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Matrix protein 1 (M1)

 R4L5T4_9INFA            Unreviewed;       252 AA.
R4L5T4;
24-JUL-2013, integrated into UniProtKB/TrEMBL.
24-JUL-2013, sequence version 1.
25-OCT-2017, entry version 32.
RecName: Full=Matrix protein 1 {ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00051333};
Short=M1 {ECO:0000256|RuleBase:RU362105};
Name=M1 {ECO:0000313|EMBL:AGL07285.1};
Synonyms=M {ECO:0000256|RuleBase:RU362105};
Influenza A virus (A/South Dakota/03/2011(H3N2)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=1320997 {ECO:0000313|EMBL:AGL07285.1};
[1] {ECO:0000313|EMBL:AGL07285.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/South Dakota/03/2011 {ECO:0000313|EMBL:AGL07285.1};
Klimov A., Barnes J., Shaw M., Cox N., Garten R., Xu X.;
"Influenza Sequencing Activity group.";
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Determines the virion's shape: spherical or filamentous.
Clinical isolates of influenza are characterized by the presence
of significant proportion of filamentous virions, whereas after
multiple passage on eggs or cell culture, virions have only
spherical morphology. Filamentous virions are thought to be
important to infect neighboring cells, and spherical virions more
suited to spread through aerosol between hosts organisms.
{ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00043117}.
-!- FUNCTION: Plays critical roles in virus replication, from virus
entry and uncoating to assembly and budding of the virus particle.
M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit
viral transcription. Interaction of viral NEP with M1-RNP is
thought to promote nuclear export of the complex, which is
targeted to the virion assembly site at the apical plasma membrane
in polarized epithelial cells. Interactions with NA and HA may
bring M1, a non-raft-associated protein, into lipid rafts. Forms a
continuous shell on the inner side of the lipid bilayer in virion,
where it binds the RNP. During virus entry into cell, the M2 ion
channel acidifies the internal virion core, inducing M1
dissociation from the RNP. M1-free RNPs are transported to the
nucleus, where viral transcription and replication can take place.
{ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00043108}.
-!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP. Binds
ribonucleocapsid by both interacting with genomic RNA and NP
protein. May interact with HA and NA. Cannot bind NP without
genomic RNA. {ECO:0000256|RuleBase:RU362105,
ECO:0000256|SAAS:SAAS00841835}.
-!- SUBCELLULAR LOCATION: Host nucleus
{ECO:0000256|SAAS:SAAS00552517}.
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000256|RuleBase:RU362105}; Peripheral membrane protein
{ECO:0000256|RuleBase:RU362105}; Cytoplasmic side
{ECO:0000256|RuleBase:RU362105}. Host nucleus
{ECO:0000256|RuleBase:RU362105}.
-!- MISCELLANEOUS: Most abundant protein in virion. When expressed
alone can form virus-like particles in transfected cells.
{ECO:0000256|RuleBase:RU362105}.
-!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1
family. {ECO:0000256|RuleBase:RU362105,
ECO:0000256|SAAS:SAAS00841834}.
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EMBL; KC893049; AGL07285.1; -; Viral_cRNA.
ProteinModelPortal; R4L5T4; -.
SMR; R4L5T4; -.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
Gene3D; 1.10.10.180; -; 1.
InterPro; IPR036039; Flu_matrix_M1.
InterPro; IPR013188; Flu_matrix_M1_C.
InterPro; IPR001561; Flu_matrix_M1_N.
InterPro; IPR015799; Flu_matrix_M1_N_sub2.
Pfam; PF00598; Flu_M1; 1.
Pfam; PF08289; Flu_M1_C; 1.
ProDom; PD596253; Flu_matrix_M1_C; 1.
ProDom; PD001061; Flu_matrix_M1_N; 1.
SMART; SM00759; Flu_M1_C; 1.
SUPFAM; SSF48145; SSF48145; 1.
3: Inferred from homology;
Host nucleus {ECO:0000256|RuleBase:RU362105,
ECO:0000256|SAAS:SAAS00043126};
Membrane {ECO:0000256|RuleBase:RU362105,
ECO:0000256|SAAS:SAAS00043401};
RNA-binding {ECO:0000256|RuleBase:RU362105,
ECO:0000256|SAAS:SAAS00043183};
Viral matrix protein {ECO:0000256|RuleBase:RU362105,
ECO:0000256|SAAS:SAAS00043306};
Virion {ECO:0000256|RuleBase:RU362105, ECO:0000256|SAAS:SAAS00043306}.
DOMAIN 158 252 Flu_M1_C. {ECO:0000259|SMART:SM00759}.
SEQUENCE 252 AA; 27850 MW; F8AD48FA35AE2CBF CRC64;
MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDKAVKLY RKLKREITFH GAKEIALSYS
AGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMVATTN PLIKHENRMV
LASTTAKAME QMAGSSEQAA EAMEIASQAR QMVQAMRAIG THPSSSTGLR DDLLENLQTY
QKRMGVQMQR FK


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