GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery
Matrix protein 2 (Proton channel protein M2)
B6GV28_9INFA Unreviewed; 97 AA.
B6GV28;
16-DEC-2008, integrated into UniProtKB/TrEMBL.
16-DEC-2008, sequence version 1.
13-FEB-2019, entry version 51.
RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040803};
AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069};
Name=M2 {ECO:0000313|EMBL:CAJ43192.1};
Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069};
Influenza A virus (A/mallard/France/710/2002(H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=356355 {ECO:0000313|EMBL:CAJ43192.1};
[1] {ECO:0000313|EMBL:CAJ43192.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/mallard/France/710/2002 {ECO:0000313|EMBL:CAJ43192.1};
Rousset J., Le Gall-Recule G., Ogor K., Bureau E., Hars J., Jestin V.;
"Characterisation of avian influenza viruses isolated from wild birds
and sentinel ducks during winter seasons 2000-2001, 2001-2002 and
2003-2004 in France.";
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Forms a proton-selective ion channel that is necessary
for the efficient release of the viral genome during virus entry.
After attaching to the cell surface, the virion enters the cell by
endocytosis. Acidification of the endosome triggers M2 ion channel
activity. The influx of protons into virion interior is believed
to disrupt interactions between the viral ribonucleoprotein (RNP),
matrix protein 1 (M1), and lipid bilayers, thereby freeing the
viral genome from interaction with viral proteins and enabling RNA
segments to migrate to the host cell nucleus, where influenza
virus RNA transcription and replication occur. Also plays a role
in viral proteins secretory pathway. Elevates the intravesicular
pH of normally acidic compartments, such as trans-Golgi network,
preventing newly formed hemagglutinin from premature switching to
the fusion-active conformation. {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040783}.
-!- ACTIVITY REGULATION: The M2 protein from most influenza A strains
is inhibited by amantadine and rimantadine, resulting in viral
uncoating incapacity. Emergence of amantadine-resistant variants
is usually rapid. {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01073786}.
-!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers
held together by non-covalent interactions. May interact with
matrix protein 1. {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040791}.
-!- SUBCELLULAR LOCATION: Host apical cell membrane
{ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|SAAS:SAAS01040793};
Single-pass type III membrane protein {ECO:0000256|HAMAP-
Rule:MF_04069, ECO:0000256|SAAS:SAAS01040793}. Virion membrane
{ECO:0000256|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at
the apical plasma membrane in infected polarized epithelial cells,
in close proximity to budding and assembled virions. Minor
component of virions (only 16-20 molecules/virion).
{ECO:0000256|HAMAP-Rule:MF_04069}.
-!- DOMAIN: Cytoplasmic tail plays an important role in virion
assembly and morphogenesis. {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247}.
-!- MISCELLANEOUS: When the channel is activated, one or more
imidazole moities of His-37 probably become bi-protonated.
{ECO:0000256|HAMAP-Rule:MF_04069}.
-!- SIMILARITY: Belongs to the influenza viruses matrix protein M2
family. {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040773}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04069}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AM157388; CAJ43192.1; -; Genomic_RNA.
SMR; B6GV28; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-UniRule.
GO; GO:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-UniRule.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-UniRule.
GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-UniRule.
HAMAP; MF_04069; INFV_M2; 1.
InterPro; IPR002089; Flu_M2.
Pfam; PF00599; Flu_M2; 1.
ProDom; PD001031; Flu_M2; 1.
3: Inferred from homology;
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040795};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040804};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040804};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040755};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040774};
Inhibition of host autophagy by virus {ECO:0000256|HAMAP-
Rule:MF_04069, ECO:0000256|SAAS:SAAS01040755};
Ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040754};
Ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040754,
ECO:0000256|SAAS:SAAS01040774};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
Membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
ECO:0000256|SAAS:SAAS01040804, ECO:0000256|SAM:Phobius};
Palmitate {ECO:0000256|HAMAP-Rule:MF_04069};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040754,
ECO:0000256|SAAS:SAAS01040774};
Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040754};
Virion {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040766}.
TOPO_DOM 1 22 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04069}.
TRANSMEM 26 48 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 44 97 Intravirion. {ECO:0000256|HAMAP-
Rule:MF_04069}.
SITE 37 37 Essential for channel activity, possibly
by being protonated during channel
activation, and by forming the channel
gate and the selective filter.
{ECO:0000256|HAMAP-Rule:MF_04069}.
SITE 41 41 Seems to be involved in pH gating.
{ECO:0000256|HAMAP-Rule:MF_04069}.
MOD_RES 64 64 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04069}.
MOD_RES 82 82 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04069}.
LIPID 50 50 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04069}.
DISULFID 17 17 Interchain (with Cys-17).
{ECO:0000256|HAMAP-Rule:MF_04069}.
DISULFID 19 19 Interchain (with Cys-19).
{ECO:0000256|HAMAP-Rule:MF_04069}.
SEQUENCE 97 AA; 11158 MW; FF12EFFCB4370398 CRC64;
MSLLTEVETP TRNGWECKCS DSSDPLVIAA SIIGILHLIL WILDRLFFKC IYRRLKYGLK
RGPSTEGVPE SMREEYRQEQ QSAVDVDDGH FVNIELE
Related products :
GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45
Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur
GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur
GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50
Fax 01 43 25 01 60
RCS Paris B 484 237 888
SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur
GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88
Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur
GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com
Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123
GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel: 0208-080893 Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62 SWIFT RABONL2U
GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur
ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX 058 710 33 48
poland@gentaur.com | Gentaur | Gentaur
Other countries
Österreich +43720880899
Canada Montreal +15149077481
Ceská republika Praha +420246019719
Danmark +4569918806
Finland Helsset +358942419041
Magyarország Budapest +3619980547
Ireland Dublin+35316526556
Luxembourg+35220880274
Norge Oslo+4721031366
Sverige Stockholm+46852503438
Schweiz Züri+41435006251
US New York+17185132983
GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo
Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur
Pathways :
WP1438: Influenza A virus infection
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
Related Genes :
Bibliography :
[30672572] A unique activation-promotion mechanism of the influenza B M2 proton channel uncovered by multiscale simulations.
[30282713] Salinomycin Inhibits Influenza Virus Infection by Disrupting Endosomal Acidification and Viral Matrix Protein 2 Function.
[29500549] Study on the Mechanisms of Active Compounds in Traditional Chinese Medicine for the Treatment of Influenza Virus by Virtual Screening.
[29303574] Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR.
[29210473] Analysis by metadynamics simulation of binding pathway of influenza virus M2 channel blockers.
[29158386] Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
[28740490] Inhibition of the NOD-Like Receptor Protein 3 Inflammasome Is Protective in Juvenile Influenza A Virus Infection.
[28646429] Decoupled side chain and backbone dynamics for proton translocation - M2 of influenza A.
[28467842] Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH Jump.
[28107633] Binding and Proton Blockage by Amantadine Variants of the Influenza M2 and M2 Explained.
Enter catalog number :
Favorites Pages:
No Favorits