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Protein

Piezo-type mechanosensitive ion channel component 2

Gene

Piezo2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of a mechanosensitive channel required for rapidly adapting mechanically activated (MA) currents (PubMed:20813920, PubMed:24717433). Required for Merkel-cell mechanotransduction (PubMed:24717433). Plays a major role in light-touch mechanosensation (PubMed:25471886).3 Publications

GO - Molecular functioni

  • cation channel activity Source: MGI
  • mechanically-gated ion channel activity Source: MGI

GO - Biological processi

  • cation transmembrane transport Source: GOC
  • cation transport Source: UniProtKB
  • detection of mechanical stimulus involved in sensory perception Source: UniProtKB
  • ion transmembrane transport Source: GOC
  • regulation of membrane potential Source: MGI
  • response to mechanical stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Sensory transduction, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Piezo-type mechanosensitive ion channel component 2
Alternative name(s):
Protein FAM38B
Gene namesi
Name:Piezo2
Synonyms:Fam38b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1918781. Piezo2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2521HelicalSequence analysisAdd
BLAST
Transmembranei27 – 4721HelicalSequence analysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence analysisAdd
BLAST
Transmembranei119 – 13921HelicalSequence analysisAdd
BLAST
Transmembranei214 – 23421HelicalSequence analysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence analysisAdd
BLAST
Transmembranei266 – 28621HelicalSequence analysisAdd
BLAST
Transmembranei336 – 35621HelicalSequence analysisAdd
BLAST
Transmembranei505 – 52521HelicalSequence analysisAdd
BLAST
Transmembranei541 – 56121HelicalSequence analysisAdd
BLAST
Transmembranei581 – 59818HelicalSequence analysisAdd
BLAST
Transmembranei682 – 70221HelicalSequence analysisAdd
BLAST
Transmembranei708 – 72821HelicalSequence analysisAdd
BLAST
Transmembranei736 – 75621HelicalSequence analysisAdd
BLAST
Transmembranei786 – 80621HelicalSequence analysisAdd
BLAST
Transmembranei949 – 96921HelicalSequence analysisAdd
BLAST
Transmembranei975 – 99521HelicalSequence analysisAdd
BLAST
Transmembranei1002 – 102221HelicalSequence analysisAdd
BLAST
Transmembranei1070 – 109021HelicalSequence analysisAdd
BLAST
Transmembranei1151 – 117121HelicalSequence analysisAdd
BLAST
Transmembranei1187 – 120721HelicalSequence analysisAdd
BLAST
Transmembranei1234 – 125421HelicalSequence analysisAdd
BLAST
Transmembranei1308 – 132821HelicalSequence analysisAdd
BLAST
Transmembranei1332 – 135221HelicalSequence analysisAdd
BLAST
Transmembranei1371 – 139121HelicalSequence analysisAdd
BLAST
Transmembranei1422 – 144221HelicalSequence analysisAdd
BLAST
Transmembranei1979 – 200123HelicalSequence analysisAdd
BLAST
Transmembranei2008 – 202821HelicalSequence analysisAdd
BLAST
Transmembranei2037 – 205721HelicalSequence analysisAdd
BLAST
Transmembranei2261 – 228121HelicalSequence analysisAdd
BLAST
Transmembranei2302 – 232221HelicalSequence analysisAdd
BLAST
Transmembranei2330 – 235021HelicalSequence analysisAdd
BLAST
Transmembranei2360 – 238021HelicalSequence analysisAdd
BLAST
Transmembranei2397 – 241418HelicalSequence analysisAdd
BLAST
Transmembranei2428 – 244821HelicalSequence analysisAdd
BLAST
Transmembranei2476 – 249621HelicalSequence analysisAdd
BLAST
Transmembranei2732 – 275221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Perinatal lethality. Conditional knockout in sensory neurons and Merkel cells causes severe defects in light-touch sensation, although detection of pain (nociception) is unaffected.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 28222822Piezo-type mechanosensitive ion channel component 2PRO_0000186819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence analysis
Modified residuei856 – 8561PhosphoserineCombined sources
Glycosylationi1030 – 10301N-linked (GlcNAc...)Sequence analysis
Glycosylationi1102 – 11021N-linked (GlcNAc...)Sequence analysis
Glycosylationi2692 – 26921N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ8CD54.
PRIDEiQ8CD54.

