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P55926

- ASIC1_RAT

UniProt

P55926 - ASIC1_RAT

Protein

Acid-sensing ion channel 1

Gene

Asic1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 discrimates stronger than isoform 1 between monovalent cations. Isoform 3 can flux Ca2+ while isoform 1 cannot. Heteromeric channels composed of isoform 2 and isoform 3 are active but have a lower pH-sensitivity. Mediates glutamate-independent Ca2+ entry into neurons upon acidosis. This Ca2+ overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties.7 Publications

    Enzyme regulationi

    Inhibited by the diuretic amiloride.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei71 – 711Important for channel gatingBy similarity
    Sitei79 – 791Important for channel desensitizingBy similarity
    Sitei287 – 2871Important for channel gatingBy similarity

    GO - Molecular functioni

    1. acid-sensing ion channel activity Source: UniProtKB
    2. ion channel activity Source: RGD
    3. ion gated channel activity Source: Ensembl

    GO - Biological processi

    1. associative learning Source: Ensembl
    2. calcium ion transmembrane transport Source: Ensembl
    3. cellular response to pH Source: UniProtKB
    4. ion transmembrane transport Source: RGD
    5. memory Source: Ensembl
    6. negative regulation of neurotransmitter secretion Source: Ensembl
    7. protein homotrimerization Source: UniProtKB
    8. regulation of membrane potential Source: Ensembl
    9. response to acid chemical Source: Ensembl
    10. sensory perception of pain Source: RGD
    11. sodium ion transmembrane transport Source: UniProtKB

    Keywords - Molecular functioni

    Ion channel, Sodium channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    Calcium, Sodium

    Protein family/group databases

    TCDBi1.A.6.1.2. the epithelial na(+) channel (enac) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acid-sensing ion channel 1
    Short name:
    ASIC1
    Alternative name(s):
    Amiloride-sensitive cation channel 2, neuronal
    Brain sodium channel 2
    Short name:
    BNaC2
    Gene namesi
    Name:Asic1
    Synonyms:Accn2, Bnac2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome X

    Organism-specific databases

    RGDi71062. Asic1.

    Subcellular locationi

    Cell membrane 3 Publications; Multi-pass membrane protein 3 Publications
    Note: Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4 By similarity.By similarity

    GO - Cellular componenti

    1. cell surface Source: RGD
    2. integral component of plasma membrane Source: UniProtKB
    3. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 831S → P: No effect. Increases desensitization rates; when associated with L-84 and M-85. 1 Publication
    Mutagenesisi84 – 841Q → L: No effect. Increases desensitization rates; when associated with P-83 and M-85. 1 Publication
    Mutagenesisi85 – 851L → M: No effect. Increases desensitization rates; when associated with P-83 and L-84. 1 Publication
    Mutagenesisi100 – 1001F → L: No effect on channel activation and inactivation. 1 Publication
    Mutagenesisi103 – 1031V → L: No effect on channel activation and inactivation. 1 Publication
    Mutagenesisi105 – 1051K → Y: Activated and inactivated at lower pH. 1 Publication
    Mutagenesisi106 – 1061N → P: Activated and inactivated at lower pH. 1 Publication
    Mutagenesisi128 – 1314QMAD → HLVE: No effect on desensitization rates.
    Mutagenesisi425 – 4251E → G: Reduction of Ca(2+) block. Loss of Ca(2+) block; when associated with C-432. 1 Publication
    Mutagenesisi431 – 4311G → V or F: Constitutive channel activity. 1 Publication
    Mutagenesisi432 – 4321D → A: Reduction of Ca(2+) block. 1 Publication
    Mutagenesisi432 – 4321D → C: Reduction of Ca(2+) block. Loss of Ca(2+) block; when associated with G-425. 1 Publication
    Mutagenesisi436 – 4361Q → N: No effect on Ca(2+) block. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 526526Acid-sensing ion channel 1PRO_0000181300Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi93 ↔ 194By similarity
    Disulfide bondi172 ↔ 179By similarity
    Disulfide bondi290 ↔ 365By similarity
    Disulfide bondi308 ↔ 361By similarity
    Disulfide bondi312 ↔ 359By similarity
    Disulfide bondi321 ↔ 343By similarity
    Disulfide bondi323 ↔ 335By similarity
    Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
    Modified residuei477 – 4771PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by PKA regulates interaction with PRKCABP and subcellular location. Phosphorylation by PKC may regulate the channel By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiP55926.

    PTM databases

    PhosphoSiteiP55926.

