M1_I02A1
ID M1_I02A1 Reviewed; 245 AA.
AC Q6DPU2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 29-SEP-2021, entry version 63.
DE RecName: Full=Matrix protein 1;
DE Short=M1;
DE Flags: Fragment;
GN Name=M;
OS Influenza A virus (strain A/Guinea fowl/Hong Kong/38/2002 H5N1 genotype
OS X0).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=284208;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH NCBI_TaxID=9694; Panthera tigris (Tiger).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15241415; DOI=10.1038/nature02746;
RA Li K.S., Guan Y., Wang J., Smith G.J.D., Xu K.M., Duan L., Rahardjo A.P.,
RA Puthavathana P., Buranathai C., Nguyen T.D., Estoepangestie A.T.S.,
RA Chaisingh A., Auewarakul P., Long H.T., Hanh N.T.H., Webby R.J.,
RA Poon L.L.M., Chen H., Shortridge K.F., Yuen K.Y., Webster R.G.,
RA Peiris J.S.M.;
RT "Genesis of a highly pathogenic and potentially pandemic H5N1 influenza
RT virus in eastern Asia.";
RL Nature 430:209-213(2004).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP (By
CC similarity). Binds ribonucleocapsid by both interacting with genomic
CC RNA and NP protein. May interact with HA and NA (By similarity). Cannot
CC bind NP without genomic RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein.
CC Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Only the first 9 residues are shared by the 2 isoforms.;
CC Name=M1;
CC IsoId=Q6DPU2-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=Q6DPU3-1; Sequence=External;
CC -!- MISCELLANEOUS: Most abundant protein in virion. When expressed alone
CC can form virus-like particles in transfected cells.
CC -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family.
CC {ECO:0000305}.
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; AY651399; AAT70551.1; -; Genomic_RNA.
DR SMR; Q6DPU2; -.
DR IntAct; Q6DPU2; 1.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.10.10.180; -; 1.
DR Gene3D; 1.20.91.10; -; 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 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 Alternative splicing; Host nucleus; Membrane; RNA-binding;
KW Viral matrix protein; Virion.
FT CHAIN <1..245
FT /note="Matrix protein 1"
FT /id="PRO_0000311611"
FT REGION <1..157
FT /note="Membrane-binding"
FT /evidence="ECO:0000250"
FT REGION 158..245
FT /note="RNP-binding"
FT /evidence="ECO:0000250"
FT MOTIF 94..98
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 245 AA; 27162 MW; F10A531595088BCF CRC64;
ETYVLSIVPS GPLKAEIAQR LEDVFAGKNT DLEALMEWLK TRPILSPLTK GILGFVFTLT
VPSERGLQRR RFVQNALNGN GDPNNMDRAV KLYKKLKREI TFHGAKEVAL SYSTGALASC
MGLIYNRMGT VTTEVAFGLV CATCEQIADS QHRSHRQMAT ITNPLIRHEN RMVLASTTAK
AMEQMAGSSE QAAEAMEVAS QARQMVQAMR TIGTHPNSST GLRDNLLENL QAYQNRMGVQ
MQRFK
