ID   A0A291LTF6_9INFA        Unreviewed;       252 AA.
AC   A0A291LTF6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-FEB-2018, entry version 3.
DE   RecName: Full=Matrix protein 1 {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|SAAS:SAAS00051333};
DE            Short=M1 {ECO:0000256|HAMAP-Rule:MF_04068};
GN   Name=M1 {ECO:0000313|EMBL:ATI25890.1};
GN   Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04068};
OS   Influenza A virus (A/feline/New York/WVDL-14/2016(H7N2)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=2038749 {ECO:0000313|EMBL:ATI25890.1};
RN   [1] {ECO:0000313|EMBL:ATI25890.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/feline/New York/WVDL-14/2016 {ECO:0000313|EMBL:ATI25890.1};
RA   Hatta M., Zhong G., Gao Y., Nakajima N., Fan S., Chiba S.,
RA   Deering K.M., Ito M., Imai M., Kiso M., Nakatsu S., Lopes T.J.,
RA   Thompson A.J., McBride R., Suarez D.L., Macken C.A., Sugita S.,
RA   Neumann G., Hasegawa H., Paulson J.C., Toohey-Kurth K.L., Kawaoka Y.;
RT   "Characterization of a Novel Feline H7N2 Influenza Virus.";
RL   Submitted (SEP-2017) 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
CC       of significant proportion of filamentous virions, whereas after
CC       multiple passage on eggs or cell culture, virions have only
CC       spherical morphology. Filamentous virions are thought to be
CC       important to infect neighboring cells, and spherical virions more
CC       suited to spread through aerosol between hosts organisms.
CC       {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|SAAS:SAAS00043117}.
CC   -!- FUNCTION: Plays critical roles in virus replication, from virus
CC       entry and uncoating to assembly and budding of the virus particle.
CC       M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit
CC       viral transcription. Interaction of viral NEP with M1-RNP is
CC       thought to promote nuclear export of the complex, which is
CC       targeted to the virion assembly site at the apical plasma membrane
CC       in polarized epithelial cells. Interactions with NA and HA may
CC       bring M1, a non-raft-associated protein, into lipid rafts. Forms a
CC       continuous shell on the inner side of the lipid bilayer in virion,
CC       where it binds the RNP. During virus entry into cell, the M2 ion
CC       channel acidifies the internal virion core, inducing M1
CC       dissociation from the RNP. M1-free RNPs are transported to the
CC       nucleus, where viral transcription and replication can take place.
CC       {ECO:0000256|HAMAP-Rule:MF_04068, ECO:0000256|SAAS:SAAS00043108}.
CC   -!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP. Binds
CC       ribonucleocapsid by both interacting with genomic RNA and NP
CC       protein. May interact with HA and NA. Cannot bind NP without
CC       genomic RNA. {ECO:0000256|HAMAP-Rule:MF_04068,
CC       ECO:0000256|SAAS:SAAS00841835}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP-
CC       Rule:MF_04068, ECO:0000256|SAAS:SAAS00552517}. Virion membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04068}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_04068}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_04068}.
CC   -!- MISCELLANEOUS: Most abundant protein in virion. When expressed
CC       alone can form virus-like particles in transfected cells.
CC       {ECO:0000256|HAMAP-Rule:MF_04068}.
CC   -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1
CC       family. {ECO:0000256|HAMAP-Rule:MF_04068,
CC       ECO:0000256|SAAS:SAAS00841834}.
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; MF978407; ATI25890.1; -; Viral_cRNA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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   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; 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   ProDom; PD596253; Flu_matrix_M1_C; 1.
DR   ProDom; PD001061; Flu_matrix_M1_N; 1.
DR   SMART; SM00759; Flu_M1_C; 1.
DR   SUPFAM; SSF48145; SSF48145; 1.
PE   3: Inferred from homology;
KW   Host nucleus {ECO:0000256|HAMAP-Rule:MF_04068,
KW   ECO:0000256|SAAS:SAAS00043126};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04068,
KW   ECO:0000256|SAAS:SAAS00043401};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_04068,
KW   ECO:0000256|SAAS:SAAS00043183};
KW   Viral matrix protein {ECO:0000256|HAMAP-Rule:MF_04068,
KW   ECO:0000256|SAAS:SAAS00043306};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04068,
KW   ECO:0000256|SAAS:SAAS00043120}.
FT   DOMAIN      158    252       Flu_M1_C. {ECO:0000259|SMART:SM00759}.
FT   REGION        1    164       Membrane-binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_04068}.
FT   REGION      165    252       RNP-binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_04068}.
FT   MOTIF       101    105       Nuclear localization signal.
FT                                {ECO:0000256|HAMAP-Rule:MF_04068}.
SQ   SEQUENCE   252 AA;  27899 MW;  25E2ADADF62F3935 CRC64;
     MSLLTEVETY VLSIIPSGPL KAEIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL
     GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAIKLY RKLKREITFH GAKEVALSYS
     TGALASCMGL IYNRMGTVTT EGAFGLVCAT CEQIADSQHR SHRQMVTTTN PLIRHENRMV
     LASTTAKAME QVAGSSEQAA EAMEVASQAK QMVQAMRTIG THPSSSTGLR DDLLEKLQAY
     QKRMGVQLHR FK
//