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Unreviewed, UniProtKB/TrEMBL A0A1C9 (A0A1C9_9INFA)

Last modified September 2, 2008. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesSubmitted name:
    Matrix protein 1 EMBL ABJ90272.2
Gene names
Name: M1 EMBL ABJ90272.2
OrganismInfluenza A virus (A/ostrich/Italy/984/00(H7N1)) EMBL ABJ90272.2
Taxonomic identifier338859 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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 By similarity. Spearmint SPM013188

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 By similarity. Spearmint SPM013188

Sequences

Sequence LengthMass (Da)Tools
A0A1C9-1 [UniParc].

Last modified February 20, 2007. Version 2.
Checksum: 20BD8D105A13BB4E

FASTA25227,854
        10         20         30         40         50         60 
MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL 

        70         80         90        100        110        120 
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAVKLY RKLKREITFH GAKEVALSYS 

       130        140        150        160        170        180 
TGALASCMGL IYNKMGTVTT EVAFGLVCAT CEQIADSQHR SHRQMATTTN PLIRHENRMV 

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

       250 
QKRMGVQMQR FK 

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References

[1]"Pneumo- and neurotropism of avian origin Italian highly pathogenic avian influenza H7N1 isolates in experimentally infected mice."
Rigoni M., Shinya K., Toffan A., Milani A., Bettini F., Kawaoka Y., Cattoli G., Capua I.
Virology 364:28-35(2007) [PubMed: 17408714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/ostrich/Italy/984/00 EMBL ABJ90272.2.

Cross-references

Sequence databases

DQ991338 Viral cRNA. Translation: ABJ90272.2.
DQ991346 Viral cRNA. Translation: ABJ90283.2.

3D structure databases

SMRA0A1C9. Positions 1-158.
ModBaseSearch...

Family and domain databases

InterProIPR013188. Flu_matrix_M1_C.
IPR001561. Flu_matrix_M1_N.
IPR015799. Flu_matrix_M1_N_sub2.
[Graphical view]
Gene3DG3DSA:1.10.10.180. Flu_matrix_M1_N_sub2. 1 hit.
PfamPF00598. Flu_M1. 1 hit.
PF08289. Flu_M1_C. 1 hit.
[Graphical view]
ProDomPD001061. Flu_M1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00759. Flu_M1_C. 1 hit.
[Graphical view]

Entry information

Entry nameA0A1C9_9INFA
AccessionPrimary (citable) accession number: A0A1C9
Secondary accession number(s): A0A1E1
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: February 20, 2007
Last modified: September 2, 2008
This is version 16 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)

Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information · Relevant documents