Q8CD54 · PIEZ2_MOUSE
- ProteinPiezo-type mechanosensitive ion channel component 2
- GenePiezo2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2822 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- Ca2+(in) = Ca2+(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cuticular plate | |
Cellular Component | neuronal cell body membrane | |
Cellular Component | plasma membrane | |
Cellular Component | stereocilium | |
Molecular Function | mechanosensitive monoatomic ion channel activity | |
Molecular Function | monoatomic cation channel activity | |
Biological Process | cellular response to mechanical stimulus | |
Biological Process | detection of mechanical stimulus | |
Biological Process | detection of mechanical stimulus involved in sensory perception | |
Biological Process | monoatomic cation transport | |
Biological Process | regulation of membrane potential | |
Biological Process | response to mechanical stimulus |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePiezo-type mechanosensitive ion channel component 2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8CD54
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4 | Cytoplasmic | ||||
Sequence: MASE | ||||||
Transmembrane | 5-25 | Helical | ||||
Sequence: VVCGLIFRLLLPICLAVACAF | ||||||
Transmembrane | 27-47 | Helical | ||||
Sequence: YNGLSFVYLIYLLLIPLFSEP | ||||||
Transmembrane | 62-82 | Helical | ||||
Sequence: SLCITSLSFLLLHIIFHITLA | ||||||
Transmembrane | 119-139 | Helical | ||||
Sequence: GIRVFVPDIGMFIASLTIWLV | ||||||
Transmembrane | 214-234 | Helical | ||||
Sequence: FIGNMITTAGKVVVTILLGSS | ||||||
Transmembrane | 237-257 | Helical | ||||
Sequence: MLPSLTSAVYFFVFLGLCTWW | ||||||
Transmembrane | 266-286 | Helical | ||||
Sequence: LLFGCLCVLLAIFTAGHLIGL | ||||||
Transmembrane | 336-356 | Helical | ||||
Sequence: ANPILLLVMYYTLATLIRIWL | ||||||
Transmembrane | 505-525 | Helical | ||||
Sequence: LIAMMAWSITYHSWLTFVLLI | ||||||
Transmembrane | 541-561 | Helical | ||||
Sequence: MISSPFMVVYANLLLVLQYIW | ||||||
Transmembrane | 581-598 | Helical | ||||
Sequence: GELASKILFTITFWLLLR | ||||||
Transmembrane | 682-702 | Helical | ||||
Sequence: LVVALFIKYWIYVCGGMFFFV | ||||||
Transmembrane | 708-728 | Helical | ||||
Sequence: IVMYKIIYMVLFLFCVALYQV | ||||||
Transmembrane | 736-756 | Helical | ||||
Sequence: ILKYFWMSVVIYTMLVLIFIY | ||||||
Transmembrane | 786-806 | Helical | ||||
Sequence: FTVAELFTRIFIPTSFLLVCI | ||||||
Transmembrane | 949-969 | Helical | ||||
Sequence: VFMWWILELHIIKIVSSYIIW | ||||||
Transmembrane | 975-995 | Helical | ||||
Sequence: VSLFNYVFLISWAFALPYAKL | ||||||
Transmembrane | 1002-1022 | Helical | ||||
