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Protein

Piezo-type mechanosensitive ion channel component 1

Gene

Piezo1

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

Functioni

Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology.5 Publications

Miscellaneous

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

GO - Molecular functioni

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

GO - Biological processi

  • cation transport Source: UniProtKB
  • cellular response to mechanical stimulus Source: GO_Central
  • detection of mechanical stimulus Source: MGI
  • positive regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
  • positive regulation of integrin activation Source: UniProtKB
  • regulation of membrane potential Source: MGI

Keywordsi

Molecular functionIon channel
Biological processIon transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Piezo-type mechanosensitive ion channel component 1
Alternative name(s):
Protein FAM38A
Gene namesi
Name:Piezo1
Synonyms:Fam38a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:3603204. Piezo1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei5 – 25HelicalSequence analysisAdd BLAST21
Transmembranei27 – 47HelicalSequence analysisAdd BLAST21
Transmembranei62 – 82HelicalSequence analysisAdd BLAST21
Transmembranei120 – 140HelicalSequence analysisAdd BLAST21
Transmembranei217 – 237HelicalSequence analysisAdd BLAST21
Transmembranei250 – 270HelicalSequence analysisAdd BLAST21
Transmembranei317 – 337HelicalSequence analysisAdd BLAST21
Transmembranei435 – 455HelicalSequence analysisAdd BLAST21
Transmembranei467 – 487HelicalSequence analysisAdd BLAST21
Transmembranei520 – 540HelicalSequence analysisAdd BLAST21
Transmembranei577 – 597HelicalSequence analysisAdd BLAST21
Transmembranei608 – 628HelicalSequence analysisAdd BLAST21
Transmembranei635 – 655HelicalSequence analysisAdd BLAST21
Transmembranei687 – 707HelicalSequence analysisAdd BLAST21
Transmembranei818 – 838HelicalSequence analysisAdd BLAST21
Transmembranei847 – 867HelicalSequence analysisAdd BLAST21
Transmembranei921 – 941HelicalSequence analysisAdd BLAST21
Transmembranei982 – 1002HelicalSequence analysisAdd BLAST21
Transmembranei1006 – 1023HelicalSequence analysisAdd BLAST18
Transmembranei1038 – 1058HelicalSequence analysisAdd BLAST21
Transmembranei1155 – 1175HelicalSequence analysisAdd BLAST21
Transmembranei1179 – 1199HelicalSequence analysisAdd BLAST21
Transmembranei1207 – 1227HelicalSequence analysisAdd BLAST21
Transmembranei1232 – 1252HelicalSequence analysisAdd BLAST21
Transmembranei1272 – 1292HelicalSequence analysisAdd BLAST21
Transmembranei1678 – 1698HelicalSequence analysisAdd BLAST21
Transmembranei1700 – 1720HelicalSequence analysisAdd BLAST21
Transmembranei1734 – 1754HelicalSequence analysisAdd BLAST21
Transmembranei1978 – 1998HelicalSequence analysisAdd BLAST21
Transmembranei2019 – 2039HelicalSequence analysisAdd BLAST21
Transmembranei2048 – 2068HelicalSequence analysisAdd BLAST21
Transmembranei2077 – 2097HelicalSequence analysisAdd BLAST21
Transmembranei2145 – 2165HelicalSequence analysisAdd BLAST21
Transmembranei2193 – 2213HelicalSequence analysisAdd BLAST21
Topological domaini2214 – 2457Extracellular1 PublicationAdd BLAST244
Transmembranei2458 – 2478HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Cell projection, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryo lethality at midgestation with defects in vascular remodeling.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004039591 – 2547Piezo-type mechanosensitive ion channel component 1Add BLAST2547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi389N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei758PhosphoserineBy similarity1
Modified residuei1385PhosphoserineCombined sources1
Modified residuei1390PhosphoserineBy similarity1
Modified residuei1627PhosphoserineCombined sources1
Modified residuei1631PhosphoserineCombined sources1
Modified residuei1646PhosphoserineCombined sources1
Disulfide bondi2437 ↔ 24411 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiE2JF22.
MaxQBiE2JF22.
PaxDbiE2JF22.
PeptideAtlasiE2JF22.
PRIDEiE2JF22.

