GP_BUNL8
ID GP_BUNL8 Reviewed; 1441 AA.
AC Q8JPR1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N;
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;
DE Short=Gc;
DE AltName: Full=Glycoprotein G1;
DE Flags: Precursor;
GN Name=GP;
OS Bunyavirus La Crosse (isolate Human/United States/L78/1978).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus;
OC La Crosse orthobunyavirus.
OX NCBI_TaxID=796210;
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=7162; Ochlerotatus triseriatus (Eastern treehole mosquito) (Aedes triseriatus).
OH NCBI_TaxID=13712; Tamias.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Hughes M.T., Kempf B.J., Blair C.D., Beaty B.J.;
RT "Complete sequence of the Bunyavirus, La Crosse virus, Human/78 strain.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17488515; DOI=10.1186/1743-422x-4-41;
RA Bennett R.S., Ton D.R., Hanson C.T., Murphy B.R., Whitehead S.S.;
RT "Genome sequence analysis of La Crosse virus and in vitro and in vivo
RT phenotypes.";
RL Virol. J. 4:41-41(2007).
RN [3]
RP MUTAGENESIS OF TRP-1066.
RX PubMed=17027056; DOI=10.1016/j.virol.2006.08.050;
RA Plassmeyer M.L., Soldan S.S., Stachelek K.M., Roth S.M., Martin-Garcia J.,
RA Gonzalez-Scarano F.;
RT "Mutagenesis of the La Crosse Virus glycoprotein supports a role for Gc
RT (1066-1087) as the fusion peptide.";
RL Virology 358:273-282(2007).
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 -!- SIMILARITY: Belongs to the orthobunyaviruses M polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AF528166; AAM94388.1; -; Genomic_RNA.
DR EMBL; EF485034; ABQ12634.1; -; Viral_cRNA.
DR RefSeq; NP_671969.1; NC_004109.1.
DR PDB; 6H3W; X-ray; 2.10 A; A=477-723.
DR PDB; 7A57; X-ray; 3.15 A; A/B/C=918-1364.
DR PDBsum; 6H3W; -.
DR PDBsum; 7A57; -.
DR SMR; Q8JPR1; -.
DR PRIDE; Q8JPR1; -.
DR GeneID; 956555; -.
DR KEGG; vg:956555; -.
DR Proteomes; UP000008768; Genome.
DR Proteomes; UP000121242; 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: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 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; Glycoprotein; Host endoplasmic reticulum;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT CHAIN 14..1441
FT /note="Envelopment polyprotein"
FT /id="PRO_0000397205"
FT CHAIN 14..299
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397184"
FT CHAIN 300..473
FT /note="Non-structural protein M"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397185"
FT CHAIN 474..1441
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397186"
FT TOPO_DOM 14..200
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..361
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..1395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1396..1416
FT /evidence="ECO:0000255"
FT TOPO_DOM 1417..1433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1066..1087
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT MUTAGEN 1066
FT /note="W->A: Complete loss of viral fusion and entry."