Sequence: VCTVWTCVIIVCKMLYQLQTI | ||||||
Transmembrane | 1070-1090 | Helical | ||||
Sequence: LLVYLRNNLLMLAILAFEVTV | ||||||
Transmembrane | 1151-1171 | Helical | ||||
Sequence: VIGQRMDFYAMIHACWLIGVL | ||||||
Transmembrane | 1187-1207 | Helical | ||||
Sequence: CCFLACIITFQYFVCIGIPPA | ||||||
Transmembrane | 1234-1254 | Helical | ||||
Sequence: FIVRPNPVFLVYDFMLLLCAS | ||||||
Transmembrane | 1308-1328 | Helical | ||||
Sequence: VIIFSYLFWFVLTIIFITGTT | ||||||
Transmembrane | 1332-1352 | Helical | ||||
Sequence: IFCMGYLVACFYFLLFGGDLL | ||||||
Transmembrane | 1371-1391 | Helical | ||||
Sequence: VFVITMKNILSIGACGYIGAL | ||||||
Transmembrane | 1422-1442 | Helical | ||||
Sequence: LPSGEAGIIWDSICFAFLLLQ | ||||||
Topological domain | 1443-1978 | Cytoplasmic | ||||
Sequence: RRVFMSYYFLHVVADIKASQILASRGAELFQATIVKAVKARIEEEKKSMDQLKRQMDRIKARQQKYKKGKERMLSLTQESGEGQDIQKVSEEDDEREADKQKAKGKKKQWWRPWVDHASMVRSGDYYLFETDSEEEEEEELKKEDEEPPRKSAFQFVYQAWITDPKTALRQRRKEKKKLAREEQKERRKGSGDGPVEWEDREDEPVKKKSDGPDNIIKRIFNILKFTWVLFLATVDSFTTWLNSISREHIDISTVLRIERCMLTREIKKGNVPTRESIHMYYQNHIMNLSRESGLDTIDEHSGAGSRAQAAHRMDSLDSRDSISSCYTEATLLISRQSTLDDLDGQDPVPKTSERARPRLRKMFSLDMSSSSADSGSVASSEPTQCTMLYSRQGTTETIEEVEAEAEEEVVEGLEPELHDAEEKEYAAEYEAGVEEISLTPDEELPQFSTDDCEAPPSYSKAVSFEHLSFASQDDSGAKNHMVVSPDDSRTDKLESSILPPLTHELTASDLLMSKMFHDDELEESEKFYVDQPRFL | ||||||
Transmembrane | 1979-2001 | Helical | ||||
Sequence: LLFYAMYNTLVARSEMVCYFVII | ||||||
Transmembrane | 2008-2028 | Helical | ||||
Sequence: ASIITLLLPILIFLWAMLSVP | ||||||
Transmembrane | 2037-2057 | Helical | ||||
Sequence: MAIVYTEVAIVVKYFFQFGFF | ||||||
Transmembrane | 2261-2281 | Helical | ||||
Sequence: VLMFLADTVDFIIIVFGFWAF | ||||||
Transmembrane | 2302-2322 | Helical | ||||
Sequence: PFLVMVLIQFGTMVVDRALYL | ||||||
Transmembrane | 2330-2350 | Helical | ||||
Sequence: VIFQVILVFGIHFWMFFILPG | ||||||
Transmembrane | 2360-2380 | Helical | ||||
Sequence: LVAQLWYFVKCVYFGLSAYQI | ||||||
Transmembrane | 2397-2414 | Helical | ||||
Sequence: YNYVNLFLFQGFRLVPFL | ||||||
Transmembrane | 2428-2448 | Helical | ||||
Sequence: TTLSLSSWICVEDIYAHIFIL | ||||||
Transmembrane | 2476-2496 | Helical | ||||
Sequence: GMIIVLLICIVWFPLLFMSLI | ||||||
Topological domain | 2497-2731 | Extracellular | ||||
Sequence: KSVAGVINQPLDVSVTITLGGYQPIFTMSAQQSQLKVMDNSKYNEFLKSFGPNSGAMQFLENYEREDVTVAELEGNSNSLWTISPPSKQKMIQELTDPNSCFSVVFSWSIQRNMTLGAKAEIATDKLSFPLAVATRNSIAKMIAGNDTESSNTPVTIEKIYPYYVKAPSDSNSKPIKQLLSENNFMNITIILFRDNVTKSNSEWWVLNLTGSRIFNQGSQALELVVFNDKVSPPS | ||||||
Transmembrane | 2732-2752 | Helical | ||||
Sequence: LGFLAGYGIMGLYASVVLVIG | ||||||
Topological domain | 2753-2822 | Cytoplasmic | ||||
