ID Q910H2_9INFA Unreviewed; 252 AA. AC Q910H2; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 07-OCT-2020, entry version 90. DE RecName: Full=Matrix protein 1 {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}; DE Short=M1 {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}; GN Name=M {ECO:0000256|HAMAP-Rule:MF_04068, GN ECO:0000256|RuleBase:RU362105, ECO:0000313|EMBL:AAK49251.1}; OS Influenza A virus (A/HongKong/97/98(H5N1)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=88097 {ECO:0000313|EMBL:AAK49251.1}; RN [1] {ECO:0000313|EMBL:AAK49251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/97/98 {ECO:0000313|EMBL:AAK49251.1}; RA Shaw M.W., Cooper L.A., Xu X., Thompson W.W., Krauss S.L., Guan Y., RA Zhou N.N., Klimov A., Cox N.J., Webster R.G., Lim W., Shortridge K.F., RA Subbarao K.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAK49251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/97/98 {ECO:0000313|EMBL:AAK49251.1}; RX PubMed=11748666; DOI=10.1002/jmv.2118; RA Shaw M., Cooper L., Xu X., Thompson W., Krauss S., Guan Y., Zhou N., RA Klimov A., Cox N., Webster R., Lim W., Shortridge K., Subbarao K.; RT "Molecular changes associated with the transmission of avian influenza a RT H5N1 and H9N2 viruses to humans."; RL J. Med. Virol. 66:107-114(2002). RN [3] {ECO:0000313|EMBL:AAK49251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/97/98 {ECO:0000313|EMBL:AAK49251.1}; RX PubMed=16318689; RG World Health Organization Global Influenza Program Surveillance Network; RT "Evolution of H5N1 avian influenza viruses in Asia."; RL Emerg. Infect. Dis. 11:1515-1521(2005). CC -!- FUNCTION: Determines the virion's shape: spherical or filamentous. CC Clinical isolates of influenza are characterized by the presence of CC significant proportion of filamentous virions, whereas after multiple CC passage on eggs or cell culture, virions have only spherical CC morphology. Filamentous virions are thought to be important to infect CC neighboring cells, and spherical virions more suited to spread through CC aerosol between hosts organisms. {ECO:0000256|HAMAP-Rule:MF_04068, CC ECO:0000256|RuleBase:RU362105}. CC -!- FUNCTION: Plays critical roles in virus replication, from virus entry CC and uncoating to assembly and budding of the virus particle. M1 binding CC to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral CC transcription. Interaction of viral NEP with M1-RNP is thought to CC promote nuclear export of the complex, which is targeted to the virion CC assembly site at the apical plasma membrane in polarized epithelial CC cells. Interactions with NA and HA may bring M1, a non-raft-associated CC protein, into lipid rafts. Forms a continuous shell on the inner side CC of the lipid bilayer in virion, where it binds the RNP. During virus CC entry into cell, the M2 ion channel acidifies the internal virion core, CC inducing M1 dissociation from the RNP. M1-free RNPs are transported to CC the nucleus, where viral transcription and replication can take place. CC {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}. CC -!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP. Binds CC ribonucleocapsid by both interacting with genomic RNA and NP protein. CC May interact with HA and NA. Cannot bind NP without genomic RNA. CC {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-Rule:MF_04068, CC ECO:0000256|RuleBase:RU362105}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04068, CC ECO:0000256|RuleBase:RU362105}. Host nucleus {ECO:0000256|HAMAP- CC Rule:MF_04068, ECO:0000256|RuleBase:RU362105}. CC -!- MISCELLANEOUS: Most abundant protein in virion. When expressed alone CC can form virus-like particles in transfected cells. {ECO:0000256|HAMAP- CC Rule:MF_04068, ECO:0000256|RuleBase:RU362105}. CC -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family. CC {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}. 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; AF255374; AAK49251.1; -; Viral_cRNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-UniRule. DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.10.180; -; 1. DR Gene3D; 1.20.91.10; -; 1. DR HAMAP; MF_04068; INFV_M1; 1. DR InterPro; IPR036039; Flu_matrix_M1. DR InterPro; IPR013188; Flu_matrix_M1_C. DR InterPro; IPR001561; Flu_matrix_M1_N. DR InterPro; IPR015423; Flu_matrix_M1_N_sub1. DR InterPro; IPR015799; Flu_matrix_M1_N_sub2. DR InterPro; IPR037533; INFV_M1. DR Pfam; PF00598; Flu_M1; 1. DR Pfam; PF08289; Flu_M1_C; 1. DR SMART; SM00759; Flu_M1_C; 1. DR SUPFAM; SSF48145; SSF48145; 1. PE 3: Inferred from homology; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP- KW Rule:MF_04068, ECO:0000256|RuleBase:RU362105}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04068, KW ECO:0000256|RuleBase:RU362105}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_04068, ECO:0000256|RuleBase:RU362105}; KW Viral matrix protein {ECO:0000256|ARBA:ARBA00023311, ECO:0000256|HAMAP- KW Rule:MF_04068, ECO:0000256|RuleBase:RU362105}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04068, KW ECO:0000256|RuleBase:RU362105}. FT DOMAIN 158..252 FT /note="Flu_M1_C" FT /evidence="ECO:0000259|SMART:SM00759" FT REGION 1..164 FT /note="Membrane-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04068" FT REGION 165..252 FT /note="RNP-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04068" FT MOTIF 101..105 FT /note="Nuclear localization signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04068" SQ SEQUENCE 252 AA; 27821 MW; C2E7A890688CDFEE CRC64; MSLLTEVETY VLSIVPSGPL KAQIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAVKLY KKLKREMTFH GAKEVALSYS TGALASCMGL IYNRMGTVTT EVALGLVCAT CEQIADAQHR SHRQMATTTN PLIRHENRMV LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRTIG THPSSSAGLK DDLIENLQAY QKRMGVQMQR FK //