ID   GP_SBVBH                Reviewed;        1403 AA.
AC   H2AM12;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   08-NOV-2023, entry version 40.
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   Bovine Schmallenberg virus (isolate Bovine/BH80/Germany/2011) (SBV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus;
OC   Orthobunyavirus schmallenbergense.
OX   NCBI_TaxID=1318464;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=22376991; DOI=10.3201/eid1803.111905;
RA   Hoffmann B., Scheuch M., Hoper D., Jungblut R., Holsteg M., Schirrmeier H.,
RA   Eschbaumer M., Goller K.V., Wernike K., Fischer M., Breithaupt A.,
RA   Mettenleiter T.C., Beer M.;
RT   "Novel orthobunyavirus in cattle, europe, 2011.";
RL   Emerg. Infect. Dis. 18:469-472(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Hoeper D.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Germany;
RX   PubMed=23326235; DOI=10.1371/journal.ppat.1003133;
RA   Varela M., Schnettler E., Caporale M., Murgia C., Barry G., McFarlane M.,
RA   McGregor E., Piras I.M., Shaw A., Lamm C., Janowicz A., Beer M., Glass M.,
RA   Herder V., Hahn K., Baumgartner W., Kohl A., Palmarini M.;
RT   "Schmallenberg virus pathogenesis, tropism and interaction with the innate
RT   immune system of the host.";
RL   PLoS Pathog. 9:E1003133-E1003133(2013).
RN   [4]
RP   DISULFIDE BOND, MUTAGENESIS OF CYS-580 AND CYS-589, AND GLYCOSYLATION AT
RP   ASN-40; ASN-493; ASN-686 AND ASN-1353.
RX   PubMed=28640745; DOI=10.1099/jgv.0.000810;
RA   Roman-Sosa G., Karger A., Kraatz F., Aebischer A., Wernike K., Maksimov P.,
RA   Lillig C.H., Reimann I., Brocchi E., Keller M., Beer M.;
RT   "The amino terminal subdomain of glycoprotein Gc of Schmallenberg virus:
RT   disulfide bonding and structural determinants of neutralization.";
RL   J. Gen. Virol. 98:1259-1273(2017).
RN   [5] {ECO:0007744|PDB:6H3S, ECO:0007744|PDB:6H3T, ECO:0007744|PDB:6H3U}
RP   X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 465-874, FUNCTION (GLYCOPROTEIN
RP   C), AND SUBUNIT (GLYCOPROTEIN C).
RX   PubMed=30787296; DOI=10.1038/s41467-019-08832-8;
RA   Hellert J., Aebischer A., Wernike K., Haouz A., Brocchi E., Reiche S.,
RA   Guardado-Calvo P., Beer M., Rey F.A.;
RT   "Orthobunyavirus spike architecture and recognition by neutralizing
RT   antibodies.";
RL   Nat. Commun. 10:879-879(2019).
CC   -!- FUNCTION: [Glycoprotein N]: Glycoprotein C and glycoprotein N interact
CC       with each other and are present at the surface of the virion (By
CC       similarity). Glycoprotein N probably locks the Gn-Gc complex in a
CC       prefusion state (By similarity). Glycoprotein N and glycoprotein C are
CC       able to attach the virion to host cell receptors (By similarity). This
CC       attachment induces virion internalization predominantly through
CC       clathrin-dependent endocytosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- FUNCTION: [Glycoprotein C]: Glycoprotein C and glycoprotein N interact
CC       with each other and are present at the surface of the virion (By
CC       similarity). The spikes at the surface of the virion are formed by an
CC       N-terminal extension of glycoprotein C (PubMed:30787296). Glycoprotein
CC       N and glycoprotein C are able to attach the virion to host cell
CC       receptors (By similarity). This attachment induces virion
CC       internalization predominantly through clathrin-dependent endocytosis
CC       (By similarity). Class II fusion protein that promotes fusion of viral
CC       membrane with host endosomal membrane after endocytosis of the virion
CC       (By similarity). Exposure to potassium is necessary for the
CC       conformational change leading to fusion (By similarity).
