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   16-OCT-2019, entry version 32.
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; Reoviridae; Sedoreovirinae; Rotavirus;
OC   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
RT   are influenced by viral protein interactions.";
RL   J. Virol. 82:11106-11116(2008).
CC   -!- FUNCTION: Plays an important role in stimulating the translation
CC       of viral mRNAs. These mRNAs are capped but not polyadenylated,
CC       instead terminating in a conserved sequence 'GACC' at the 3' that
CC       is recognized by NSP3, which competes with host PABPC1 for EIF4G1
CC       binding. The interaction between NSP3 and host EIF4G1 stabilizes
CC       the EIF4E-EIF4G1 interaction, thereby facilitating the initiation
CC       of capped mRNA translation. {ECO:0000255|HAMAP-Rule:MF_04094}.
CC   -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with
CC       host ZC3H7B (via LD motif). Interacts with host EIF4G1.
CC       {ECO:0000255|HAMAP-Rule:MF_04094}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_04094}.
CC   -!- SIMILARITY: Belongs to the rotavirus NSP3 family.
CC       {ECO:0000255|HAMAP-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   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.550; -; 1.
DR   HAMAP; MF_04094; ROTA_A_NSP3; 1.
DR   HAMAP; MF_04090; ROTA_NSP3; 1.
DR   InterPro; IPR042519; NSP3_N.
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; Complete proteome; Host cytoplasm;
KW   Host-virus interaction; RNA-binding; Translation regulation.
FT   CHAIN         1    310       Non-structural protein 3.
FT                                /FTId=PRO_0000369457.
FT   REGION        1    146       RNA-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_04094}.
FT   REGION      147    203       Dimerization. {ECO:0000255|HAMAP-
FT                                Rule:MF_04094}.
FT   REGION      167    231       Interaction with host ZC3H7B.
FT                                {ECO:0000255|HAMAP-Rule:MF_04094}.
FT   REGION      205    310       Interaction with host EIF4G1.
FT                                {ECO:0000255|HAMAP-Rule:MF_04094}.
FT   COILED      163    234       {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
//