PTM databases

PhosphoSiteiQ8CD54.

Expressioni

Tissue specificityi

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). Expressed in a wide range of cutaneous low-threshold mechanoreceptors (LTMRs), including Merkel cells and Meissner's corpuscles (PubMed:24717433, PubMed:25471886).3 Publications

Gene expression databases

BgeeiQ8CD54.
ExpressionAtlasiQ8CD54. baseline and differential.
GenevisibleiQ8CD54. MM.

Interactioni

Subunit structurei

Homooligomer, most likely homotetramer. Interacts with STOML3.2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040019.

Structurei

3D structure databases

ProteinModelPortaliQ8CD54.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili455 – 48228Sequence analysisAdd
BLAST
Coiled coili1475 – 151541Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi609 – 66961Glu-richAdd
BLAST
Compositional biasi879 – 91840Glu-richAdd
BLAST
Compositional biasi1839 – 188648Glu-richAdd
BLAST
Compositional biasi2169 – 220537Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1893. Eukaryota.
ENOG410YVF6. LUCA.
GeneTreeiENSGT00390000013029.
HOVERGENiHBG060934.
InParanoidiQ8CD54.
PhylomeDBiQ8CD54.

Family and domain databases

InterProiIPR027272. Piezo.
IPR031805. Piezo_dom.
IPR031334. Piezo_RRas-bd_dom.
[Graphical view]
PANTHERiPTHR13167. PTHR13167. 3 hits.
PfamiPF15917. PIEZO. 1 hit.
PF12166. Piezo_RRas_bdg. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CD54-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MASEVVCGLI FRLLLPICLA VACAFRYNGL SFVYLIYLLL IPLFSEPTKA
60 70 80 90 100
TMQGHTGRLL QSLCITSLSF LLLHIIFHIT LASLEAQHRI TPAYNCSTWE
110 120 130 140 150
KTFRQIGFES LKGADAGNGI RVFVPDIGMF IASLTIWLVC RTIVKKPDTE
160 170 180 190 200
EIAQLNSECE NEELAGGEKM DSEEALIYEE DLDGEEGMEG ELEESTKLKI
210 220 230 240 250
LRRFASVASK LKEFIGNMIT TAGKVVVTIL LGSSGMMLPS LTSAVYFFVF
260 270 280 290 300
LGLCTWWSWC RTFDPLLFGC LCVLLAIFTA GHLIGLYLYQ FQFFQEAVPP
310 320 330 340 350
NDYYARLFGI KSVIQTDCAS TWKIIVNPDL SWYHHANPIL LLVMYYTLAT
360 370 380 390 400
LIRIWLQEPL VQEEMAKEDE GALDCSSNQN TAERRRSLWY ATQYPTDERK