CC       {ECO:0000250|UniProtKB:A6XIP3, ECO:0000250|UniProtKB:Q8JSZ3,
CC       ECO:0000269|PubMed:30787296}.
CC   -!- SUBUNIT: [Glycoprotein N]: Heterodimer with glycoprotein C; in
CC       prefusion state. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein N; in
CC       prefusion state (By similarity). Homotrimeric; in postfusion state
CC       (Probable). {ECO:0000250|UniProtKB:Q8JSZ3,
CC       ECO:0000305|PubMed:30787296}.
CC   -!- SUBCELLULAR LOCATION: [Envelopment polyprotein]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavage by host
CC       MBTPS1/S1P/SKI-1 endopeptidase yield glycoprotein N. Specific enzymatic
CC       cleavages by host furin-like protease and MBTPS1/S1P endopeptidase
CC       yield GP38. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SIMILARITY: Belongs to the nairovirus envelope glycoprotein family.
CC       {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; JX853180; AGC84161.1; -; Viral_cRNA.
DR   EMBL; HE649913; CCF55030.1; -; Genomic_RNA.
DR   PDB; 6H3S; X-ray; 2.02 A; A/B=465-874.
DR   PDB; 6H3T; X-ray; 2.84 A; A/B=465-702.
DR   PDB; 6H3U; X-ray; 3.17 A; A/B=465-702.
DR   PDB; 7A56; X-ray; 1.85 A; A=881-1306.
DR   PDBsum; 6H3S; -.
DR   PDBsum; 6H3T; -.
DR   PDBsum; 6H3U; -.
DR   PDBsum; 7A56; -.
DR   SMR; H2AM12; -.
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   NCBIfam; TIGR04210; bunya_NSm; 1.
DR   Pfam; PF03557; Bunya_G1; 1.
DR   Pfam; PF03563; Bunya_G2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 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 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..1403
FT                   /note="Envelopment polyprotein"
FT                   /id="PRO_0000422470"
FT   CHAIN           18..308
FT                   /note="Glycoprotein N"
FT                   /id="PRO_0000422471"
FT   CHAIN           309..466
FT                   /note="Non-structural protein M"
FT                   /id="PRO_0000422472"
FT   CHAIN           467..1403
FT                   /note="Glycoprotein C"
FT                   /id="PRO_0000422473"
FT   TOPO_DOM        18..209
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..314
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        336..361
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..448
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        470..1361
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1362..1382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1383..1403
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   CARBOHYD        686
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   CARBOHYD        1353
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        471..487
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   DISULFID        523..550
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   DISULFID        580..589
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   DISULFID        591..598
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   MUTAGEN         580
FT                   /note="C->S: Loss of disulfide bond; when associated with
FT                   S-589."
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   MUTAGEN         589
FT                   /note="C->S: Loss of disulfide bond; when associated with
FT                   S-580."
FT                   /evidence="ECO:0000269|PubMed:28640745"
FT   STRAND          471..473
FT                   /evidence="ECO:0007829|PDB:6H3T"
FT   HELIX           476..478
FT                   /evidence="ECO:0007829|PDB:6H3T"
FT   HELIX           481..484
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           485..487
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           489..492
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           501..504
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           505..507
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           510..517
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   TURN            523..525
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           526..532
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           536..549
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           551..555
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           556..558
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          559..561
FT                   /evidence="ECO:0007829|PDB:6H3T"
FT   HELIX           563..565
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           566..574
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           578..580
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           587..594
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           598..600
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   TURN            601..605
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           606..613
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           617..631
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   TURN            632..634
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           638..649
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           652..655
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           656..662
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           663..665
