ID A0A3P8MIK8_9INFA Unreviewed; 121 AA. AC A0A3P8MIK8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 13-SEP-2023, entry version 18. DE RecName: Full=Nuclear export protein {ECO:0000256|HAMAP-Rule:MF_04067}; DE Short=NEP {ECO:0000256|HAMAP-Rule:MF_04067}; DE AltName: Full=Non-structural protein 2 {ECO:0000256|HAMAP-Rule:MF_04067}; DE Short=NS2 {ECO:0000256|HAMAP-Rule:MF_04067}; GN Name=NEP {ECO:0000313|EMBL:ATW74973.1}; GN Synonyms=NS {ECO:0000256|HAMAP-Rule:MF_04067, GN ECO:0000256|RuleBase:RU362104}, NS2 {ECO:0000313|EMBL:ATW74973.1}; OS Influenza A virus (A/blue-winged teal/Wyoming/AH0099021/2016(H7N9)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=2049446 {ECO:0000313|EMBL:ATW74973.1}; RN [1] {ECO:0000313|EMBL:ATW74973.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/blue-winged teal/Wyoming/AH0099021/2016 RC {ECO:0000313|EMBL:ATW74973.1}; RX PubMed=28880836; RA Lee D.H., Torchetti M.K., Killian M.L., Berhane Y., Swayne D.E.; RT "Highly Pathogenic Avian Influenza A(H7N9) Virus, Tennessee, USA, March RT 2017."; RL Emerg. Infect. Dis. 23:0-0(2017). CC -!- FUNCTION: Mediates the nuclear export of encapsidated genomic RNAs CC (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs CC complexes and the nuclear export machinery of the cell. Possesses no CC intrinsic RNA-binding activity, but includes a C-terminal M1-binding CC domain. This domain is believed to allow recognition of RNPs bound to CC the protein M1. Since protein M1 is not available in large quantities CC before late stages of infection, such an indirect recognition mechanism CC probably ensures that genomic RNPs are not exported from the host CC nucleus until sufficient quantities of viral mRNA and progeny genomic CC RNA have been synthesized. Furthermore, the RNPs enter the host CC cytoplasm only when associated with the M1 protein that is necessary to CC guide them to the plasma membrane. May down-regulate viral RNA CC synthesis when overproduced. {ECO:0000256|HAMAP-Rule:MF_04067, CC ECO:0000256|RuleBase:RU362104}. CC -!- FUNCTION: Mediates the nuclear export of encapsidated genomic RNAs CC (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs CC complexes and the nuclear export machinery of the cell. Possesses no CC intrinsic RNA-binding activity, but includes a C-terminal M1-binding CC domain. This domain is believed to allow recognition of RNPs to which CC the M1 protein is bound. Because the M1 protein is not available in CC large quantities until the later stages of infection, such an indirect CC recognition mechanism probably ensures that genomic RNPs are not CC exported from the nucleus before sufficient quantities of viral mRNA CC and progeny genomic RNA have been synthesized. Furthermore, the RNPs CC enters the cytoplasm only when they have associated with the M1 protein CC that is necessary to guide them to the plasma membrane. May down- CC regulate viral RNA synthesis when overproduced. CC {ECO:0000256|ARBA:ARBA00024714}. CC -!- SUBUNIT: Binds M1 protein. May interact with host nucleoporin RAB/HRB CC and exportin XPO1/CRM1. {ECO:0000256|RuleBase:RU362104}. CC -!- SUBUNIT: Binds M1 protein. May interact with human nucleoporin RAB/HRB CC and exportin XPO1/CRM1. {ECO:0000256|ARBA:ARBA00026037}. CC -!- SUBUNIT: Interacts with protein M1. May interact with host nucleoporin CC RAB/HRB and exportin XPO1/CRM1. {ECO:0000256|HAMAP-Rule:MF_04067}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. Virion CC {ECO:0000256|HAMAP-Rule:MF_04067, ECO:0000256|RuleBase:RU362104}. Host CC nucleus {ECO:0000256|HAMAP-Rule:MF_04067, CC ECO:0000256|RuleBase:RU362104}. CC -!- SIMILARITY: Belongs to the influenza viruses NEP family. CC {ECO:0000256|ARBA:ARBA00010673, ECO:0000256|HAMAP-Rule:MF_04067, CC ECO:0000256|RuleBase:RU362104}. 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; MG266068; ATW74973.1; -; Viral_cRNA. DR SMR; A0A3P8MIK8; -. DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule. DR GO; GO:0039675; P:exit of virus from host cell nucleus through nuclear pore; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.287.230; -; 1. DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1. DR HAMAP; MF_04067; INFV_NEP; 1. DR InterPro; IPR000968; Flu_NS2. DR Pfam; PF00601; Flu_NS2; 1. DR SUPFAM; SSF101156; Nonstructural protein ns2, Nep, M1-binding domain; 1. PE 3: Inferred from homology; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04067, KW ECO:0000256|RuleBase:RU362104}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04067, KW ECO:0000256|RuleBase:RU362104}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_04067}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04067, ECO:0000256|RuleBase:RU362104}. FT MOTIF 12..21 FT /note="Nuclear export signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04067" FT MOTIF 85..94 FT /note="Nuclear export signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04067" SQ SEQUENCE 121 AA; 14366 MW; 607DF23FA291D2E8 CRC64; MDSNTVSSFQ DILMRMSKMQ LGSSSEDLNG MITQFESLRL YRDSLGEAVM RMGDLHSLQS RNGKWREQLS QKFEEIRWLI EEVRHRLKIT ENSFEQITFM QALQLLLEVE QEIRTFSFQL I //