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P03485

- M1_I34A1

UniProt

P03485 - M1_I34A1

Protein

Matrix protein 1

Gene

M

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.1 Publication
    Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: UniProtKB-KW
    3. structural constituent of virion Source: UniProtKB-KW

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: Reactome
    2. intracellular transport of virus Source: Reactome
    3. receptor-mediated endocytosis of virus by host cell Source: Reactome
    4. suppression by virus of host complement activation Source: UniProtKB-KW
    5. uncoating of virus Source: Reactome
    6. viral entry into host cell Source: Reactome
    7. viral genome maturation Source: Reactome
    8. viral genome packaging Source: Reactome
    9. viral life cycle Source: Reactome
    10. viral process Source: Reactome
    11. viral release from host cell Source: Reactome
    12. viral transcription Source: Reactome
    13. virion assembly Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, Inhibition of host complement factors by virus, Viral immunoevasion

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_6145. Influenza Life Cycle.
    REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
    REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
    REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
    REACT_6212. Budding.
    REACT_6235. Packaging of Eight RNA Segments.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_6321. Uncoating of the Influenza Virion.
    REACT_6326. Release.
    REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
    REACT_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix protein 1
    Short name:
    M1
    Gene namesi
    Name:M
    OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
    Taxonomic identifieri211044 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000009255: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endocytic vesicle membrane Source: Reactome
    3. endosome lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. host cell nucleus Source: UniProtKB-SubCell
    6. nucleoplasm Source: Reactome
    7. plasma membrane Source: Reactome
    8. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host nucleus, Membrane, Viral matrix protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Matrix protein 1PRO_0000078864Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer and homomultimer. Interacts with NEP. Binds ribonucleocapsid by both interacting with genomic RNA and NP protein. May interact with HA and NA By similarity. Cannot bind NP without genomic RNA.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSPA8P111424EBI-2547543,EBI-351896From a different organism.
    NPP034662EBI-2547543,EBI-2547640
    NSP035083EBI-2547543,EBI-2547979
    PAP034332EBI-2547543,EBI-2547616

    Protein-protein interaction databases

    IntActiP03485. 24 interactions.
    MINTiMINT-3375011.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1210
    Helixi19 – 3214
    Helixi39 – 479
    Beta strandi50 – 523
    Helixi54 – 6714
    Helixi78 – 836
    Helixi86 – 883
    Helixi90 – 10314
    Helixi109 – 1168
    Helixi121 – 13212
    Helixi134 – 1374
    Helixi140 – 15718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AA7X-ray2.08A/B1-158[»]
    1EA3X-ray2.30A/B1-164[»]
    1HHIX-ray2.50C/F58-66[»]
    2VLLX-ray1.60C/F58-66[»]
    2VLRX-ray2.30C/H58-66[»]
    3VDXX-ray3.00A/B/C3-164[»]
    4D9JX-ray3.92A/B/C/D/E/F/G/H/I/J/K/L3-164[»]
    4IQ4X-ray3.50A/B/C/D/E/F3-164[»]
    4ITVX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L3-164[»]
    4IVJX-ray7.35A/B/C3-164[»]
    ProteinModelPortaliP03485.
    SMRiP03485. Positions 1-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03485.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 164164Membrane-bindingAdd
    BLAST
    Regioni165 – 25288RNP-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi101 – 1055Nuclear localization signal

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.10.180. 1 hit.
    1.20.91.10. 1 hit.
    InterProiIPR013188. Flu_matrix_M1_C.
    IPR001561. Flu_matrix_M1_N.
    IPR015423. Flu_matrix_M1_N_sub1.
    IPR015799. Flu_matrix_M1_N_sub2.
    [Graphical view]
    PfamiPF00598. Flu_M1. 1 hit.
    PF08289. Flu_M1_C. 1 hit.
    [Graphical view]
    ProDomiPD596253. Flu_matrix_M1_C. 1 hit.
    PD001061. Flu_matrix_M1_N. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00759. Flu_M1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48145. SSF48145. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Only the first 9 residues are shared by the 2 isoforms.

    Isoform M1 (identifier: P03485-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSLLTEVETY VLSIIPSGPL KAEIAQRLED VFAGKNTDLE VLMEWLKTRP    50
    ILSPLTKGIL GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDKAVKLY 100
    RKLKREITFH GAKEISLSYS AGALASCMGL IYNRMGAVTT EVAFGLVCAT 150
    CEQIADSQHR SHRQMVTTTN PLIRHENRMV LASTTAKAME QMAGSSEQAA 200
    EAMEVASQAR QMVQAMRTIG THPSSSAGLK NDLLENLQAY QKRMGVQMQR 250
    FK 252
    Length:252
    Mass (Da):27,893
    Last modified:July 21, 1986 - v1
    Checksum:i2A54EEC87C3D4638
    GO
    Isoform M2 (identifier: P06821-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P06821.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:97
    Mass (Da):11,045
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2082SQ → IR in ABD77676. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01099 Genomic RNA. Translation: CAA24282.1.
    AF389121 Genomic RNA. Translation: AAM75161.1.
    EF467824 Viral cRNA. Translation: ABO21712.1.
    CY009445 Genomic RNA. Translation: ABD77676.1.
    RefSeqiNP_040978.1. NC_002016.1. [P03485-1]