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   TURN            666..668
FT                   /evidence="ECO:0007829|PDB:6H3U"
FT   HELIX           670..683
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           699..703
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          719..731
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          733..736
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          740..745
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          748..751
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          757..759
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          766..771
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           783..786
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          788..793
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   TURN            801..803
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          806..819
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          822..829
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          834..836
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          842..844
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          847..854
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   HELIX           866..868
FT                   /evidence="ECO:0007829|PDB:6H3S"
FT   STRAND          887..889
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   HELIX           892..909
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          913..915
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          930..936
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          939..949
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          955..961
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          967..990
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          993..1006
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1019..1028
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1039..1052
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1056..1061
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1066..1075
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1078..1083
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1093..1100
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1109..1114
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1117..1123
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1131..1133
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1135..1139
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1142..1144
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1150..1154
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1157..1159
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1162..1169
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   HELIX           1174..1177
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1185..1187
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1194..1197
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1204..1213
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1215..1219
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1225..1234
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1242..1265
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1267..1271
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1277..1283
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1291..1295
FT                   /evidence="ECO:0007829|PDB:7A56"
FT   STRAND          1298..1302
FT                   /evidence="ECO:0007829|PDB:7A56"
SQ   SEQUENCE   1403 AA;  158806 MW;  90B360E3EE5BA3E5 CRC64;
     MLLNIVLISN LACLAFALPL KEGTRGSRCF LNGELVKTVN TSKVVSECCV KDDISIIKSN
     AEHYKSGDRL AAVIKYYRLY QVKDWHSCNP IYDDHGSFMI LDIDNTGTLI PKMHTCRVEC
     EIALNKDTGE VILNSYRINH YRISGTMHVS GWFKNKIEIP LENTCESIEV TCGLKTLNFH
     ACFHTHKSCT RYFKGSILPE LMIESFCTNL ELILLVTFIL VGSVMMMILT KTYIVYVFIP
     IFYPFVKLYA YMYNKYFKLC KNCLLAVHPF TNCPSTCICG MIYTTTESLK LHRMCNNCSG
     YKALPKTRKL CKSKISNIVL CVITSLIFFS FITPISSQCI DIEKLPDEYI TCKRELANIK
     SLTIDDTYSF IYSCTCIIVL ILLKKAAKYI LYCNCSFCGM VHERRGLKIM DNFTNKCLSC
     VCAENKGLTI HRASEKCLFK FESSYNRTGL IIFMLLLVPT IVMTQETSIN CKNIQSTQLT
     IEHLSKCMAF YQNKTSSPVV INEIISDASV DEQELIKSLN LNCNVIDRFI SESSVIETQV
     YYEYIKSQLC PLQVHDIFTI NSASNIQWKA LARSFTLGVC NTNPHKHICR CLESMQMCTS
     TKTDHAREMS IYYDGHPDRF EHDMKIILNI MRYIVPGLGR VLLDQIKQTK DYQALRHIQG
     KLSPKSQSNL QLKGFLEFVD FILGANVTIE KTPQTLTTLS LIKGAHRNLD QKDPGPTPIL
     VCKSPQKVVC YSPRGVTHPG DYISCKSKMY KWPSLGVYKH NRDQQQACSS DTHCLEMFEP
     AERTITTKIC KVSDMTYSES PYSTGIPSCN VKRFGSCNVR GHQWQIAECS NGLFYYVSAK
     AHSKTNDITL YCLSANCLDL RYAFRSSSCS DIVWDTSYRN KLTPKSINHP DIENYIAALQ
     SDIANDLTMH YFKPLKNLPA IIPQYKTMTL NGDKVSNGIR NSYIESHIPA INGLSAGINI
     AMPNGESLFS IIIYVRRVIN KASYRFLYET GPTIGINAKH EEVCTGKCPS PIPHQDGWVT
     FSKERSSNWG CEEWGCLAIN DGCLYGSCQD IIRPEYKIYK KSSIEQKDVE VCITMAHESF
     CSTVDVLQPL ISDRIQLDIQ TIQMDSMPNI IAVKNGKVYV GDINDLGSTA KKCGSVQLYS
     EGIIGSGTPK FDYVCHAFNR KDVILRRCFD NSYQSCLLLE QDNTLTIAST SHMEVHKKVS
     SVGTINYKIM LGDFDYNAYS TQATVTIDEI RCGGCYGCPE GMACALKLST NTIGSCSIKS
     NCDTYIKIIA VDPMQSEYSI KLNCPLATET VSVSVCSASA YTKPSISKNQ PKIVLNSLDE
     TSYIEQHDKK CSTWLCRVYK EGISVIFQPL FGNLSFYWRL TIYIIISLIM LILFLYILIP
     LCKRLKGLLE YNERIYQMEN KFK
//