    Expressioni

    Tissue specificityi

    Expressed in dorsal root ganglia and sciatic nerve (at protein level). Widely distributed throughout the brain. Expressed in olfactory bulb, neo and allocortical regions, dentate granule cells, pyramidal cells of CA1-CA3 subfields of the hippocampal formation, habenula, basolateral amygdaloid nuclei, and in the Purkinje and granule cells of the cerebellum. Diffusely detected over most other regions of the basal ganglia, including thalamic nuclei, substantia nigra, striatum and globus pallidus, hypothalamus, midbrain, pons, medulla and choroid plexus. Isoform 3 is expressed only in dorsal root ganglion (DRG) while isoform 1 is expressed in DRG, spinal chord, trigeminal ganglia and the trigeminal mesencephalic nucleus.4 Publications

    Inductioni

    Up-regulation upon tissues inflammation is abolished by anti-inflammatory drugs.1 Publication

    Gene expression databases

    GenevestigatoriP55926.

    Interactioni

    Subunit structurei

    Homotrimer or heterotrimer with other ASIC proteins By similarity. Interacts with STOM and PRKCABP By similarity. Interacts with ASIC2.By similarity1 Publication

    Protein-protein interaction databases

    MINTiMINT-223538.

    Structurei

    3D structure databases

    ProteinModelPortaliP55926.
    SMRiP55926. Positions 40-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4545CytoplasmicBy similarityAdd
    BLAST
    Topological domaini70 – 425356ExtracellularBy similarityAdd
    BLAST
    Topological domaini453 – 52674CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei46 – 6924HelicalBy similarityAdd
    BLAST
    Transmembranei426 – 45227Discontinuously helicalBy similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 256Involved in divalent cations permeability

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi442 – 4443Selectivity filterCurated

    Domaini

    Channel opening involves a conformation change that affects primarily the extracellular domain and the second transmembrane helix and its orientation in the membrane. In the open state, the second transmembrane helix is nearly perpendicular to the plane of the membrane; in the desensitized state it is strongly tilted. Besides, the second transmembrane domain is discontinuously helical in the open state. The GAS motif of the selectivity filter is in an extended conformation, giving rise to a distinct kink in the polypeptide chain. A domain swap between subunits gives rise to a full-length transmembrane helix By similarity.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG262945.
    GeneTreeiENSGT00640000091217.
    HOGENOMiHOG000247010.
    HOVERGENiHBG004150.
    KOiK04829.
    OMAiIQYYFLY.
    OrthoDBiEOG72VH5P.
    PhylomeDBiP55926.
    TreeFamiTF330663.

    Family and domain databases

    InterProiIPR004724. EnaC.
    IPR001873. Na+channel_ASC.
    IPR020903. Na+channel_ASC_CS.
    [Graphical view]
    PANTHERiPTHR11690. PTHR11690. 1 hit.
    PfamiPF00858. ASC. 1 hit.
    [Graphical view]
    PRINTSiPR01078. AMINACHANNEL.
    TIGRFAMsiTIGR00859. ENaC. 1 hit.
    PROSITEiPS01206. ASC. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55926-1) [UniParc]FASTAAdd to Basket

    Also known as: ASIC-alpha, asic1alpha

    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

    MELKTEEEEV GGVQPVSIQA FASSSTLHGL AHIFSYERLS LKRALWALCF    50
    LGSLAVLLCV CTERVQYYFC YHHVTKLDEV AASQLTFPAV TLCNLNEFRF 100
    SQVSKNDLYH AGELLALLNN RYEIPDTQMA DEKQLEILQD KANFRSFKPK 150
    PFNMREFYDR AGHDIRDMLL SCHFRGEACS AEDFKVVFTR YGKCYTFNSG 200
    QDGRPRLKTM KGGTGNGLEI MLDIQQDEYL PVWGETDETS FEAGIKVQIH 250
    SQDEPPFIDQ LGFGVAPGFQ TFVSCQEQRL IYLPSPWGTC NAVTMDSDFF 300
    DSYSITACRI DCETRYLVEN CNCRMVHMPG DAPYCTPEQY KECADPALDF 350
    LVEKDQEYCV CEMPCNLTRY GKELSMVKIP SKASAKYLAK KFNKSEQYIG 400
    ENILVLDIFF EVLNYETIEQ KKAYEIAGLL GDIGGQMGLF IGASILTVLE 450
    LFDYAYEVIK HRLCRRGKCQ KEAKRSSADK GVALSLDDVK RHNPCESLRG 500
    HPAGMTYAAN ILPHHPARGT FEDFTC 526
    Length:526
    Mass (Da):59,641
    Last modified:November 1, 1997 - v1
    Checksum:i5462A7786E2A1726
    GO
    Isoform 2 (identifier: P55926-2) [UniParc]FASTAAdd to Basket

    Also known as: ASIC-beta2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-185: Missing.
         186-186: V → MADIWGPHHH...VIALGAFLCQ

    Note: Inactive.

    Show »
    Length:425
    Mass (Da):47,563
    Checksum:i8B4A9EDFCE348B89
    GO
    Isoform 3 (identifier: P55926-3) [UniParc]FASTAAdd to Basket

    Also known as: ASIC-beta, ASIC1b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-185: Missing.
         186-186: V → MPIQIFCSVS...GPCGPHNFSV

    Note: Blocked by Ca(2+). Mutagenesis of Asp-465 to Asn reduces Ca(2+) block.Curated

    Show »
    Length:559
    Mass (Da):62,217
    Checksum:i0F438117B95C18E5
    GO

    Sequence cautioni

    The sequence CAA07080.1 differs from that shown. Reason: Frameshift at positions 119, 122 and 142.
    Isoform 3 : The sequence CAA07080.1 differs from that shown. Reason: Frameshift at positions 7 and 14.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 3 (identifier: P55926-3)
    Sequence conflicti128 – 1281T → S in CAA07080. (PubMed:9707631)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 185185Missing in isoform 2 and isoform 3. 3 PublicationsVSP_015597Add
    BLAST
    Alternative sequencei186 – 1861V → MADIWGPHHHRQQQDSSESE EEEEKEMEAGSELDEGDDSP RDLVAFANSCTLHGASHVFV EGGPGPRQALWAVAFVIALG AFLCQ in isoform 2. 1 PublicationVSP_015598
    Alternative sequencei186 – 1861V → MPIQIFCSVSFSSGEEAPGS MADIWGPHHHRQQQDSSESE EEEEKEMEAGSELDEGDDSP RDLVAFANSCTLHGASHVFV EGGPGPRQALWAVAFVIALG AFLCQVGDRVAYYLSYPHVT LLDEVATTELVFPAVTFCNT NAVRLSQLSYPDLLYLAPML GLDESDDPGVPLAPPGPEAF SGEPFNLHRFYNRSCHRLED MLLYCSYCGGPCGPHNFSV in isoform 3. 2 PublicationsVSP_015599

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94403 mRNA. Translation: AAB53002.1.
    AJ006519 mRNA. Translation: CAA07080.1. Frameshift.
    AJ309926 mRNA. Translation: CAC44267.1.
    AB049451 mRNA. Translation: BAB39864.1.
    RefSeqiNP_077068.1. NM_024154.2. [P55926-1]
    XP_006257440.1. XM_006257378.1. [P55926-3]
    XP_006257443.1. XM_006257381.1. [P55926-1]
    UniGeneiRn.37385.

    Genome annotation databases

    EnsembliENSRNOT00000025476; ENSRNOP00000025476; ENSRNOG00000018789. [P55926-1]
    ENSRNOT00000047887; ENSRNOP00000041786; ENSRNOG00000018789. [P55926-3]
    GeneIDi79123.
    KEGGirno:79123.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94403 mRNA. Translation: AAB53002.1 .
    AJ006519 mRNA. Translation: CAA07080.1 . Frameshift.
    AJ309926 mRNA. Translation: CAC44267.1 .
    AB049451 mRNA. Translation: BAB39864.1 .
    RefSeqi NP_077068.1. NM_024154.2. [P55926-1 ]
    XP_006257440.1. XM_006257378.1. [P55926-3 ]
    XP_006257443.1. XM_006257381.1. [P55926-1 ]
    UniGenei Rn.37385.

    3D structure databases

    ProteinModelPortali P55926.
    SMRi P55926. Positions 40-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-223538.

    Chemistry

    GuidetoPHARMACOLOGYi 684.

    Protein family/group databases

    TCDBi 1.A.6.1.2. the epithelial na(+) channel (enac) family.

    PTM databases

    PhosphoSitei P55926.

    Proteomic databases

    PRIDEi P55926.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025476 ; ENSRNOP00000025476 ; ENSRNOG00000018789 . [P55926-1 ]
    ENSRNOT00000047887 ; ENSRNOP00000041786 ; ENSRNOG00000018789 . [P55926-3 ]
    GeneIDi 79123.
    KEGGi rno:79123.

    Organism-specific databases

    CTDi 41.
    RGDi 71062. Asic1.

    Phylogenomic databases

    eggNOGi NOG262945.
    GeneTreei ENSGT00640000091217.
    HOGENOMi HOG000247010.
    HOVERGENi HBG004150.
    KOi K04829.
    OMAi IQYYFLY.
    OrthoDBi EOG72VH5P.
    PhylomeDBi P55926.
    TreeFami TF330663.

    Miscellaneous databases

    NextBioi 614550.
    PROi P55926.

    Gene expression databases

    Genevestigatori P55926.

    Family and domain databases

    InterProi IPR004724. EnaC.
    IPR001873. Na+channel_ASC.
    IPR020903. Na+channel_ASC_CS.
    [Graphical view ]
    PANTHERi PTHR11690. PTHR11690. 1 hit.
    Pfami PF00858. ASC. 1 hit.
    [Graphical view ]
    PRINTSi PR01078. AMINACHANNEL.
    TIGRFAMsi TIGR00859. ENaC. 1 hit.
    PROSITEi PS01206. ASC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A proton-gated cation channel involved in acid-sensing."
      Waldmann R., Champigny G., Bassilana F., Heurteaux C., Lazdunski M.
      Nature 386:173-177(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Spinal ganglion.
    3. "Molecular and functional characterization of acid-sensing ion channel (ASIC) 1b."
      Baessler E.-L., Ngo-Anh T.J., Geisler H.-S., Ruppersberg J.P., Gruender S.
      J. Biol. Chem. 276:33782-33787(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), DOMAIN, FUNCTION.
      Tissue: Inner ear.
    4. "Cloning and functional expression of ASIC-beta2, a splice variant of ASIC-beta."
      Ugawa S., Ueda T., Takahashi E., Hirabayashi Y., Yoneda T., Komai S., Shimada S.
      NeuroReport 12:2865-2869(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION.
      Tissue: Trigeminal ganglion.
    5. "The acid-sensitive ionic channel subunit ASIC and the mammalian degenerin MDEG form a heteromultimeric H+-gated Na+ channel with novel properties."
      Bassilana F., Champigny G., Waldmann R., de Weille J.R., Heurteaux C., Lazdunski M.
      J. Biol. Chem. 272:28819-28822(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH ASIC1, MUTAGENESIS OF GLY-431, FUNCTION.
    6. "Isolation of a tarantula toxin specific for a class of proton-gated Na+ channels."
      Escoubas P., de Weille J.R., Lecoq A., Diochot S., Waldmann R., Champigny G., Moinier D., Menez A., Lazdunski M.
      J. Biol. Chem. 275:25116-25121(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION BY PCTX1 TOXIN.
    7. "Neuropeptide FF and FMRFamide potentiate acid-evoked currents from sensory neurons and proton-gated DEG/ENaC channels."
      Askwith C.C., Cheng C., Ikuma M., Benson C., Price M.P., Welsh M.J.
      Neuron 26:133-141(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGULATION BY FMRFAMIDE-RELATED PEPTIDES.
    8. "Nonsteroid anti-inflammatory drugs inhibit both the activity and the inflammation-induced expression of acid-sensing ion channels in nociceptors."
      Voilley N., de Weille J.R., Mamet J., Lazdunski M.
      J. Neurosci. 21:8026-8033(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, INHIBITION BY DRUGS.
    9. "Alternative splicing and interaction with di- and polyvalent cations control the dynamic range of acid-sensing ion channel 1 (ASIC1)."
      Babini E., Paukert M., Geisler H.-S., Gruender S.
      J. Biol. Chem. 277:41597-41603(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PHE-100; VAL-103; LYS-105 AND ASN-106, FUNCTION.
    10. "Functional implications of the localization and activity of acid-sensitive channels in rat peripheral nervous system."
      Alvarez de la Rosa D., Zhang P., Shao D., White F., Canessa C.M.
      Proc. Natl. Acad. Sci. U.S.A. 99:2326-2331(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    11. "The extracellular domain determines the kinetics of desensitization in acid-sensitive ion channel 1."
      Coric T., Zhang P., Todorovic N., Canessa C.M.
      J. Biol. Chem. 278:45240-45247(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-83; GLN-84; LEU-85 AND 128-GLN--ASP-131.
    12. "Neuroprotection in ischemia: blocking calcium-permeable acid-sensing ion channels."
      Xiong Z.-G., Zhu X.-M., Chu X.-P., Minami M., Hey J., Wei W.-L., MacDonald J.F., Wemmie J.A., Price M.P., Welsh M.J., Simon R.P.
      Cell 118:687-698(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Identification of the Ca2+ blocking site of acid-sensing ion channel (ASIC) 1: implications for channel gating."
      Paukert M., Babini E., Pusch M., Grunder S.
      J. Gen. Physiol. 124:383-394(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-425; ASP-432 AND GLN-436.

    Entry informationi

    Entry nameiASIC1_RAT
    AccessioniPrimary (citable) accession number: P55926
    Secondary accession number(s): O88762, Q91YB8, Q99NA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Potentiated by Ca2+, Mg2+, Ba2+, multivalent cations and potentiated by FMRFamide-related neuropeptides. PH dependence may be regulated by serine proteases. Inhibited by anti-inflammatory drugs like salicylic acid. Isoform 1 homomultimeric channel is specifically and reversibly inhibited by PcTX1, a tarantula venom toxin, while isoform 2 and other ASICs are insensitive.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3