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   25-OCT-2017, entry version 24.
DE   RecName: Full=Non-structural protein 3;
DE            Short=NSP3;
DE   AltName: Full=NCVP4;
DE   AltName: Full=Non-structural RNA-binding protein 34;
DE            Short=NS34;
OS   Rotavirus A (strain RVA/Human/United States/P/1974/G3P1A[8]) (RV-A).
OC   Viruses; dsRNA viruses; 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: Involved in translation of viral mRNAs and shutoff of
CC       host protein synthesis. It is unclear whether it is required for
CC       the translation of viral mRNAs as well. Functions similarly to,
CC       and competes with the cellular poly(A)-binding protein PABPC1.
CC       Binds the conserved sequence 'GACC' at the 3' end of viral mRNAs
CC       and allows circularization of viral mRNAs in translation.
CC       Interacts with ZC3H7B/RoXaN and with the eukaryotic translation
CC       initiation factor eIF4G, using the same region employed by PABP-
CC       C1. NSP3 thus displaces PABPC1 from eIF4G, inhibiting the
CC       translation of cellular poly(A) mRNAs. Also responsible for the
CC       nuclear relocalization of PABPC1 upon rotavirus infection (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with
CC       host ZC3H7B (via LD motif). Interacts with host EIF4G1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the rotavirus A NSP3 family. {ECO:0000305}.
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DR   EMBL; EF672600; ABV53278.1; -; Genomic_RNA.
DR   SMR; B3SRV3; -.
DR   OrthoDB; VOG090000G7; -.
DR   Proteomes; UP000007047; Genome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
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;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus;
KW   Host gene expression shutoff by virus; Host-virus interaction;
KW   RNA-binding; Translation regulation.
FT   CHAIN         1    310       Non-structural protein 3.
FT                                /FTId=PRO_0000369457.
FT   REGION        1    146       RNA-binding. {ECO:0000250}.
FT   REGION      147    203       Dimerization. {ECO:0000250}.
FT   REGION      167    231       Interaction with ZC3H7B. {ECO:0000250}.
FT   REGION      205    310       Interaction with EIF4G1. {ECO:0000250}.
FT   COILED      163    234       {ECO:0000255}.
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
//