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P03485 (M1_I34A1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix protein 1

Short name=M1
Gene names
Name:M
OrganismInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1) [Reference proteome]
Taxonomic identifier211044 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

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. Ref.9

Subunit structure

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. Ref.6 Ref.7 Ref.8

Subcellular location

Virion membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus.

Miscellaneous

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

Sequence similarities

Belongs to the influenza viruses Matrix protein M1 family.

Ontologies

Keywords
   Biological processHost-virus interaction
Inhibition of host complement factors by virus
Viral immunoevasion
   Cellular componentHost nucleus
Membrane
Viral matrix protein
Virion
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfusion of virus membrane with host plasma membrane

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

receptor-mediated endocytosis of virus by host cell

Traceable author statement. Source: Reactome

suppression by virus of host complement activation

Inferred from electronic annotation. Source: UniProtKB-KW

uncoating of virus

Traceable author statement. Source: Reactome

viral entry into host cell

Traceable author statement. Source: Reactome

viral genome maturation

Traceable author statement. Source: Reactome

viral genome packaging

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral release from host cell

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

endosome lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of virion

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Only the first 9 residues are shared by the 2 isoforms.
Isoform M1 (identifier: P03485-1)

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.
Isoform M2 (identifier: P06821-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Matrix protein 1
PRO_0000078864

Regions

Region1 – 164164Membrane-binding
Region165 – 25288RNP-binding
Motif101 – 1055Nuclear localization signal

Experimental info

Sequence conflict207 – 2082SQ → IR in ABD77676. Ref.4

Secondary structure

......................... 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform M1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 2A54EEC87C3D4638

FASTA25227,893
        10         20         30         40         50         60 
MSLLTEVETY VLSIIPSGPL KAEIAQRLED VFAGKNTDLE VLMEWLKTRP ILSPLTKGIL 

        70         80         90        100        110        120 
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDKAVKLY RKLKREITFH GAKEISLSYS 

       130        140        150        160        170        180 
AGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMVTTTN PLIRHENRMV 

       190        200        210        220        230        240 
LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRTIG THPSSSAGLK NDLLENLQAY 

       250 
QKRMGVQMQR FK 

« Hide

Isoform M2 [UniParc].

See P06821.

References

[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]"Plasmid-only rescue of influenza A virus vaccine candidates."
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L., Garcia-Sastre A., Palese P.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001) [PubMed] [Europe PMC] [Abstract]
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]"The NIAID influenza genome sequencing project."
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y. expand/collapse author list , Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01099 Genomic RNA. Translation: CAA24282.1.
AF389121 Genomic RNA. Translation: AAM75161.1.
EF467824 Viral cRNA. Translation: ABO21712.1.
CY009445 Genomic RNA. Translation: ABD77676.1.
RefSeqNP_040978.1. NC_002016.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA7X-ray2.08A/B1-158[»]
1EA3X-ray2.30A/B1-164[»]
1HHIX-ray2.50C/F58-66[»]
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[»]
ProteinModelPortalP03485.
SMRP03485. Positions 1-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP03485. 24 interactions.
MINTMINT-3375011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956527.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Family and domain databases

Gene3D1.10.10.180. 1 hit.
1.20.91.10. 1 hit.
InterProIPR013188. Flu_matrix_M1_C.
IPR001561. Flu_matrix_M1_N.
IPR015423. Flu_matrix_M1_N_sub1.
IPR015799. Flu_matrix_M1_N_sub2.
[Graphical view]
PfamPF00598. Flu_M1. 1 hit.
PF08289. Flu_M1_C. 1 hit.
[Graphical view]
ProDomPD596253. Flu_matrix_M1_C. 1 hit.
PD001061. Flu_matrix_M1_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00759. Flu_M1_C. 1 hit.
[Graphical view]
SUPFAMSSF48145. SSF48145. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03485.

Entry information

Entry nameM1_I34A1
AccessionPrimary (citable) accession number: P03485
Secondary accession number(s): A4GXH8, Q20N36, Q77HF4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references