycoprotein C is essential for proper targeting of Glycoprotein C
CC to the Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- DOMAIN: [Glycoprotein N]: Contains a Golgi retention signal on its C-
CC terminus. The cytoplasmic tail specifically interacts with the
CC ribonucleoproteins and is critical for genome packaging.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo
CC yield mature proteins Glycoprotein C, and Glycoprotein N.
CC {ECO:0000250|UniProtKB:P21401}.
CC -!- PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- MISCELLANEOUS: The sequence shown is that of isolate Human/United
CC States/1/2009. {ECO:0000305}.
CC -!- MISCELLANEOUS: Terminal conserved complementary sequences assemble as a
CC 'panhandle structure' in each genome segment.
CC {ECO:0000269|PubMed:23325688}.
CC -!- SIMILARITY: Belongs to the phlebovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; JX961617; AGC60116.1; -; Genomic_RNA.
DR RefSeq; YP_009141014.1; NC_027141.1.
DR GeneID; 24404825; -.
DR KEGG; vg:24404825; -.
DR Proteomes; UP000202403; Genome.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR043603; Phlebo_G2_C.
DR InterPro; IPR010826; Phlebovirus_G1.
DR InterPro; IPR009878; Phlebovirus_G2_fusion.
DR Pfam; PF19019; Phlebo_G2_C; 1.
DR Pfam; PF07243; Phlebovirus_G1; 1.
DR Pfam; PF07245; Phlebovirus_G2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1070
FT /note="Envelopment polyprotein"
FT /id="PRO_0000455550"
FT CHAIN 18..549
FT /note="Glycoprotein N"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455551"
FT PROPEP 550..560
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT /id="PRO_0000455552"
FT CHAIN 561..1070
FT /note="Glycoprotein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455553"
FT TOPO_DOM 18..457
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT TOPO_DOM 550..1023
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1024..1044
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1045..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 480..522
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 541..560
FT /note="Internal signal sequence for glycoprotein C"
FT /evidence="ECO:0000303|PubMed:23325688"
FT REGION 648..654
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT REGION 690..701
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT SITE 560..561
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT SITE 1068
FT /note="Important for glycoprotein C and glycoprotein N
FT subcellular location"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 22..55
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 152..165
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 211..221
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 267..309
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 296..301
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 353..356
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 360..429
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 380..385
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 561..602
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 574..584
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 642..831
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 648..696
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 654..703
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 659..685
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 689..694
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 799..813
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 896..966
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 906..909
FT /evidence="ECO:0000250|UniProtKB:P21401"
SQ SEQUENCE 1070 AA; 118551 MW; 1ABE4FCE2CC9ABC3 CRC64;
MMFSRVMQLA LICAVTCEDN PCLWERFTNS RDIEFMIPVV NLSTSRRLSM SQRICMVSMG
KHWSRIFSEG EEDRGMKDLD PLLMSSLNWR GTAKTRSSNS FNFDILDGIF LGFLDLVKWG
EEADRHTPIH PECIKSKVCG FMTASGPRIK TCTGKFRGAD RHGHCTNRAT PHEATNVISV
GVQHAQEANQ VDEHEARYIS EARKSINPEI CSIDGVEINQ CDLASPGRWL MLHYASFRLQ
EGSLVYLSPG LNIKWSQINV PASDFYCINV SDHLNTHYRP CEVNCTDNCQ GDELYCSVHQ
CARSAECKCS FIGSRGMAEV QIGDRWFKPA VVGSQQFFVK EDVPVLQQPS ADCTTCSMTC
TAEGIAISSI KDELKDVTVC VEGFCSTRVS KGSKVWKIEF HNQYPSSGSV ALARGTTVSG
ETFELTAECG RRTGCEQINC LFCREMLSNP QCYPYGKWFL LFLILATLYI IVALLKTIMR
IFMACLSVLY GPFIIIIKIS RCLGRLGKRK GERTYVRLME ALDDERKPEV VRAPVSLGRT
KQPRIVLFIV LALLVHMALC CDESRLVEET SVTCNPGPDN IFSCSTKEMI TVKELRAGKT
ICVSLKGPGG SLSSPIKIKM LDIVGRSDLL DIYFTFNGHA NCKSVRRCRW AGSCGNSGCL
GVGKEDYDRE LGDQESSLHP NWRDCYDGCG GAACGCFNAA PSCIFLKRYV TNADSRVFKV
FKPSAWFLST KIVVETTSHK EDVTLKSGEA KVIDKVSFHY RTDKNLFAGM SIPPIVTEVK
REGKPLSFFL ENQGQHPKCK DENSARTSSA SNCIVDQNTI SANVRVDDVS CRSNLVSISG
MSTLKPLPQR VGDFLIQLHN DEPVLLATGD SGVVEGELQI DLSHKKISIK VDTTVCRGTV
KELKGCVGCT KGAFASLEIH STSAGSASLQ CSLSSCYMEV QKGVNNVNCS LRFSKAVVEE
TCVLACSGSK EQLSIKGNLI IGGDFKKLTE DSATSFSHTD SKDTRIHLQT GLMNWLDTLF
GASLLGKILG IGLAILSPFI LILILRWILR VVLRRSRIRR EPKYEMAKYS
