POLG_CSFVA
ID POLG_CSFVA Reviewed; 3898 AA.
AC P19712;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=N-terminal protease;
DE Short=N-pro;
DE EC=3.4.22.-;
DE AltName: Full=Autoprotease p20;
DE Contains:
DE RecName: Full=Capsid protein C;
DE AltName: Full=Core protein;
DE Contains:
DE RecName: Full=E(rns) glycoprotein;
DE AltName: Full=gp44/48;
DE Contains:
DE RecName: Full=Envelope glycoprotein E1;
DE AltName: Full=gp33;
DE Contains:
DE RecName: Full=Envelope glycoprotein E2;
DE AltName: Full=gp55;
DE Contains:
DE RecName: Full=Viroporin p7 {ECO:0000303|PubMed:22496228};
DE Contains:
DE RecName: Full=Non-structural protein 2-3;
DE Short=NS2-3;
DE Contains:
DE RecName: Full=Cysteine protease NS2;
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 2;
DE Contains:
DE RecName: Full=Serine protease NS3;
DE EC=3.4.21.113;
DE EC=3.6.1.15;
DE EC=3.6.4.13;
DE AltName: Full=Non-structural protein 3;
DE Contains:
DE RecName: Full=Non-structural protein 4A;
DE Short=NS4A;
DE Contains:
DE RecName: Full=Non-structural protein 4B;
DE Short=NS4B;
DE Contains:
DE RecName: Full=Non-structural protein 5A;
DE Short=NS5A;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=NS5B;
OS Classical swine fever virus (strain Alfort) (CSFV) (Hog cholera virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus.
OX NCBI_TaxID=11097;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2763466; DOI=10.1016/0042-6822(89)90625-9;
RA Meyers G., Ruemenapf T., Thiel H.-J.;
RT "Molecular cloning and nucleotide sequence of the genome of hog cholera
RT virus.";
RL Virology 171:555-567(1989).
RN [2]
RP SEQUENCE REVISION TO 2731.
RA Meyers G.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT (ENVELOPE GLYCOPROTEIN E1), AND SUBUNIT (ENVELOPE GLYCOPROTEIN E2).
RX PubMed=2370675; DOI=10.1128/jvi.64.8.3563-3569.1990;
RA Weiland E., Stark R., Haas B., Ruemenapf T., Meyers G., Thiel H.J.;
RT "Pestivirus glycoprotein which induces neutralizing antibodies forms part
RT of a disulfide-linked heterodimer.";
RL J. Virol. 64:3563-3569(1990).
RN [4]
RP SUBUNIT (E(RNS) GLYCOPROTEIN), AND GLYCOSYLATION (E(RNS) GLYCOPROTEIN).
RX PubMed=1870198; DOI=10.1128/jvi.65.9.4705-4712.1991;
RA Thiel H.-J., Stark R., Weiland E., Ruemenapf T., Meyers G.;
RT "Hog cholera virus: molecular composition of virions from a pestivirus.";
RL J. Virol. 65:4705-4712(1991).
RN [5]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND PROTEIN SEQUENCE OF 169-178.
RX PubMed=8388499; DOI=10.1128/jvi.67.6.3288-3294.1993;
RA Ruemenapf T., Unger G., Strauss J.H., Thiel H.-J.;
RT "Processing of the envelope glycoproteins of pestiviruses.";
RL J. Virol. 67:3288-3294(1993).
RN [6]
RP PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
RX PubMed=8230432; DOI=10.1128/jvi.67.12.7088-7095.1993;
RA Stark R., Meyers G., Ruemenapf T., Thiel H.-J.;
RT "Processing of pestivirus polyprotein: cleavage site between autoprotease
RT and nucleocapsid protein of classical swine fever virus.";
RL J. Virol. 67:7088-7095(1993).
RN [7]
RP FUNCTION (E(RNS) GLYCOPROTEIN).
RX PubMed=8356450; DOI=10.1126/science.8356450;
RA Schneider R., Unger G., Stark R., Schneider-Scherzer E., Thiel H.J.;
RT "Identification of a structural glycoprotein of an RNA virus as a
RT ribonuclease.";
RL Science 261:1169-1171(1993).
RN [8]
RP ACTIVE SITE (N-TERMINAL PROTEASE), AND MUTAGENESIS OF GLU-22; HIS-40;
RP HIS-49; CYS-69; HIS-99; CYS-112; HIS-130; CYS-134; CYS-138 AND CYS-161.
RX PubMed=9499122; DOI=10.1128/jvi.72.3.2544-2547.1998;
RA Ruemenapf T., Stark R., Heimann M., Thiel H.-J.;
RT "N-terminal protease of pestiviruses: identification of putative catalytic
RT residues by site-directed mutagenesis.";
RL J. Virol. 72:2544-2547(1998).
RN [9]
RP INDUCTION.
RX PubMed=9573242; DOI=10.1128/jvi.72.6.4775-4782.1998;
RA Sizova D.V., Kolupaeva V.G., Pestova T.V., Shatsky I.N., Hellen C.U.;
RT "Specific interaction of eukaryotic translation initiation factor 3 with
RT the 5' nontranslated regions of hepatitis C virus and classical swine fever
RT virus RNAs.";
RL J. Virol. 72:4775-4782(1998).
RN [10]
RP FUNCTION (CAPSID PROTEIN C).
RX PubMed=9617770; DOI=10.1016/s0168-1702(97)00132-9;
RA Liu J.J., Wong M.L., Chang T.J.;
RT "The recombinant nucleocapsid protein of classical swine fever virus can
RT act as a transcriptional regulator.";
RL Virus Res. 53:75-80(1998).
RN [11]
RP SUBCELLULAR LOCATION (E(RNS) GLYCOPROTEIN), AND SUBCELLULAR LOCATION
RP (ENVELOPE GLYCOPROTEIN E2).
