P35_NPVAC
ID P35_NPVAC Reviewed; 299 AA.
AC P08160;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Early 35 kDa protein;
DE AltName: Full=Apoptosis-preventing protein;
DE AltName: Full=p35;
GN Name=P35;
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=L1;
RX PubMed=3035225; DOI=10.1128/jvi.61.7.2264-2272.1987;
RA Friesen P.D., Miller L.K.;
RT "Divergent transcription of early 35- and 94-kilodalton protein genes
RT encoded by the HindIII K genome fragment of the baculovirus Autographa
RT californica nuclear polyhedrosis virus.";
RL J. Virol. 61:2264-2272(1987).
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 FUNCTION.
RX PubMed=1962198; DOI=10.1126/science.1962198;
RA Clem R.J., Fechheimer M., Miller L.K.;
RT "Prevention of apoptosis by a baculovirus gene during infection of insect
RT cells.";
RL Science 254:1388-1390(1991).
RN [4]
RP FUNCTION.
RX PubMed=16081248; DOI=10.1016/j.resmic.2005.06.001;
RA da Silveira E.B., Cordeiro B.A., Ribeiro B.M., Bao S.N.;
RT "In vivo apoptosis induction and reduction of infectivity by an Autographa
RT californica multiple nucleopolyhedrovirus p35(-) recombinant in hemocytes
RT from the velvet bean caterpillar Anticarsia gemmatalis (Huebner)
RT (Lepidoptera: Noctuidae).";
RL Res. Microbiol. 156:1014-1025(2005).
RN [5]
RP FUNCTION.
RX PubMed=26018163; DOI=10.1128/jvi.00802-15;
RA Mehrabadi M., Hussain M., Matindoost L., Asgari S.;
RT "The Baculovirus antiapoptotic p35 protein functions as an inhibitor of the
RT host RNA interference antiviral response.";
RL J. Virol. 89:8182-8192(2015).
CC -!- FUNCTION: Functions as an inhibitor of the host RNA interference
CC antiviral response. Inhibits the insect host cell apoptotic response
CC initiated by the viral infection. Blocks as well the activity of
CC members of the caspase family of proteases. Required for late and very
CC late gene expression. {ECO:0000269|PubMed:16081248,
CC ECO:0000269|PubMed:1962198, ECO:0000269|PubMed:26018163}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I50 (p35) 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; M16821; AAA46703.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66765.1; -; Genomic_DNA.
DR PIR; A27840; WMNV35.
DR RefSeq; NP_054165.1; NC_001623.1.
DR PDB; 1I3P; X-ray; 3.10 A; A=2-299.
DR PDB; 1I3S; X-ray; 2.70 A; A/B/C=2-299.
DR PDB; 1I4E; X-ray; 3.00 A; A=2-299.
DR PDB; 1P35; X-ray; 2.20 A; A/B/C=2-299.
DR PDB; 2FUN; X-ray; 3.00 A; A/C=2-299.
DR PDBsum; 1I3P; -.
DR PDBsum; 1I3S; -.
DR PDBsum; 1I4E; -.
DR PDBsum; 1P35; -.
DR PDBsum; 2FUN; -.
DR SMR; P08160; -.
DR IntAct; P08160; 1.
DR MINT; P08160; -.
DR MEROPS; I50.001; -.
DR GeneID; 1403968; -.
DR KEGG; vg:1403968; -.
DR EvolutionaryTrace; P08160; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:GOC.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:UniProtKB.
DR GO; GO:0039650; P:suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0140533; P:suppression of host RNAi-mediated antiviral immune response; IDA:UniProtKB.
DR Gene3D; 2.60.250.10; -; 1.
DR InterPro; IPR003429; Baculovirus_p35.
DR InterPro; IPR036562; Baculovirus_p35_sf.
DR Pfam; PF02331; P35; 1.
DR SUPFAM; SSF49894; SSF49894; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Early protein; Host-virus interaction;
KW Inhibition of host caspases by virus;
KW Modulation of host cell apoptosis by virus; Protease inhibitor;
KW Reference proteome; Suppressor of RNA silencing; Thiol protease inhibitor.
FT CHAIN 1..299
FT /note="Early 35 kDa protein"
FT /id="PRO_0000132898"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 11..22
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1I3P"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1P35"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:1P35"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1I3S"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1P35"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1P35"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1P35"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:1P35"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1I3S"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1P35"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:1I3S"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1I3S"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:1P35"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 237..250
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 260..272
FT /evidence="ECO:0007829|PDB:1P35"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 277..288
FT /evidence="ECO:0007829|PDB:1P35"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:1P35"
SQ SEQUENCE 299 AA; 34829 MW; F8BC3BEB9E64382E CRC64;
MCVIFPVEID VSQTIIRDCQ VDKQTRELVY INKIMNTQLT KPVLMMFNIS GPIRSVTRKN
NNLRDRIKSK VDEQFDQLER DYSDQMDGFH DSIKYFKDEH YSVSCQNGSV LKSKFAKILK
SHDYTDKKSI EAYEKYCLPK LVDERNDYYV AVCVLKPGFE NGSNQVLSFE YNPIGNKVIV
PFAHEINDTG LYEYDVVAYV DSVQFDGEQF EEFVQSLILP SSFKNSEKVL YYNEASKNKS
MIYKALEFTT ESSWGKSEKY NWKIFCNGFI YDKKSKVLYV KLHNVTSALN KNVILNTIK
