NSP3_ROTBU
ID NSP3_ROTBU Reviewed; 313 AA.
AC P04514;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 29-SEP-2021, entry version 77.
DE RecName: Full=Non-structural protein 3 {ECO:0000255|HAMAP-Rule:MF_04094};
DE Short=NSP3 {ECO:0000255|HAMAP-Rule:MF_04094};
DE AltName: Full=NCVP4 {ECO:0000255|HAMAP-Rule:MF_04094};
DE AltName: Full=Non-structural RNA-binding protein 34 {ECO:0000255|HAMAP-Rule:MF_04094};
DE Short=NS34 {ECO:0000255|HAMAP-Rule:MF_04094};
OS Rotavirus A (strain RVA/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10934;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6324473; DOI=10.1016/0042-6822(84)90292-7;
RA Ward C.W., Elleman T.C., Azad A.A., Dyall-Smith M.L.;
RT "Nucleotide sequence of gene segment 9 encoding a nonstructural protein of
RT UK bovine rotavirus.";
RL Virology 134:249-253(1984).
CC -!- FUNCTION: Plays an important role in stimulating the translation of
CC viral mRNAs. These mRNAs are capped but not polyadenylated, instead
CC terminating in a conserved sequence 'GACC' at the 3' that is recognized
CC by NSP3, which competes with host PABPC1 for EIF4G1 binding. The
CC interaction between NSP3 and host EIF4G1 stabilizes the EIF4E-EIF4G1
CC interaction, thereby facilitating the initiation of capped mRNA
CC translation. {ECO:0000255|HAMAP-Rule:MF_04094}.
CC -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with host
CC ZC3H7B (via LD motif). Interacts with host EIF4G1. {ECO:0000255|HAMAP-
CC Rule:MF_04094}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04094}.
CC -!- SIMILARITY: Belongs to the rotavirus NSP3 family. {ECO:0000255|HAMAP-
CC Rule:MF_04094}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47317.1; Type=Erroneous initiation;
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DR EMBL; K02170; AAA47317.1; ALT_INIT; Genomic_RNA.
DR SMR; P04514; -.
DR Proteomes; UP000008657; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.280.20; -; 1.
DR HAMAP; MF_04094; ROTA_A_NSP3; 1.
DR HAMAP; MF_04090; ROTA_NSP3; 1.
DR InterPro; IPR042519; NSP3_N_rotavirus.
DR InterPro; IPR036082; NSP3_sf.
DR InterPro; IPR002873; Rotavirus_NSP3.
DR Pfam; PF01665; Rota_NSP3; 1.
DR SUPFAM; SSF69903; SSF69903; 1.
PE 3: Inferred from homology;
KW Coiled coil; Host cytoplasm; Host-virus interaction; RNA-binding;
KW Translation regulation.
FT CHAIN 1..313
FT /note="Non-structural protein 3"
FT /id="PRO_0000149540"
FT REGION 1..149
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT REGION 150..206
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT REGION 170..234
FT /note="Interaction with host ZC3H7B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT REGION 208..313
FT /note="Interaction with host EIF4G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT COILED 166..237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
SQ SEQUENCE 313 AA; 36153 MW; D6A044D66F27A02E CRC64;
MLKMESTQQM ASSIINTSFE AAVVAATSTL ELMGIQYDYN EIYTRVKSKF DYVMDDSGVK
NNLLGKAATI DQALNGKFGS VMRNKNWMTD SRTVAKLDED VNKLRMMLSS KGIDQKMRVL
NACFSVKRIP GKSSSVIKCT RLMKDKIERG AVEVDDSFVE EKMEVDTVDW KSRYDQLERR
FESLKQRVNE KYTTWVQKAK KVNENMYSLQ NVISQQQNQI ADLQNYCSKL EADLQNKVGS
LVSSVEWYLK SMELPDEVKT DIEQQLNSID TISPINAIDD LEILIRNLIH DYDRTFLMFK
GLLRQCNYEY AYE
