M1_I72A8
ID M1_I72A8 Reviewed; 252 AA.
AC P0DOF7; P03486; P10919; P63233; Q1K9D7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 29-SEP-2021, entry version 35.
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/Udorn/1972 H3N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=385599;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7257189; DOI=10.1016/0042-6822(81)90319-6;
RA Lamb R.A., Lai C.-J.;
RT "Conservation of the influenza virus membrane protein (M1) amino acid
RT sequence and an open reading frame of RNA segment 7 encoding a second
RT protein (M2) in H1N1 and H3N2 strains.";
RL Virology 112:746-751(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-13 AND 210-252.
RX PubMed=6945577; DOI=10.1073/pnas.78.7.4170;
RA Lamb R.A., Lai C.-J., Choppin P.W.;
RT "Sequences of mRNAs derived from genome RNA segment 7 of influenza virus:
RT colinear and interrupted mRNAs code for overlapping proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4170-4174(1981).
RN [3]
RP MUTAGENESIS OF ALA-41; ARG-95; ALA-167; THR-168; GLU-204; VAL-205 AND
RP ALA-218.
RX PubMed=12604801; DOI=10.1099/vir.0.18803-0;
RA Bourmakina S.V., Garcia-Sastre A.;
RT "Reverse genetics studies on the filamentous morphology of influenza A
RT virus.";
RL J. Gen. Virol. 84:517-527(2003).
RN [4]
RP FUNCTION.
RX PubMed=15033573; DOI=10.1016/j.virol.2003.12.009;
RA Elleman C.J., Barclay W.S.;
RT "The M1 matrix protein controls the filamentous phenotype of influenza A
RT virus.";
RL Virology 321:144-153(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 {ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:15033573}.
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 ECO:0000269|PubMed:15033573}.
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=P0DOF7-1, P03486-1, P63233-1;
CC Sequence=Displayed;
CC Name=M2;
CC IsoId=P0DOF8-1, P03490-1, P63231-1;
CC Sequence=External;
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; J02167; AAA43304.1; -; Genomic_RNA.
DR PIR; A94326; MFIVC.
DR SMR; P0DOF7; -.
DR Proteomes; UP000171580; 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 1: Evidence at protein level;
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_0000078866"
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"
FT MUTAGEN 41
FT /note="A->V: No effect on filamentous virion particles
FT morphology."
FT /evidence="ECO:0000269|PubMed:12604801"
FT MUTAGEN 95
FT /note="R->K: Complete loss of filamentous virion particles
FT morphology."
FT /evidence="ECO:0000269|PubMed:12604801"
FT MUTAGEN 167
FT /note="A->T: No effect on filamentous virion particles
FT morphology."
FT /evidence="ECO:0000269|PubMed:12604801"
FT MUTAGEN 168
FT /note="T->A: No effect on filamentous virion particles
FT morphology."
FT /evidence="ECO:0000269|PubMed:12604801"
FT MUTAGEN 204
FT /note="E->D: Complete loss of filamentous virion particles
FT morphology."
FT /evidence="ECO:0000269|PubMed:12604801"
FT MUTAGEN 205
FT /note="V->I: No effect on filamentous virion particles
FT morphology."
FT /evidence="ECO:0000269|PubMed:12604801"
FT MUTAGEN 218
FT /note="A->T: No effect on filamentous virion particles
FT morphology."
FT /evidence="ECO:0000269|PubMed:12604801"
SQ SEQUENCE 252 AA; 27804 MW; 92522D3E87D4C3C6 CRC64;
MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAVKLY RKLKREITFH GAKEIALSYS
AGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMVATTN PLIRHENRMV
LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRAIG THPSSSAGLK DDLLENLQAY
QKRMGVQMQR FK
