FUS_NPVAC
ID FUS_NPVAC Reviewed; 512 AA.
AC P17501;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 29-SEP-2021, entry version 103.
DE RecName: Full=Major envelope glycoprotein;
DE AltName: Full=gp64;
DE Flags: Precursor;
GN Name=GP64; Synonyms=GP67; ORFNames=ORF128;
OS Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46015;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HR3;
RX PubMed=2644449; DOI=10.1128/jvi.63.3.1393-1399.1989;
RA Whitford M., Stewart S., Kuzio J., Faulkner P.;
RT "Identification and sequence analysis of a gene encoding gp67, an abundant
RT envelope glycoprotein of the baculovirus Autographa californica nuclear
RT polyhedrosis virus.";
RL J. Virol. 63:1393-1399(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6;
RX PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT virus.";
RL Virology 202:586-605(1994).
RN [3]
RP PALMITOYLATION.
RX PubMed=2672565; DOI=10.1016/0042-6822(89)90145-1;
RA Roberts T.E., Faulkner P.;
RT "Fatty acid acylation of the 67K envelope glycoprotein of a baculovirus:
RT Autographa californica nuclear polyhedrosis virus.";
RL Virology 172:377-381(1989).
RN [4]
RP FUNCTION.
RX PubMed=1404622; DOI=10.1128/jvi.66.11.6829-6835.1992;
RA Blissard G.W., Wenz J.R.;
RT "Baculovirus gp64 envelope glycoprotein is sufficient to mediate pH-
RT dependent membrane fusion.";
RL J. Virol. 66:6829-6835(1992).
RN [5]
RP FUNCTION.
RX PubMed=9986796; DOI=10.1006/viro.1998.9523;
RA Oomens A.G., Blissard G.W.;
RT "Requirement for GP64 to drive efficient budding of Autographa californica
RT multicapsid nucleopolyhedrovirus.";
RL Virology 254:297-314(1999).
RN [6]
RP PALMITOYLATION AT CYS-503, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-503.
RX PubMed=12743283; DOI=10.1128/jvi.77.11.6265-6273.2003;
RA Zhang S.X., Han Y., Blissard G.W.;
RT "Palmitoylation of the Autographa californica multicapsid
RT nucleopolyhedrovirus envelope glycoprotein GP64: mapping, functional
RT studies, and lipid rafts.";
RL J. Virol. 77:6265-6273(2003).
RN [7]
RP FUNCTION.
RX PubMed=20739531; DOI=10.1128/jvi.00862-10;
RA Wang M., Yin F., Shen S., Tan Y., Deng F., Vlak J.M., Hu Z., Wang H.;
RT "Partial functional rescue of Helicoverpa armigera single nucleocapsid
RT nucleopolyhedrovirus infectivity by replacement of F protein with GP64 from
RT Autographa californica multicapsid nucleopolyhedrovirus.";
RL J. Virol. 84:11505-11514(2010).
RN [8]
RP DISULFIDE BOND, AND SUBUNIT.
RX PubMed=20573818; DOI=10.1128/jvi.00264-10;
RA Li Z., Blissard G.W.;
RT "Baculovirus GP64 disulfide bonds: the intermolecular disulfide bond of
RT Autographa californica multicapsid nucleopolyhedrovirus GP64 is not
RT essential for membrane fusion and virion budding.";
RL J. Virol. 84:8584-8595(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=25142609; DOI=10.1128/jvi.01313-14;
RA Yang M., Wang S., Yue X.L., Li L.L.;
RT "Autographa californica multiple nucleopolyhedrovirus orf132 encodes a
RT nucleocapsid-associated protein required for budded-virus and multiply
RT enveloped occlusion-derived virus production.";
RL J. Virol. 88:12586-12598(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 21-499, AND SUBUNIT.
RX PubMed=18776902; DOI=10.1038/nsmb.1484;
RA Kadlec J., Loureiro S., Abrescia N.G., Stuart D.I., Jones I.M.;
RT "The postfusion structure of baculovirus gp64 supports a unified view of
RT viral fusion machines.";
RL Nat. Struct. Mol. Biol. 15:1024-1030(2008).
CC -!- FUNCTION: Class III viral fusion protein. Envelope phosphoglycoprotein
CC which mediates the fusion of viral and host endosomal membranes leading
CC to virus entry into the host cell. After receptor-mediated
CC internalization of the virus, gp64 undergoes conformational change into
CC a fusion-competent state at low pH, and the nucleocapsid is released
CC into the cytoplasm after cell fusion. May also play role in budding.