PTM databases

iPTMnetiE2JF22.
PhosphoSitePlusiE2JF22.

Expressioni

Tissue specificityi

Expressed in bladder, colon, kidney and skin. Also expressed in bone marrow, liver, lung, spleen and erythrocytes (at protein level).3 Publications

Developmental stagei

Expressed at least from 9.5 dpc. Expression levels increase up to 15.5 dpc and remain high at least until birth.1 Publication

Interactioni

Subunit structurei

Homotrimer (PubMed:26390154). Interacts with PKD2 (PubMed:24157948). Interacts with STOML3 (PubMed:24662763).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Pkd2O352453EBI-9837938,EBI-9823400

Protein-protein interaction databases

DIPiDIP-59655N.
IntActiE2JF22. 1 interactor.
STRINGi10090.ENSMUSP00000089777.

Structurei

Secondary structure

12547
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2224 – 2232Combined sources9
Beta strandi2238 – 2243Combined sources6
Beta strandi2247 – 2250Combined sources4
Helixi2253 – 2263Combined sources11
Helixi2267 – 2273Combined sources7
Helixi2278 – 2280Combined sources3
Beta strandi2281 – 2289Combined sources9
Helixi2298 – 2310Combined sources13
Beta strandi2315 – 2324Combined sources10
Helixi2327 – 2329Combined sources3
Beta strandi2334 – 2344Combined sources11
Helixi2349 – 2357Combined sources9
Beta strandi2366 – 2372Combined sources7
Beta strandi2375 – 2378Combined sources4
Beta strandi2380 – 2383Combined sources4
Turni2388 – 2390Combined sources3
Helixi2394 – 2397Combined sources4
Beta strandi2398 – 2409Combined sources12
Beta strandi2426 – 2434Combined sources9
Beta strandi2443 – 2450Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JACelectron microscopy4.80A/B/C1-2547[»]
4RAXX-ray1.45A2214-2457[»]
ProteinModelPortaliE2JF22.
SMRiE2JF22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1334 – 1365Sequence analysisAdd BLAST32

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi6 – 142Leu-richAdd BLAST137
Compositional biasi157 – 170Asp-richAdd BLAST14

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1893. Eukaryota.
ENOG410YVF6. LUCA.
InParanoidiE2JF22.

Family and domain databases

InterProiView protein in InterPro
IPR027272. Piezo.
IPR031805. Piezo_dom.
IPR031334. Piezo_RRas-bd_dom.
PANTHERiPTHR13167. PTHR13167. 1 hit.
PfamiView protein in Pfam
PF15917. PIEZO. 1 hit.
PF12166. Piezo_RRas_bdg. 1 hit.

Sequencei

Sequence statusi: Complete.

