Tmem63b
entrez
224807
canonical
uniprot
Q3TWI9
canonical
ensembl
ENSMUSG00000036026
resolver
ensp
ENSMUSP00000109151
resolver
ensp
ENSMUSP00000210366
resolver
ensp
ENSMUSP00000210383
resolver
ensp
ENSMUSP00000210386
resolver
ensp
ENSMUSP00000336715
resolver
genesymbol
Tmem63b
resolver
uniprot
Q6PCL2
resolver
uniprot
Q6PGA4
resolver
uniprot
Q8C1V5
resolver
uniprot
Q8R0W7
resolver
uniprot_entry
TM63B_MOUSE
resolver
uniprot_sec
Q6PCL2
resolver
uniprot_sec
Q6PGA4
resolver
uniprot_sec
Q8C1V5
resolver
uniprot_sec
Q8R0W7
resolver
amino_acid_sequence
MLPFLLATLGTAALNSSNPKDYCYSARIRSTVLQGLPFGGVPTVLALDFMCFLALLFLFSILRKVAWDYGRLALVTDADRLRRQERERVEQEYVASAMHGDSHDRYERLTSVSSSVDFDQRDNGFCSWLTAIFRIKDDEIRDKCGGDAVHYLSFQRHIIGLLVVVGVLSVGIVLPVNFSGDLLENNAYSFGRTTIANLKSGNNLLWLHTSFAFLYLLLTVYSMRRHTSKMRYKEDDLVKRTLFINGISKYAESEKIKKHFEEAYPNCTVLEARPCYNVARLMFLDAERKKAERGKLYFTNLQSKENVPAMINPKPCGHLCCCVVRGCEQVEAIEYYTKLEQRLKEDYRREKEKVNEKPLGMAFVTFHNETITAIILKDFNVCKCQGCTCRGEPRASSCSEALHISNWTVTYAPDPQNIYWEHLSIRGFIWWLRCLVINVVLFILLFFLTTPAIIITTMDKFNVTKPVEYLNNPIITQFFPTLLLWCFSALLPTIVYYSAFFEAHWTRSGENRTTMHKCYTFLIFMVLLLPSLGLSSLDLFFRWLFDKKFLAEAAIRFECVFLPDNGAFFVNYVIASAFIGNAMDLLRIPGLLMYMIRLCLARSAAERRNVKRHQAYEFQFGAAYAWMMCVFTVVMTYSITCPIIVPFGLMYMLLKHLVDRYNLYYAYLPAKLDKKIHSGAVNQVVAAPILCLFWLLFFSTMRTGFLAPTSMFTFVVLVITIVICLCHVCFGHFKYLSAHNYKIEHTETDAVSSRSNGRPPTAGAVPKSAKYIAQVLQDSEGDGDGDGAPGSSGDEPPSSSSQDEELLMPPDGLTDTDFQSCEDSLIENEIHQ
uniprot
proteins
function
FUNCTION: Mechanosensitive cation channel with low conductance and high activation threshold (PubMed:27045885, PubMed:30382938, PubMed:31243992, PubMed:37543036, PubMed:37945568, PubMed:38127458). Osmosensitive cation channel preferentially activated by hypotonic stress (PubMed:27045885). Also acts as a phospholipid scramblase in response to changes in membrane structure: upon changes in membrane curvature and thickness, alters its conformation and translocates phospholipids, such as phosphatidylcholine and sphingomyelin, thereby controlling plasma membrane lipid distribution (PubMed:39217145, PubMed:39424995). Forms a heterodimer with SLC19A2, which mediates phospholipid scramblase activity following Ca(2+) stimulation (PubMed:39217145). Expressed in excitatory neurons of the subfornical organ and functions as a thirst receptor that mediates neuronal response to hyperosmolality to drive thirst and drinking behavior (PubMed:38172113, PubMed:40107268). Facilitates intestinal motility by promoting proliferation of intestinal stem cells (PubMed:39513891). Essential for the baby's first breath and respiration throughout life (PubMed:38127458). Upon lung inflation conducts cation currents in alveolar type 1 and 2 cells triggering lamellar body exocytosis and surfactant secretion into airspace (PubMed:38127458). Acts as an osmosensor in cochlear outer hair cells (OHCs) where it mediates calcium influx and regulatory volume decrease response (PubMed:32375046). Required for the maintenance of OHC morphology, OHC survival and normal hearing (PubMed:32375046). {ECO:0000269|PubMed:27045885, ECO:0000269|PubMed:30382938, ECO:0000269|PubMed:31243992, ECO:0000269|PubMed:32375046, ECO:0000269|PubMed:37543036, ECO:0000269|PubMed:37945568, ECO:0000269|PubMed:38127458, ECO:0000269|PubMed:38172113, ECO:0000269|PubMed:39217145, ECO:0000269|PubMed:39424995, ECO:0000269|PubMed:39513891, ECO:0000269|PubMed:40107268}.; FUNCTION: [Isoform 2]: Brain-specific osmosensitive calcium channel isoform. {ECO:0000269|PubMed:33100268}.
