NSP5_ROTSH
ID NSP5_ROTSH Reviewed; 198 AA.
AC A2T3Q9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Non-structural protein 5 {ECO:0000255|HAMAP-Rule:MF_04092};
DE Short=NSP5 {ECO:0000255|HAMAP-Rule:MF_04092};
DE AltName: Full=NS26 {ECO:0000255|HAMAP-Rule:MF_04092};
OS Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=450149;
OH NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA Small C., Barro M., Brown T.L., Patton J.T.;
RT "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT agent.";
RL Virology 359:415-424(2007).
RN [2]
RP PHOSPHORYLATION.
RX PubMed=8811003; DOI=10.1099/0022-1317-77-9-2059;
RA Afrikanova I., Miozzo M.C., Giambiagi S., Burrone O.R.;
RT "Phosphorylation generates different forms of rotavirus NSP5.";
RL J. Gen. Virol. 77:2059-2065(1996).
RN [3]
RP RNA-BINDING.
RX PubMed=11967345; DOI=10.1128/jvi.76.10.5291-5299.2002;
RA Vende P., Taraporewala Z.F., Patton J.T.;
RT "RNA-binding activity of the rotavirus phosphoprotein NSP5 includes
RT affinity for double-stranded RNA.";
RL J. Virol. 76:5291-5299(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-154; SER-156;
RP SER-164 AND SER-166, AND MUTAGENESIS OF 154-SER--SER-166.
RX PubMed=11884570; DOI=10.1128/jvi.76.7.3461-3470.2002;
RA Eichwald C., Vascotto F., Fabbretti E., Burrone O.R.;
RT "Rotavirus NSP5: mapping phosphorylation sites and kinase activation and
RT viroplasm localization domains.";
RL J. Virol. 76:3461-3470(2002).
RN [5]
RP PHOSPHORYLATION AT SER-67 BY CK1, AND MUTAGENESIS OF SER-67.
RX PubMed=15520389; DOI=10.1073/pnas.0406691101;
RA Eichwald C., Jacob G., Muszynski B., Allende J.E., Burrone O.R.;
RT "Uncoupling substrate and activation functions of rotavirus NSP5:
RT phosphorylation of Ser-67 by casein kinase 1 is essential for
RT hyperphosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16304-16309(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NSP2.
RX PubMed=14993647; DOI=10.1099/vir.0.19611-0;
RA Eichwald C., Rodriguez J.F., Burrone O.R.;
RT "Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of
RT viroplasm formation.";
RL J. Gen. Virol. 85:625-634(2004).
RN [7]
RP ROLE OF PHOSPHORYLATION BY CK1.
RX PubMed=17872534; DOI=10.1099/vir.0.82922-0;
RA Campagna M., Budini M., Arnoldi F., Desselberger U., Allende J.E.,
RA Burrone O.R.;
RT "Impaired hyperphosphorylation of rotavirus NSP5 in cells depleted of
RT casein kinase 1alpha is associated with the formation of viroplasms with
RT altered morphology and a moderate decrease in virus replication.";
RL J. Gen. Virol. 88:2800-2810(2007).
RN [8]
RP FUNCTION.
RX PubMed=17825341; DOI=10.1016/j.virol.2007.07.029;
RA Bar-Magen T., Spencer E., Patton J.T.;
RT "An ATPase activity associated with the rotavirus phosphoprotein NSP5.";
RL Virology 369:389-399(2007).
RN [9]
RP INTERACTION WITH VP1, AND SUBCELLULAR LOCATION.
RX PubMed=17182692; DOI=10.1128/jvi.01494-06;
RA Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.;
RT "Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is
RT stronger than that with NSP2.";
RL J. Virol. 81:2128-2137(2007).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) IN COMPLEX WITH NSP2.
RX PubMed=16928740; DOI=10.1128/jvi.01347-06;
RA Jiang X., Jayaram H., Kumar M., Ludtke S.J., Estes M.K., Prasad B.V.V.;
RT "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA
RT complexes: implications for genome replication.";
RL J. Virol. 80:10829-10835(2006).
