NSP5_ROTP5
ID NSP5_ROTP5 Reviewed; 197 AA.
AC P19715;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 (strain RVA/Pig/United States/OSU/1977/G5P9[7]) (RV-A)
OS (Rotavirus A (strain Ohio State University)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10915;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2549514; DOI=10.1093/nar/17.15.6402;
RA Gonzalez S.A., Burrone O.R.;
RT "Porcine OSU rotavirus segment II sequence shows common features with the
RT viral gene of human origin.";
RL Nucleic Acids Res. 17:6402-6402(1989).
RN [2]
RP GLYCOSYLATION.
RX PubMed=1850914; DOI=10.1016/0042-6822(91)90642-o;
RA Gonzalez S.A., Burrone O.R.;
RT "Rotavirus NS26 is modified by addition of single O-linked residues of N-
RT acetylglucosamine.";
RL Virology 182:8-16(1991).
RN [3]
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 [4]
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 [5]
RP ROLE OF PHOSPHORYLATION BY HOST 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).
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 -!- 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 -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092,
CC ECO:0000269|PubMed:14993647}. 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 ECO:0000269|PubMed:1850914}.
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: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; X15519; CAA33540.1; -; Genomic_RNA.
DR PIR; A34009; VHXRPU.
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; RNA-binding.
FT CHAIN 1..197
FT /note="Non-structural protein 5"
FT /id="PRO_0000149638"
FT REGION 17..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 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..166
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 MOD_RES 153
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT MOD_RES 155
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT MOD_RES 163
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT MOD_RES 165
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
SQ SEQUENCE 197 AA; 21459 MW; 28536725F281CDDA CRC64;
MSLSIDVTSL PSISSSIFKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFNK YMLSKSPEDI
GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSTQSRPS SNVGCDQVDF SLTKGINVSA
NLDSCVSIST DNKKEKSKKD KSRKHYPRIE ADSDSEDYVL DDSDSDDGKC KNCKYKKRCF
ALRVRMKQVA MQLIEDL
