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   24-JAN-2024, entry version 68.
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; Sedoreoviridae; 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. Participates in the selective
CC       exclusion of host proteins from stress granules (SG) and P bodies (PB).
CC       Participates also in the sequestration of these remodeled organelles in
CC       viral factories. {ECO:0000255|HAMAP-Rule:MF_04092}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         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. Participates in the selective exclusion of host proteins from
CC       stress granules (SG) and P bodies (PB). Participates also in the
CC       sequestration of these remodeled organelles in viral factories.
CC       {ECO:0000255|HAMAP-Rule:MF_04092}.
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
//