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Major envelope glycoprotein (gp64)

 FUS_NPVAC               Reviewed;         512 AA.
P17501;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
23-MAY-2018, entry version 93.
RecName: Full=Major envelope glycoprotein;
AltName: Full=gp64;
Flags: Precursor;
Name=GP64; Synonyms=GP67; ORFNames=ORF128;
Autographa californica nuclear polyhedrosis virus (AcMNPV).
Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
NCBI_TaxID=46015;
NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=HR3;
PubMed=2644449;
Whitford M., Stewart S., Kuzio J., Faulkner P.;
"Identification and sequence analysis of a gene encoding gp67, an
abundant envelope glycoprotein of the baculovirus Autographa
californica nuclear polyhedrosis virus.";
J. Virol. 63:1393-1399(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C6;
PubMed=8030224; DOI=10.1006/viro.1994.1380;
Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
"The complete DNA sequence of Autographa californica nuclear
polyhedrosis virus.";
Virology 202:586-605(1994).
[3]
PALMITOYLATION.
PubMed=2672565; DOI=10.1016/0042-6822(89)90145-1;
Roberts T.E., Faulkner P.;
"Fatty acid acylation of the 67K envelope glycoprotein of a
baculovirus: Autographa californica nuclear polyhedrosis virus.";
Virology 172:377-381(1989).
[4]
FUNCTION.
PubMed=1404622;
Blissard G.W., Wenz J.R.;
"Baculovirus gp64 envelope glycoprotein is sufficient to mediate pH-
dependent membrane fusion.";
J. Virol. 66:6829-6835(1992).
[5]
FUNCTION.
PubMed=9986796; DOI=10.1006/viro.1998.9523;
Oomens A.G., Blissard G.W.;
"Requirement for GP64 to drive efficient budding of Autographa
californica multicapsid nucleopolyhedrovirus.";
Virology 254:297-314(1999).
[6]
PALMITOYLATION AT CYS-503, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
CYS-503.
PubMed=12743283; DOI=10.1128/JVI.77.11.6265-6273.2003;
Zhang S.X., Han Y., Blissard G.W.;
"Palmitoylation of the Autographa californica multicapsid
nucleopolyhedrovirus envelope glycoprotein GP64: mapping, functional
studies, and lipid rafts.";
J. Virol. 77:6265-6273(2003).
[7]
FUNCTION.
PubMed=20739531; DOI=10.1128/JVI.00862-10;
Wang M., Yin F., Shen S., Tan Y., Deng F., Vlak J.M., Hu Z., Wang H.;
"Partial functional rescue of Helicoverpa armigera single nucleocapsid
nucleopolyhedrovirus infectivity by replacement of F protein with GP64
from Autographa californica multicapsid nucleopolyhedrovirus.";
J. Virol. 84:11505-11514(2010).
[8]
DISULFIDE BOND, AND SUBUNIT.
PubMed=20573818; DOI=10.1128/JVI.00264-10;
Li Z., Blissard G.W.;
"Baculovirus GP64 disulfide bonds: the intermolecular disulfide bond
of Autographa californica multicapsid nucleopolyhedrovirus GP64 is not
essential for membrane fusion and virion budding.";
J. Virol. 84:8584-8595(2010).
[9]
SUBCELLULAR LOCATION.
PubMed=25142609; DOI=10.1128/JVI.01313-14;
Yang M., Wang S., Yue X.L., Li L.L.;
"Autographa californica multiple nucleopolyhedrovirus orf132 encodes a
nucleocapsid-associated protein required for budded-virus and multiply
enveloped occlusion-derived virus production.";
J. Virol. 88:12586-12598(2014).
[10]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 21-499, AND SUBUNIT.
PubMed=18776902; DOI=10.1038/nsmb.1484;
Kadlec J., Loureiro S., Abrescia N.G., Stuart D.I., Jones I.M.;
"The postfusion structure of baculovirus gp64 supports a unified view
of viral fusion machines.";
Nat. Struct. Mol. Biol. 15:1024-1030(2008).
-!- FUNCTION: Class III viral fusion protein. Envelope
phosphoglycoprotein which mediates the fusion of viral and host
endosomal membranes leading to virus entry into the host cell.
After receptor-mediated internalization of the virus, gp64
undergoes conformational change into a fusion-competent state at
low pH, and the nucleocapsid is released into the cytoplasm after
cell fusion. May also play role in budding.
{ECO:0000269|PubMed:1404622, ECO:0000269|PubMed:20739531,
ECO:0000269|PubMed:9986796}.
-!- SUBUNIT: Homotrimer; disulfide-linked.
{ECO:0000269|PubMed:18776902, ECO:0000269|PubMed:20573818}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15727661, EBI-15727661;
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000269|PubMed:25142609}; Single-pass membrane protein
{ECO:0000305}. Host cell membrane {ECO:0000269|PubMed:12743283};
Single-pass membrane protein {ECO:0000305}.
