ID   NSP3_ROTHP              Reviewed;         310 AA.
AC   B3SRV3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-MAY-2023, entry version 38.
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/United States/P/1974/G3P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10957;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18786998; DOI=10.1128/jvi.01402-08;
RA   Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T.,
RA   Patton J.T.;
RT   "Group A human rotavirus genomics: evidence that gene constellations are
RT   influenced by viral protein interactions.";
RL   J. Virol. 82:11106-11116(2008).
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; EF672600; ABV53278.1; -; Genomic_RNA.
DR   SMR; B3SRV3; -.
DR   Proteomes; UP000007047; 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   CDD; cd20714; NSP3_rotavirus; 1.
DR   Gene3D; 3.30.70.1610; -; 1.
DR   Gene3D; 1.20.5.970; Nonstructural RNA-binding protein; 1.
DR   Gene3D; 6.10.280.20; Rotavirus non-structural protein NSP3, N-terminal domain; 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; NSP3 homodimer; 1.
DR   SUPFAM; SSF58030; Rotavirus nonstructural proteins; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Host cytoplasm; Host-virus interaction; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..310
FT                   /note="Non-structural protein 3"
FT                   /id="PRO_0000369457"
FT   REGION          1..146
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   REGION          147..203
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   REGION          167..231
FT                   /note="Interaction with host ZC3H7B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   REGION          205..310
FT                   /note="Interaction with host EIF4G1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   COILED          163..234
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
SQ   SEQUENCE   310 AA;  35826 MW;  F756CB2EBF997FFE CRC64;
     MESTQQMVSS IINTSFEAAV VAATSTLELM GIQYDYNEVF TRVKSKFDYV MDDSGVKNNL
     LGKAITIDQA LNGKFGSAIR NRNWMTDSKT VAKLDEDVNK LRMTLSSKGI DQKMRVLNAC
     FSVKRIPGKS SSIIKCTRLM KDKIERGEVE VDDSYVDEKM EIDTIDWKSR YDQLEKRFES
     LKQRVSEKYN TWVQKAKKVN ENMYSLQNVI SQQQNQIADL QQYCNKLEAD LQGKFSSLVS
     SVEWYLRSME LSDDVKNDIE QQLNSIDLIN PINAIDDIES LIRNLIQDYD RTFLMLKGLL
     KQCNYEYAYE
//