Q8CD54 · PIEZ2_MOUSE

  • Protein
    Piezo-type mechanosensitive ion channel component 2
  • Gene
    Piezo2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Pore-forming subunit of the mechanosensitive non-specific cation Piezo channel required for rapidly adapting mechanically activated (MA) currents and has a key role in sensing touch and tactile pain (PubMed:20813920, PubMed:24717433, PubMed:31435011).
Piezo channels are homotrimeric three-blade propeller-shaped structure that utilize a cap-motion and plug-and-latch mechanism to gate their ion-conducting pathways (PubMed:31435011).
In inner ear hair cells, PIEZO1/2 subunits may constitute part of the mechanotransducer (MET) non-selective cation channel complex where they may act as pore-forming ion-conducting component in the complex (PubMed:38228630).
Required for Merkel-cell mechanotransduction (PubMed:24717433).
Plays a major role in light-touch mechanosensation (PubMed:25471886).

Miscellaneous

Piezo comes from the Greek 'piesi' meaning pressure.

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcuticular plate
Cellular Componentneuronal cell body membrane
Cellular Componentplasma membrane
Cellular Componentstereocilium
Molecular Functionmechanosensitive monoatomic ion channel activity
Molecular Functionmonoatomic cation channel activity
Biological Processcellular response to mechanical stimulus
Biological Processdetection of mechanical stimulus
Biological Processdetection of mechanical stimulus involved in sensory perception
Biological Processmonoatomic cation transport
Biological Processregulation of membrane potential
Biological Processresponse to mechanical stimulus

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Piezo-type mechanosensitive ion channel component 2
  • Alternative names
    • Protein FAM38B

Gene names

    • Name
      Piezo2
    • Synonyms
      Fam38b

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8CD54
  • Secondary accessions
    • E2JF23
    • Q8BSM4
    • Q9D341

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Note: Located at the tips and sides of stereocilia and cuticular plate membranes.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-4Cytoplasmic
Transmembrane5-25Helical
Transmembrane27-47Helical
Transmembrane62-82Helical
Transmembrane119-139Helical
Transmembrane214-234Helical
Transmembrane237-257Helical
Transmembrane266-286Helical
Transmembrane336-356Helical
Transmembrane505-525Helical
Transmembrane541-561Helical
Transmembrane581-598Helical
Transmembrane682-702Helical
Transmembrane708-728Helical
Transmembrane736-756Helical
Transmembrane786-806Helical
Transmembrane949-969Helical
Transmembrane975-995Helical
Transmembrane1002-1022Helical
Transmembrane1070-1090Helical
Transmembrane1151-1171Helical
Transmembrane1187-1207Helical
Transmembrane1234-1254Helical
Transmembrane1308-1328Helical
Transmembrane1332-1352Helical
Transmembrane1371-1391Helical
Transmembrane1422-1442Helical
Topological domain1443-1978Cytoplasmic
Transmembrane1979-2001Helical
Transmembrane2008-2028Helical
Transmembrane2037-2057Helical
Transmembrane2261-2281Helical
Transmembrane2302-2322Helical
Transmembrane2330-2350Helical
Transmembrane2360-2380Helical
Transmembrane2397-2414Helical
Transmembrane2428-2448Helical
Transmembrane2476-2496Helical
Topological domain2497-2731Extracellular
Transmembrane2732-2752Helical
Topological domain2753-2822Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Perinatal lethality. Conditional knockout in sensory neurons and Merkel cells causes severe defects in light-touch sensation, although detection of pain (nociception) is unaffected. Conditional knockout in inner ear hair cells show no auditory and vestibular defects (PubMed:38228630).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis2757Reduces to around 50% the permeability of Ca2+.
Mutagenesis2767-2770Hearing and vestibular impairment in conditional knockin mice in inner ear hair cells.

PTM/Processing

Features

Showing features for chain, glycosylation, modified residue, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001868191-2822Piezo-type mechanosensitive ion channel component 2
Glycosylation95N-linked (GlcNAc...) asparagine
Modified residue856Phosphoserine
Glycosylation1030N-linked (GlcNAc...) asparagine
Disulfide bond1031↔1209
Glycosylation1102N-linked (GlcNAc...) asparagine
Glycosylation2692N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in bladder, colon, and lung, but less abundant in kidney or skin (PubMed:20813920).
Strong expression is observed in dorsal root ganglia (DRG) sensory neurons (PubMed:20813920, PubMed:38568807).
Expressed in a wide range of cutaneous low-threshold mechanoreceptors (LTMRs), including Merkel cells and Meissner's corpuscles (PubMed:24717433, PubMed:25471886).
Expressed in sensory neurons (PubMed:24662763).
Expressed in cochlear inner and outer hair cells and vestibular organ hair cells (PubMed:38228630).

