NSP3_ROTS4
ID NSP3_ROTS4 Reviewed; 315 AA.
AC Q00721;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 29-SEP-2021, 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/SA11-4F/G3P6[1]) (RV-A) (Simian Agent 11 (strain
OS 4F)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=36436;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1326821; DOI=10.1016/0042-6822(92)91193-x;
RA Mattion N.M., Cohen J., Aponte C., Estes M.K.;
RT "Characterization of an oligomerization domain and RNA-binding properties
RT on rotavirus nonstructural protein NS34.";
RL Virology 190:68-83(1992).
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}.
CC -!- INTERACTION:
CC Q00721; Q9UGR2: ZC3H7B; Xeno; NbExp=6; IntAct=EBI-1263962, EBI-948845;
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; M87502; AAA47295.1; -; Genomic_RNA.
DR SMR; Q00721; -.
DR IntAct; Q00721; 2.
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..315
FT /note="Non-structural protein 3"
FT /id="PRO_0000149542"
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..315
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 315 AA; 36451 MW; 9E5D39FDE6FCE73B CRC64;
MLKMESTQQM AVSIINSSFE AAVVAATSAL ENMGIEYDYQ DIYSRVKNKF DFVMDDSGVK
NNLIGKAITI DQALNNKFGS AIRNRNWLAD TSRPAKLDED VNKLRMMLSS KGIDQKMRVL
NACFSVKRIP GKSSSIIKCT KLMRDKLERG EVEVDDSFVD EKMEVDTIDW KSRYEQLEQR
FESLKSRVNE KYNNWVLKAR KMNENMHSLQ NVISQQQAHI AELQVYNNKL ERDLQNKIGS
LTSSIEWYLR SMELDPEIKA DIEQQINSID AINPLHAFDD LESVIRNLIS DYDKLFLMFK
GLIQRCNYQY SFGCE
