GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

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)

 A0A096XG29_9INFA        Unreviewed;        97 AA.
A0A096XG29;
07-JAN-2015, integrated into UniProtKB/TrEMBL.
07-JAN-2015, sequence version 1.
03-JUL-2019, entry version 30.
RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199250};
AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069};
Name=M2 {ECO:0000313|EMBL:AHM24377.1};
Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069};
Influenza A virus (A/Korean native chicken/Korea/H257/2014(H5N8)).
Viruses; Riboviria; Negarnaviricota; Polyploviricotina;
Insthoviricetes; Articulavirales; Orthomyxoviridae;
Alphainfluenzavirus.
NCBI_TaxID=1470226 {ECO:0000313|EMBL:AHM24377.1, ECO:0000313|Proteomes:UP000137253};
[1] {ECO:0000313|EMBL:AHM24377.1, ECO:0000313|Proteomes:UP000137253}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=A/Korean native chicken/Korea/H257/2014
{ECO:0000313|EMBL:AHM24377.1};
PubMed=25192767; DOI=10.1016/j.vetmic.2014.08.002;
Jeong J., Kang H.M., Lee E.K., Song B.M., Kwon Y.K., Kim H.R.,
Choi K.S., Kim J.Y., Lee H.J., Moon O.K., Jeong W., Choi J.,
Baek J.H., Joo Y.S., Park Y.H., Lee H.S., Lee Y.J.;
"Highly pathogenic avian influenza virus (H5N8) in domestic poultry
and its relationship with migratory birds in South Korea during
2014.";
Vet. Microbiol. 173:249-257(2014).
-!- 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:SAAS01199231}.
-!- 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:SAAS01199254}.
-!- 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:SAAS01199237}.
-!- SUBCELLULAR LOCATION: Host apical cell membrane
{ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|SAAS:SAAS01199239};
Single-pass type III membrane protein {ECO:0000256|HAMAP-
Rule:MF_04069, ECO:0000256|SAAS:SAAS01199239}. 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:SAAS01199247}.
-!- 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; KJ509127; AHM24377.1; -; Viral_cRNA.
Proteomes; UP000137253; Genome.
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.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000137253};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01199248};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199252};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199252};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01199229};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199235};
Inhibition of host autophagy by virus {ECO:0000256|HAMAP-
Rule:MF_04069, ECO:0000256|SAAS:SAAS01199229};
Ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01199243};
Ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199235,
ECO:0000256|SAAS:SAAS01199243};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
Membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199233,
ECO:0000256|SAAS:SAAS01199252, 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:SAAS01199233,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199233,
ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199235,
ECO:0000256|SAAS:SAAS01199243};
Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01199243};
Virion {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199241}.
TOPO_DOM 1 22 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04069}.
TRANSMEM 28 48 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 44 97 Intravirion. {ECO:0000256|HAMAP-
Rule:MF_04069}.
REGION 64 83 Disordered. {ECO:0000256|MobiDB-
lite:A0A096XG29}.
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; 11215 MW; 1AD705BBB34C6872 CRC64;
MSLLTEVETP TRTEWECRCS DSSDPLVVAA NIIGILHLIL WILDRLFFKC IYRRLKYGLK
IGPSTEGVPE SMREEYRQEQ QSAVDVDDGH FVNIELE


Related products :

