NSP3_ROTS1
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 29-SEP-2021, entry version 109.
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; Reoviridae; Sedoreovirinae; 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}.
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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 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 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