CC -!- FUNCTION: Plays an essential role in the viral genome replication.
CC Participates, together with NSP2, in the formation of viral factories
CC (viroplasms) which are large inclusions in the host cytoplasm where
CC replication intermediates are assembled and viral RNA replication takes
CC place. Orchestrates the recruitment of viroplasmic proteins such as
CC capsid proteins to these factories. {ECO:0000255|HAMAP-Rule:MF_04092,
CC ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:17825341}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04092};
CC -!- SUBUNIT: Homodimer. Interacts with VP1. Interacts with VP2. Interacts
CC with NSP2; this interaction leads to up-regulation of NSP5
CC hyperphosphorylation and formation of virus factories. Interacts with
CC NSP6. {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:14993647,
CC ECO:0000269|PubMed:16928740, ECO:0000269|PubMed:17182692}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092,
CC ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:14993647,
CC ECO:0000269|PubMed:17182692}. Note=Found in spherical cytoplasmic
CC structures, called virus factories, that appear early after infection
CC and are the site of viral replication and packaging.
CC {ECO:0000255|HAMAP-Rule:MF_04092}.
CC -!- PTM: O-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04092}.
CC -!- PTM: Hyperphosphorylated on serine residues, when in dimeric form.
CC Phosphorylation by host CK1 is required for the hyperphosphorylation of
CC NSP5 dimer. {ECO:0000255|HAMAP-Rule:MF_04092,
CC ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:15520389,
CC ECO:0000269|PubMed:17872534, ECO:0000269|PubMed:8811003}.
CC -!- SIMILARITY: Belongs to the rotavirus NSP5 family. {ECO:0000255|HAMAP-
CC Rule:MF_04092}.
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DR EMBL; DQ838630; ABG75808.1; -; Genomic_RNA.
DR RefSeq; YP_002302224.1; NC_011505.2.
DR iPTMnet; A2T3Q9; -.
DR GeneID; 7011364; -.
DR KEGG; vg:7011364; -.
DR Proteomes; UP000001119; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019079; P:viral genome replication; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04092; ROTA_NSP5; 1.
DR InterPro; IPR002512; Rotavirus_A/C_NSP5.
DR Pfam; PF01525; Rota_NS26; 1.
DR PIRSF; PIRSF004006; Rota_NS26; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..198
FT /note="Non-structural protein 5"
FT /id="PRO_0000367825"
FT REGION 1..48
FT /note="Interaction with VP1"
FT /evidence="ECO:0000269|PubMed:17182692"
FT REGION 13..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT MOD_RES 67
FT /note="Phosphoserine; by host CK1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092,
FT ECO:0000269|PubMed:15520389"
FT MOD_RES 154
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092,
FT ECO:0000305|PubMed:11884570"
FT MOD_RES 156
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092,
FT ECO:0000305|PubMed:11884570"
FT MOD_RES 164
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092,
FT ECO:0000305|PubMed:11884570"
FT MOD_RES 166
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092,
FT ECO:0000305|PubMed:11884570"
FT MUTAGEN 67
FT /note="S->A: Loss of hyperphosphorylation."
FT /evidence="ECO:0000269|PubMed:15520389"
FT MUTAGEN 67
FT /note="S->D: Constitutively hyperphosphorylated even in the
FT absence of infection."
FT /evidence="ECO:0000269|PubMed:15520389"
FT MUTAGEN 154..166
FT /note="SDSDDYVLDDSDS->ADADDYVLDDADA: Loss of
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:11884570"
SQ SEQUENCE 198 AA; 21722 MW; 1DE1EC4A803E1D57 CRC64;
MSLSIDVTSL PSIPSTIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFNK YMLSKSPEDI
GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSAQSRPS SNVGCDQVDF SLNKGLKVKA
NLDSSISIST DTKKEKSKQN HKSRKHYPRI EAESDSDDYV LDDSDSDDGK CKNCKYKKKY
FALRMRMKQV AMQLIEDL