RX PubMed=10355762; DOI=10.1099/0022-1317-80-5-1157;
RA Weiland F., Weiland E., Unger G., Saalmuller A., Thiel H.-J.;
RT "Localization of pestiviral envelope proteins E(rns) and E2 at the cell
RT surface and on isolated particles.";
RL J. Gen. Virol. 80:1157-1165(1999).
RN [12]
RP FUNCTION (ENVELOPE GLYCOPROTEIN E2).
RX PubMed=10438869; DOI=10.1128/jvi.73.9.7787-7794.1999;
RA Moser C., Stettler P., Tratschin J.D., Hofmann M.A.;
RT "Cytopathogenic and noncytopathogenic RNA replicons of classical swine
RT fever virus.";
RL J. Virol. 73:7787-7794(1999).
RN [13]
RP FUNCTION (ENVELOPE GLYCOPROTEIN E1), AND FUNCTION (ENVELOPE GLYCOPROTEIN
RP E2).
RX PubMed=15527858; DOI=10.1016/j.virol.2004.09.023;
RA Wang Z., Nie Y., Wang P., Ding M., Deng H.;
RT "Characterization of classical swine fever virus entry by using pseudotyped
RT viruses: E1 and E2 are sufficient to mediate viral entry.";
RL Virology 330:332-341(2004).
RN [14]
RP FUNCTION (NON-STRUCTURAL PROTEIN 2-3), AND FUNCTION (NON-STRUCTURAL PROTEIN
RP 4A).
RX PubMed=17482232; DOI=10.1016/j.virol.2007.03.056;
RA Moulin H.R., Seuberlich T., Bauhofer O., Bennett L.C., Tratschin J.D.,
RA Hofmann M.A., Ruggli N.;
RT "Nonstructural proteins NS2-3 and NS4A of classical swine fever virus:
RT essential features for infectious particle formation.";
RL Virology 365:376-389(2007).
RN [15]
RP FUNCTION (N-TERMINAL PROTEASE), INTERACTION WITH HOST IRF3 (N-TERMINAL
RP PROTEASE), AND SUBCELLULAR LOCATION (N-TERMINAL PROTEASE).
RX PubMed=17215286; DOI=10.1128/jvi.02032-06;
RA Bauhofer O., Summerfield A., Sakoda Y., Tratschin J.D., Hofmann M.A.,
RA Ruggli N.;
RT "Classical swine fever virus Npro interacts with interferon regulatory
RT factor 3 and induces its proteasomal degradation.";
RL J. Virol. 81:3087-3096(2007).
RN [16]
RP FUNCTION (E(RNS) GLYCOPROTEIN).
RX PubMed=19264773; DOI=10.1128/jvi.01710-08;
RA Tews B.A., Schuermann E.M., Meyers G.;
RT "Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer
RT formation and leads to attenuation of classical swine fever virus.";
RL J. Virol. 83:4823-4834(2009).
RN [17]
RP FUNCTION (E(RNS) GLYCOPROTEIN).
RX PubMed=19767841; DOI=10.1139/w09-013;
RA Luo X., Ling D., Li T., Wan C., Zhang C., Pan Z.;
RT "Classical swine fever virus Erns glycoprotein antagonizes induction of
RT interferon-beta by double-stranded RNA.";
RL Can. J. Microbiol. 55:698-704(2009).
RN [18]
RP FUNCTION (NON-STRUCTURAL PROTEIN 3), INTERACTION WITH RNA-DIRECTED RNA
RP POLYMERASE (NON-STRUCTURAL PROTEIN 3), AND INTERACTION WITH NON-STRUCTURAL
RP PROTEIN 3 (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=19185595; DOI=10.1016/j.virusres.2008.12.014;
RA Wen G., Xue J., Shen Y., Zhang C., Pan Z.;
RT "Characterization of classical swine fever virus (CSFV) nonstructural
RT protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent
RT RNA polymerase.";
RL Virus Res. 141:63-70(2009).
RN [19]
RP FUNCTION (NON-STRUCTURAL PROTEIN 5A).
RX PubMed=22261205; DOI=10.1016/j.virusres.2012.01.004;
RA Sheng C., Chen Y., Xiao J., Xiao J., Wang J., Li G., Chen J., Xiao M.;
RT "Classical swine fever virus NS5A protein interacts with 3'-untranslated
RT region and regulates viral RNA synthesis.";
RL Virus Res. 163:636-643(2012).
RN [20]
RP FUNCTION (NON-STRUCTURAL PROTEIN 5A), INTERACTION WITH RNA-DIRECTED RNA
RP POLYMERASE (NON-STRUCTURAL PROTEIN 5A), AND INTERACTION WITH NON-STRUCTURAL
RP PROTEIN 5A (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=22795973; DOI=10.1016/j.virol.2012.04.014;
RA Chen Y., Xiao J., Xiao J., Sheng C., Wang J., Jia L., Zhi Y., Li G.,
RA Chen J., Xiao M.;
RT "Classical swine fever virus NS5A regulates viral RNA replication through
RT binding to NS5B and 3'UTR.";
RL Virology 432:376-388(2012).
RN [21]
RP FUNCTION (VIROPORIN P7).
RX PubMed=22496228; DOI=10.1128/jvi.00560-12;
RA Gladue D.P., Holinka L.G., Largo E., Fernandez Sainz I., Carrillo C.,
RA O'Donnell V., Baker-Branstetter R., Lu Z., Ambroggio X., Risatti G.R.,
RA Nieva J.L., Borca M.V.;
RT "Classical swine fever virus p7 protein is a viroporin involved in
RT virulence in swine.";
RL J. Virol. 86:6778-6791(2012).
RN [22]
RP ACTIVE SITE (N-TERMINAL PROTEASE), AND FUNCTION (N-TERMINAL PROTEASE).