FT /evidence="ECO:0000269|PubMed:17027056"
FT HELIX 478..483
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 510..519
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 528..532
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 538..547
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 551..564
FT /evidence="ECO:0007829|PDB:6H3W"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 581..589
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 602..609
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 623..628
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 632..649
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 653..663
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 667..680
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 685..698
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 701..705
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:6H3W"
FT HELIX 918..920
FT /evidence="ECO:0007829|PDB:7A57"
FT HELIX 929..946
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 966..973
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 976..986
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 992..999
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1002..1027
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1030..1043
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1056..1065
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1076..1089
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1093..1098
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1103..1112
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1115..1121
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1123..1125
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1130..1137
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1146..1151
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1154..1160
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1168..1170
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1172..1176
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1179..1182
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1187..1191
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1194..1196
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1199..1206
FT /evidence="ECO:0007829|PDB:7A57"
FT HELIX 1210..1215
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1222..1227
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1230..1235
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1242..1248
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1253..1257
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1263..1271
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1273..1277
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1279..1289
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1291..1308
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1314..1320
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1327..1333
FT /evidence="ECO:0007829|PDB:7A57"
FT STRAND 1336..1344
FT /evidence="ECO:0007829|PDB:7A57"
SQ SEQUENCE 1441 AA; 162364 MW; D9A2BECC01821D1D CRC64;
MICILVLITV AAASPVYQRC FQDGAIVKQN PSKEAVTEVC LKDDVSMIKT EARYVRNATG
VFSNNVAIRK WLVSDWHDCR PKKIVGGHIN VIEVGDDLSL HTESYVCSAD CTIGVDKETA
QVRLQTDTTN HFEIAGTTVK SGWFKSTTYI TLDQTCEHLK VSCGPKSVQF HACFNQHMSC
VRFLHRTILP GSIANSICQN IEIIILVTLT LLIFILLSIL SKTYICYLLM PIFIPIAYIY
GIIYNKSCKK CKLCGLVYHP FTECGTHCVC GARYDTSDRM KLHRASGLCP GYKSLRAARV
MCKSKGPASI LSIITAVLVL TFVTPINSMV LGESKETFEL EDLPDDMLEM ASRINSYYLT
CILNYAVSWG LVIIGLLIGL LFKKYQHRFL NVYAMYCEEC DMYHDKSGLK RHGDFTNKCR
QCTCGQYEDA AGLMAHRKTY NCLVQYKAKW MMNFLIIYIF LILIKDSAIV VQAAGTDFTT
CLETESINWN CTGPFLNLGN CQKQQKKEPY TNIATQLKGL KAISVLDVPI ITGIPDDIAG
ALRYIEEKED FHVQLTIEYA MLSKYCDYYT QFSDNSGYSQ TTWRVYLRSH DFEACILYPN
QHFCRCVKNG EKCSSSNWDF ANEMKDYYSG KQTKFDKDLN LALTALHHAF RGTSSAYIAT
MLSKKSNDDL IAYTNKIKTK FPGNALLKAI IDYIAYMKSL PGMANFKYDE FWDELLYKPN
PAKASNLARG KESSYNFKLA ISSKSIKTCK NVKDVACLSP RSGAIYASII ACGEPNGPSV
YRKPSGGVFQ SSTDRSIYCL LDSHCLEEFE AIGQEELDAV KKSKCWEIEY PDVKLIQEGD
GTKSCRMKDS GNCNVATNRW PVIQCENDKF YYSELQKDYD KAQDIGHYCL SPGCTTVRYP
INPKHISNCN WQVSRSSIAK IDVHNIEDIE QYKKAITQKL QTSLSLFKYA KTKNLPHIKP
IYKYITIEGT ETAEGIESAY IESEVPALAG TSIGFKINSK EGKHLLDVIA YVKSASYSSV
YTKLYSTGPT SGINTKHDEL CTGPCPANIN HQVGWLTFAR ERTSSWGCEE FGCLAVSDGC
VFGSCQDIIK EELSVYRKET EEVTDVELCL TFSDKTYCTN LNPVTPIITD LFEVQFKTVE
TYSLPRIVAV QNHEIKIGQI NDLGVYSKGC GNVQKVNGTI YGNGVPRFDY LCHLASRKEV
IVRKCFDNDY QACKFLQSPA SYRLEEDSGT VTIIDYKKIL GTIKMKAILG DVKYKTFADS
VDITAEGSCT GCINCFENIH CELTLHTTIE ASCPIKSSCT VFHDRILVTP NEHKYALKMV
CTEKPGNTLT IKVCNTKVEA SMALVDAKPI IELAPVDQTA YIREKDERCK TWMCRVRDEG
LQVILEPFKN LFGSYIGIFY TFIISIVVLL VIIYVLLPIC FKLRDTLRKH EDAYKREMKI
R