410 420 430 440 450
LLSMTQDDYK PSDGLLVTVN GNPVDYHTIH PSLPIENGPA KTDLYTTPQY
460 470 480 490 500
RWEPSEESSE KKEEEEDKRE DSEGEGSQEE KRSVRMHAMV AVFQFIMKQS
510 520 530 540 550
YICALIAMMA WSITYHSWLT FVLLIWSCTL WMIRNRRKYA MISSPFMVVY
560 570 580 590 600
ANLLLVLQYI WSFELPEIKK VPGFLEKKEP GELASKILFT ITFWLLLRQH
610 620 630 640 650
LTEQKALREK EALLSEVKIG SQELEEKEDE ELQDVQVEGE PTEKEEEEEE
660 670 680 690 700
EIKEERHEVK KEEEEEVEED DDQDIMKVLG NLVVALFIKY WIYVCGGMFF
710 720 730 740 750
FVSFEGKIVM YKIIYMVLFL FCVALYQVHY EWWRKILKYF WMSVVIYTML
760 770 780 790 800
VLIFIYTYQF ENFPGLWQNM TGLKKEKLED LGLKQFTVAE LFTRIFIPTS
810 820 830 840 850
FLLVCILHLH YFHDRFLELT DLKSIPSKED NTIYSHAKVN GRVYLIINRL
860 870 880 890 900
AHPEGSLPDL AIMNMTASLD KPEVQKLAES GEERPEECVK KTEKGEAGKD
910 920 930 940 950
SDESEEEEDE EEESEEEESS DLRNKWHLVI DRLTVLFLKF LEYFHKLQVF
960 970 980 990 1000
MWWILELHII KIVSSYIIWV TVKEVSLFNY VFLISWAFAL PYAKLRRAAS
1010 1020 1030 1040 1050
SVCTVWTCVI IVCKMLYQLQ TIKPENFSVN CSLPNENQTN IPLHELNKSL
1060 1070 1080 1090 1100
LYSAPVDPTE WVGLRKSSPL LVYLRNNLLM LAILAFEVTV YRHQEYYRGR
1110 1120 1130 1140 1150
NNLTAPVSKT IFHDITRLHL DDGLINCAKY FVNYFFYKFG LETCFLMSVN
1160 1170 1180 1190 1200
VIGQRMDFYA MIHACWLIGV LYRRRRKAIA EVWPKYCCFL ACIITFQYFV
1210 1220 1230 1240 1250
CIGIPPAPCR DYPWRFKGAY FNDNIIKWLY FPDFIVRPNP VFLVYDFMLL
1260 1270 1280 1290 1300
LCASLQRQIF EDENKAAVRI MAGDNVEICM NLDAASFSQH NPVPDFIHCR
1310 1320 1330 1340 1350
SYLDMSKVII FSYLFWFVLT IIFITGTTRI SIFCMGYLVA CFYFLLFGGD
1360 1370 1380 1390 1400
LLLKPIKSIL RYWDWLIAYN VFVITMKNIL SIGACGYIGA LVRNSCWLIQ
1410 1420 1430 1440 1450
AFSLACTVKG YQMPEDDSRC KLPSGEAGII WDSICFAFLL LQRRVFMSYY
1460 1470 1480 1490 1500
FLHVVADIKA SQILASRGAE LFQATIVKAV KARIEEEKKS MDQLKRQMDR
1510 1520 1530 1540 1550
IKARQQKYKK GKERMLSLTQ ESGEGQDIQK VSEEDDEREA DKQKAKGKKK
1560 1570 1580 1590 1600
QWWRPWVDHA SMVRSGDYYL FETDSEEEEE EELKKEDEEP PRKSAFQFVY
1610 1620 1630 1640 1650
QAWITDPKTA LRQRRKEKKK LAREEQKERR KGSGDGPVEW EDREDEPVKK
1660 1670 1680 1690 1700
KSDGPDNIIK RIFNILKFTW VLFLATVDSF TTWLNSISRE HIDISTVLRI
1710 1720 1730 1740 1750
