NSP3_ROTHS
ID NSP3_ROTHS Reviewed; 313 AA.
AC Q82052;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 63.
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/S2/1980/G2P1B[4]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10959;
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).
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; X81428; CAA57187.1; -; mRNA.
DR PIR; S51729; S51729.
DR SMR; Q82052; -.
DR PRIDE; Q82052; -.
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 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_0000369451"
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"
SQ SEQUENCE 313 AA; 36389 MW; C455B5B8D2920580 CRC64;
MLKMESTQQM ASSIINSSFE AAVVAATSTL ELMGIQYDYN EVYTRVKSKF DFVMDDSGVE
NNLMGKAATI DQALNGKFSS SIRNRNWMTD SKTVARLDED VNKLRLLLSS KGIDQKMRVL
NACFSVKRVP GKSSSVIKCT RLMKEKIERG EVEVDDTFIE ERMEIDTIDW KSRYDQLERR
FESLKQRVNE KYNNWVIKAR KVNENMNSLQ NVISQQQAHI NELQIYNNKL ERDLQSKIGS
VISSIEWYLR SMELSDDIKS DIEQQLNSID LINPVNAFDD FESILRNLIS DYDRIFIMFK
GLLQQSNYTY TYE