Sequence: KFVREFFSGISHSIMFEELPNVDRILKLCTDIFLVRETGELELEEDLYAKLIFLYRSPETMIKWTREKTN |
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2757 | Reduces to around 50% the permeability of Ca2+. | ||||
Sequence: E → A | ||||||
Mutagenesis | 2767-2770 | Hearing and vestibular impairment in conditional knockin mice in inner ear hair cells. | ||||
Sequence: MFEE → AAAA |
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000186819 | 1-2822 | Piezo-type mechanosensitive ion channel component 2 | |||
Sequence: MASEVVCGLIFRLLLPICLAVACAFRYNGLSFVYLIYLLLIPLFSEPTKATMQGHTGRLLQSLCITSLSFLLLHIIFHITLASLEAQHRITPAYNCSTWEKTFRQIGFESLKGADAGNGIRVFVPDIGMFIASLTIWLVCRTIVKKPDTEEIAQLNSECENEELAGGEKMDSEEALIYEEDLDGEEGMEGELEESTKLKILRRFASVASKLKEFIGNMITTAGKVVVTILLGSSGMMLPSLTSAVYFFVFLGLCTWWSWCRTFDPLLFGCLCVLLAIFTAGHLIGLYLYQFQFFQEAVPPNDYYARLFGIKSVIQTDCASTWKIIVNPDLSWYHHANPILLLVMYYTLATLIRIWLQEPLVQEEMAKEDEGALDCSSNQNTAERRRSLWYATQYPTDERKLLSMTQDDYKPSDGLLVTVNGNPVDYHTIHPSLPIENGPAKTDLYTTPQYRWEPSEESSEKKEEEEDKREDSEGEGSQEEKRSVRMHAMVAVFQFIMKQSYICALIAMMAWSITYHSWLTFVLLIWSCTLWMIRNRRKYAMISSPFMVVYANLLLVLQYIWSFELPEIKKVPGFLEKKEPGELASKILFTITFWLLLRQHLTEQKALREKEALLSEVKIGSQELEEKEDEELQDVQVEGEPTEKEEEEEEEIKEERHEVKKEEEEEVEEDDDQDIMKVLGNLVVALFIKYWIYVCGGMFFFVSFEGKIVMYKIIYMVLFLFCVALYQVHYEWWRKILKYFWMSVVIYTMLVLIFIYTYQFENFPGLWQNMTGLKKEKLEDLGLKQFTVAELFTRIFIPTSFLLVCILHLHYFHDRFLELTDLKSIPSKEDNTIYSHAKVNGRVYLIINRLAHPEGSLPDLAIMNMTASLDKPEVQKLAESGEERPEECVKKTEKGEAGKDSDESEEEEDEEEESEEEESSDLRNKWHLVIDRLTVLFLKFLEYFHKLQVFMWWILELHIIKIVSSYIIWVTVKEVSLFNYVFLISWAFALPYAKLRRAASSVCTVWTCVIIVCKMLYQLQTIKPENFSVNCSLPNENQTNIPLHELNKSLLYSAPVDPTEWVGLRKSSPLLVYLRNNLLMLAILAFEVTVYRHQEYYRGRNNLTAPVSKTIFHDITRLHLDDGLINCAKYFVNYFFYKFGLETCFLMSVNVIGQRMDFYAMIHACWLIGVLYRRRRKAIAEVWPKYCCFLACIITFQYFVCIGIPPAPCRDYPWRFKGAYFNDNIIKWLYFPDFIVRPNPVFLVYDFMLLLCASLQRQIFEDENKAAVRIMAGDNVEICMNLDAASFSQHNPVPDFIHCRSYLDMSKVIIFSYLFWFVLTIIFITGTTRISIFCMGYLVACFYFLLFGGDLLLKPIKSILRYWDWLIAYNVFVITMKNILSIGACGYIGALVRNSCWLIQAFSLACTVKGYQMPEDDSRCKLPSGEAGIIWDSICFAFLLLQRRVFMSYYFLHVVADIKASQILASRGAELFQATIVKAVKARIEEEKKSMDQLKRQMDRIKARQQKYKKGKERMLSLTQESGEGQDIQKVSEEDDEREADKQKAKGKKKQWWRPWVDHASMVRSGDYYLFETDSEEEEEEELKKEDEEPPRKSAFQFVYQAWITDPKTALRQRRKEKKKLAREEQKERRKGSGDGPVEWEDREDEPVKKKSDGPDNIIKRIFNILKFTWVLFLATVDSFTTWLNSISREHIDISTVLRIERCMLTREIKKGNVPTRESIHMYYQNHIMNLSRESGLDTIDEHSGAGSRAQAAHRMDSLDSRDSISSCYTEATLLISRQSTLDDLDGQDPVPKTSERARPRLRKMFSLDMSSSSADSGSVASSEPTQCTMLYSRQGTTETIEEVEAEAEEEVVEGLEPELHDAEEKEYAAEYEAGVEEISLTPDEELPQFSTDDCEAPPSYSKAVSFEHLSFASQDDSGAKNHMVVSPDDSRTDKLESSILPPLTHELTASDLLMSKMFHDDELEESEKFYVDQPRFLLLFYAMYNTLVARSEMVCYFVIILNHMTSASIITLLLPILIFLWAMLSVPRPSRRFWMMAIVYTEVAIVVKYFFQFGFFPWNKDLEIYKERPYFPPNIIGVEKKEGYVLYDLIQLLALFFHRSILKCHGLWDEDDIVDSNTDKEGSDDELSLDQGRRGSSDSLKSINLAASVESVHVTFPEQPAAIRRKRSCSSSQISPRSSFSSNRSKRGSTSTRNSSQKGSSVLSLKQKSKRELYMEKLQEHLIKAKAFTIKKTLQIYVPIRQFFYDLIHPDYSAVTDVYVLMFLADTVDFIIIVFGFWAFGKHSAAADITSSLSEDQVPGPFLVMVLIQFGTMVVDRALYLRKTVLGKVIFQVILVFGIHFWMFFILPGVTERKFSQNLVAQLWYFVKCVYFGLSAYQIRCGYPTRVLGNFLTKSYNYVNLFLFQGFRLVPFLTELRAVMDWVWTDTTLSLSSWICVEDIYAHIFILKCWRESEKRYPQPRGQKKKKAVKYGMGGMIIVLLICIVWFPLLFMSLIKSVAGVINQPLDVSVTITLGGYQPIFTMSAQQSQLKVMDNSKYNEFLKSFGPNSGAMQFLENYEREDVTVAELEGNSNSLWTISPPSKQKMIQELTDPNSCFSVVFSWSIQRNMTLGAKAEIATDKLSFPLAVATRNSIAKMIAGNDTESSNTPVTIEKIYPYYVKAPSDSNSKPIKQLLSENNFMNITIILFRDNVTKSNSEWWVLNLTGSRIFNQGSQALELVVFNDKVSPPSLGFLAGYGIMGLYASVVLVIGKFVREFFSGISHSIMFEELPNVDRILKLCTDIFLVRETGELELEEDLYAKLIFLYRSPETMIKWTREKTN | ||||||
Glycosylation | 95 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 856 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 1030 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1031↔1209 | |||||
Sequence: CSLPNENQTNIPLHELNKSLLYSAPVDPTEWVGLRKSSPLLVYLRNNLLMLAILAFEVTVYRHQEYYRGRNNLTAPVSKTIFHDITRLHLDDGLINCAKYFVNYFFYKFGLETCFLMSVNVIGQRMDFYAMIHACWLIGVLYRRRRKAIAEVWPKYCCFLACIITFQYFVCIGIPPAPC | ||||||
Glycosylation | 1102 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2692 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
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).
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 450-481 | Disordered | ||||
Sequence: YRWEPSEESSEKKEEEEDKREDSEGEGSQEEK | ||||||
Compositional bias | 454-481 | Basic and acidic residues | ||||
Sequence: PSEESSEKKEEEEDKREDSEGEGSQEEK | ||||||
Coiled coil | 455-482 | |||||
Sequence: SEESSEKKEEEEDKREDSEGEGSQEEKR | ||||||
Region | 624-668 | Disordered | ||||
Sequence: LEEKEDEELQDVQVEGEPTEKEEEEEEEIKEERHEVKKEEEEEVE | ||||||
Compositional bias | 626-652 | Acidic residues | ||||
Sequence: EKEDEELQDVQVEGEPTEKEEEEEEEI | ||||||
Compositional bias | 875-899 | Basic and acidic residues | ||||
Sequence: QKLAESGEERPEECVKKTEKGEAGK | ||||||
Region | 875-919 | Disordered | ||||
Sequence: QKLAESGEERPEECVKKTEKGEAGKDSDESEEEEDEEEESEEEES | ||||||
Compositional bias | 900-918 | Acidic residues | ||||
Sequence: DSDESEEEEDEEEESEEEE | ||||||
Coiled coil | 1475-1515 | |||||
Sequence: TIVKAVKARIEEEKKSMDQLKRQMDRIKARQQKYKKGKERM | ||||||
Region | 1505-1551 | Disordered | ||||
Sequence: QQKYKKGKERMLSLTQESGEGQDIQKVSEEDDEREADKQKAKGKKKQ | ||||||
Compositional bias | 1527-1551 | Basic and acidic residues | ||||
Sequence: DIQKVSEEDDEREADKQKAKGKKKQ | ||||||
Region | 1611-1653 | Disordered | ||||
Sequence: LRQRRKEKKKLAREEQKERRKGSGDGPVEWEDREDEPVKKKSD | ||||||