Catalog number Product name Quantity
EIAAB45633 ATP6AP1L,Homo sapiens,Human,Vacuolar proton pump subunit S1-like protein,V-type proton ATPase subunit S1-like protein
18-003-42634 Kv channel-interacting protein 1 - KChIP1; A-type potassium channel modulatory protein 1; Potassium channel-interacting protein 1; Vesicle APC-binding protein Polyclonal 0.1 mg Protein A
U1639p CLIA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
E1639p ELISA kit 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
orb81536 SARS Associated Coronavirus Matrix protein The E.coli derived 30kDa recombinant protein contains the Matrix protein 182-216 amino acids immunodominant regions. For research use only. 100
E1639p ELISA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
U1639b CLIA 22 kDa extracellular matrix protein,Bos taurus,Bovine,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,TRAMP,Tyrosine-rich acidic matrix protein 96T
E1639b ELISA kit 22 kDa extracellular matrix protein,Bos taurus,Bovine,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,TRAMP,Tyrosine-rich acidic matrix protein 96T
E1639b ELISA 22 kDa extracellular matrix protein,Bos taurus,Bovine,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,TRAMP,Tyrosine-rich acidic matrix protein 96T
18-003-42669 Kv channel-interacting protein 2 - KChIP2; A-type potassium channel modulatory protein 2; Potassium channel-interacting protein 2; Cardiac voltage-gated potassium channel modulatory subunit Polyclonal 0.05 mg Aff Pur
18-003-42670 Kv channel-interacting protein 2 - KChIP2; A-type potassium channel modulatory protein 2; Potassium channel-interacting protein 2; Cardiac voltage-gated potassium channel modulatory subunit Polyclonal 0.05 mg Aff Pur
EIAAB39941 Homo sapiens,Human,Ser_Arg-related nuclear matrix protein,Serine_arginine repetitive matrix protein 1,SRm160,SRM160,SR-related nuclear matrix protein of 160 kDa,SRRM1
EIAAB45632 ATP6AP1,ATP6IP1,ATP6S1,Homo sapiens,Human,Protein XAP-3,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,VATPS1,V-type proton ATPase subunit S1,X
EIAAB45630 Atp6ap1,Atp6ip1,Atp6s1,C7-1 protein,Rat,Rattus norvegicus,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45631 Atp6ap1,Atp6ip1,Atp6s1,Mouse,Mus musculus,Protein C7-1,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB37554 CAP-1A,Clathrin-associated protein 1A,Rat,Rattus norvegicus,Sap1,Sclt1,Sodium channel and clathrin linker 1,Sodium channel Nav1.8-binding protein,Sodium channel-associated protein 1
EIAAB39943 300 kDa nuclear matrix antigen,Homo sapiens,HSPC075,Human,KIAA0324,Ser_Arg-related nuclear matrix protein of 300 kDa,Serine_arginine repetitive matrix protein 2,Serine_arginine-rich splicing factor-re
EIAAB45691 ATP6V1H,CGI-11,Homo sapiens,Human,NBP1,Nef-binding protein 1,Protein VMA13 homolog,Vacuolar proton pump subunit H,Vacuolar proton pump subunit SFD,V-ATPase 50_57 kDa subunits,V-ATPase subunit H,V-type
EIAAB45563 32 kDa accessory protein,ATP6D,ATP6V0D1,Homo sapiens,Human,p39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase
EIAAB45564 32 kDa accessory protein,ATP6D,ATP6V0D1,Bos taurus,Bovine,P39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase
EIAAB39674 Ecm2,Extracellular matrix protein 2,Matrix glycoprotein Sc1,Mouse,Mus musculus,Sc1,Sparcl1,SPARC-like protein 1
EIAAB37619 hNaN,Homo sapiens,Human,Peripheral nerve sodium channel 5,PN5,SCN11A,SCN12A,Sensory neuron sodium channel 2,SNS2,Sodium channel protein type 11 subunit alpha,Sodium channel protein type XI subunit alp
EIAAB09907 Ca(v)-like protein,Cation channel sperm-associated protein 3,CatSper3,CATSPER3,Homo sapiens,Human,One-repeat calcium channel-like protein
EIAAB26323 Four domain-type voltage-gated ion channel alpha-1 subunit,Nalcn,Nca,Rat,Rattus norvegicus,Sodium leak channel non-selective protein,Vgcnl1,Voltage gated channel-like protein 1
EIAAB47428 CAG repeat protein 1,CAGH1,CAS-interacting zinc finger protein,CIZ,Homo sapiens,Human,NMP4,Nuclear matrix protein 4,Nuclear matrix transcription factor 4,TNRC1,Trinucleotide repeat-containing gene 1 p
Pathways :
WP1438: Influenza A virus infection
WP1690: Propanoate metabolism
WP931: G Protein Signaling Pathways
WP1625: Base excision repair
WP2203: TSLP Signaling Pathway
WP1654: gamma-Hexachlorocyclohexane degradation
WP2292: Chemokine signaling pathway
WP1694: Pyrimidine metabolism
WP1714: Tyrosine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP2371: Parkinsons Disease Pathway
WP1672: Mismatch repair
WP35: G Protein Signaling Pathways
WP1493: Carbon assimilation C4 pathway
WP1909: Signal regulatory protein (SIRP) family interactions
WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP1676: Non-homologous end-joining
WP73: G Protein Signaling Pathways
WP1689: Porphyrin and chlorophyll metabolism
WP1624: Bacterial secretion system
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP1049: G Protein Signaling Pathways
WP1693: Purine metabolism

Related Genes :
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M M2] Matrix protein 2 (Proton channel protein M2)
[M M2] Matrix protein 2 (Proton channel protein M2)
[M M2] Matrix protein 2 (Proton channel protein M2)
[M2 M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M M2] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2)
[M] Matrix protein 2 (Proton channel protein M2) (Fragment)
[M] Matrix protein 2 (Proton channel protein M2) (Fragment)

Bibliography :
[31261944] Viroporins in the Influenza Virus.
[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.
[30230312] A Robust Proton Flux (pHlux) Assay for Studying the Function and Inhibition of the Influenza A M2 Proton Channel.
[30230310] Random Mutagenesis Analysis of the Influenza A M2 Proton Channel Reveals Novel Resistance Mutants.
[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.