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Truncated polyprotein 1aTF [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2TF]

 1ATF_PRRSS              Reviewed;        1268 AA.
P0DJY0;
24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
24-JUL-2013, sequence version 1.
23-MAY-2018, entry version 16.
RecName: Full=Truncated polyprotein 1aTF;
Contains:
RecName: Full=Nsp1;
EC=3.4.22.-;
Contains:
RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-alpha;
Contains:
RecName: Full=Nsp1-beta papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-beta;
Contains:
RecName: Full=Nsp2TF;
Porcine reproductive and respiratory syndrome virus (isolate
Pig/United States/SD 01-08/2001) (PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=857306;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15019241; DOI=10.1016/j.virusres.2003.12.026;
Fang Y., Kim D.Y., Ropp S., Steen P., Christopher-Hennings J.,
Nelson E.A., Rowland R.R.;
"Heterogeneity in Nsp2 of European-like porcine reproductive and
respiratory syndrome viruses isolated in the United States.";
Virus Res. 100:229-235(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Infectious clone SD 01-08;
PubMed=16971421; DOI=10.1128/JVI.01032-06;
Fang Y., Rowland R.R., Roof M., Lunney J.K., Christopher-Hennings J.,
Nelson E.A.;
"A full-length cDNA infectious clone of North American type 1 porcine
reproductive and respiratory syndrome virus: expression of green
fluorescent protein in the Nsp2 region.";
J. Virol. 80:11447-11455(2006).
[3]
IDENTIFICATION, RIBOSOMAL FRAMESHIFTING, AND DISRUPTION PHENOTYPE.
PubMed=23043113; DOI=10.1073/pnas.1211145109;
Fang Y., Treffers E.E., Li Y., Tas A., Sun Z., van der Meer Y.,
de Ru A.H., van Veelen P.A., Atkins J.F., Snijder E.J., Firth A.E.;
"Efficient -2 frameshifting by mammalian ribosomes to synthesize an
additional arterivirus protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2920-E2928(2012).
[4]
FUNCTION (NSP1-BETA).
STRAIN=SD95-21;
PubMed=24825891; DOI=10.1073/pnas.1321930111;
Li Y., Treffers E.E., Napthine S., Tas A., Zhu L., Sun Z., Bell S.,
Mark B.L., van Veelen P.A., van Hemert M.J., Firth A.E., Brierley I.,
Snijder E.J., Fang Y.;
"Transactivation of programmed ribosomal frameshifting by a viral
protein.";
Proc. Natl. Acad. Sci. U.S.A. 111:E2172-E2181(2014).
-!- FUNCTION: Nsp1: is essential for viral subgenomic mRNA synthesis.
{ECO:0000250}.
-!- FUNCTION: Nsp1-alpha papain-like cysteine proteinase: inhibits
IFN-beta production. Counteracts the action of NF-kappaB by
decreasing the phosphorylation of IkappaB-alpha, such that the
degradation of IkappaB-alpha is suppressed. This leads to the
blockage of NF-kappaB nuclear translocation and thus interference
of NF-kappaB activation. Also seems to inhibit IRF3-dependent
pathways (By similarity). {ECO:0000250}.
-!- FUNCTION: Nsp1-beta transactivates the programmed ribosomal
frameshifting event leading to the expression of the 1aTF
polyprotein. {ECO:0000269|PubMed:24825891}.
-!- SUBCELLULAR LOCATION: Nsp1: Host nucleus {ECO:0000250}. Host
cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nsp1-alpha papain-like cysteine proteinase:
Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nsp1-beta papain-like cysteine proteinase:
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nsp2TF: Host endoplasmic reticulum membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Truncated polyprotein 1aTF;
IsoId=P0DJY0-1; Sequence=Displayed;
Note=Produced by -2 ribosomal frameshifting in the nsp2 gene.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=A0MD28-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=A0MD28-2; Sequence=External;
Note=Produced by conventional translation.;
-!- DISRUPTION PHENOTYPE: Knockout mutants display reduced
infectivity. {ECO:0000269|PubMed:23043113}.
-----------------------------------------------------------------------
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EMBL; AY375474; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; DQ489311; -; NOT_ANNOTATED_CDS; Genomic_RNA.
SMR; P0DJY0; -.
PRIDE; P0DJY0; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000000937; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 3.90.70.60; -; 1.
Gene3D; 3.90.70.70; -; 1.
InterPro; IPR008743; Arterivirus_Nsp2_C33.
InterPro; IPR008741; AV_PCPalpha.
InterPro; IPR038155; AV_PCPalpha_sf.
InterPro; IPR025773; AV_PCPbeta.
InterPro; IPR038154; AV_PCPbeta_sf.
InterPro; IPR032855; NSP2-B_epitope.
InterPro; IPR032841; NSP2_assoc.
Pfam; PF14757; NSP2-B_epitope; 1.
Pfam; PF14758; NSP2_assoc; 1.
Pfam; PF05410; Peptidase_C31; 1.
Pfam; PF05411; Peptidase_C32; 1.
Pfam; PF05412; Peptidase_C33; 1.
PROSITE; PS51538; AV_CP; 1.