RX PubMed=24606708; DOI=10.1016/j.virol.2014.01.026;
RA Gottipati K., Acholi S., Ruggli N., Choi K.H.;
RT "Autocatalytic activity and substrate specificity of the pestivirus N-
RT terminal protease Npro.";
RL Virology 452:303-309(2014).
RN [23]
RP INTERACTION WITH HOST OS9 (CAPSID PROTEIN C).
RX PubMed=25010283; DOI=10.1016/j.virol.2014.05.008;
RA Gladue D.P., O'Donnell V., Fernandez-Sainz I.J., Fletcher P.,
RA Baker-Branstetter R., Holinka L.G., Sanford B., Carlson J., Lu Z.,
RA Borca M.V.;
RT "Interaction of structural core protein of classical swine fever virus with
RT endoplasmic reticulum-associated degradation pathway protein OS9.";
RL Virology 460:173-179(2014).
RN [24]
RP FUNCTION (VIROPORIN P7).
RX PubMed=24189547; DOI=10.1016/j.antiviral.2013.10.015;
RA Largo E., Gladue D.P., Huarte N., Borca M.V., Nieva J.L.;
RT "Pore-forming activity of pestivirus p7 in a minimal model system supports
RT genus-specific viroporin function.";
RL Antiviral Res. 101:30-36(2014).
RN [25]
RP INTERACTION WITH HOST TRX2 (ENVELOPE GLYCOPROTEIN E2).
RX PubMed=26041303; DOI=10.1128/jvi.00429-15;
RA Li S., Wang J., He W.R., Feng S., Li Y., Wang X., Liao Y., Qin H.Y.,
RA Li L.F., Dong H., Sun Y., Luo Y., Qiu H.J.;
RT "Thioredoxin 2 Is a Novel E2-Interacting Protein That Inhibits the
RT Replication of Classical Swine Fever Virus.";
RL J. Virol. 89:8510-8524(2015).
RN [26]
RP INTERACTION WITH HOST RPSA (E(RNS) GLYCOPROTEIN), AND FUNCTION (E(RNS)
RP GLYCOPROTEIN).
RX PubMed=25694590; DOI=10.1128/jvi.00019-15;
RA Chen J., He W.R., Shen L., Dong H., Yu J., Wang X., Yu S., Li Y., Li S.,
RA Luo Y., Sun Y., Qiu H.J.;
RT "The laminin receptor is a cellular attachment receptor for classical Swine
RT Fever virus.";
RL J. Virol. 89:4894-4906(2015).
RN [27]
RP FUNCTION (N-TERMINAL PROTEASE), AND INTERACTION WITH HOST IRF3 (N-TERMINAL
RP PROTEASE).
RX PubMed=27334592; DOI=10.1128/jvi.00318-16;
RA Gottipati K., Holthauzen L.M., Ruggli N., Choi K.H.;
RT "Pestivirus Npro Directly Interacts with Interferon Regulatory Factor 3
RT Monomer and Dimer.";
RL J. Virol. 90:7740-7747(2016).
RN [28]
RP FUNCTION (CAPSID PROTEIN C), AND SUBCELLULAR LOCATION (CAPSID PROTEIN C).
RX PubMed=28290554; DOI=10.1038/srep44459;
RA Riedel C., Lamp B., Hagen B., Indik S., Ruemenapf T.;
RT "The core protein of a pestivirus protects the incoming virus against IFN-
RT induced effectors.";
RL Sci. Rep. 7:44459-44459(2017).
RN [29]
RP FUNCTION (NON-STRUCTURAL PROTEIN 3), AND INTERACTION WITH HOST TRAF6
RP (NON-STRUCTURAL PROTEIN 3).
RX PubMed=28751780; DOI=10.1038/s41598-017-06934-1;
RA Lv H., Dong W., Cao Z., Li X., Wang J., Qian G., Lv Q., Wang C., Guo K.,
RA Zhang Y.;
RT "TRAF6 is a novel NS3-interacting protein that inhibits classical swine
RT fever virus replication.";
RL Sci. Rep. 7:6737-6737(2017).
RN [30]
RP FUNCTION (NON-STRUCTURAL PROTEIN 4B), INTERACTION WITH HOST RAB5
RP (NON-STRUCTURAL PROTEIN 4B), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN
RP 4B), SUBCELLULAR LOCATION (SERINE PROTEASE NS3), AND SUBCELLULAR LOCATION
RP (NON-STRUCTURAL PROTEIN 5A).
RX PubMed=28848503; DOI=10.3389/fmicb.2017.01468;
RA Lin J., Wang C., Zhang L., Wang T., Zhang J., Liang W., Li C., Qian G.,
RA Ouyang Y., Guo K., Zhang Y.;
RT "Rab5 Enhances Classical Swine Fever Virus Proliferation and Interacts with
RT Viral NS4B Protein to Facilitate Formation of NS4B Related Complex.";
RL Front. Microbiol. 8:1468-1468(2017).
RN [31]
RP FUNCTION (E(RNS) GLYCOPROTEIN), AND SUBUNIT (E(RNS) GLYCOPROTEIN).
RX PubMed=29235980; DOI=10.1099/jgv.0.000990;
RA Tucakov A.K., Yavuz S., Schuermann E.M., Mischler M., Klingebeil A.,
RA Meyers G.;
RT "dimerization via pseudoreversion partially restores virulence of classical
RT swine fever virus.";
RL J. Gen. Virol. 99:86-96(2018).
RN [32]
RP FUNCTION (NON-STRUCTURAL PROTEIN 4B), INTERACTION WITH HOST FTH1
RP (NON-STRUCTURAL PROTEIN 4B), AND SUBCELLULAR LOCATION (NON-STRUCTURAL
RP PROTEIN 4B).
RX PubMed=29844394; DOI=10.1038/s41598-018-26777-8;
RA Qian G., Lv H., Lin J., Li X., Lv Q., Wang T., Zhang J., Dong W., Guo K.,
RA Zhang Y.;
RT "FHC, an NS4B-interacting Protein, Enhances Classical Swine Fever Virus
RT Propagation and Acts Positively in Viral Anti-apoptosis.";
RL Sci. Rep. 8:8318-8318(2018).
RN [33]
RP INTERACTION WITH HOST RSAD2 (NON-STRUCTURAL PROTEIN 5A).
RX PubMed=31517388; DOI=10.1002/jmv.25595;
RA Xu C., Feng L., Chen P., Li A., Guo S., Jiao X., Zhang C., Zhao Y., Jin X.,
RA Zhong K., Guo Y., Zhu H., Han L., Yang G., Li H., Wang Y.;
RT "Viperin inhibits classical swine fever virus replication by interacting
RT with viral nonstructural 5A protein.";
RL J. Med. Virol. 92:149-160(2020).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1782-2280.
RX PubMed=25653438; DOI=10.1128/jvi.03165-14;
RA Tortorici M.A., Duquerroy S., Kwok J., Vonrhein C., Perez J., Lamp B.,
RA Bricogne G., Ruemenapf T., Vachette P., Rey F.A.;
RT "X-ray structure of the pestivirus NS3 helicase and its conformation in
RT solution.";
RL J. Virol. 89:4356-4371(2015).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1590-2280, AND INTERACTION WITH
RP NS4A (SERINE PROTEASE NS3).
RX PubMed=28151973; DOI=10.1371/journal.ppat.1006134;
RA Dubrau D., Tortorici M.A., Rey F.A., Tautz N.;
RT "A positive-strand RNA virus uses alternative protein-protein interactions
RT within a viral protease/cofactor complex to switch between RNA replication
RT and virion morphogenesis.";
RL PLoS Pathog. 13:E1006134-E1006134(2017).
CC -!- FUNCTION: [N-terminal protease]: Leader cysteine autoprotease that
CC cleaves itself from the nascent polyprotein during translation of the
CC viral mRNA. Once released, plays a role in the inhibition of host
CC innate immune response by interacting with host IRF3 and inducing its
CC proteasomal degradation. {ECO:0000269|PubMed:17215286,
CC ECO:0000269|PubMed:24606708, ECO:0000269|PubMed:27334592}.
CC -!- FUNCTION: [Capsid protein C]: Packages viral RNA to form a viral
CC nucleocapsid and thereby protects viral RNA. Also plays a role in
CC transcription regulation. Protects the incoming virus against IFN-
CC induced effectors. {ECO:0000269|PubMed:28290554,
CC ECO:0000269|PubMed:9617770}.
CC -!- FUNCTION: [E(rns) glycoprotein]: Plays a role in viral entry. Interacts
CC with host RPSA that acts as a cellular attachment receptor for the
CC virus. Possesses also intrinsic ribonuclease (RNase) activity that can
CC inhibit the production of type I interferon and assist in the
CC development of persistent infections. {ECO:0000269|PubMed:19264773,
CC ECO:0000269|PubMed:19767841, ECO:0000269|PubMed:25694590,
CC ECO:0000269|PubMed:29235980, ECO:0000269|PubMed:8356450}.
CC -!- FUNCTION: [Envelope glycoprotein E1]: Plays a role in cell attachment
CC and subsequent fusion of viral and cellular membranes. Therefore,
CC mediates together with envelope glycoprotein E2 the viral entry.
CC {ECO:0000269|PubMed:15527858}.
CC -!- FUNCTION: [Envelope glycoprotein E2]: Plays a role in cell attachment
CC and subsequent fusion of viral and cellular membranes. Therefore,
CC mediates together with envelope glycoprotein E1 the viral entry.
CC {ECO:0000269|PubMed:15527858}.
CC -!- FUNCTION: [Viroporin p7]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin. Forms ion conductive pores,
CC which alters the cell permeability allowing the transport of ions and
CC other small molecules. {ECO:0000269|PubMed:22496228,
CC ECO:0000269|PubMed:24189547}.
CC -!- FUNCTION: [Non-structural protein 2-3]: Autoprotease that associates
CC with the host chaperone JIV and cleaves the NS2-3 protein between NS2
CC and NS3. Also plays a role in the formation of infectious particles.
CC {ECO:0000269|PubMed:17482232}.
CC -!- FUNCTION: [Cysteine protease NS2]: Plays a role in the regulation of
CC viral RNA replication. {ECO:0000269|PubMed:10438869}.
CC -!- FUNCTION: [Serine protease NS3]: Multifunctional protein that contains
CC an N-terminal protease and a C-terminal helicase, playing essential
CC roles in viral polyprotein processing and viral genome replication. The
CC chymotrypsin-like serine protease activity utilizes NS4A as an
CC essential cofactor and catalyzes the cleavage of the polyprotein
CC leading to the release of NS4A, NS4B, NS5A, and NS5B. Plays a role in
CC the inhibition of host NF-kappa-B activation by interacting with and
CC inhibiting host TRAF6. Interacts with NS5B to enhance RNA-dependent RNA
CC polymerase activity. {ECO:0000269|PubMed:19185595,
CC ECO:0000269|PubMed:28751780}.
CC -!- FUNCTION: [Non-structural protein 4A]: Acts as a cofactor for the NS3
CC protease activity. {ECO:0000269|PubMed:17482232}.
CC -!- FUNCTION: [Non-structural protein 4B]: Induces a specific membrane
CC alteration that serves as a scaffold for the virus replication complex
CC (By similarity). Antagonizes host cell apoptosis by interacting with
CC host ferritin heavy chain. The ORF4 protein physically binds host
CC FTH1/FHC, resulting in the reduction of FTH1 protein levels in host
CC cells. Reduction of FTH1 concentration further inhibits the
CC accumulation of reactive oxygen in host cells, leading to reduced
CC apoptosis (PubMed:29844394) (By similarity).
