1ATF_PRRSS
ID 1ATF_PRRSS Reviewed; 1268 AA.
AC P0DJY0;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Truncated polyprotein 1aTF;
DE Contains:
DE RecName: Full=Nsp1;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-alpha;
DE Contains:
DE RecName: Full=Nsp1-beta papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-beta;
DE Contains:
DE RecName: Full=Nsp2TF;
OS Porcine reproductive and respiratory syndrome virus (isolate Pig/United
OS States/SD 01-08/2001) (PRRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; unclassified Arteriviridae.
OX NCBI_TaxID=857306;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15019241; DOI=10.1016/j.virusres.2003.12.026;
RA Fang Y., Kim D.Y., Ropp S., Steen P., Christopher-Hennings J., Nelson E.A.,
RA Rowland R.R.;
RT "Heterogeneity in Nsp2 of European-like porcine reproductive and
RT respiratory syndrome viruses isolated in the United States.";
RL Virus Res. 100:229-235(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone SD 01-08;
RX PubMed=16971421; DOI=10.1128/jvi.01032-06;
RA Fang Y., Rowland R.R., Roof M., Lunney J.K., Christopher-Hennings J.,
RA Nelson E.A.;
RT "A full-length cDNA infectious clone of North American type 1 porcine
RT reproductive and respiratory syndrome virus: expression of green
RT fluorescent protein in the Nsp2 region.";
RL J. Virol. 80:11447-11455(2006).
RN [3]
RP IDENTIFICATION, RIBOSOMAL FRAMESHIFTING, AND DISRUPTION PHENOTYPE.
RX PubMed=23043113; DOI=10.1073/pnas.1211145109;
RA Fang Y., Treffers E.E., Li Y., Tas A., Sun Z., van der Meer Y., de Ru A.H.,
RA van Veelen P.A., Atkins J.F., Snijder E.J., Firth A.E.;
RT "Efficient -2 frameshifting by mammalian ribosomes to synthesize an
RT additional arterivirus protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2920-E2928(2012).
RN [4]
RP FUNCTION (NSP1-BETA).
RC STRAIN=SD95-21;
RX PubMed=24825891; DOI=10.1073/pnas.1321930111;
RA Li Y., Treffers E.E., Napthine S., Tas A., Zhu L., Sun Z., Bell S.,
RA Mark B.L., van Veelen P.A., van Hemert M.J., Firth A.E., Brierley I.,
RA Snijder E.J., Fang Y.;
RT "Transactivation of programmed ribosomal frameshifting by a viral
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2172-E2181(2014).
CC -!- FUNCTION: [Nsp1]: Is essential for viral subgenomic mRNA synthesis.
CC {ECO:0000250}.
CC -!- FUNCTION: [Nsp1-alpha papain-like cysteine proteinase]: Inhibits IFN-
CC beta production. Counteracts the action of NF-kappaB by decreasing the
CC phosphorylation of IkappaB-alpha, such that the degradation of IkappaB-
CC alpha is suppressed. This leads to the blockage of NF-kappaB nuclear
CC translocation and thus interference of NF-kappaB activation. Also seems
CC to inhibit IRF3-dependent pathways (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Nsp1-beta transactivates the programmed ribosomal
CC frameshifting event leading to the expression of the 1aTF polyprotein.
CC {ECO:0000269|PubMed:24825891}.
CC -!- SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000250}. Host
CC cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]:
CC Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host
CC cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Nsp2TF]: Host endoplasmic reticulum membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Truncated polyprotein 1aTF;
CC IsoId=P0DJY0-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=A0MD28-1; Sequence=External;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=A0MD28-2; Sequence=External;
CC -!- DISRUPTION PHENOTYPE: Knockout mutants display reduced infectivity.
CC {ECO:0000269|PubMed:23043113}.
CC -!- MISCELLANEOUS: [Isoform Truncated polyprotein 1aTF]: Produced by -2
CC ribosomal frameshifting in the nsp2 gene.
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DR EMBL; AY375474; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; DQ489311; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0DJY0; -.
DR Proteomes; UP000000937; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR Gene3D; 3.90.70.60; -; 1.
DR Gene3D; 3.90.70.70; -; 1.
DR InterPro; IPR008743; Arterivirus_Nsp2_C33.
DR InterPro; IPR008741; AV_PCPalpha.
DR InterPro; IPR038155; AV_PCPalpha_sf.
DR InterPro; IPR025773; AV_PCPbeta.
DR InterPro; IPR038154; AV_PCPbeta_sf.
DR InterPro; IPR032855; NSP2-B_epitope.
DR InterPro; IPR032841; NSP2_assoc.
DR Pfam; PF14757; NSP2-B_epitope; 1.
DR Pfam; PF14758; NSP2_assoc; 1.
DR Pfam; PF05410; Peptidase_C31; 1.
DR Pfam; PF05411; Peptidase_C32; 1.
DR Pfam; PF05412; Peptidase_C33; 1.
DR PROSITE; PS51538; AV_CP; 1.
DR PROSITE; PS51539; AV_PCP_ALPHA; 1.
DR PROSITE; PS51540; AV_PCP_BETA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Host cytoplasm; Host endoplasmic reticulum;
KW Host membrane; Host nucleus; Host-virus interaction; Hydrolase; Membrane;
KW Metal-binding; Nucleotide-binding; Protease; Ribosomal frameshifting;
KW Thiol protease; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1268
FT /note="Truncated polyprotein 1aTF"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423161"
FT CHAIN 1..384
FT /note="Nsp1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423162"
FT CHAIN 1..180
FT /note="Nsp1-alpha papain-like cysteine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423163"
FT CHAIN 181..385
FT /note="Nsp1-beta papain-like cysteine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423164"
FT CHAIN 386..1268
FT /note="Nsp2TF"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423165"
FT TRANSMEM 1119..1139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1153..1173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1233..1253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..180
FT /note="Peptidase C31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT DOMAIN 269..385
FT /note="Peptidase C32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT DOMAIN 420..527
FT /note="Peptidase C33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ZN_FING 8..28
FT /note="C4-type; atypical"
FT REGION 69..182
FT /note="PCP1-alpha"
FT /evidence="ECO:0000250"
FT REGION 269..384
FT /note="PCP1-beta"
FT /evidence="ECO:0000250"
FT REGION 728..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 146
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 276
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 345
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 429
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 498
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT SITE 180..181
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 385..386
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
SQ 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
