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P03485

- M1_I34A1

UniProt

P03485 - M1_I34A1

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.3 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.

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

Sequence conflict

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

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: September 3, 2014
This is version 111 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

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