ID C5MLK8_9INFA Unreviewed; 252 AA. AC C5MLK8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 05-OCT-2016, entry version 43. DE RecName: Full=Matrix protein 1 {ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00043269}; DE Short=M1 {ECO:0000256|RuleBase:RU362105}; GN Name=M1 {ECO:0000313|EMBL:ACR48966.1}; GN Synonyms=M {ECO:0000256|RuleBase:RU362105}; OS Influenza A virus (A/chicken/East Java/UT6016/2006(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=644246 {ECO:0000313|EMBL:ACR48966.1}; RN [1] {ECO:0000313|EMBL:ACR48966.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/East Java/UT6016/2006 {ECO:0000313|EMBL:ACR48966.1}; RX PubMed=19464724; DOI=10.1016/j.virol.2009.04.024; RA Takano R., Nidom C.A., Kiso M., Muramoto Y., Yamada S., RA Sakai-Tagawa Y., Macken C., Kawaoka Y.; RT "Phylogenetic characterization of H5N1 avian influenza viruses RT isolated in Indonesia from 2003-2007."; RL Virology 390:13-21(2009). RN [2] {ECO:0000313|EMBL:ACR48966.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/East Java/UT6016/2006 {ECO:0000313|EMBL:ACR48966.1}; RA Tankano R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Determines the virion's shape: spherical or filamentous. CC Clinical isolates of influenza are characterized by the presence CC of significant proportion of filamentous virions, whereas after CC multiple passage on eggs or cell culture, virions have only CC spherical morphology. Filamentous virions are thought to be CC important to infect neighboring cells, and spherical virions more CC suited to spread through aerosol between hosts organisms. CC {ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00043117}. CC -!- FUNCTION: Plays critical roles in virus replication, from virus CC entry and uncoating to assembly and budding of the virus particle. CC M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit CC viral transcription. Interaction of viral NEP with M1-RNP is CC thought to promote nuclear export of the complex, which is CC targeted to the virion assembly site at the apical plasma membrane CC in polarized epithelial cells. Interactions with NA and HA may CC bring M1, a non-raft-associated protein, into lipid rafts. Forms a CC continuous shell on the inner side of the lipid bilayer in virion, CC where it binds the RNP. During virus entry into cell, the M2 ion CC channel acidifies the internal virion core, inducing M1 CC dissociation from the RNP. M1-free RNPs are transported to the CC nucleus, where viral transcription and replication can take place. CC {ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00043108}. CC -!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP. Binds CC ribonucleocapsid by both interacting with genomic RNA and NP CC protein. May interact with HA and NA. Cannot bind NP without CC genomic RNA. {ECO:0000256|RuleBase:RU362105}. CC -!- SUBCELLULAR LOCATION: Host nucleus CC {ECO:0000256|SAAS:SAAS00552517}. CC -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|RuleBase:RU362105}; Peripheral membrane protein CC {ECO:0000256|RuleBase:RU362105}; Cytoplasmic side CC {ECO:0000256|RuleBase:RU362105}. Host nucleus CC {ECO:0000256|RuleBase:RU362105}. CC -!- MISCELLANEOUS: Most abundant protein in virion. When expressed CC alone can form virus-like particles in transfected cells. CC {ECO:0000256|RuleBase:RU362105}. CC -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1 CC family. {ECO:0000256|RuleBase:RU362105, CC ECO:0000256|SAAS:SAAS00584684}. 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; GQ122500; ACR48966.1; -; Viral_cRNA. DR ProteinModelPortal; C5MLK8; -. 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-KW. DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW. DR GO; GO:0039573; P:suppression by virus of host complement activation; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.180; -; 1. DR Gene3D; 1.20.91.10; -; 1. 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 Pfam; PF00598; Flu_M1; 1. DR Pfam; PF08289; Flu_M1_C; 1. DR ProDom; PD596253; Flu_matrix_M1_C; 1. DR ProDom; PD001061; Flu_matrix_M1_N; 1. DR SMART; SM00759; Flu_M1_C; 1. DR SUPFAM; SSF48145; SSF48145; 1. PE 3: Inferred from homology; KW Host nucleus {ECO:0000256|RuleBase:RU362105, KW ECO:0000256|SAAS:SAAS00438288}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00272173}; KW Inhibition of host complement factors by virus KW {ECO:0000256|SAAS:SAAS00272174}; KW Membrane {ECO:0000256|RuleBase:RU362105, KW ECO:0000256|SAAS:SAAS00438292}; KW RNA-binding {ECO:0000256|RuleBase:RU362105, KW ECO:0000256|SAAS:SAAS00438289}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00272174}; KW Viral matrix protein {ECO:0000256|RuleBase:RU362105, KW ECO:0000256|SAAS:SAAS00438110}; KW Virion {ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00438277}. FT DOMAIN 158 252 Flu_M1_C. {ECO:0000259|SMART:SM00759}. SQ SEQUENCE 252 AA; 27854 MW; B06DD4FF36C2C0ED CRC64; MSLLTEVETY VLSIIPSGPL KAEIAQKLED VFAGKNADLE ALMEWLKTRP ILSPLTKGIL GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDKAVKLY KKLKREITFH GAKEVALSYS TGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMATITN PLIRHENRMV LASTTAKAME QMAGSSEQAA EAMEVANQAR QMVQAMRTIG THPNSSAGLR DNLLENLQAY QKRMGVQMHR FK //