CC {ECO:0000250|UniProtKB:O56125, ECO:0000250|UniProtKB:Q9Q6P4,
CC ECO:0000269|PubMed:29844394}.
CC -!- FUNCTION: [Non-structural protein 5A]: Regulates viral RNA replication
CC by interacting with the 3'-untranslated region of viral RNA in a dose-
CC dependent manner. At small concentrations promotes viral synthesis by
CC interacting with the polymerase NS5B while at large concentrations,
CC inhibits replication. {ECO:0000269|PubMed:22261205,
CC ECO:0000269|PubMed:22795973}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral (+) and
CC (-) genome. {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=Leu is conserved at position P1 for all four cleavage sites.
CC Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: [N-terminal protease]: Interacts with host IRF3.
CC {ECO:0000269|PubMed:17215286, ECO:0000269|PubMed:27334592}.
CC -!- SUBUNIT: [Capsid protein C]: Interacts with host OS9 (PubMed:25010283).
CC {ECO:0000269|PubMed:25010283}.
CC -!- SUBUNIT: [E(rns) glycoprotein]: Homodimer; disulfide-linked
CC (PubMed:29235980, PubMed:1870198). Interacts with host RPSA
CC (PubMed:25694590). {ECO:0000269|PubMed:1870198,
CC ECO:0000269|PubMed:25694590, ECO:0000269|PubMed:29235980}.
CC -!- SUBUNIT: [Envelope glycoprotein E1]: Homodimer; disulfide-linked
CC (PubMed:2370675). Heterodimer with E1; disulfide-linked
CC (PubMed:2370675). {ECO:0000269|PubMed:2370675}.
CC -!- SUBUNIT: [Envelope glycoprotein E2]: Homodimer; disulfide-linked
CC (PubMed:2370675). Heterodimer with E1; disulfide-linked
CC (PubMed:2370675). Interacts with host TRX2 (PubMed:26041303).
CC {ECO:0000269|PubMed:2370675, ECO:0000269|PubMed:26041303}.
CC -!- SUBUNIT: [Serine protease NS3]: Interacts with host TRAF6; this
CC interaction inhibits host NF-kappa-B pathway. Interacts with NS5B; this
CC interaction enhances RNA-dependent RNA polymerase activity. Interacts
CC with protein NS4A. {ECO:0000305}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with host RAB5, this
CC interaction facilitates the formation of NS4B-related complex
CC (PubMed:28848503). Interacts with host FTH1; this interaction plays a
CC positive role in viral anti-apoptosis (PubMed:29844394).
CC {ECO:0000269|PubMed:28848503, ECO:0000269|PubMed:29844394}.
CC -!- SUBUNIT: [Non-structural protein 5A]: Interacts with RNA-directed RNA
CC polymerase (PubMed:22795973). Interacts with host RSAD2; this
CC interaction inhibits viral replication (PubMed:31517388).
CC {ECO:0000269|PubMed:22795973, ECO:0000269|PubMed:31517388}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with NS5A; this
CC interaction promotes viral replication. {ECO:0000269|PubMed:22795973,
CC ECO:0000269|PubMed:31517388}.
CC -!- INTERACTION:
CC PRO_0000038050; Q08211: DHX9; Xeno; NbExp=6; IntAct=EBI-10901281, EBI-352022;
CC PRO_0000038050; Q764M6: IRF3; Xeno; NbExp=4; IntAct=EBI-10901281, EBI-12512266;
CC PRO_0000038050; P67809: YBX1; Xeno; NbExp=4; IntAct=EBI-10901281, EBI-354065;
CC PRO_0000038060; F1S912: FKBP8; Xeno; NbExp=4; IntAct=EBI-12513719, EBI-12512146;
CC -!- SUBCELLULAR LOCATION: [N-terminal protease]: Host cytoplasm
CC {ECO:0000269|PubMed:17215286}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000269|PubMed:28290554}.
CC -!- SUBCELLULAR LOCATION: [E(rns) glycoprotein]: Host cell membrane
CC {ECO:0000269|PubMed:28290554}; Peripheral membrane protein. Virion
CC membrane {ECO:0000269|PubMed:28290554}; Peripheral membrane protein
CC {ECO:0000305}. Note=The C-terminus membrane anchor of Erns represents
CC an amphipathic helix embedded in plane into the membrane.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Host cell surface
CC {ECO:0000269|PubMed:28290554}. Virion membrane
CC {ECO:0000269|PubMed:28290554}.
CC -!- SUBCELLULAR LOCATION: [Cysteine protease NS2]: Host membrane
CC {ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU01029}.
CC -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host cytoplasm
CC {ECO:0000269|PubMed:28848503}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host cytoplasm
CC {ECO:0000269|PubMed:28848503, ECO:0000269|PubMed:29844394}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host cytoplasm
CC {ECO:0000269|PubMed:28848503}.
CC -!- INDUCTION: Translated cap independently from an internal ribosome entry
CC site (IRES). {ECO:0000269|PubMed:9573242}.
CC -!- PTM: [E(rns) glycoprotein]: Heavily glycosylated.
CC {ECO:0000269|PubMed:1870198}.
CC -!- PTM: The viral RNA of pestiviruses is expressed as a single polyprotein
CC which undergoes post-translational proteolytic processing resulting in
CC the production of at least eleven individual proteins. The N-terminal
CC protease cleaves itself from the nascent polyprotein autocatalytically
CC and thereby generates the N-terminus of the adjacent viral capsid
CC protein C. {ECO:0000269|PubMed:8230432, ECO:0000269|PubMed:8388499}.
