ID X4YQE0_9REOV Unreviewed; 310 AA.
AC X4YQE0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 03-MAY-2023, entry version 25.
DE RecName: Full=Non-structural protein 3 {ECO:0000256|HAMAP-Rule:MF_04094};
DE Short=NSP3 {ECO:0000256|HAMAP-Rule:MF_04094};
DE AltName: Full=NCVP4 {ECO:0000256|HAMAP-Rule:MF_04094};
DE AltName: Full=Non-structural RNA-binding protein 34 {ECO:0000256|HAMAP-Rule:MF_04094};
DE Short=NS34 {ECO:0000256|HAMAP-Rule:MF_04094};
GN Name=NSP3 {ECO:0000313|EMBL:AHV80420.1};
GN ORFNames=W907_45296gpNSP3 {ECO:0000313|EMBL:AHV80420.1},
GN W907_45297gpNSP3 {ECO:0000313|EMBL:AHV80661.1}, W907_45300gpNSP3
GN {ECO:0000313|EMBL:AHV80166.1}, W907_45302gpNSP3
GN {ECO:0000313|EMBL:AHV80154.1};
OS Rotavirus A.
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Sedoreoviridae; Rotavirus.
OX NCBI_TaxID=28875 {ECO:0000313|EMBL:AHV80420.1, ECO:0000313|Proteomes:UP000160911};
RN [1] {ECO:0000313|Proteomes:UP000121663, ECO:0000313|Proteomes:UP000128748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RVA/Human-wt/PRY/467/2000/G9P[8] {ECO:0000313|EMBL:AHV80420.1},
RC RVA/Human-wt/PRY/469/2000/G9P[8] {ECO:0000313|EMBL:AHV80166.1},
RC RVA/Human-wt/PRY/472/2000/G9P[8] {ECO:0000313|EMBL:AHV80661.1}, and
RC RVA/Human-wt/PRY/475/2000/G9P[8] {ECO:0000313|EMBL:AHV80154.1};
RA Kirkness E., Halpin R.A., Akopov A., Fedorova N., Tsitrin T., Stockwell T.,
RA Amedeo P., Bishop B., Edworthy P., Gupta N., Hoover J., Katzel D.,
RA Schobel S., Shrivastava S., Martinez M., Russomando G., Arbiza J.,
RA Wentworth D.E., Parra G.I.;
RL Submitted (MAR-2014) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_04094}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04094}.
CC -!- SIMILARITY: Belongs to the rotavirus A NSP3 protein family.
CC {ECO:0000256|HAMAP-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; KJ626657; AHV80154.1; -; Genomic_RNA.
DR EMBL; KJ626668; AHV80166.1; -; Genomic_RNA.
DR EMBL; KJ626902; AHV80420.1; -; Genomic_RNA.
DR EMBL; KJ627124; AHV80661.1; -; Genomic_RNA.
DR Proteomes; UP000121663; Genome.
DR Proteomes; UP000128748; Genome.
DR Proteomes; UP000140195; Genome.
DR Proteomes; UP000160911; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_04094};
KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04094};
KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04094};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04094};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW Rule:MF_04094}.
FT REGION 1..146
FT /note="RNA-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT REGION 147..203
FT /note="Dimerization"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT REGION 167..231
FT /note="Interaction with host ZC3H7B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT REGION 205..310
FT /note="Interaction with host EIF4G1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT COILED 163..234
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
SQ SEQUENCE 310 AA; 35875 MW; E2995A5895D2051B CRC64;
MESTQQMVSS IINTSFEAAV VAATSTLELM GIQYDYNEIF TRVKSKFDYV MDDSGVKNNL
LGKAITIDQA LNGKFGSAIR NRNWMTDSKT VAKLDEDVNK LRMTLSSKGI DQKMRVLNAC
FSVKRIPGKS SSIIKCTKLM KDKIERGEVE VDDSYVDEKM EIDTIDWKSR YDQLEKRFES
LKQRVNEKYN IWVQKAKKVN ENMYSLQNVI SQQQNQIADL QQYCNKLEAD LQGKFSSLVS
SVEWYLRSME LPDDVKNDIE QQLNSIDLIN PINAIDDIES LIRNLVQDYD RTFLMLKGLL
KQCNYEYVYE
//