    Genome annotation databases

    GeneIDi956527.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01099 Genomic RNA. Translation: CAA24282.1 .
    AF389121 Genomic RNA. Translation: AAM75161.1 .
    EF467824 Viral cRNA. Translation: ABO21712.1 .
    CY009445 Genomic RNA. Translation: ABD77676.1 .
    RefSeqi NP_040978.1. NC_002016.1. [P03485-1 ]

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AA7 X-ray 2.08 A/B 1-158 [» ]
    1EA3 X-ray 2.30 A/B 1-164 [» ]
    1HHI X-ray 2.50 C/F 58-66 [» ]
    2VLL X-ray 1.60 C/F 58-66 [» ]
    2VLR X-ray 2.30 C/H 58-66 [» ]
    3VDX X-ray 3.00 A/B/C 3-164 [» ]
    4D9J X-ray 3.92 A/B/C/D/E/F/G/H/I/J/K/L 3-164 [» ]
    4IQ4 X-ray 3.50 A/B/C/D/E/F 3-164 [» ]
    4ITV X-ray 3.60 A/B/C/D/E/F/G/H/I/J/K/L 3-164 [» ]
    4IVJ X-ray 7.35 A/B/C 3-164 [» ]
    ProteinModelPortali P03485.
    SMRi P03485. Positions 1-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03485. 24 interactions.
    MINTi MINT-3375011.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 956527.

    Enzyme and pathway databases

    Reactomei REACT_6145. Influenza Life Cycle.
    REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
    REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
    REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
    REACT_6212. Budding.
    REACT_6235. Packaging of Eight RNA Segments.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_6321. Uncoating of the Influenza Virion.
    REACT_6326. Release.
    REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
    REACT_9491. Viral mRNA Translation.

    Miscellaneous databases

    EvolutionaryTracei P03485.

    Family and domain databases

    Gene3Di 1.10.10.180. 1 hit.
    1.20.91.10. 1 hit.
    InterProi IPR013188. Flu_matrix_M1_C.
    IPR001561. Flu_matrix_M1_N.
    IPR015423. Flu_matrix_M1_N_sub1.
    IPR015799. Flu_matrix_M1_N_sub2.
    [Graphical view ]
    Pfami PF00598. Flu_M1. 1 hit.
    PF08289. Flu_M1_C. 1 hit.
    [Graphical view ]
    ProDomi PD596253. Flu_matrix_M1_C. 1 hit.
    PD001061. Flu_matrix_M1_N. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00759. Flu_M1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48145. SSF48145. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of influenza cDNA into M13: the sequence of the RNA segment encoding the A/PR/8/34 matrix protein."
      Winter G., Fields S.
      Nucleic Acids Res. 8:1965-1974(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: A/Puerto Rico/8/34/Mount Sinai.
    3. "Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments."
      de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M.
      Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    5. "Variation in nucleotide sequences coding for the N-terminal regions of the matrix and nonstructural proteins of influenza A viruses."
      Hall R.M., Air G.M.
      J. Virol. 38:1-7(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-106.
    6. "Molecular assembly of influenza virus: association of the NS2 protein with virion matrix."
      Yasuda J., Nakada S., Kato A., Toyoda T., Ishihama A.
      Virology 196:249-255(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEP PROTEIN.
    7. "The M1 and NP proteins of influenza A virus form homo- but not heterooligomeric complexes when coexpressed in BHK-21 cells."
      Zhao H., Ekstrom M., Garoff H.
      J. Gen. Virol. 79:2435-2446(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMOMULTIMERIZATION.
    8. "In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein."
      Baudin F., Petit I., Weissenhorn W., Ruigrok R.W.
      Virology 281:102-108(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEMBRANE AND VIRAL RNP.
    9. "Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export."
      Huang X., Liu T., Muller J., Levandowski R.A., Ye Z.
      Virology 287:405-416(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Assembly and budding of influenza virus."
      Nayak D.P., Hui E.K., Barman S.
      Virus Res. 106:147-165(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides."
      Garboczi D.N., Hung D.T., Wiley D.C.
      Proc. Natl. Acad. Sci. U.S.A. 89:3429-3433(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-66.
    12. "Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1."
      Sha B., Luo M.
      Nat. Struct. Biol. 4:239-244(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-158.
    13. "Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer."
      Arzt S., Baudin F., Barge A., Timmins P., Burmeister W.P., Ruigrok R.W.
      Virology 279:439-446(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-164.

    Entry informationi

    Entry nameiM1_I34A1
    AccessioniPrimary (citable) accession number: P03485
    Secondary accession number(s): A4GXH8, Q20N36, Q77HF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Most abundant protein in virion. When expressed alone can form virus-like particles in transfected cells.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3