ID X2GHF2_9INFA Unreviewed; 252 AA.
AC X2GHF2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 08-NOV-2023, entry version 52.
DE RecName: Full=Matrix protein 1 {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105};
DE Short=M1 {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105};
GN Name=M1 {ECO:0000313|EMBL:AHN19621.1};
GN Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04068,
GN ECO:0000256|RuleBase:RU362105};
OS Influenza A virus (A/American green-winged teal/Ohio/13OS1769/2013(H7N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=1471205 {ECO:0000313|EMBL:AHN19621.1, ECO:0000313|Proteomes:UP000139444};
RN [1] {ECO:0000313|EMBL:AHN19621.1, ECO:0000313|Proteomes:UP000139444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A/American green-winged teal/Ohio/13OS1769/2013
RC {ECO:0000313|EMBL:AHN19621.1};
RA Nolting J., Bowman A.S., Slemons R.D., Fries A.C.;
RT "IAV Surveillance in Wild Birds.";
RL Submitted (MAR-2014) 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 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:0000256|ARBA:ARBA00025019,
CC ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}.
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:0000256|ARBA:ARBA00024859, ECO:0000256|HAMAP-Rule:MF_04068,
CC ECO:0000256|RuleBase:RU362105}.
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:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-Rule:MF_04068,
CC ECO:0000256|RuleBase:RU362105}; Peripheral membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04068,
CC ECO:0000256|RuleBase:RU362105}. Host nucleus {ECO:0000256|HAMAP-
CC Rule:MF_04068, ECO:0000256|RuleBase:RU362105}.
CC -!- MISCELLANEOUS: Most abundant protein in virion. When expressed alone
CC can form virus-like particles in transfected cells. {ECO:0000256|HAMAP-
CC Rule:MF_04068, ECO:0000256|RuleBase:RU362105}.
CC -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family.
CC {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|RuleBase:RU362105}.
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DR EMBL; KJ527625; AHN19621.1; -; Viral_cRNA.
DR SMR; X2GHF2; -.
DR Proteomes; UP000139444; 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; Influenza virus matrix protein M1; 1.
PE 3: Inferred from homology;
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP-
KW Rule:MF_04068};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04068};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_04068};
KW Viral matrix protein {ECO:0000256|ARBA:ARBA00023311, ECO:0000256|HAMAP-
KW Rule:MF_04068};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04068}.
FT DOMAIN 158..252
FT /note="Influenza matrix M1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00759"
FT REGION 1..164
FT /note="Membrane-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04068"
FT REGION 165..252
FT /note="RNP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04068"
FT MOTIF 101..105
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04068"
SQ SEQUENCE 252 AA; 27910 MW; 9FCCEA062413A96F CRC64;
MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAVKLY RKLKREITFH GAKEVALSYS
TGALASCMGL IYNRMGTVTT EVAFGLVCAT CEQIADSQHR SHRQMVTTTN PLIRHENRMV
LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRTIG THPSSSAGLK DDLLENLQAY
QKRMGVQMQR FK
//