E2JF22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPHVLGAGL YWLLLPCTLL AASLLRFNAL SLVYLLFLLL LPWLPGPSRH
60 70 80 90 100
SIPGHTGRLL RALLCLSLLF LVAHLAFQIC LHTVPHLDQF LGQNGSLWVK
110 120 130 140 150
VSQHIGVTRL DLKDIFNTTR LVAPDLGVLL ASSLCLGLCG RLTRKAGQSR
160 170 180 190 200
RTQELQDDDD DDDDDDEDID AAPAVGLKGA PALATKRRLW LASRFRVTAH
210 220 230 240 250
WLLMTSGRTL VIVLLALAGI AHPSAFSSIY LVVFLAICTW WSCHFPLSPL
260 270 280 290 300
GFNTLCVMVS CFGAGHLICL YCYQTPFIQD MLPPGNIWAR LFGLKNFVDL
310 320 330 340 350
PNYSSPNALV LNTKHAWPIY VSPGILLLLY YTATSLLKLH KSCPSELRKE
360 370 380 390 400
TPREDEEHEL ELDHLEPEPQ ARDATQGEMP MTTEPDLDNC TVHVLTSQSP
410 420 430 440 450
VRQRPVRPRL AELKEMSPLH GLGHLIMDQS YVCALIAMMV WSIMYHSWLT
460 470 480 490 500
FVLLLWACLI WTVRSRHQLA MLCSPCILLY GLTLCCLRYV WAMELPELPT
510 520 530 540 550
TLGPVSLHQL GLEHTRYPCL DLGAMLLYLL TFWLLLRQFV KEKLLKKQKV
560 570 580 590 600
PAALLEVTVA DTEPTQTQTL LRSLGELVTG IYVKYWIYVC AGMFIVVSFA
610 620 630 640 650
GRLVVYKIVY MFLFLLCLTL FQVYYTLWRK LLRVFWWLVV AYTMLVLIAV
660 670 680 690 700
YTFQFQDFPT YWRNLTGFTD EQLGDLGLEQ FSVSELFSSI LIPGFFLLAC
710 720 730 740 750
ILQLHYFHRP FMQLTDLEHV PPPGTRHPRW AHRQDAVSEA PLLEHQEEEE
760 770 780 790 800
VFREDGQSMD GPHQATQVPE GTASKWGLVA DRLLDLAASF SAVLTRIQVF
810 820 830 840 850
VRRLLELHVF KLVALYTVWV ALKEVSVMNL LLVVLWAFAL PYPRFRPMAS
860 870 880 890 900
CLSTVWTCII IVCKMLYQLK IVNPHEYSSN CTEPFPNNTN LQPLEINQSL
910 920 930 940 950
LYRGPVDPAN WFGVRKGYPN LGYIQNHLQI LLLLVFEAVV YRRQEHYRRQ
960 970 980 990 1000
HQQAPLPAQA VCADGTRQRL DQDLLSCLKY FINFFFYKFG LEICFLMAVN
1010 1020 1030 1040 1050
VIGQRMNFMV ILHGCWLVAI LTRRRREAIA RLWPNYCLFL TLFLLYQYLL
1060 1070 1080 1090 1100
CLGMPPALCI DYPWRWSKAI PMNSALIKWL YLPDFFRAPN STNLISDFLL
1110 1120 1130 1140 1150
LLCASQQWQV FSAERTEEWQ RMAGINTDHL EPLRGEPNPI PNFIHCRSYL
1160 1170 1180 1190 1200
DMLKVAVFRY LFWLVLVVVF VAGATRISIF GLGYLLACFY LLLFGTTLLQ
1210 1220 1230 1240 1250
KDTRAQLVLW DCLILYNVTV IISKNMLSLL SCVFVEQMQS NFCWVIQLFS
1260 1270 1280 1290 1300
LVCTVKGYYD PKEMMTRDRD CLLPVEEAGI IWDSICFFFL LLQRRIFLSH
1310 1320 1330 1340 1350
YFLHVSADLK ATALQASRGF ALYNAANLKS INFHRQIEEK SLAQLKRQMK
1360 1370 1380 1390 1400
RIRAKQEKYR QSQASRGQLQ SKDPQDPSQE PGPDSPGGSS PPRRQWWRPW
1410 1420 1430 1440 1450
LDHATVIHSG DYFLFESDSE EEEEALPEDP RPAAQSAFQM AYQAWVTNAQ
1460 1470 1480 1490 1500
TVLRQRRERA RQERAEQLAS GGDLNPDVEP VDVPEDEMAG RSHMMQRVLS
1510 1520 1530 1540 1550
TMQFLWVLGQ ATVDGLTRWL RAFTKHHRTM SDVLCAERYL LTQELLRVGE
1560 1570 1580 1590 1600
VRRGVLDQLY VGEDEATLSG PVETRDGPST ASSGLGAEEP LSSMTDDTSS
1610 1620 1630 1640 1650
PLSTGYNTRS GSEEIVTDAG DLQAGTSLHG SQELLANART RMRTASELLL
1660 1670 1680 1690 1700
DRRLHIPELE EAERFEAQQG RTLRLLRAGY QCVAAHSELL CYFIIILNHM
1710 1720 1730 1740 1750
VTASAASLVL PVLVFLWAML TIPRPSKRFW MTAIVFTEVM VVTKYLFQFG
1760 1770 1780 1790 1800