CC -!- PTM: [Genome polyprotein]: Cleavage between E2 and p7 is partial.
CC -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC {ECO:0000305}.
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DR EMBL; J04358; AAA43844.2; -; Genomic_RNA.
DR PDB; 4CBG; X-ray; 2.82 A; A/B/C/D=1782-2280.
DR PDB; 4CBH; X-ray; 2.51 A; A/B/C/D=1782-2280.
DR PDB; 4CBI; X-ray; 3.00 A; A/B/C/D=1782-2280.
DR PDB; 4CBL; X-ray; 3.05 A; A/B/C/D=1792-2280.
DR PDB; 4CBM; X-ray; 3.27 A; A/B/C/D=1782-2280.
DR PDB; 5MZ4; X-ray; 3.05 A; A/B=1590-2280.
DR PDBsum; 4CBG; -.
DR PDBsum; 4CBH; -.
DR PDBsum; 4CBI; -.
DR PDBsum; 4CBL; -.
DR PDBsum; 4CBM; -.
DR PDBsum; 5MZ4; -.
DR SMR; P19712; -.
DR IntAct; P19712; 96.
DR MEROPS; C53.001; -.
DR MEROPS; S31.001; -.
DR PRIDE; P19712; -.
DR BRENDA; 3.4.21.113; 1439.
DR Proteomes; UP000008568; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IDA:UniProtKB.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IDA:AgBase.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IDA:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:AgBase.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IDA:UniProtKB.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IDA:UniProtKB.
DR GO; GO:0039501; P:suppression by virus of host type I interferon production; IDA:AgBase.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.30.140.40; -; 1.
DR Gene3D; 2.60.320.20; -; 1.
DR Gene3D; 2.60.40.3000; -; 1.
DR Gene3D; 2.60.40.4200; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR021824; Capsid-C_pestivirus.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022120; NS2.
DR InterPro; IPR030399; NS2_C74.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008751; Peptidase_C53.
DR InterPro; IPR042542; Peptidase_C53_interaction.
DR InterPro; IPR032521; Pestivirus_E2.
DR InterPro; IPR042309; Pestivirus_E2_A.
DR InterPro; IPR042310; Pestivirus_E2_B.
DR InterPro; IPR042311; Pestivirus_E2_D.
DR InterPro; IPR000280; Pestivirus_NS3_S31.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR Pfam; PF11889; DUF3409; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF05550; Peptidase_C53; 1.
DR Pfam; PF12387; Peptidase_C74; 1.
DR Pfam; PF05578; Peptidase_S31; 1.
DR Pfam; PF16329; Pestivirus_E2; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR PRINTS; PR00729; CDVENDOPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR PROSITE; PS51876; PV_NPRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Direct protein sequencing; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW Hydrolase; Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW Ion channel; Ion transport; Membrane; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
KW Serine protease; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Transport; Viral attachment to host cell;
KW Viral immunoevasion; Viral ion channel;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus entry into host cell.
FT CHAIN 1..3898
FT /note="Genome polyprotein"
FT /id="PRO_0000450893"
FT CHAIN 1..168
FT /note="N-terminal protease"
FT /id="PRO_0000038050"
FT CHAIN 169..267
FT /note="Capsid protein C"
FT /id="PRO_0000038051"
FT CHAIN 268..494
FT /note="E(rns) glycoprotein"
FT /id="PRO_0000038052"
FT CHAIN 495..656
FT /note="Envelope glycoprotein E1"
FT /id="PRO_0000038053"
FT CHAIN 657..1062
FT /note="Envelope glycoprotein E2"
FT /id="PRO_0000038054"
FT CHAIN 1063..1132
FT /note="Viroporin p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038055"
FT CHAIN 1133..2272
FT /note="Non-structural protein 2-3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038056"
FT CHAIN 1133..1589
FT /note="Cysteine protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT /id="PRO_0000349361"
FT CHAIN 1590..2272
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038057"
FT CHAIN 2273..2336
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038058"
FT CHAIN 2337..2683
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038059"
FT CHAIN 2684..3180
FT /note="Non-structural protein 5A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038060"
FT CHAIN 3181..3898
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038061"
FT TRANSMEM 1140..1164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1281..1301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1360..1380
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1568..1588
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1..168
FT /note="Peptidase C53"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT DOMAIN 1441..1589
FT /note="Peptidase C74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1590..1763
FT /note="Peptidase S31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT DOMAIN 1802..1960
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1978..2179
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 3519..3642
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 32..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224,
FT ECO:0000269|PubMed:9499122"
FT ACT_SITE 69
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224,
FT ECO:0000269|PubMed:24606708, ECO:0000269|PubMed:9499122"
FT ACT_SITE 1447
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1461
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1512
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1658
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1695
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1752
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT SITE 168..169
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT SITE 267..268
FT /note="Cleavage; by host signal peptidase"
FT SITE 494..495
FT /note="Cleavage"
FT SITE 656..657
FT /note="Cleavage; by host signal peptidase"
FT SITE 1062..1063