ERCMLTREIK KGNVPTRESI HMYYQNHIMN LSRESGLDTI DEHSGAGSRA
1760 1770 1780 1790 1800
QAAHRMDSLD SRDSISSCYT EATLLISRQS TLDDLDGQDP VPKTSERARP
1810 1820 1830 1840 1850
RLRKMFSLDM SSSSADSGSV ASSEPTQCTM LYSRQGTTET IEEVEAEAEE
1860 1870 1880 1890 1900
EVVEGLEPEL HDAEEKEYAA EYEAGVEEIS LTPDEELPQF STDDCEAPPS
1910 1920 1930 1940 1950
YSKAVSFEHL SFASQDDSGA KNHMVVSPDD SRTDKLESSI LPPLTHELTA
1960 1970 1980 1990 2000
SDLLMSKMFH DDELEESEKF YVDQPRFLLL FYAMYNTLVA RSEMVCYFVI
2010 2020 2030 2040 2050
ILNHMTSASI ITLLLPILIF LWAMLSVPRP SRRFWMMAIV YTEVAIVVKY
2060 2070 2080 2090 2100
FFQFGFFPWN KDLEIYKERP YFPPNIIGVE KKEGYVLYDL IQLLALFFHR
2110 2120 2130 2140 2150
SILKCHGLWD EDDIVDSNTD KEGSDDELSL DQGRRGSSDS LKSINLAASV
2160 2170 2180 2190 2200
ESVHVTFPEQ PAAIRRKRSC SSSQISPRSS FSSNRSKRGS TSTRNSSQKG
2210 2220 2230 2240 2250
SSVLSLKQKS KRELYMEKLQ EHLIKAKAFT IKKTLQIYVP IRQFFYDLIH
2260 2270 2280 2290 2300
PDYSAVTDVY VLMFLADTVD FIIIVFGFWA FGKHSAAADI TSSLSEDQVP
2310 2320 2330 2340 2350
GPFLVMVLIQ FGTMVVDRAL YLRKTVLGKV IFQVILVFGI HFWMFFILPG
2360 2370 2380 2390 2400
VTERKFSQNL VAQLWYFVKC VYFGLSAYQI RCGYPTRVLG NFLTKSYNYV
2410 2420 2430 2440 2450
NLFLFQGFRL VPFLTELRAV MDWVWTDTTL SLSSWICVED IYAHIFILKC
2460 2470 2480 2490 2500
WRESEKRYPQ PRGQKKKKAV KYGMGGMIIV LLICIVWFPL LFMSLIKSVA
2510 2520 2530 2540 2550
GVINQPLDVS VTITLGGYQP IFTMSAQQSQ LKVMDNSKYN EFLKSFGPNS
2560 2570 2580 2590 2600
GAMQFLENYE REDVTVAELE GNSNSLWTIS PPSKQKMIQE LTDPNSCFSV
2610 2620 2630 2640 2650
VFSWSIQRNM TLGAKAEIAT DKLSFPLAVA TRNSIAKMIA GNDTESSNTP
2660 2670 2680 2690 2700
VTIEKIYPYY VKAPSDSNSK PIKQLLSENN FMNITIILFR DNVTKSNSEW
2710 2720 2730 2740 2750
WVLNLTGSRI FNQGSQALEL VVFNDKVSPP SLGFLAGYGI MGLYASVVLV
2760 2770 2780 2790 2800
IGKFVREFFS GISHSIMFEE LPNVDRILKL CTDIFLVRET GELELEEDLY
2810 2820
AKLIFLYRSP ETMIKWTREK TN
Length:2,822
Mass (Da):325,628
Last modified:January 11, 2011 - v2
Checksum:iD786FBB41F48BA79
GO
Isoform 2 (identifier: Q8CD54-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2457-2504: RYPQPRGQKK...LIKSVAGVIN → VKSRWKCLCH...TTCREPEIQH
     2505-2822: Missing.

