ID NSP3_ROTHK Reviewed; 313 AA. AC Q82050; Q9QNA7; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-MAY-2023, entry version 67. 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/Human/Japan/KU/1995/G1P1A[8]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=10952; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7871749; DOI=10.1006/viro.1995.1087; RA Rao C.D., Das M., Ilango P., Lalwani R., Rao B.S., Gowda K.; RT "Comparative nucleotide and amino acid sequence analysis of the sequence- RT specific RNA-binding rotavirus nonstructural protein NSP3."; RL Virology 207:327-333(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Taniguchi K.; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X81435; CAA57194.1; -; mRNA. DR EMBL; AB022771; BAA84968.1; -; mRNA. DR PIR; S51727; S51727. DR SMR; Q82050; -. DR Proteomes; UP000001458; 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 2: Evidence at transcript 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_0000369450" 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" FT CONFLICT 1..3 FT /note="Missing (in Ref. 2; BAA84968)" FT CONFLICT 71..76 FT /note="DQALNG -> GPACNE (in Ref. 2; BAA84968)" FT CONFLICT 276 FT /note="N -> G (in Ref. 2; BAA84968)" SQ SEQUENCE 313 AA; 36218 MW; 71185ADCE4276F58 CRC64; MLKMESTQQM VSSIINTSFE AAVVAATSTL ELMGIQYDYN EVFTRVKSKF DYVMDDSGVK NNLLGKAITI DQALNGKFGS AIRNRNWMID SKTVAKLDED VNKLRMTLSS KGIDQKMRVL NACFSVKRIP GKSSSIIKCT RLMKDKLERG EVEVDDSYVD EKMEIDTIDW KSRYDQLEKR FESLKQRVNE KYNAWVQKAK KVNENMYSLQ NVISQQQNQI ADLQQYCNKL EVDLQGKFSS LVSSVEWYLR SMELPDDVKT DVEQQLNSID LINPINAIDD IESLIRNLIQ DYDRTFLMLK GLLKQCNYEY AYE //