NSP3_ROT41
ID NSP3_ROT41 Reviewed; 313 AA.
AC Q3ZK63;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 29-SEP-2021, entry version 46.
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 (isolate RVA/Human/Belgium/B4106/2000/G3P11[14]) (RV-A)
OS (Rotavirus A (isolate B4106)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=578843;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16571797; DOI=10.1128/jvi.80.8.3801-3810.2006;
RA Matthijnssens J., Rahman M., Martella V., Xuelei Y., De Vos S.,
RA De Leener K., Ciarlet M., Buonavoglia C., Van Ranst M.;
RT "Full genomic analysis of human rotavirus strain B4106 and lapine rotavirus
RT strain 30/96 provides evidence for interspecies transmission.";
RL J. Virol. 80:3801-3810(2006).
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; AY740733; AAU43791.1; -; Genomic_RNA.
DR SMR; Q3ZK63; -.
DR Proteomes; UP000008655; 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 3: Inferred from homology;
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_0000369442"
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; 36407 MW; 7103EDB05A7B8203 CRC64;
MLKMESTQQM ASSIINTSFE AAVVAATSTL ELMGIQYDYN EVYTRVKSKF DYVMDDSGVK
NNLLGKAATI DQALNGKFGS AVRNRNWMTD TRTTARLDED VNKLRMMLSS KGIDQKMRVL
NACFSVKRIP GKSSSIIKCT RLMRDKIERG EVEVDDSFVE EKMEVDTIDW KSRYEQLEKR
FESLKQRVNE KYTSWVQKAK KVNENMYSLQ NVISQQQSQI ADLQHYCNKL EVDLQNKISS
LVSSIEWYMK SMELPDEVKT DIEQQLNSID VINPINAIDD FESLIRNVIL DYDRTFLMFK
GLMRQCNYEY TYE