PROSITE; PS51539; AV_PCP_ALPHA; 1.
PROSITE; PS51540; AV_PCP_BETA; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Helicase; Host cytoplasm;
Host endoplasmic reticulum; Host membrane; Host nucleus;
Host-virus interaction; Hydrolase; Membrane; Metal-binding;
Nucleotide-binding; Protease; Ribosomal frameshifting; Thiol protease;
Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
CHAIN 1 1268 Truncated polyprotein 1aTF.
{ECO:0000255}.
/FTId=PRO_0000423161.
CHAIN 1 384 Nsp1. {ECO:0000250}.
/FTId=PRO_0000423162.
CHAIN 1 180 Nsp1-alpha papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000423163.
CHAIN 181 385 Nsp1-beta papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000423164.
CHAIN 386 1268 Nsp2TF. {ECO:0000250}.
/FTId=PRO_0000423165.
TRANSMEM 1119 1139 Helical. {ECO:0000255}.
TRANSMEM 1153 1173 Helical. {ECO:0000255}.
TRANSMEM 1194 1214 Helical. {ECO:0000255}.
TRANSMEM 1233 1253 Helical. {ECO:0000255}.
DOMAIN 69 180 Peptidase C31. {ECO:0000255|PROSITE-
ProRule:PRU00872}.
DOMAIN 269 385 Peptidase C32. {ECO:0000255|PROSITE-
ProRule:PRU00873}.
DOMAIN 420 527 Peptidase C33. {ECO:0000255|PROSITE-
ProRule:PRU00871}.
ZN_FING 8 28 C4-type; atypical.
REGION 69 182 PCP1-alpha. {ECO:0000250}.
REGION 269 384 PCP1-beta. {ECO:0000250}.
ACT_SITE 76 76 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 146 146 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 276 276 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 345 345 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 429 429 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 498 498 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
SITE 180 181 Cleavage; by autolysis. {ECO:0000255}.
SITE 385 386 Cleavage; by autolysis. {ECO:0000250}.
SEQUENCE 1268 AA; 139092 MW; 1F4FC8488B70AA65 CRC64;
MSGTFSRCMC TPAARVFWNA GQVFCTRCLS ARPLLSPELQ DTDLGVVGLF YKPKDKIHWK
VPIGIPQVEC TPSGCCWLSA VFPLARMTSG NHNFLQRLVK VADVLYRDGC LAPRHLRELQ
VYERGCSWYP ITGPVPGMGL FANSMHVSDQ PFPGATHVLT NSPLPQRACR QPFCPFEEAH
SDVYRWKKFV IFTDSSPNGR FRMMWTPESD DSAALEVLPP ELERQVEILT RSFPAHHPIN
LADWELTESP ENGFSFGTSH SCGHIVQNPN VFDGKCWLTC FLGQSAEVCY HEEHLANALG
YQTKWGVHGK YLQRRLQVRG MRAVVDPDGP IHVEALSCSQ SWVRHLTLNN DVTPGFVRLT
SIRIVSNTEP TAFRIFRFGA HKWYGAAGKR ARAKRATKSG KDSALAPKIA PPVPTCGITT
YSPPTDGSCG WHVLAAIVNR MINGDFTSPL PQYNRPEDDW ASDYDLAQAI QCLQLPATVV
RNRACPNAKY LIKLNGVHWE VEVRSGMAPR SLSRECVVGV CSEGCVAPPY PADGLPKRAL
EALASAYRLP SDCVSSGIAD FLADPPPQEF WTLDKMLTSP SPERSGFSSL YKLLLEVVPQ
KCGATEGAFV YAVERMLKDC PSPEQAMALL AKIKVPSSKA PSVSLDECFP AGVPADFEPA
FQERPRSPGA AVALCSPDAK GFEGTASEEA QESGHKAVHA VPLAEGPNNE QVQVVAGEQL
ELGGCGLAIG SAQSSSDSKR ENMHNSREDE PLDLSHPAPA ATTTLVGEQT PDNPGSDASA
LPIAVRGFVP TGPILRHVEH CGTESGDSSS PLDLSFAQTL DQPLDLSLAA WPVKATASDP
GWVRGRCEPV FLKPRKAFSD GDSALQFGEL SESSSVIEFD QTKDTLVADA PVDLTTSNEA
LSAVDPSEFV ELRRPRHSAQ ALIDRGGPLA DVHAKIKNRV YEQCLQACEP GSRATPATRE
WLDKMWDRVD MKTWRCTSQF QAGRILASLK FLPDMIQDTP PPVPRKNRAS DNAGLKQLVA
RWDKKLSVTP PPKSAGLVLD QTVPPPTDIQ QEDATPSDGL SHASDFSSRV STSWSWKGLM
LSGTRLAGSA GQRLMTWVFL KFTPISQLLY SHFSRRGALW LQAIGCLQVL FYLLSCSVVL
TQYSDAFPYW VSFLVLCGVF VWVFLVLGWL LLYFYSRLHP TQSVLLVTTI RRNVMLSFWL
LSSANFGNLC AALWLAPQVS YVSSLASYSV GHVISGMLSY VYACLQIWPF LLFMWCPKGV
VTSVGESV


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