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-OCT-2012, entry version 15.
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 Human/United States/P/1974
OS   G3-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (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 the shutoff of host protein synthesis. It is
CC       unclear whether it is required for the translation of viral mRNAs
CC       as well. Functions similarly to, and competes with the cellular
CC       poly(A)-binding protein PABPC1. Binds the conserved sequence
CC       'GACC' at the 3' end of viral mRNAs and allows circularization of
CC       viral mRNAs in translation. Interacts with ZC3H7B/RoXaN and with
CC       the eukaryotic translation initiation factor eIF4G, using the same
CC       region employed by PABP-C1. NSP3 thus displaces PABPC1 from eIF4G,
CC       inhibiting the translation of cellular poly(A) mRNAs. Also
CC       responsible for the nuclear relocalization of PABPC1 upon
CC       rotavirus infection (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with
CC       host ZC3H7B (via LD motif). Interacts with host EIF4G1 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the rotavirus A NSP3 family.
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DR   EMBL; EF672600; ABV53278.1; -; Genomic_RNA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
DR   InterPro; IPR002873; Rotavirus_NSP3.
DR   Pfam; PF01665; Rota_NSP3; 1.
DR   SUPFAM; SSF69903; Non-struct_prot_NSP3_Rotavir; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Complete proteome; Host-virus interaction; RNA-binding;
KW   Translation regulation.
FT   CHAIN         1    310       Non-structural protein 3.
FT                                /FTId=PRO_0000369457.
FT   REGION        1    146       RNA-binding (By similarity).
FT   REGION      147    203       Dimerization (By similarity).
FT   REGION      167    231       Interaction with ZC3H7B (By similarity).
FT   REGION      205    310       Interaction with EIF4G1 (By similarity).
FT   COILED      163    234       Potential.
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
//