M1_I80A2
ID M1_I80A2 Reviewed; 252 AA.
AC Q2VC89;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 29-SEP-2021, entry version 68.
DE RecName: Full=Matrix protein 1 {ECO:0000255|HAMAP-Rule:MF_04068};
DE Short=M1 {ECO:0000255|HAMAP-Rule:MF_04068};
GN Name=M {ECO:0000255|HAMAP-Rule:MF_04068};
OS Influenza A virus (strain A/Seal/Massachusetts/1/1980 H7N7).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=384493;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=SC35M mouse-adapted;
RX PubMed=16339318; DOI=10.1073/pnas.0507415102;
RA Gabriel G., Dauber B., Wolff T., Planz O., Klenk H.D., Stech J.;
RT "The viral polymerase mediates adaptation of an avian influenza virus to a
RT mammalian host.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18590-18595(2005).
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:0000255|HAMAP-Rule:MF_04068}.
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:0000255|HAMAP-Rule:MF_04068}.
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:0000255|HAMAP-Rule:MF_04068}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04068}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04068}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04068}.
CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04068}.
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=Q2VC89-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=Q2VC90-1; Sequence=External;
CC -!- MISCELLANEOUS: SC35 was derived from A/Seal/Massachussetts/1/80 (H7N7)
CC by serial passages in chicken embryo cells, thereby acquiring a
CC multibasic cleavage site in its hemagglutinin (HA) and becoming 100%
CC lethal for chickens. SC35 was then passaged 11 times in mouse lung,
CC yielding the mouse-adapted variant SC35M.
CC -!- MISCELLANEOUS: Most abundant protein in virion. When expressed alone
CC can form virus-like particles in transfected cells. {ECO:0000255|HAMAP-
CC Rule:MF_04068}.
CC -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04068}.
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DR EMBL; DQ266100; ABB90273.1; -; Genomic_RNA.
DR SMR; Q2VC89; -.
DR Proteomes; UP000008576; Genome.
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-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 Alternative splicing; Host nucleus; Membrane; RNA-binding;
KW Viral matrix protein; Virion.
FT CHAIN 1..252
FT /note="Matrix protein 1"
FT /id="PRO_0000326310"
FT REGION 1..164
FT /note="Membrane-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04068"
FT REGION 165..252
FT /note="RNP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04068"
FT MOTIF 101..105
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04068"
SQ SEQUENCE 252 AA; 27938 MW; 333CD504DBC15440 CRC64;
MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAVKLY RKLKREITFH GAKEVALSYS
TGALASCMGL IYNRMGTVTT EVAFGLVCAT CERIADSQHR SHRQMVTTTN PLIRHENRMV
LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRTIG THPSSSAGLK DDLLENLQAY
QKRMGVQMQR FK
