ID NSP3_ROTS1 Reviewed; 315 AA. AC P03536; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 03-MAY-2023, entry version 112. 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-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain OS Both)). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=37137; OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=6322111; DOI=10.1093/nar/12.3.1621; RA Both G.W., Bellamy A.R., Siegman L.J.; RT "Nucleotide sequence of the dsRNA genomic segment 7 of Simian 11 RT rotavirus."; RL Nucleic Acids Res. 12:1621-1626(1984). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 4-164, AND RNA-BINDING. RX PubMed=11792322; DOI=10.1016/s0092-8674(01)00632-8; RA Deo R.C., Groft C.M., Rajashankar K.R., Burley S.K.; RT "Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 RT homodimer."; RL Cell 108:71-81(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 206-315. RX PubMed=12086624; DOI=10.1016/s1097-2765(02)00555-5; RA Groft C.M., Burley S.K.; RT "Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA RT circularization."; RL Mol. Cell 9:1273-1283(2002). 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; X00355; CAA25102.1; -; Genomic_RNA. DR PIR; A04142; MNXR4S. DR PDB; 1KNZ; X-ray; 2.45 A; A/B/C/D/I/J/M/N=4-164. DR PDB; 1LJ2; X-ray; 2.38 A; A/B=206-315. DR PDBsum; 1KNZ; -. DR PDBsum; 1LJ2; -. DR SMR; P03536; -. DR IntAct; P03536; 1. DR EvolutionaryTrace; P03536; -. DR Proteomes; UP000007180; 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 3D-structure; Coiled coil; Host cytoplasm; Host-virus interaction; KW Reference proteome; RNA-binding; Translation regulation. FT CHAIN 1..315 FT /note="Non-structural protein 3" FT /id="PRO_0000149541" 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" FT HELIX 8..32 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 39..56 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 61..74 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 79..89 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 93..107 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 114..123 FT /evidence="ECO:0007829|PDB:1KNZ" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:1KNZ" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 141..147 FT /evidence="ECO:0007829|PDB:1KNZ" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 156..161 FT /evidence="ECO:0007829|PDB:1KNZ" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:1LJ2" FT HELIX 212..250 FT /evidence="ECO:0007829|PDB:1LJ2" FT HELIX 256..266 FT /evidence="ECO:0007829|PDB:1LJ2" FT HELIX 274..303 FT /evidence="ECO:0007829|PDB:1LJ2" FT TURN 304..307 FT /evidence="ECO:0007829|PDB:1LJ2" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:1LJ2" SQ SEQUENCE 315 AA; 36445 MW; 06BE050DDE9218E9 CRC64; MLKMESTQQM AVSIINSSFE AAVVAATSAL ENMGIEYDYQ DIYSRVKNKF DFVMDDSGVK NNPIGKAITI DQALNNKFGS AIRNRNWLAD TSRPAKLDED VNKLRMMLSS KGIDQKMRVL NACFSVKRIP GKSSSIIKCT KLMRDKLERG EVEVDDSFVD EKMEVDTIDW KSRYEQLEQR FESLKSRVNE KYNNWVLKAR KMNENMHSLQ NVIPQQQAHI AELQVYNNKL ERDLQNKIGS LTSSIEWYLR SMELDPEIKA DIEQQINSID AINPLHAFDD LESVIRNLIS DYDKLFLMFK GLIQRCNYQY SFGCE //