FT /note="Cleavage; by host signal peptidase; partial"
FT /evidence="ECO:0000250"
FT SITE 1132..1133
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1589..1590
FT /note="Cleavage; partial; cysteine protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT SITE 2272..2273
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 2336..2337
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 2683..2684
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 3180..3181
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1713
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2134
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2217
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2494
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2787
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2815
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2891
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3211
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3316
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3689
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3698
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3794
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 387
FT /note="T -> A"
FT VARIANT 3542
FT /note="R -> S"
FT MUTAGEN 22
FT /note="E->V: Almost complete loss of cleavage between N-pro
FT and C."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 40
FT /note="H->L: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 49
FT /note="H->L: Complete loss of cleavage between N-pro and
FT C."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 69
FT /note="C->A: Complete loss of cleavage between N-pro and
FT C."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 69
FT /note="C->S: Complete loss of cleavage between N-pro and
FT C."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 99
FT /note="H->L: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 112
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 112
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 130
FT /note="H->L: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 134
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 134
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 138
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 138
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 161
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT MUTAGEN 161
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:9499122"
FT STRAND 1592..1602
FT /evidence="ECO:0007829|PDB:5MZ4"
FT HELIX 1607..1614
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1632..1639
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1642..1649
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1652..1655
FT /evidence="ECO:0007829|PDB:5MZ4"
FT HELIX 1657..1660
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1665..1669
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1672..1676
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1680..1682
FT /evidence="ECO:0007829|PDB:5MZ4"
FT TURN 1683..1686
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1687..1691
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1703..1712
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1718..1727
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1730..1734
FT /evidence="ECO:0007829|PDB:5MZ4"
FT HELIX 1745..1748
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1755..1758
FT /evidence="ECO:0007829|PDB:5MZ4"
FT TURN 1759..1761
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1764..1767
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1770..1777
FT /evidence="ECO:0007829|PDB:5MZ4"
FT STRAND 1780..1782
FT /evidence="ECO:0007829|PDB:5MZ4"
FT HELIX 1792..1803
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1810..1814
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1817..1819
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1821..1823
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 1824..1833
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1839..1845
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 1846..1859
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1865..1871
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1880..1885
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 1886..1889
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 1894..1901
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1905..1910
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 1912..1914
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 1917..1927
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 1928..1932
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1935..1939
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 1956..1958
FT /evidence="ECO:0007829|PDB:4CBH"
FT TURN 1970..1972
FT /evidence="ECO:0007829|PDB:4CBL"
FT STRAND 1973..1976
FT /evidence="ECO:0007829|PDB:4CBG"
FT STRAND 1979..1982
FT /evidence="ECO:0007829|PDB:4CBG"
FT HELIX 1983..1987
FT /evidence="ECO:0007829|PDB:4CBG"
FT STRAND 1990..1993
FT /evidence="ECO:0007829|PDB:4CBG"
FT HELIX 1997..2009
FT /evidence="ECO:0007829|PDB:4CBG"
FT STRAND 2014..2017
FT /evidence="ECO:0007829|PDB:4CBG"
FT HELIX 2024..2030
FT /evidence="ECO:0007829|PDB:4CBG"
FT STRAND 2032..2034
FT /evidence="ECO:0007829|PDB:4CBG"
FT STRAND 2036..2041
FT /evidence="ECO:0007829|PDB:4CBG"
FT HELIX 2042..2045
FT /evidence="ECO:0007829|PDB:4CBI"
FT STRAND 2054..2057
FT /evidence="ECO:0007829|PDB:4CBG"
FT STRAND 2061..2068
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2070..2073
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2075..2082
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2086..2093
