ID   GP_BUNGE                Reviewed;        1437 AA.
AC   P12430;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   08-NOV-2023, entry version 99.
DE   RecName: Full=Envelopment polyprotein;
DE   AltName: Full=M polyprotein;
DE   Contains:
DE     RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P04505};
DE              Short=Gn;
DE     AltName: Full=Glycoprotein G2;
DE   Contains:
DE     RecName: Full=Non-structural protein M {ECO:0000250|UniProtKB:P04505};
DE              Short=NSm;
DE   Contains:
DE     RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P04505};
DE              Short=Gc;
DE     AltName: Full=Glycoprotein G1;
DE   Flags: Precursor;
GN   Name=GP;
OS   Bunyavirus germiston.
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus;
OC   Orthobunyavirus bunyamweraense.
OX   NCBI_TaxID=11574;
OH   NCBI_TaxID=53527; Culex.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3176688; DOI=10.1016/0168-1702(88)90068-8;
RA   Pardigon N., Vialat P., Gerbaud S., Girard M., Bouloy M.;
RT   "Nucleotide sequence of the M segment of Germiston virus: comparison of the
RT   M gene product of several bunyaviruses.";
RL   Virus Res. 11:73-85(1988).
CC   -!- FUNCTION: Glycoprotein C and Glycoprotein N 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   -!- SUBUNIT: Glycoprotein C and Glycoprotein N 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 C and
CC       Glycoprotein N 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 (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000250}.
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}.
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; M21951; AAA42778.1; -; Genomic_RNA.
DR   PIR; S07430; S07430.
DR   SMR; P12430; -.
DR   GlyCosmos; P12430; 4 sites, No reported glycans.
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   3: Inferred from homology;
KW   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; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1437
FT                   /note="Envelopment polyprotein"
FT                   /id="PRO_0000036786"
FT   CHAIN           22..306
FT                   /note="Glycoprotein N"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036787"
FT   CHAIN           307..481
FT                   /note="Non-structural protein M"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036788"
FT   CHAIN           482..1437
FT                   /note="Glycoprotein C"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036789"
FT   TOPO_DOM        22..207
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..373
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..1391
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1392..1412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1413..1437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   SITE            481..482
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        627
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1173
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1437 AA;  162494 MW;  C4FB3001BD09A30D CRC64;
     MAISTSLLIV ALLIKLCLVN TAPPISKCFQ DGILIAELKS SSGISEFCIK DDISILKSEI
     TYSKNDTGIF MHSKVFRHWT VADWKQCNHT SAGGSTNVLE VDKNLNLVAK NYMCTRPCVI
     TIDKENAQLL FQTEQLNQFE VTGTTISTGW FKSKTSVSLD NTCEHIKVTC GKKSLQFHAC
     FKQHMSCVRF LHRSVLPGYM ASSICQNIEL IIIIILTLAI FIFMCIITRT YICYLMLPLF
     APIAYLYGWL YNRSCKKCIC CGLAYHPFTN CGSYCVCGSR FETSDRMRLH RESGLCQGFK
     SLRVARSLCK SKGSSLVISI LTAMLILSFI TPLEAMTTNY PDDKKFTLKE VNDIVLGRDM
     EQELKSSILI LMSICGIGII LIFFGLTVLL EIVLELIAKR STIFCKECNL IHDKKSMTYR
     GDFTNKCGFC PCGELEDPEG LVIHTTRKSC TYYIKIRNLK LIMLIFSIVI LMQNATMLVV
     AGENCWTNTE IKADCVGPLI GPSACTNKGS KTYKTVAQEL VTASKITQLD ADKYVLLGDT
     IESALDAITS QKHYSAMHLL ETMFLMKHCD YYKVYEHNSG YSQTKWRLIA IANSFDICTN
     TPTPNFCKCL SDSSCSTTTL NFATSMNATY TSKVEFFNHD FTLFLDIFEA AFPGSATAFL
     FKKIKEKNPY QAFEMMGKIA NKYPNNKLLV VILKYGQYMV GLSHASTYQL KQEWVAKSLS
     LTRAQRTGLK MSMANAEPGP ATKECSDAKT IACLTPKFQV EVNNLMSCGA SPNFKIYVKT
     GELYKAHDRN SVWCLNDMHC LTPYTPANAE IITTMKKMDC WQDNPKQPTD EYAIPKRSCQ
     MKDRGLCNSG ADKWKIIKCD NHKLFYTDAL ERRDPASIVG SNHCFSEKCQ IERYPINPTS
     LTNCEWLYRA VRPEYIKKLS LQTIEEYKKA IADKLTHTLQ LYHFAPLLEN LPHIKPTYKY
     ITAQGTYTAD GIEGASITTS IPALSGTSVG FKINAKDGTD LLDIVVYIKA SVVKSIYNHI
     YDTGPTININ SKHDELCTGQ CPKKIPADPN WLTFSQERTS RWGCEEFGCL AINTGCVYGS
     CQDVIRTETK VYRKANEETV MLTVCITYPG HTFCTDVNAH EPKITDELEL QFKTIDIKSL
     PNLVAVTNHK LYTGQINDLG TFGQMCGNVQ KTNTSHTGAG TPKFDYTCYS ASRKDIIIRR
     CYNNNYDSCR LLNQESDLLF DDNHETLVVY NNKRLNGELA LKLLLGDIQY KLYTENMELE
     LEAKCVGCVG CFESYQCNLQ ITSSLDETAL YLVPVSHFHD RIQIKTTKKD YAMKISCTRD
     PGDKASFRVC GKSYDFNFHT VPKNDKIEVN VGDETSYIKE KDNRCGRWLC RVRDEGLSVI
     FEPLNNFFGN YLNMFLYILG GIILLFLALY ILMPMCARLR DELKRNERLH QMEMKKR
//