RPOTF_PRRSL
ID RPOTF_PRRSL Reviewed; 1285 AA.
AC P0DJZ9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Replicase polyprotein 1TF;
DE AltName: Full=ORF1ab polyprotein;
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 (strain Lelystad)
OS (PRRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Variarterivirinae;
OC Betaarterivirus; Eurpobartevirus; Betaarterivirus suid 1.
OX NCBI_TaxID=11049;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8517032; DOI=10.1006/viro.1993.1008;
RA Meulenberg J.J.M., Hulst M.M., de Meijer E.J., Moonen P.L.J.M.,
RA den Besten A., de Kluyver E.P., Wensvoort G., Moormann R.J.M.;
RT "Lelystad virus, the causative agent of porcine epidemic abortion and
RT respiratory syndrome (PEARS), is related to LDV and EAV.";
RL Virology 192:62-72(1993).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [3]
RP FUNCTION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE), AND SUBCELLULAR
RP LOCATION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE).
RC STRAIN=PA8;
RX PubMed=23287061; DOI=10.1016/j.virusres.2012.12.012;
RA Han M., Du Y., Song C., Yoo D.;
RT "Degradation of CREB-binding protein and modulation of type I interferon
RT induction by the zinc finger motif of the porcine reproductive and
RT respiratory syndrome virus nsp1alpha subunit.";
RL Virus Res. 172:54-65(2013).
CC -!- FUNCTION: [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host
CC IFN-beta production. Plays a role in the degradation of the host
CC transcriptional activator CREBBP protein. The degradation of host
CC CREBBP which is a key component of the IFN enhanceosome is likely
CC responsible for the inhibition of interferon mediated by Nsp1-alpha.
CC Participates also in the inhibition of host NF-kappa-B activation.
CC {ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:23287061}.
CC -!- FUNCTION: [Nsp1-beta papain-like cysteine proteinase]: Plays a role in
CC the inhibition of the interferon-activated JAK/STAT signal transduction
CC by mediating the ubiquitination and subsequent proteasomal degradation
CC of host KPNA1. {ECO:0000250|UniProtKB:Q9WJB2}.
CC -!- FUNCTION: [Nsp2TF]: Plays a role in viral replication.
CC {ECO:0000269|PubMed:23043113}.
CC -!- SUBCELLULAR LOCATION: [Nsp1]: Host nucleus
CC {ECO:0000269|PubMed:23287061}. Host cytoplasm
CC {ECO:0000269|PubMed:23287061}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]:
CC Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm
CC {ECO:0000269|PubMed:23287061}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host
CC nucleus {ECO:0000269|PubMed:23287061}.
CC -!- SUBCELLULAR LOCATION: [Nsp2TF]: Host cytoplasm
CC {ECO:0000269|PubMed:23043113}. Host membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Nsp2 and nsp2TF localize to
CC different intracellular compartments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Replicase polyprotein 1TF;
CC IsoId=P0DJZ9-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=Q04561-1; Sequence=External;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=Q04561-2; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1TF]: Produced by a -2
CC ribosomal frameshift.
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DR EMBL; M96262; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0DJZ9; -.
DR Proteomes; UP000006687; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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 Host cytoplasm; Host membrane; Host nucleus; Hydrolase; Membrane;
KW Metal-binding; Protease; Reference proteome; Ribosomal frameshifting;
KW Thiol protease; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1285
FT /note="Replicase polyprotein 1TF"
FT /id="PRO_0000434874"
FT CHAIN 1..384
FT /note="Nsp1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000434875"
FT CHAIN 1..180
FT /note="Nsp1-alpha papain-like cysteine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434876"
FT CHAIN 181..385
FT /note="Nsp1-beta papain-like cysteine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434877"
FT CHAIN 386..1285
FT /note="Nsp2TF"
FT /id="PRO_0000434878"
FT TRANSMEM 1136..1156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1211..1231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1250..1270
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 ZN_FING 8..28
FT /note="C4-type; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q04561"
FT REGION 69..182
FT /note="PCP1-alpha"
FT /evidence="ECO:0000250|UniProtKB:Q04561"
FT REGION 269..384
FT /note="PCP1-beta"
FT /evidence="ECO:0000250|UniProtKB:Q04561"
FT REGION 752..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..788
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:0000250|UniProtKB:Q04561,
FT ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 146
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:Q04561,
FT ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 276
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:Q04561,
FT ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 345
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:Q04561,
FT ECO:0000255|PROSITE-ProRule:PRU00873"
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 1285 AA; 141133 MW; 548F4A21A77E6BE1 CRC64;
MSGTFSRCMC TPAARVFWNA GQVFCTRCLS ARSLLSPELQ DTDLGAVGLF YKPRDKLHWK
VPIGIPQVEC TPSGCCWLSA VFPLARMTSG NHNFLQRLVK VADVLYRDGC LAPRHLRELQ
VYERGCNWYP ITGPVPGMGL FANSMHVSDQ PFPGATHVLT NSPLPQQACR QPFCPFEEAH
SSVYRWKKFV VFTDSSLNGR SRMMWTPESD DSAALEVLPP ELERQVEILI RSFPAHHPVD
LADWELTESP ENGFSFNTSH SCGHLVQNPD VFDGKCWLSC FLGQSVEVRC HEEHLADAFG
YQTKWGVHGK YLQRRLQVRG IRAVVDPDGP IHVEALSCPQ SWIRHLTLDD DVTPGFVRLT
SLRIVPNTEP TTSRIFRFGA HKWYGAAGKR ARAKRAAKSE KDSAPTPKVA LPVPTCGITT
YSPPTDGSCG WHVLAAIMNR MINGDFTSPL TQYNRPEDDW ASDYDLVQAI QCLRLPATVV
RNRACPNAKY LIKLNGVHWE VEVRSGMAPR SLSRECVVGV CSEGCVAPPY PADGLPKRAL
EALASAYRLP SDCVSSGIAD FLANPPPQEF WTLDKMLTSP SPERSGFSSL YKLLLEVVPQ
KCGATEGAFI YAVERMLKDC PSSKQAMALL AKIKVPSSKA PSVSLDECFP TDVLADFEPA
SQERPQSSGA AVVLCSPDAK EFEEAAPEEV QESGHKAVHS ALLAEGPNNE QVQVVAGEQL
KLGGCGLAVG NAHEGALVSA GLINLVGGNL SPSDPMKENM LNSREDEPLD LSQPAPASTT
TLVREQTPDN PGSDAGALPV TVREFVPTGP ILCHVEHCGT ESGDSSSPLD LSDAQTLDQP
LNLSLAAWPV RATASDPGWV HGRREPVFVK PRNAFSDGDS ALQFGELSES SSVIEFDRTK
DAPVVDAPVD LTTSNEALSV VDPFEFAELK RPRFSAQALI DRGGPLADVH AKIKNRVYEQ
CLQACEPGSR ATPATREWLD KMWDRVDMKT WRCTSQFQAG RILASLKFLP DMIQDTPPPV
PRKNRASDNA GLKQLVAQWD RKLSVTPPPK PVGPVLDQIV PPPTDIQQED VTPSDGPPHA
PDFPSRVSTG GSWKGLMLSG TRLAGSISQR LMTWVFLKFS PTSQLLCSHF SRRGALWLQV
IGCLQVSFYL LSCSVVLTRY SDAFPYWVSF LVLCGVFVWV FLVLGWLLLY FYSRLHPTQS
VLLVTTIRRS VMLSFWLLSS ANFGNLCAAL WSAPQASYVS FLASYSVGHV ISGMFSYVYA
CLQIWPFLLF MWCPRGVVTS VGESV