Note: No experimental confirmation available.
Show »
Length:2,504
Mass (Da):290,127
Checksum:i8BC99089B37DAEE3
GO
Isoform 3 (identifier: Q8CD54-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-644: DEELQDVQVEGEPTEK → MLFPMKDNTKCQRNFL
     645-2822: Missing.

Note: No experimental confirmation available.
Show »
Length:644
Mass (Da):73,825
Checksum:iC7A22ACB01852F15
GO

Sequence cautioni

The sequence BAB31242.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC27312.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC27396.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2810 – 28101P → Q in BAC27396 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei629 – 64416DEELQ…EPTEK → MLFPMKDNTKCQRNFL in isoform 3. 1 PublicationVSP_040631Add
BLAST
Alternative sequencei645 – 28222178Missing in isoform 3. 1 PublicationVSP_040632Add
BLAST
Alternative sequencei2457 – 250448RYPQP…AGVIN → VKSRWKCLCHACRPRAQVCY KINMDTAWLVARWMEAGDTT CREPEIQH in isoform 2. 1 PublicationVSP_040473Add
BLAST
Alternative sequencei2505 – 2822318Missing in isoform 2. 1 PublicationVSP_040474Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ215521 mRNA. Translation: ADN28065.1.
AK018503 mRNA. Translation: BAB31242.1. Different initiation.
AK031235 mRNA. Translation: BAC27312.1. Different initiation.
AK031422 mRNA. Translation: BAC27396.1. Different initiation.
RefSeqiNP_001034574.4. NM_001039485.4.
UniGeneiMm.158720.

Genome annotation databases

EnsembliENSMUST00000046860; ENSMUSP00000036099; ENSMUSG00000041482. [Q8CD54-3]
GeneIDi667742.
KEGGimmu:667742.
UCSCiuc008fdw.1. mouse. [Q8CD54-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ215521 mRNA. Translation: ADN28065.1.
AK018503 mRNA. Translation: BAB31242.1. Different initiation.
AK031235 mRNA. Translation: BAC27312.1. Different initiation.
AK031422 mRNA. Translation: BAC27396.1. Different initiation.
RefSeqiNP_001034574.4. NM_001039485.4.
UniGeneiMm.158720.

3D structure databases

ProteinModelPortaliQ8CD54.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040019.

PTM databases

PhosphoSiteiQ8CD54.

Proteomic databases

PaxDbiQ8CD54.
PRIDEiQ8CD54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046860; ENSMUSP00000036099; ENSMUSG00000041482. [Q8CD54-3]
GeneIDi667742.
KEGGimmu:667742.
UCSCiuc008fdw.1. mouse. [Q8CD54-3]

Organism-specific databases

CTDi63895.
MGIiMGI:1918781. Piezo2.

Phylogenomic databases

eggNOGiKOG1893. Eukaryota.
ENOG410YVF6. LUCA.
GeneTreeiENSGT00390000013029.
HOVERGENiHBG060934.
InParanoidiQ8CD54.
PhylomeDBiQ8CD54.

Miscellaneous databases

NextBioi433239.
PROiQ8CD54.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CD54.
ExpressionAtlasiQ8CD54. baseline and differential.
GenevisibleiQ8CD54. MM.

Family and domain databases

InterProiIPR027272. Piezo.
IPR031805. Piezo_dom.
IPR031334. Piezo_RRas-bd_dom.
[Graphical view]
PANTHERiPTHR13167. PTHR13167. 3 hits.
PfamiPF15917. PIEZO. 1 hit.
PF12166. Piezo_RRas_bdg. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels."
    Coste B., Mathur J., Schmidt M., Earley T.J., Ranade S., Petrus M.J., Dubin A.E., Patapoutian A.
    Science 330:55-60(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-2822 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2049-2822 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2142-2822 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Colon, Forelimb and Testis.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.
  4. "Piezo proteins are pore-forming subunits of mechanically activated channels."
    Coste B., Xiao B., Santos J.S., Syeda R., Grandl J., Spencer K.S., Kim S.E., Schmidt M., Mathur J., Dubin A.E., Montal M., Patapoutian A.
    Nature 483:176-181(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMOOLIGOMERIZATION.
  5. "Tuning Piezo ion channels to detect molecular-scale movements relevant for fine touch."
    Poole K., Herget R., Lapatsina L., Ngo H.D., Lewin G.R.
    Nat. Commun. 5:3520-3520(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STOML3.
  6. Cited for: TISSUE SPECIFICITY, FUNCTION.
  7. Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPIEZ2_MOUSE
AccessioniPrimary (citable) accession number: Q8CD54
Secondary accession number(s): E2JF23, Q8BSM4, Q9D341
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 11, 2011
Last modified: November 11, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Piezo comes from the Greek 'piesi' meaning pressure.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.