GP_BUNYW
ID GP_BUNYW Reviewed; 1433 AA.
AC P04505;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000305|PubMed:17609275};
DE Short=Gn;
DE AltName: Full=Glycoprotein G2;
DE Contains:
DE RecName: Full=Non-structural protein M;
DE Short=NSm;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000305|PubMed:17609275};
DE Short=Gc;
DE AltName: Full=Glycoprotein G1;
DE Flags: Precursor;
GN Name=GP;
OS Bunyamwera virus (BUNV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus.
OX NCBI_TaxID=35304;
OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3753629; DOI=10.1016/0042-6822(86)90398-3;
RA Lees J.F., Pringle C.R., Elliott R.M.;
RT "Nucleotide sequence of the Bunyamwera virus M RNA segment: conservation of
RT structural features in the Bunyavirus glycoprotein gene product.";
RL Virology 148:1-14(1986).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=7996137; DOI=10.1099/0022-1317-75-12-3441;
RA Lappin D.F., Nakitare G.W., Palfreyman J.W., Elliott R.M.;
RT "Localization of Bunyamwera bunyavirus G1 glycoprotein to the Golgi
RT requires association with G2 but not with NSm.";
RL J. Gen. Virol. 75:3441-3451(1994).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15367646; DOI=10.1128/jvi.78.19.10793-10802.2004;
RA Shi X., Lappin D.F., Elliott R.M.;
RT "Mapping the Golgi targeting and retention signal of Bunyamwera virus
RT glycoproteins.";
RL J. Virol. 78:10793-10802(2004).
RN [4]
RP TOPOLOGY (NON-STRUCTURAL PROTEIN M), AND FUNCTION (NON-STRUCTURAL PROTEIN
RP M).
RX PubMed=16873265; DOI=10.1128/jvi.00579-06;
RA Shi X., Kohl A., Leonard V.H., Li P., McLees A., Elliott R.M.;
RT "Requirement of the N-terminal region of orthobunyavirus nonstructural
RT protein NSm for virus assembly and morphogenesis.";
RL J. Virol. 80:8089-8099(2006).
RN [5]
RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=17609275; DOI=10.1128/jvi.00573-07;
RA Shi X., Kohl A., Li P., Elliott R.M.;
RT "Role of the cytoplasmic tail domains of Bunyamwera orthobunyavirus
RT glycoproteins Gn and Gc in virus assembly and morphogenesis.";
RL J. Virol. 81:10151-10160(2007).
CC -!- FUNCTION: Glycoprotein N and Glycoprotein C interact with each other
CC and are present at the surface of the virion. They are able to attach
CC the virion to a cell receptor and to promote fusion of membranes after
CC endocytosis of the virion (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Non-structural protein M]: Plays a role virion budding at
CC Golgi tubes and in subcellular location of Glycoprotein C protein.
CC {ECO:0000269|PubMed:16873265}.
CC -!- SUBUNIT: Glycoprotein N and Glycoprotein C interact with each other.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Glycoprotein C
CC alone is retained in the membrane of the endoplasmic reticulum, but not
CC transported to the Golgi. Coexpression of Glycoprotein N and
CC Glycoprotein C results in efficient transport of Glycoprotein C to the
CC Golgi complex, indicating that their interaction is essential for
CC proper targeting to this organelle, where virion budding occurs.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Glycoprotein N is retained in the Golgi complex
CC through a Golgi retention signal, which resides in the Glycoprotein N
CC transmembrane region.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein M]: Host Golgi apparatus
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC including nonstructural protein NSm, Glycoprotein C, and Glycoprotein
CC N.
CC -!- SIMILARITY: Belongs to the orthobunyavirus envelope glycoprotein
CC family. {ECO:0000305}.
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DR EMBL; M11852; AAA42777.1; -; Genomic_RNA.
DR PIR; A04101; GNVUBW.
DR RefSeq; NP_047212.1; NC_001926.1.
DR PDB; 6H3V; X-ray; 2.90 A; A=478-721.
DR PDBsum; 6H3V; -.
DR SMR; P04505; -.
DR DIP; DIP-404N; -.
DR GeneID; 2648216; -.
DR KEGG; vg:2648216; -.
DR Proteomes; UP000002476; 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:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR005167; Bunya_G1.
DR InterPro; IPR005168; Bunya_G2.
DR InterPro; IPR026400; Bunya_nonstruc_pro_NSm.
DR InterPro; IPR014413; M_poly_OrthobunV.
DR Pfam; PF03557; Bunya_G1; 1.
DR Pfam; PF03563; Bunya_G2; 1.
DR PIRSF; PIRSF003944; M_poly_OrthobunV; 1.
DR TIGRFAMs; TIGR04210; bunya_NSm; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..16
FT CHAIN 17..1433
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036798"
FT CHAIN 17..302
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036799"
FT CHAIN 303..477
FT /note="Non-structural protein M"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036800"
FT CHAIN 478..1433
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036801"
FT TOPO_DOM 17..203
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..369
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..1387
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1388..1408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1409..1433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 477..478
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1169
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:6H3V"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 509..518
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 524..529
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 537..546
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 550..563
FT /evidence="ECO:0007829|PDB:6H3V"
FT TURN 565..568
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 580..588
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 592..596
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 601..605
FT /evidence="ECO:0007829|PDB:6H3V"
FT TURN 606..609
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 620..629
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 631..648
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 652..662
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 670..679
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 684..698
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 700..704
FT /evidence="ECO:0007829|PDB:6H3V"
FT HELIX 709..714
FT /evidence="ECO:0007829|PDB:6H3V"
SQ SEQUENCE 1433 AA; 162078 MW; CD61ABDE782018E0 CRC64;
MRILILLLAV TQLAVSSPVI TRCFHGGQLI AERKSQTSIS EFCIKDDVSM LKSEIVYTKN
DTGIFGHSKV FRHWTITDWK ACNPVVTAGG SINVIEVDKN LNLVTRNYVC TGDCTITVDR
KNAQIIFQTD KLNHFEVTGT TISTGWFKSK ASVTLDRTCE HIKVSCGKKT LQFHACFKQH
MSCVRFLHRS ILPGSMAISI CQNIELIIIT ILALCIFIIM IILTKTYICY VLIPVFMPIA
FAYGWAYNRS CKKCTCCGLA YHPFTNCGSY CVCGSKFETS DRMRMHRESG LCQGFKSLRV
ARRLCKSKGS SLIISILLSV LILSFVTPIE GTLTNYPTDQ KYTLDEIADV LQAKTHEDST
KYYIILYTSL FGAGLTIIFA GVALGLTIIL EVLTKINVIF CNECNMYHSK KSIKYVGDFT
NKCGFCTCGL LEDPEGVVVH KAKKSCTYSY QINWVRGIMI FVAFLFVIQN TIIMVAAEED
CWKNEELKED CVGPLIAPKD CTDKDHKTYL SEASLLATAK KITQVDAENV EILGKTMESA
IRVIERQKTY HRMHLLEAVF LNKHCDYYKM FEHNSGYSQV KWRMMIKTQH FDICALQANS
PFCAQCIADN SCAQGSWEFD THMNSTYSSK VDNFKHDFSL FLRIFEAAFP GTAYVHLLTN
IKEKKPYQAV SMIEKIKKKF PNNKLLIGYL DFGKYLLGLS HASTYELQQR QLDKLYQPTE
LTRSGGQQTS LANSVVGQAT KECKKYKDVS CLSPRFGIPL EDLISCCDQP NYNIYKKPKK
VYKAHDKEET WCINDQHCLV DFVPAEADTV EKLKPMKCWL VDPGKNDDVY SIAIKTCRVV
DKGVCTVNSQ KWNIIKCDSG PLYYSDHIPG EDTGNDIGHY CVSAGCKTDR YPINPDVVTD
CVWEFTSRKS QYIGKISMQS LEDYEKALTD RLTHTLETYS FAPLENLPHI KPVYKYITAQ
GVENSDGIEG AFITASIPAA GGTSIGYNVR SKDGFPLLDL IVFVKSAVIK STYNHIYDTG
PTISINTKHD EHCTGQCPSN IEHEANWLTF SQERTSRWGC EEFGCLAVNT GCVFGSCQDV
IRPETKVYRK AVDEVVILTV CITYPGHTFC TEINAIEPKI TEEIELQFKT VDTKTLPYIV
AVNNHKLYSG QINDLGTFGQ MCGNVQKTNS SILGTGTPKF DYTCHGASRK DIIVRRCYNN
NFDSCKLLKE ETQLIFNDDH DTITVYNTNH LIGELAIKLI LGDIQYKLFT ETLDLQIDAK
CVGCPDCFES YSCNFQIVSN IDTICSLEGP CDTFHNRISI KAMQQNYAVK LSCQKDPRPS
GTFKICNREY TVVFHTVAKD DKIEINVGDQ TSFIKEKDDR CKTWLCRVRD EGISVIFEPI
KAFFGSYFSI FFYIIVVVVV GFLIIYIFMP MFMKLKEVLK ANEKLYLQEI KQK
