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   08-NOV-2023, entry version 116.
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;
OC   Orthobunyavirus bunyamweraense.
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   GlyCosmos; P04505; 3 sites, No reported glycans.
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:0016020; C: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: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   NCBIfam; TIGR04210; bunya_NSm; 1.
DR   Pfam; PF03557; Bunya_G1; 1.
DR   Pfam; PF03563; Bunya_G2; 1.
DR   PIRSF; PIRSF003944; M_poly_OrthobunV; 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
//