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2096..2100
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2103..2105
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2112..2114
FT /evidence="ECO:0007829|PDB:4CBG"
FT HELIX 2118..2124
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2125..2128
FT /evidence="ECO:0007829|PDB:4CBH"
FT TURN 2129..2132
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2135..2146
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2153..2166
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2173..2181
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2188..2193
FT /evidence="ECO:0007829|PDB:4CBH"
FT TURN 2194..2196
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2204..2207
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2210..2215
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2234..2237
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2238..2246
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2257..2270
FT /evidence="ECO:0007829|PDB:4CBH"
FT HELIX 2272..2275
FT /evidence="ECO:0007829|PDB:4CBH"
FT STRAND 2276..2279
FT /evidence="ECO:0007829|PDB:5MZ4"
SQ SEQUENCE 3898 AA; 438578 MW; 2C1F17B8A359D0F6 CRC64;
MELNHFELLY KTSKQKPVGV EEPVYDTAGR PLFGNPSEVH PQSTLKLPHD RGRGDIRTTL
RDLPRKGDCR SGNHLGPVSG IYIKPGPVYY QDYTGPVYHR APLEFFDEAQ FCEVTKRIGR
VTGSDGKLYH IYVCVDGCIL LKLAKRGTPR TLKWIRNFTN CPLWVTSCSD DGASGSKDKK
PDRMNKGKLK IAPREHEKDS KTKPPDATIV VEGVKYQIKK KGKVKGKNTQ DGLYHNKNKP
PESRKKLEKA LLAWAVITIL LYQPVAAENI TQWNLSDNGT NGIQRAMYLR GVNRSLHGIW
PEKICKGVPT HLATDTELKE IRGMMDASER TNYTCCRLQR HEWNKHGWCN WYNIDPWIQL
MNRTQTNLTE GPPDKECAVT CRYDKNTDVN VVTQARNRPT TLTGCKKGKN FSFAGTVIEG
PCNFNVSVED ILYGDHECGS LLQDTALYLL DGMTNTIENA RQGAARVTSW LGRQLSTAGK
KLERRSKTWF GAYALSPYCN VTRKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI
LHEMGGHLSE FLLLSLVILS DFAPETASTL YLILHYAIPQ SHEEPEGCDT NQLNLTVKLR
TEDVVPSSVW NIGKYVCVRP DWWPYETKVA LLFEEAGQVI KLVLRALRDL TRVWNSASTT
AFLICLIKVL RGQVVQGIIW LLLVTGAQGR LACKEDYRYA ISSTNEIGLL GAEGLTTTWK
EYSHGLQLDD GTVKAVCTAG SFKVTALNVV SRRYLASLHK RALPTSVTFE LLFDGTNPAI
EEMDDDFGFG LCPFDTSPVI KGKYNTTLLN GSAFYLVCPI GWTGVVECTA VSPTTLRTEV
VKTFRRDKPF PHRVDCVTTI VEKEDLFHCK LGGNWTCVKG DPVTYKGGQV KQCRWCGFEF
KEPYGLPHYP IGKCILTNET GYRVVDSTDC NRDGVVISTE GEHECLIGNT TVKVHALDER
LGPMPCRPKE IVSSEGPVRK TSCTFNYTKT LRNKYYEPRD SYFQQYMLKG EYQYWFNLDV
TDHHTDYFAE FVVLVVVALL GGRYVLWLIV TYIILTEQLA AGLQLGQGEV VLIGNLITHT
DNEVVVYFLL LYLVIRDEPI KKWILLLFHA MTNNPVKTIT VALLMISGVA KGGKIDGGWQ
RQPVTSFDIQ LALAVVVVVV MLLAKRDPTT FPLVITVATL RTAKITNGFS TDLVIATVSA
ALLTWTYISD YYKYKTWLQY LVSTVTGIFL IRVLKGIGEL DLHAPTLPSH RPLFYILVYL
ISTAVVTRWN LDVAGLLLQC VPTLLMVFTM WADILTLILI LPTYELTKLY YLKEVKIGAE
RGWLWKTNYK RVNDIYEVDQ TSEGVYLFPS KQRTSAITST MLPLIKAILI SCISNKWQLI
YLLYLIFEVS YYLHKKVIDE IAGGTNFVSR LVAALIEVNW AFDNEEVKGL KKFFLLSSRV
KELIIKHKVR NEVVVRWFGD EEIYGMPKLI GLVKAATLSR NKHCMLCTVC EDRDWRGETC
PKCGRFGPPV VCGMTLADFE EKHYKRIFIR EDQSGGPLRE EHAGYLQYKA RGQLFLRNLP
VLATKVKMLL VGNLGTEIGD LEHLGWVLRG PAVCKKVTEH ERCTTSIMDK LTAFFGVMPR
GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ GGISSVDHVT CGKDLLVCDT MGRTRVVCQS
NNKMTDESEY GVKTDSGCPE GARCYVFNPE AVNISGTKGA MVHLQKTGGE FTCVTASGTP
AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK SATDLTEMVK
KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE SVYQYMRQKH
PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMSQPKLRAA MVEYSFIFLD EYHCATPEQL
AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG QKHPIEEFIA PEVMKGEDLG SEYLDIAGLK
IPVEEMKNNM LVFVPTRNMA VEAAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT
NAIESGVTLP DLDVVVDTGL KCEKRIRLSP KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK
PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE EDSLMITQLE
ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP VLFPKIRNGE VTDTYDNYTF
LNARKLGDDV PPYVYATEDE DLAVELLGLD WPDPGNQGTV EAGRALKQVV GLSTAENALL
VALFGYVGYQ ALSKRHIPVV TDIYSVEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD
VQRCVEAVTN YAREGIQFMK SQALKVRETP TYKETMNTVA DYVKKFIEAL TDSKEDIIKY
GLWGAHTALY KSIGARLGHE TAFATLVVKW LAFGGESISD HIKQAATDLV VYYIINRPQF
PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE PALATLPYAA KALKLFAPTR
LESVVILSTA IYKTYLSIRR GKSDGLLGTG VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN
AIEASEQKRT LLMKVFVKNF LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHLYG
VFYKGWEAKE LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDNIK
SSVREIAISW APAPFSCDWT PTDDRIGLPH ENYLRVETKC PCGYRMKAVK NCAGELRLLE
EGGSFLCRNK FGRGSQNYRV TKYYDDNLSE IKPVIRMEGH VELYYKGATI KLDFNNSKTV
LATDKWEVDH STLVRALKRY TGAGYRGAYL GEKPNHKHLI QRDCATITKD KVCFIKMKRG
CAFTYDLSLH NLTRLIELVH KNNLEDREIP AVTVTTWLAY TFVNEDIGTI KPTFGEKVTP
EKQEEVVLQP AVVVDTTDVA VTVVGETSTM TTGETPTTFT SLGSDSKVRQ VLKLGVDDGQ
YPGPNQQRAS LLEAIQGVDE RPSVLILGSD KATSNRVKTA KNVKIYRSRD PLELREMMKR
GKILVVALSR VDTALLKFVD YKGTFLTRET LEALSLGKPK KRDITKAEAQ WLLRLEDQIE
ELPDWFAAKE PIFLEANIKR DKYHLVGDIA TIKEKAKQLG ATDSTKISKE VGAKVYSMKL
SNWVIQEENK QGSLAPLFEE LLQQCPPGGQ NKTTHMVSAY QLAQGNWVPV SCHVFMGTIP
ARRTKTHPYE AYVKLRELVD EHKMKALCGG SGLSKHNEWV IGKVKYQGNL RTKHMLNPGK
VAEQLHREGY RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR DKIDKEENLQ
TPGLHKKLME VFNALKRPEL EASYDAVDWE ELERGINRKG AAGFFERKNI GEVLDSEKNK
VEEVIDSLKK GRNIRYYETA IPKNEKRDVN DDWTAGDFVD EKKPRVIQYP EAKTRLAITK
VMYKWVKQKP VVIPGYEGKT PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTRDLEL
IRDIQKFYFK KKWHKFIDTL TKHMSEVPVI SADGEVYIRK GQRGSGQPDT SAGNSMLNVL
TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL YEAGKPQKIT
EGDKMKVAYQ FDDIEFCSHT PVQVRWSDNT SSYMPGRNTT TILAKMATRL DSSGERGTIA
YEKAVAFSFL LMYSWNPLIR RICLLVLSTE LQVRPGKSTT YYYEGDPISA YKEVIGHNLF
DLKRTSFEKL AKLNLSMSTL GVWTRHTSKR LLQDCVNVGT KEGNWLVNAD RLVSSKTGNR
YIPGEGHTLQ GKHYEELILA RKPIGNFEGT DRYNLGPIVN VVLRRLKIMM MALIGRGV