Compositional bias | 1618-1653 | Basic and acidic residues | ||||
Sequence: KKKLAREEQKERRKGSGDGPVEWEDREDEPVKKKSD | ||||||
Region | 2120-2139 | Disordered | ||||
Sequence: DKEGSDDELSLDQGRRGSSD | ||||||
Region | 2164-2205 | Disordered | ||||
Sequence: IRRKRSCSSSQISPRSSFSSNRSKRGSTSTRNSSQKGSSVLS | ||||||
Compositional bias | 2166-2205 | Polar residues | ||||
Sequence: RKRSCSSSQISPRSSFSSNRSKRGSTSTRNSSQKGSSVLS |
Sequence similarities
Belongs to the PIEZO (TC 1.A.75) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length2,822
- Mass (Da)325,628
- Last updated2011-01-11 v2
- ChecksumD786FBB41F48BA79
Q8CD54-2
- Name2
- NoteDue to intron retention.
- Differences from canonical
- 2457-2504: RYPQPRGQKKKKAVKYGMGGMIIVLLICIVWFPLLFMSLIKSVAGVIN → VKSRWKCLCHACRPRAQVCYKINMDTAWLVARWMEAGDTTCREPEIQH
- 2505-2822: Missing
Q8CD54-3
- Name3
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5S8DII4 | A0A5S8DII4_MOUSE | Piezo2 | 375 | ||
A0A494B9E4 | A0A494B9E4_MOUSE | Piezo2 | 378 | ||
A0A494B9D1 | A0A494B9D1_MOUSE | Piezo2 | 2690 | ||
F6YYK4 | F6YYK4_MOUSE | Piezo2 | 409 | ||
A0A494B9V6 | A0A494B9V6_MOUSE | Piezo2 | 2778 | ||
S4R2S0 | S4R2S0_MOUSE | Piezo2 | 2753 | ||
A0A494BB29 | A0A494BB29_MOUSE | Piezo2 | 230 | ||
E9QNW4 | E9QNW4_MOUSE | Piezo2 | 2824 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 454-481 | Basic and acidic residues | ||||
Sequence: PSEESSEKKEEEEDKREDSEGEGSQEEK | ||||||
Compositional bias | 626-652 | Acidic residues | ||||
Sequence: EKEDEELQDVQVEGEPTEKEEEEEEEI | ||||||
Alternative sequence | VSP_040631 | 629-644 | in isoform 3 | |||
Sequence: DEELQDVQVEGEPTEK → MLFPMKDNTKCQRNFL | ||||||
Alternative sequence | VSP_040632 | 645-2822 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 875-899 | Basic and acidic residues | ||||
Sequence: QKLAESGEERPEECVKKTEKGEAGK | ||||||
Compositional bias | 900-918 | Acidic residues | ||||
Sequence: DSDESEEEEDEEEESEEEE | ||||||
Compositional bias | 1527-1551 | Basic and acidic residues | ||||
Sequence: DIQKVSEEDDEREADKQKAKGKKKQ | ||||||
Compositional bias | 1618-1653 | Basic and acidic residues | ||||
Sequence: KKKLAREEQKERRKGSGDGPVEWEDREDEPVKKKSD | ||||||
Compositional bias | 2166-2205 | Polar residues | ||||
Sequence: RKRSCSSSQISPRSSFSSNRSKRGSTSTRNSSQKGSSVLS | ||||||
Alternative sequence | VSP_040473 | 2457-2504 | in isoform 2 | |||
Sequence: RYPQPRGQKKKKAVKYGMGGMIIVLLICIVWFPLLFMSLIKSVAGVIN → VKSRWKCLCHACRPRAQVCYKINMDTAWLVARWMEAGDTTCREPEIQH | ||||||
Alternative sequence | VSP_040474 | 2505-2822 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 2810 | in Ref. 2; BAC27396 | ||||
Sequence: P → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |