NSP3_ROTRH
ID NSP3_ROTRH Reviewed; 313 AA.
AC Q8UZL8; Q27PP2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 29-SEP-2021, entry version 57.
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/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=444185;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12050363; DOI=10.1128/jvi.76.13.6502-6509.2002;
RA Mossel E.C., Ramig R.F.;
RT "Rotavirus genome segment 7 (NSP3) is a determinant of extraintestinal
RT spread in the neonatal mouse.";
RL J. Virol. 76:6502-6509(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2-213.
RX PubMed=16699002; DOI=10.1128/jvi.02664-05;
RA Fenaux M., Cuadras M.A., Feng N., Jaimes M., Greenberg H.B.;
RT "Extraintestinal spread and replication of a homologous EC rotavirus strain
RT and a heterologous rhesus rotavirus in BALB/c mice.";
RL J. Virol. 80:5219-5232(2006).
RN [3]
RP FUNCTION.
RX PubMed=12093167; DOI=10.1006/viro.2002.1477;
RA Padilla-Noriega L., Paniagua O., Guzman-Leon S.;
RT "Rotavirus protein NSP3 shuts off host cell protein synthesis.";
RL Virology 298:1-7(2002).
RN [4]
RP FUNCTION.
RX PubMed=16940515; DOI=10.1128/jvi.00437-06;
RA Montero H., Arias C.F., Lopez S.;
RT "Rotavirus nonstructural protein NSP3 is not required for viral protein
RT synthesis.";
RL J. Virol. 80:9031-9038(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST EIF4G1.
RX PubMed=26063427; DOI=10.1128/jvi.01402-15;
RA Gratia M., Sarot E., Vende P., Charpilienne A., Baron C.H., Duarte M.,
RA Pyronnet S., Poncet D.;
RT "Rotavirus NSP3 Is a Translational Surrogate of the Poly(A) Binding
RT Protein-Poly(A) Complex.";
RL J. Virol. 89:8773-8782(2015).
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 ECO:0000269|PubMed:12093167, ECO:0000269|PubMed:16940515,
CC ECO:0000269|PubMed:26063427}.
CC -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with host
CC ZC3H7B (via LD motif). Interacts with host EIF4G1.
CC {ECO:0000250|UniProtKB:Q86504, ECO:0000255|HAMAP-Rule:MF_04094,
CC ECO:0000269|PubMed:26063427}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04094,
CC ECO:0000269|PubMed:26063427}.
CC -!- SIMILARITY: Belongs to the rotavirus NSP3 family. {ECO:0000255|HAMAP-
CC Rule:MF_04094}.
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DR EMBL; AY065842; AAL58536.1; -; Genomic_RNA.
DR EMBL; DQ391186; ABD52871.1; -; Genomic_RNA.
DR SMR; Q8UZL8; -.
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 Gene3D; 6.10.280.20; -; 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; SSF69903; 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_0000367817"
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 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; 36315 MW; C07F5AC22D8F5932 CRC64;
MLKMESTQQM ASSIINSSFE AAVVAATSTL ELMGIQYDYN EVYTRVKSKF DLVMDDSGVK
NNLIGKAITI DQALNGKFSS AIRNRNWMTD SRTVAKLDED VNKLRIMLSS KGIDQKMRVL
NACFSVKRIP GKSSSIVKCT RLMKDKLERG EVEVDDSFVE EKMEVDTIDW KSRYEQLEKR
FESLKHRVNE KYNHWVLKAR KVNENMNSLQ NVISQQQAHI NELQMYNNKL ERDLQSKIGS
VVSSIEWYLR SMELSDDVKS DIEQQLNSID QLNPVNAIDD FESILRNLIS DYDRLFIMFK
GLLQQCNYTY TYE
