ID   NSP3_ROTRF              Reviewed;         313 AA.
AC   Q86504;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 75.
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/Cow/France/RF/1975/G6P6[1]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10933;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8240020; DOI=10.1007/bf01309746;
RA   Aponte C., Mattion N.M., Estes M.K., Charpilienne A., Cohen J.;
RT   "Expression of two bovine rotavirus non-structural proteins (NSP2, NSP3) in
RT   the baculovirus system and production of monoclonal antibodies directed
RT   against the expressed proteins.";
RL   Arch. Virol. 133:85-95(1993).
RN   [2]
RP   INTERACTION WITH HUMAN ZC3H7B.
RX   PubMed=15047801; DOI=10.1128/jvi.78.8.3851-3862.2004;
RA   Vitour D., Lindenbaum P., Vende P., Becker M.M., Poncet D.;
RT   "RoXaN, a novel cellular protein containing TPR, LD, and zinc finger
RT   motifs, forms a ternary complex with eukaryotic initiation factor 4G and
RT   rotavirus NSP3.";
RL   J. Virol. 78:3851-3862(2004).
RN   [3]
RP   INTERACTION WITH HUMAN ZC3H7B, AND INTERACTION WITH HUMAN EIF4G1.
RX   PubMed=18799579; DOI=10.1128/jvi.00872-08;
RA   Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C.,
RA   Bolte S., Arold S.T., Poncet D.;
RT   "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus
RT   infection involves the interaction of NSP3 with eIF4G and RoXaN.";
RL   J. Virol. 82:11283-11293(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, ECO:0000269|PubMed:15047801,
CC       ECO:0000269|PubMed:18799579}.
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; Z21639; CAA79754.1; -; mRNA.
DR   PIR; S49006; S49006.
DR   SMR; Q86504; -.
DR   DIP; DIP-1160N; -.
DR   Proteomes; UP000007179; 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   1: Evidence at protein 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_0000367816"
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          170..234
FT                   /note="Interaction with ZC3H7B"
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"
SQ   SEQUENCE   313 AA;  36347 MW;  2AD38815AAEB349B CRC64;
     MLKMESTQQM ASSIINTSFE AAVVAATSTL ELMGIQYDYN EVYTRVKSKF DYVMDDSGVK
     NNLLGKAATI DQALNGKFGS AARNRNWMAD TRTTARLDED VNKLRMMLSS KGIDQKMRVL
     NACFNVKRVP GKSSSIIKCT RLMRDKIERG EVEVDDSFVE EKMEVDTIDW KSRYEQLEKR
     FESLKQRVNE KYTSWVQKAK KVNENMYSLQ NVISQQQSQI ADLQNYCNKL EVDLQNKISS
     LVSSVEWYLK SMELPDEIKT DIEQQLNSID VINPINAIDD FESLIRNIIL DYDRIFLMFK
     GLMRQCNYEY TYE
//