uniprot
proteins
mass_dalton
94775
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="V->K: Does not significantly affect calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 48; /note="D->A: Decreased phospholipid scramblase activity without affecting localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 79..83; /note="DRLRR->AAAA: Does not affect localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:36496074"; MUTAGEN 86..88; /note="RER->AAA: Increased localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:36496074"; MUTAGEN 126; /note="C->S: Decreased palmitoylation, abolished localization to the plasma membrane; when associated with S-144."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 144; /note="C->S: Decreased palmitoylation, abolished localization to the plasma membrane; when associated with S-144."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 316..327; /note="CGHLCCCVVRGC->SGHLSSSVVRGS: In deltaCys-hook1 mutant; decreased palmitoylation, abolished localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 382..398; /note="CKCQGCTCRGEPRASSC->SKSQGSTCRGEPRASSS: In deltaCys-hook2 mutant; decreased palmitoylation, abolished localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 477; /note="Q->K: Does not significantly affect calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 485; /note="W->A: Decreased phospholipid scramblase activity without affecting localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 568; /note="F->A: Increases calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 569; /note="F->A: Increases calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 571; /note="N->K: Increases calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 572; /note="Y->A: Decreases calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 574; /note="I->R: Increases calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 575; /note="A->K: Increases calcium influx induced by hypo-osmotic stress."; /evidence="ECO:0000269|PubMed:37945568"; MUTAGEN 584; /note="D->A: Decreased localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 587; /note="R->A: Decreased phospholipid scramblase activity without affecting localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 655; /note="K->A: Decreased localization to the plasma membrane; constitutive phospholipid scramblase activity."; /evidence="ECO:0000269|PubMed:39424995"; MUTAGEN 659; /note="D->A: Decreased localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:39424995
uniprot
proteins
post_translational_modification
PTM: Palmitoylation is required for localization to the plasma membrane and stability. {ECO:0000269|PubMed:39424995}.
uniprot
proteins
protein_family
CSC1 (TC 1.A.17) family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27045885
uniprot
proteins
pubmed
30382938
uniprot
proteins
pubmed
31243992
uniprot
proteins
pubmed
32375046
uniprot
proteins
pubmed
33100268
uniprot
proteins
pubmed
36496074
uniprot
proteins
pubmed
37402734
uniprot
proteins
pubmed
37543036
uniprot
proteins
pubmed
37945568
uniprot
proteins
pubmed
38127458
uniprot
proteins
pubmed
38172113
uniprot
proteins
pubmed
39217145
uniprot
proteins
pubmed
39424995
uniprot
proteins
pubmed
39513891
uniprot
proteins
pubmed
40107268
uniprot
proteins
sequence_length
832
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27045885, ECO:0000269|PubMed:31243992, ECO:0000269|PubMed:32375046, ECO:0000269|PubMed:36496074, ECO:0000269|PubMed:37543036, ECO:0000269|PubMed:39424995}; Multi-pass membrane protein {ECO:0000269|PubMed:39424995}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:36496074}; Multi-pass membrane protein {ECO:0000269|PubMed:39424995}. Lysosome membrane {ECO:0000269|PubMed:39424995}; Multi-pass membrane protein {ECO:0000269|PubMed:39424995}. Early endosome membrane {ECO:0000250|UniProtKB:Q5T3F8}; Multi-pass membrane protein {ECO:0000269|PubMed:39424995}. Note=Colocalizes with cortical F-actin (PubMed:31243992). Probably localizes at lamellar body membrane in alveolar type 2 cells (PubMed:38127458). {ECO:0000269|PubMed:31243992, ECO:0000269|PubMed:38127458}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:36496074}; Multi-pass membrane protein {ECO:0000255}. Note=Isoform 2 localizes exclusively to the plasma membrane. {ECO:0000269|PubMed:36496074}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..65; /note="Helical; Name=TM0"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 146..178; /note="Helical; Name=TM1"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 203..227; /note="Helical; Name=TM2"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 428..457; /note="Helical; Name=TM3"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 473..502; /note="Helical; Name=TM4"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 507..543; /note="Helical; Name=TM5"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 567..599; /note="Helical; Name=TM6"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 620..638; /note="Helical; Name=TM7"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 642..666; /note="Helical; Name=TM8"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 674..702; /note="Helical; Name=TM9"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4"; TRANSMEM 708..728; /note="Helical; Name=TM10"; /evidence="ECO:0000305|PubMed:39424995, ECO:0007744|PDB:8WG3, ECO:0007744|PDB:8WG4
uniprot
proteins