ID   NSP3_ROTHK              Reviewed;         313 AA.
AC   Q82050; Q9QNA7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 64.
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/Human/Japan/KU/1995/G1P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10952;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7871749; DOI=10.1006/viro.1995.1087;
RA   Rao C.D., Das M., Ilango P., Lalwani R., Rao B.S., Gowda K.;
RT   "Comparative nucleotide and amino acid sequence analysis of the sequence-
RT   specific RNA-binding rotavirus nonstructural protein NSP3.";
RL   Virology 207:327-333(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Taniguchi K.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; X81435; CAA57194.1; -; mRNA.
DR   EMBL; AB022771; BAA84968.1; -; mRNA.
DR   PIR; S51727; S51727.
DR   SMR; Q82050; -.
DR   Proteomes; UP000001458; 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   2: Evidence at transcript level;
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_0000369450"
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"
FT   CONFLICT        1..3
FT                   /note="Missing (in Ref. 2; BAA84968)"
FT   CONFLICT        71..76
FT                   /note="DQALNG -> GPACNE (in Ref. 2; BAA84968)"
FT   CONFLICT        276
FT                   /note="N -> G (in Ref. 2; BAA84968)"
SQ   SEQUENCE   313 AA;  36218 MW;  71185ADCE4276F58 CRC64;
     MLKMESTQQM VSSIINTSFE AAVVAATSTL ELMGIQYDYN EVFTRVKSKF DYVMDDSGVK
     NNLLGKAITI DQALNGKFGS AIRNRNWMID SKTVAKLDED VNKLRMTLSS KGIDQKMRVL
     NACFSVKRIP GKSSSIIKCT RLMKDKLERG EVEVDDSYVD EKMEIDTIDW KSRYDQLEKR
     FESLKQRVNE KYNAWVQKAK KVNENMYSLQ NVISQQQNQI ADLQQYCNKL EVDLQGKFSS
     LVSSVEWYLR SMELPDDVKT DVEQQLNSID LINPINAIDD IESLIRNLIQ DYDRTFLMLK
     GLLKQCNYEY AYE