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:12743283,
ECO:0000269|PubMed:2672565}.
-!- SIMILARITY: Belongs to the baculoviridae gp64 family.
{ECO:0000305}.
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EMBL; M25420; AAA72760.1; -; Genomic_DNA.
EMBL; L22858; AAA66758.2; -; Genomic_DNA.
PIR; A72866; A72866.
RefSeq; NP_054158.1; NC_001623.1.
PDB; 3DUZ; X-ray; 2.95 A; A=21-499.
PDBsum; 3DUZ; -.
SMR; P17501; -.
DIP; DIP-46361N; -.
TCDB; 1.G.15.1.1; the autographa californica nuclear polyhedrosis virus major envelope glycoprotein gp64 (gp64) family.
SwissPalm; P17501; -.
PRIDE; P17501; -.
GeneID; 1403961; -.
KEGG; vg:1403961; -.
OrthoDB; VOG0900006V; -.
EvolutionaryTrace; P17501; -.
Proteomes; UP000008292; Genome.
GO; GO:0020002; C:host cell plasma membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IDA:UniProtKB.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IDA:UniProtKB.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:InterPro.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
InterPro; IPR004955; Baculovirus_Gp64.
Pfam; PF03273; Baculo_gp64; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 512 Major envelope glycoprotein.
/FTId=PRO_0000036746.
TRANSMEM 482 504 Helical. {ECO:0000255}.
LIPID 503 503 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:12743283}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 384 384 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 426 426 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 24 24 Interchain (with C-372 in trimeric
partner 1).
{ECO:0000269|PubMed:20573818}.
DISULFID 111 164 {ECO:0000269|PubMed:20573818}.
DISULFID 128 158 {ECO:0000269|PubMed:20573818}.
DISULFID 177 184 {ECO:0000269|PubMed:20573818}.
DISULFID 228 246 {ECO:0000269|PubMed:20573818}.
DISULFID 262 267 {ECO:0000269|PubMed:20573818}.
DISULFID 372 372 Interchain (with C-24 in trimeric partner
2). {ECO:0000269|PubMed:20573818}.
DISULFID 382 402 {ECO:0000269|PubMed:20573818}.
MUTAGEN 503 503 C->A,S: Abolishes palmitoylation.
{ECO:0000269|PubMed:12743283}.
CONFLICT 406 406 S -> R (in Ref. 1; AAA72760).
{ECO:0000305}.
CONFLICT 414 414 D -> H (in Ref. 1). {ECO:0000305}.
CONFLICT 416 416 Missing (in Ref. 1). {ECO:0000305}.
HELIX 26 28 {ECO:0000244|PDB:3DUZ}.
STRAND 44 58 {ECO:0000244|PDB:3DUZ}.
STRAND 60 78 {ECO:0000244|PDB:3DUZ}.
TURN 80 82 {ECO:0000244|PDB:3DUZ}.
STRAND 87 95 {ECO:0000244|PDB:3DUZ}.
HELIX 99 108 {ECO:0000244|PDB:3DUZ}.
STRAND 111 113 {ECO:0000244|PDB:3DUZ}.
STRAND 117 121 {ECO:0000244|PDB:3DUZ}.
HELIX 122 126 {ECO:0000244|PDB:3DUZ}.
HELIX 127 130 {ECO:0000244|PDB:3DUZ}.
STRAND 136 140 {ECO:0000244|PDB:3DUZ}.
STRAND 146 148 {ECO:0000244|PDB:3DUZ}.
STRAND 155 177 {ECO:0000244|PDB:3DUZ}.
TURN 179 181 {ECO:0000244|PDB:3DUZ}.
STRAND 184 189 {ECO:0000244|PDB:3DUZ}.
STRAND 200 202 {ECO:0000244|PDB:3DUZ}.
STRAND 204 206 {ECO:0000244|PDB:3DUZ}.
STRAND 209 215 {ECO:0000244|PDB:3DUZ}.
STRAND 219 231 {ECO:0000244|PDB:3DUZ}.
STRAND 243 250 {ECO:0000244|PDB:3DUZ}.
STRAND 252 254 {ECO:0000244|PDB:3DUZ}.
STRAND 261 263 {ECO:0000244|PDB:3DUZ}.
STRAND 266 270 {ECO:0000244|PDB:3DUZ}.
HELIX 299 342 {ECO:0000244|PDB:3DUZ}.
HELIX 348 352 {ECO:0000244|PDB:3DUZ}.
STRAND 357 365 {ECO:0000244|PDB:3DUZ}.
STRAND 367 371 {ECO:0000244|PDB:3DUZ}.
TURN 390 392 {ECO:0000244|PDB:3DUZ}.
HELIX 433 435 {ECO:0000244|PDB:3DUZ}.
HELIX 437 452 {ECO:0000244|PDB:3DUZ}.
STRAND 455 458 {ECO:0000244|PDB:3DUZ}.
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


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