FFPWNSYVVL RRYENKPYFP PRILGLEKTD SYIKYDLVQL MALFFHRSQL
1810 1820 1830 1840 1850
LCYGLWDHEE DRYPKDHCRS SVKDREAKEE PEAKLESQSE TGTGHPKEPV
1860 1870 1880 1890 1900
LAGTPRDHIQ GKGSIRSKDV IQDPPEDLKP RHTRHISIRF RRRKETPGPK
1910 1920 1930 1940 1950
GTAVMETEHE EGEGKETTER KRPRHTQEKS KFRERMKAAG RRLQSFCVSL
1960 1970 1980 1990 2000
AQSFYQPLQR FFHDILHTKY RAATDVYALM FLADIVDIII IIFGFWAFGK
2010 2020 2030 2040 2050
HSAATDIASS LSDDQVPQAF LFMLLVQFGT MVIDRALYLR KTVLGKLAFQ
2060 2070 2080 2090 2100
VVLVVAIHIW MFFILPAVTE RMFSQNAVAQ LWYFVKCIYF ALSAYQIRCG
2110 2120 2130 2140 2150
YPTRILGNFL TKKYNHLNLF LFQGFRLVPF LVELRAVMDW VWTDTTLSLS
2160 2170 2180 2190 2200
NWMCVEDIYA NIFIIKCSRE TEKKYPQPKG QKKKKIVKYG MGGLIILFLI
2210 2220 2230 2240 2250
AIIWFPLLFM SLIRSVVGVV NQPIDVTVTL KLGGYEPLFT MSAQQPSIVP
2260 2270 2280 2290 2300
FTPQAYEELS QQFDPYPLAM QFISQYSPED IVTAQIEGSS GALWRISPPS
2310 2320 2330 2340 2350
RAQMKQELYN GTADITLRFT WNFQRDLAKG GTVEYTNEKH TLELAPNSTA
2360 2370 2380 2390 2400
RRQLAQLLEG RPDQSVVIPH LFPKYIRAPN GPEANPVKQL QPDEEEDYLG
2410 2420 2430 2440 2450
VRIQLRREQV GTGASGEQAG TKASDFLEWW VIELQDCKAD CNLLPMVIFS
2460 2470 2480 2490 2500
DKVSPPSLGF LAGYGIVGLY VSIVLVVGKF VRGFFSEISH SIMFEELPCV
2510 2520 2530 2540
DRILKLCQDI FLVRETRELE LEEELYAKLI FLYRSPETMI KWTRERE
Length:2,547
Mass (Da):292,002
Last modified:November 30, 2010 - v1
Checksum:i0C24CF18BDF502E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ215520 mRNA. Translation: ADN28064.1.
UniGeneiMm.37324.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ215520 mRNA. Translation: ADN28064.1.
UniGeneiMm.37324.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JACelectron microscopy4.80A/B/C1-2547[»]
4RAXX-ray1.45A2214-2457[»]
ProteinModelPortaliE2JF22.
SMRiE2JF22.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59655N.
IntActiE2JF22. 1 interactor.
STRINGi10090.ENSMUSP00000089777.

PTM databases

iPTMnetiE2JF22.
PhosphoSitePlusiE2JF22.

Proteomic databases

EPDiE2JF22.
MaxQBiE2JF22.
PaxDbiE2JF22.
PeptideAtlasiE2JF22.
PRIDEiE2JF22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:3603204. Piezo1.

Phylogenomic databases

eggNOGiKOG1893. Eukaryota.
ENOG410YVF6. LUCA.
InParanoidiE2JF22.

Miscellaneous databases

PROiPR:E2JF22.
SOURCEiSearch...

Family and domain databases

InterProiView protein in InterPro
IPR027272. Piezo.
IPR031805. Piezo_dom.
IPR031334. Piezo_RRas-bd_dom.
PANTHERiPTHR13167. PTHR13167. 1 hit.
PfamiView protein in Pfam
PF15917. PIEZO. 1 hit.
PF12166. Piezo_RRas_bdg. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPIEZ1_MOUSE
AccessioniPrimary (citable) accession number: E2JF22
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: November 30, 2010
Last modified: May 10, 2017
This is version 43 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.