Gene expression databases

Interaction

Subunit

Forms the Piezo channel composed of a homotrimer (PubMed:31435011).
Heterotrimeric interaction may occur between PIEZO1 and PIEZO2 (PubMed:38228630).
Interacts with STOML3. Interacts with TMC7; the interaction inhibits PIEZO2-conducted mechanically activated currents (PubMed:38568807).
Interacts with TMC1; the interaction may be part of the MET complex (PubMed:38228630).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Region450-481Disordered
Compositional bias454-481Basic and acidic residues
Coiled coil455-482
Region624-668Disordered
Compositional bias626-652Acidic residues
Compositional bias875-899Basic and acidic residues
Region875-919Disordered
Compositional bias900-918Acidic residues
Coiled coil1475-1515
Region1505-1551Disordered
Compositional bias1527-1551Basic and acidic residues
Region1611-1653Disordered
Compositional bias1618-1653Basic and acidic residues
Region2120-2139Disordered
Region2164-2205Disordered
Compositional bias2166-2205Polar residues

Sequence similarities

Belongs to the PIEZO (TC 1.A.75) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q8CD54-1

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.

  • Length
    2,822
  • Mass (Da)
    325,628
  • Last updated
    2011-01-11 v2
  • Checksum
    D786FBB41F48BA79
MASEVVCGLIFRLLLPICLAVACAFRYNGLSFVYLIYLLLIPLFSEPTKATMQGHTGRLLQSLCITSLSFLLLHIIFHITLASLEAQHRITPAYNCSTWEKTFRQIGFESLKGADAGNGIRVFVPDIGMFIASLTIWLVCRTIVKKPDTEEIAQLNSECENEELAGGEKMDSEEALIYEEDLDGEEGMEGELEESTKLKILRRFASVASKLKEFIGNMITTAGKVVVTILLGSSGMMLPSLTSAVYFFVFLGLCTWWSWCRTFDPLLFGCLCVLLAIFTAGHLIGLYLYQFQFFQEAVPPNDYYARLFGIKSVIQTDCASTWKIIVNPDLSWYHHANPILLLVMYYTLATLIRIWLQEPLVQEEMAKEDEGALDCSSNQNTAERRRSLWYATQYPTDERKLLSMTQDDYKPSDGLLVTVNGNPVDYHTIHPSLPIENGPAKTDLYTTPQYRWEPSEESSEKKEEEEDKREDSEGEGSQEEKRSVRMHAMVAVFQFIMKQSYICALIAMMAWSITYHSWLTFVLLIWSCTLWMIRNRRKYAMISSPFMVVYANLLLVLQYIWSFELPEIKKVPGFLEKKEPGELASKILFTITFWLLLRQHLTEQKALREKEALLSEVKIGSQELEEKEDEELQDVQVEGEPTEKEEEEEEEIKEERHEVKKEEEEEVEEDDDQDIMKVLGNLVVALFIKYWIYVCGGMFFFVSFEGKIVMYKIIYMVLFLFCVALYQVHYEWWRKILKYFWMSVVIYTMLVLIFIYTYQFENFPGLWQNMTGLKKEKLEDLGLKQFTVAELFTRIFIPTSFLLVCILHLHYFHDRFLELTDLKSIPSKEDNTIYSHAKVNGRVYLIINRLAHPEGSLPDLAIMNMTASLDKPEVQKLAESGEERPEECVKKTEKGEAGKDSDESEEEEDEEEESEEEESSDLRNKWHLVIDRLTVLFLKFLEYFHKLQVFMWWILELHIIKIVSSYIIWVTVKEVSLFNYVFLISWAFALPYAKLRRAASSVCTVWTCVIIVCKMLYQLQTIKPENFSVNCSLPNENQTNIPLHELNKSLLYSAPVDPTEWVGLRKSSPLLVYLRNNLLMLAILAFEVTVYRHQEYYRGRNNLTAPVSKTIFHDITRLHLDDGLINCAKYFVNYFFYKFGLETCFLMSVNVIGQRMDFYAMIHACWLIGVLYRRRRKAIAEVWPKYCCFLACIITFQYFVCIGIPPAPCRDYPWRFKGAYFNDNIIKWLYFPDFIVRPNPVFLVYDFMLLLCASLQRQIFEDENKAAVRIMAGDNVEICMNLDAASFSQHNPVPDFIHCRSYLDMSKVIIFSYLFWFVLTIIFITGTTRISIFCMGYLVACFYFLLFGGDLLLKPIKSILRYWDWLIAYNVFVITMKNILSIGACGYIGALVRNSCWLIQAFSLACTVKGYQMPEDDSRCKLPSGEAGIIWDSICFAFLLLQRRVFMSYYFLHVVADIKASQILASRGAELFQATIVKAVKARIEEEKKSMDQLKRQMDRIKARQQKYKKGKERMLSLTQESGEGQDIQKVSEEDDEREADKQKAKGKKKQWWRPWVDHASMVRSGDYYLFETDSEEEEEEELKKEDEEPPRKSAFQFVYQAWITDPKTALRQRRKEKKKLAREEQKERRKGSGDGPVEWEDREDEPVKKKSDGPDNIIKRIFNILKFTWVLFLATVDSFTTWLNSISREHIDISTVLRIERCMLTREIKKGNVPTRESIHMYYQNHIMNLSRESGLDTIDEHSGAGSRAQAAHRMDSLDSRDSISSCYTEATLLISRQSTLDDLDGQDPVPKTSERARPRLRKMFSLDMSSSSADSGSVASSEPTQCTMLYSRQGTTETIEEVEAEAEEEVVEGLEPELHDAEEKEYAAEYEAGVEEISLTPDEELPQFSTDDCEAPPSYSKAVSFEHLSFASQDDSGAKNHMVVSPDDSRTDKLESSILPPLTHELTASDLLMSKMFHDDELEESEKFYVDQPRFLLLFYAMYNTLVARSEMVCYFVIILNHMTSASIITLLLPILIFLWAMLSVPRPSRRFWMMAIVYTEVAIVVKYFFQFGFFPWNKDLEIYKERPYFPPNIIGVEKKEGYVLYDLIQLLALFFHRSILKCHGLWDEDDIVDSNTDKEGSDDELSLDQGRRGSSDSLKSINLAASVESVHVTFPEQPAAIRRKRSCSSSQISPRSSFSSNRSKRGSTSTRNSSQKGSSVLSLKQKSKRELYMEKLQEHLIKAKAFTIKKTLQIYVPIRQFFYDLIHPDYSAVTDVYVLMFLADTVDFIIIVFGFWAFGKHSAAADITSSLSEDQVPGPFLVMVLIQFGTMVVDRALYLRKTVLGKVIFQVILVFGIHFWMFFILPGVTERKFSQNLVAQLWYFVKCVYFGLSAYQIRCGYPTRVLGNFLTKSYNYVNLFLFQGFRLVPFLTELRAVMDWVWTDTTLSLSSWICVEDIYAHIFILKCWRESEKRYPQPRGQKKKKAVKYGMGGMIIVLLICIVWFPLLFMSLIKSVAGVINQPLDVSVTITLGGYQPIFTMSAQQSQLKVMDNSKYNEFLKSFGPNSGAMQFLENYEREDVTVAELEGNSNSLWTISPPSKQKMIQELTDPNSCFSVVFSWSIQRNMTLGAKAEIATDKLSFPLAVATRNSIAKMIAGNDTESSNTPVTIEKIYPYYVKAPSDSNSKPIKQLLSENNFMNITIILFRDNVTKSNSEWWVLNLTGSRIFNQGSQALELVVFNDKVSPPSLGFLAGYGIMGLYASVVLVIGKFVREFFSGISHSIMFEELPNVDRILKLCTDIFLVRETGELELEEDLYAKLIFLYRSPETMIKWTREKTN