CC {ECO:0000269|PubMed:1404622, ECO:0000269|PubMed:20739531,
CC ECO:0000269|PubMed:9986796}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000269|PubMed:18776902,
CC ECO:0000269|PubMed:20573818}.
CC -!- INTERACTION:
CC P17501; P17501: GP64; NbExp=2; IntAct=EBI-15727661, EBI-15727661;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:25142609};
CC Single-pass membrane protein {ECO:0000305}. Host cell membrane
CC {ECO:0000269|PubMed:12743283}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:12743283,
CC ECO:0000269|PubMed:2672565}.
CC -!- SIMILARITY: Belongs to the baculoviridae gp64 family. {ECO:0000305}.
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DR EMBL; M25420; AAA72760.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66758.2; -; Genomic_DNA.
DR PIR; A72866; A72866.
DR RefSeq; NP_054158.1; NC_001623.1.
DR PDB; 3DUZ; X-ray; 2.95 A; A=21-499.
DR PDBsum; 3DUZ; -.
DR SMR; P17501; -.
DR DIP; DIP-46361N; -.
DR TCDB; 1.G.15.1.1; the autographa californica nuclear polyhedrosis virus major envelope glycoprotein gp64 (gp64) family.
DR SwissPalm; P17501; -.
DR GeneID; 1403961; -.
DR KEGG; vg:1403961; -.
DR EvolutionaryTrace; P17501; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IDA:UniProtKB.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
DR InterPro; IPR004955; Baculovirus_Gp64.
DR Pfam; PF03273; Baculo_gp64; 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 cell membrane; Host membrane; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..512
FT /note="Major envelope glycoprotein"
FT /id="PRO_0000036746"
FT TRANSMEM 482..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT LIPID 503
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:12743283"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 24
FT /note="Interchain (with C-372 in trimeric partner 1)"
FT /evidence="ECO:0000269|PubMed:20573818"
FT DISULFID 111..164
FT /evidence="ECO:0000269|PubMed:20573818"
FT DISULFID 128..158
FT /evidence="ECO:0000269|PubMed:20573818"
FT DISULFID 177..184
FT /evidence="ECO:0000269|PubMed:20573818"
FT DISULFID 228..246
FT /evidence="ECO:0000269|PubMed:20573818"
FT DISULFID 262..267
FT /evidence="ECO:0000269|PubMed:20573818"
FT DISULFID 372
FT /note="Interchain (with C-24 in trimeric partner 2)"
FT /evidence="ECO:0000269|PubMed:20573818"
FT DISULFID 382..402
FT /evidence="ECO:0000269|PubMed:20573818"
FT MUTAGEN 503
FT /note="C->A,S: Abolishes palmitoylation."
FT /evidence="ECO:0000269|PubMed:12743283"
FT CONFLICT 406
FT /note="S -> R (in Ref. 1; AAA72760)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="D -> H (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 44..58
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 60..78
FT /evidence="ECO:0007829|PDB:3DUZ"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3DUZ"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3DUZ"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:3DUZ"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 155..177
FT /evidence="ECO:0007829|PDB:3DUZ"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 219..231
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:3DUZ"
FT HELIX 299..342
FT /evidence="ECO:0007829|PDB:3DUZ"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:3DUZ"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:3DUZ"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:3DUZ"
FT HELIX 437..452
FT /evidence="ECO:0007829|PDB:3DUZ"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:3DUZ"
SQ SEQUENCE 512 AA; 58566 MW; A3BC357846C7D2E2 CRC64;
MVSAIVLYVL LAAAAHSAFA AEHCNAQMKT GPYKIKNLDI TPPKETLQKD VEITIVETDY
NENVIIGYKG YYQAYAYNGG SLDPNTRVEE TMKTLNVGKE DLLMWSIRQQ CEVGEELIDR
WGSDSDDCFR DNEGRGQWVK GKELVKRQNN NHFAHHTCNK SWRCGISTSK MYSRLECQDD
TDECQVYILD AEGNPINVTV DTVLHRDGVS MILKQKSTFT TRQIKAACLL IKDDKNNPES
VTREHCLIDN DIYDLSKNTW NCKFNRCIKR KVEHRVKKRP PTWRHNVRAK YTEGDTATKG
DLMHIQEELM YENDLLKMNI ELMHAHINKL NNMLHDLIVS VAKVDERLIG NLMNNSVSST
FLSDDTFLLM PCTNPPAHTS NCYNNSIYKE GRWVANTDSS QCIDFSNYKE LAIDDDVEFW
IPTIGNTTYH DSWKDASGWS FIAQQKSNLI TTMENTKFGG VGTSLSDITS MAEGELAAKL
TSFMFGHVVN FVIILIVILF LYCMIRNRNR QY