Q8CD54-2

  • Name
    2
  • Note
    Due to intron retention.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 2457-2504: RYPQPRGQKKKKAVKYGMGGMIIVLLICIVWFPLLFMSLIKSVAGVIN → VKSRWKCLCHACRPRAQVCYKINMDTAWLVARWMEAGDTTCREPEIQH
    • 2505-2822: Missing

Q8CD54-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5S8DII4A0A5S8DII4_MOUSEPiezo2375
A0A494B9E4A0A494B9E4_MOUSEPiezo2378
A0A494B9D1A0A494B9D1_MOUSEPiezo22690
F6YYK4F6YYK4_MOUSEPiezo2409
A0A494B9V6A0A494B9V6_MOUSEPiezo22778
S4R2S0S4R2S0_MOUSEPiezo22753
A0A494BB29A0A494BB29_MOUSEPiezo2230
E9QNW4E9QNW4_MOUSEPiezo22824

Sequence caution

The sequence BAB31242.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAC27312.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAC27396.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias454-481Basic and acidic residues
Compositional bias626-652Acidic residues
Alternative sequenceVSP_040631629-644in isoform 3
Alternative sequenceVSP_040632645-2822in isoform 3
Compositional bias875-899Basic and acidic residues
Compositional bias900-918Acidic residues
Compositional bias1527-1551Basic and acidic residues
Compositional bias1618-1653Basic and acidic residues
Compositional bias2166-2205Polar residues
Alternative sequenceVSP_0404732457-2504in isoform 2
Alternative sequenceVSP_0404742505-2822in isoform 2
Sequence conflict2810in Ref. 2; BAC27396

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HQ215521
EMBL· GenBank· DDBJ
ADN28065.1
EMBL· GenBank· DDBJ
mRNA
AK018503
EMBL· GenBank· DDBJ
BAB31242.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK031235
EMBL· GenBank· DDBJ
BAC27312.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK031422
EMBL· GenBank· DDBJ
BAC27396.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp