TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.A.17.1.1









The plasma membrane Ca2 -activated chloride (IClCa) channel, TMEM16A (Anoctamin 1a; ANO1a) (Huang et al., 2012; Chen et al. 2011). The mouse orthologue (Q8BHY3), TMEM16A (956aas), is localized to the apical membranes of epithelia as well as intracellular membranes in many cell types. Knockout mice show diminished rhythmic contraction of gastric smooth muscle (Huang et al., 2009). ANO1 is also required for normal tracheal development (Ousingsawat et al., 2009). Expression is upregulated by epidermal growth factor (Mroz and Keely, 2012). Novel 5-substituted benzyloxy-2-arylbenzofuran-3-carboxylic acids are inhibitors (Kumar et al., 2012). TMEM16A channels contribute to the myogenic response in cerebral arteries (Bulley et al., 2012). Membrane stretch activates arterial myocyte TMEM16A channels, leading to membrane depolarization and vasoconstriction. A local Ca2+   signal generated by nonselective cation channels stimulates TMEM16A channels to induce myogenic constriction (Bulley et al., 2012).  Ca2+/calmodulin activates bicarbonate (anion) transport (Jung et al. 2012).  The protein exists in the membrane as a homodimer where the cytoplasmic N-terminus functions in dimerization (Tien et al. 2013).  TMSs 5-6 of the 8 TMSs may comprise parts of the pore-loop that controls Cl- conductance (Adomaviciene et al. 2013).  ANO1 confers IClCa in retinal neurons and acts as an intrinsic regulator of the presynaptic membrane potential during synaptic transmission (Jeon et al. 2013).  TMEM16A may be a primary driver of the "Grow" (tumor proliferation) or "Go" (metastasis) model for cancer progression, in which TMEM16A expression acts to balance tumor proliferation and metastasis via its promoter methylation (Shiwarski et al. 2014).  Regulation of TMEM16A/16B by Ca2+ is mediated by preassociated apo-calmodulin (Yang et al. 2014).as well asCaMKIIδ (Gui et al. 2015).  Because the Cl- channel is the only active ion-selective conductance with a reversal potential that lies within the dynamic range of spiral ganglion neurons (SGN) action potentials, developmental alteration of [Cl-], and hence the equilibrium potential for Cl- (ECl), transforms the pre- to the posthearing phenotype (Zhang et al. 2015).  Four basic residues involved in ion selectivity and pore blocker sensitivity have been identified (Peters et al. 2015).  Channel activity is required for mucus secretion induced by interleukin-13 (Lin et al. 2015; Zhang et al. 2015). May interact cooperatively with TrpV1 (TC# 1.A.4.2.1) to form a thermal sensor (Kanazawa and Matsumoto 2014). Inhibitors have been described (Boedtkjer et al. 2015).  The first intracellular loop serves as a Ca2+ binding site and includes D439, E444 and E447 (Pang et al. 2015).  Inhibited by various 4-Aryl-2-amino thiazoles at concentrations as low as 1 mμM (Piechowicz et al. 2016).  ANO1 and TRPC6 (1.A.4.1.5) are present in the same macromolecular complex and localize in close spatial proximity in the myocyte plasma membrane.  TRPC6 channels probably generate a local intracellular Ca2+ signal that activates nearby ANO1 channels in myocytes to stimulate vasoconstriction (Wang et al. 2016).  ANO1 transports bicarbonate which functions in the regulation of pancreatic acinar cell pH (Han et al. 2016).  TMEM16A contains two ion conduction pores that are independently activated by Ca2+ binding to sites that are embedded within the transmembrane part of each subunit (Lim et al. 2016).  Interactions between the carboxy- terminus and the first intracellular loop in the TMEM16A homo-dimer regulate channel activity (Scudieri et al. 2016).  A STAT6-TMEM16A-ERK1/2 signal pathway and TMEM16A channel activity are required for the Interleukin-13 (IL-13)-induced TMEM16A mediated mucus production (Qin et al. 2016). Angiotensin II elicits a TMEM16A-mediated current, and TMEM16A participates in Ang II-induced basilar constriction via the RhoA/ROCK signaling pathway (Li et al. 2016). 2-acylamino-cycloalkylthiophene-3-carboxylic acid arylamides (AACTs) are inhibitors of TMEM16A, and 48 synthesized analogs (10ab-10bw) of the original AACT compound (10aa) have been synthesized and studied.  The most potent compound (10bm), which contains an unusual bromodifluoroacetamide at the thiophene 2-position, had an IC50 ~ 30 nM (Truong et al. 2017).

Eukaryota
Metazoa
Anoctamin 1a of Homo sapiens (Q5XXA6)
*1.A.17.1.2









Anoctamin 1, isoform b (Gnathodiaphyseal dysplasia 1 protein homologue) (39% identical to Anoctamin 1a) (Planells-Cases and Jentsch, 2009).  See also Xu et al. 2015.

Eukaryota
Metazoa
Anoctamin 1b of Homo sapiens (Q75UR0)
*1.A.17.1.3









TMEM16B (Anoctamin-2, ANO2) anion channel.  Exists in the membrane as a homodimer where the cytoplasmic N-terminus functions in dimerization (Tien et al. 2013).  TMSs 5-6 may comprise parts of the pore-loop that controls Cl- conductance (Adomaviciene et al. 2013).  TMEM16A and TMEM16B are differentially expressed during development in the olfactory epithelium of the mouse (Maurya and Menini 2014).

Eukaryota
Metazoa
TMEM16B of Homo sapiens (Q9NQ90)
*1.A.17.1.4









Anoctamin-6 (ANO6: TMEM16F) Ca2+-dependent phospholipid scramblase (flippase) (Suzuki et al., 2010; Chauhan et al. 2016). Defects cause Scott syndrome. It is an essential component of the outwardly rectifying chloride channel (Martins et al., 2011; Keramidas and Lynch 2012).  It has also been reported to be an anion channel with delayed Ca2+ activation (Adomaviciene et al. 2013) as well as a Ca2+-activated cation channel with activity that is required for lipid scrambing (Yang et al. 2012).  However, Suzuki et al. (2013) showed that TMEM16F is a Ca2+-dependent phospholipid scramblase that exposes phosphatidylserine (PS) to the cell surface but lacks calcium-dependent chloride channel activity.  TMEM16C, 16D, 16G and 16J also had Ca2+-dependent scramblase but not channel activity (Suzuki et al. 2013).  The pore region resonsible for Cl- transport in TMEM16A is also responsible for phospholipid scramblase activity (Suzuki et al. 2014).  Anoctamin-6 (Ano6) plays an essential role in C2C12 myoblast proliferation, probably by regulating the ERK/AKT signaling pathway (Zhao et al. 2014).  It regulates baeline phosphatidyl serine exposure and cell viability in human embryonic kidney cells (Chauhan et al. 2016). Defects cause Scott syndrome. It is an essential component of the outwardly rectifying chloride channel (Martins et al., 2011; Keramidas and Lynch 2012).  It has also been reported to be an anion channel with delayed Ca2+ activation (Adomaviciene et al. 2013) as well as a Ca2+-activated cation channel with activity that is required for lipid scrambing (Yang et al. 2012).  However, Suzuki et al. (2013) showed that TMEM16F is a Ca2+-dependent phospholipid scramblase that exposes phosphatidylserine (PS) to the cell surface but lacks calcium-dependent chloride channel activity.  TMEM16C, 16D, 16G and 16J also had Ca2+-dependent scramblase but not channel activity (Suzuki et al. 2013).  The pore region resonsible for Cl- transport in TMEM16A is also responsible for phospholipid scramblase activity (Suzuki et al. 2014).  Anoctamin-6 (Ano6) plays an essential role in C2C12 myoblast proliferation, probably by regulating the ERK/AKT signaling pathway (Zhao et al. 2014).  It regulates baeline phosphatidyl serine exposure and cell viability in human embryonic kidney cells (Schenk et al. 2016).

Eukaryota
Metazoa
Anoctamin-6 of Homo sapiens (Q4KMQ2)
*1.A.17.1.5









Anoctamin-9 (Transmembrane protein 16J) (Tumor protein p53-inducible protein 5) (p53-induced gene 5 protein)
Eukaryota
Metazoa
ANO9 of Homo sapiens
*1.A.17.1.6









Uncharacterized protein

Eukaryota
Fungi
Uncharacterized protein of Batrachochytrium dendrobatidis
*1.A.17.1.7









Anoctamin-like protein

Eukaryota
Choanoflagellida
amoctamin-like protein of Dictyostelium purpureum
*1.A.17.1.8









Uncharacterized protein

Eukaryota
Metazoa
unchacterized protein of Aureococcus anophagefferens
*1.A.17.1.9









Anoctamin, Anoh-1 of 822 aas.  Functions in a sensory mode-specific manner.  Present inamphid sensory neurons to detect external chemical and nociceptive cues (Wang et al. 2013).

Eukaryota
Metazoa
Anoh-1 of Caenorhabditis elegans
*1.A.17.1.10









Anoctamin, Anoh-2.  Present in mechanoreceptive neurons and spermatheca (Wang et al. 2013).

Eukaryota
Metazoa
Anoh-2 of Caenorhabditis elegans
*1.A.17.1.11









Anoctamin-like protein At1g73020
Eukaryota
Viridiplantae
At1g73020 of Arabidopsis thaliana
*1.A.17.1.12









Ca-ClC Family homologue

Eukaryota
Intramacronucleata
Ca-ClC homologue of Paramecium tetraurelia (A0CAP8)
*1.A.17.1.13









Ciliate CaClC homologue

Eukaryota
Intramacronucleata
CaClC homologue of Paramecium tetraurelia (A0CIB0)
*1.A.17.1.14









Water mold Anoctamin-like protein

Eukaryota
Peronosporales
Anoctamin-like protein of Phytophthora infestans (D0NGF4)
*1.A.17.1.15









Uncharacterized protein

Eukaryota
Fungi
Uncharacterized protein of Schizosaccharomyces japonicus
*1.A.17.1.16









Anoctamin-like protein

Eukaryota
Intramacronucleata
Anoctamin-like protein of Oxytricha trifallax
*1.A.17.1.17









TMEM16 (Ist2) ion channel/phospholipid scramblase (Malvezzi et al. 2013).

Eukaryota
Fungi
Ist2 of Aspergillus fumigatus (Neosartorya fumigata)
*1.A.17.1.18









TMEM16 of 735 aas and 10 TMSs.  Operates as a Ca2+-activated lipid scramblase. Each subunit of the homodimer contains a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer as a potential site of catalysis. This cavity harbours a conserved Ca2+-binding site, located within the hydrophobic core of the membrane. Mutations of residues involved in Ca2+ coordination affect both lipid scrambling in N. haematococca TMEM16 and ion conduction in the Cl- channel of TMEM16A. The structure reveals the general architecture of the family and its mode of Ca2+ activation (Brunner et al. 2014).

Eukaryota
Fungi
TMEM16 of Nectria haematococca (Fusarium solani subsp. pisi)
*1.A.17.1.19









Increased sodium tolerance protein, Ist2, of 946 aas and 7 TMSs.  Ist2 is an endoplasmic reticulum (ER)-resident transmembrane protein that mediates associations between the plasma membrane (PM) and the cortical ER (cER) in baker's yeast (Kralt et al. 2015).

Eukaryota
Fungi
Ist2 of Saccharomyces cerevisiae
*1.A.17.1.20









Anoctamin 3, ANO3 or KCNT1, of 981 aas and 9 TMSs.  Has calcium-dependent phospholipid scramblase activity, scrambling phosphatidylcholine and galactosylceramide. Seems to act as a potassium channel regulator and may inhibit pain signaling; can facilitate KCNT1/Slack channel activity by promoting its full single-channel conductance at very low sodium concentrations and by increasing its sodium sensitivity (Scudieri et al. 2012). Mutations cause  (i) epilepsy of infancy with migrating focal seizures (EIMFS; also known as migrating partial seizures in infancy), (ii) autosomal dominant nocturnal frontal lobe epilepsy, and (iii) other types of early onset epileptic encephalopathies (EOEEs) (Ohba et al. 2015).

ANO3 or KCNT1 of Homo sapiens
*1.A.17.1.21









Ano5 (GDD1, TMEM16E) of 913 aas and 10 TMSs. Associated with bone fragility, limb girdle muscular dystrophy type 2L (LGMD2L), Miyoshi myopathy type 3 (MMD3), and gnathodiaphyseal dysplasia 1 (GDD1) in humans (Jin et al. 2017), but an Ano5 knock-out mutant in mice was not reported to exhibit such symptoms (Xu et al. 2015). The orthologue in mice is TC# 1.A.17.1.2.  TMEM16E may function as a phospholipid scramblase in intracellular membranes promoting sperm motility and function (Gyobu et al. 2016).

Eukaryota
Metazoa
Ano5 of Homo sapiens
*1.A.17.1.22









Subdued, a calcium-activated chloride channel of 1075 aas. Functions in conjunction with the thermo-TRPs in thermal nociception. Subdued channels may amplify the nociceptive neuronal firing that is initiated by thermo-TRP channels in response to thermal stimuli (Jang et al. 2015).

Eukaryota
Metazoa
Subdued of Drosophila melanogaster
*1.A.17.1.23









ANO-like protein of 921 aas and 9 predicted TMSs.

Eukaryota
Metazoa
ANO-L family protein of Strongylocentrotus purpuratus (Purple sea urchin)
*1.A.17.1.24









Duplicated full length anoctamin of 2084 aas and an etimated 20 TMSs.  The protein has two full length repeats, each of about 1000 aas with a ~500 aas hydrophilic domain followed by the first anoctamin domain, and then another 500 aa hydrophilic domain followed by the second anoctamin domain.

Eukaryota
Oomycetes
Dupicated anoctamin of Aphanomyces invadans
*1.A.17.1.25









TMem16A or Anoctamin-1 (Ano1) Ca2+-activated anion (Cl-) channel of 960 aas and 10 TMSs.  Its structure has been solved by cryoEM (Paulino et al. 2017). The protein shows a similar organization to the fungal nhTMEM16, except for changes at the site of catalysis. There, the conformation of transmembrane helices, constituting a membrane-spanning furrow that provides a path for lipids in scramblases, is replaced to form an enclosed aqueous pore that is largely shielded from the membrane (Paulino et al. 2017). It thus provides a pathway for anions such as Cl-.

Eukaryota
Metazoa
Ano1 of Mus musculus
*1.A.17.2.1









DUF590 family protein

Eukaryota
Dictyosteliida
DUF590 protein of Dicyostelium discoideum (Q54BH1)
*1.A.17.2.2









TMEM16 homologue of 701 aas.

Eukaryota
Heterolobosea
TMEM16 homologue of Naegleria gruberi (Amoeba)
*1.A.17.2.3









Anoctamin homologue of 689 aas

Eukaryota
Cryptophyta
Anoctamin of Guillardia theta
*1.A.17.2.4









DUF590 homologue of 487 aas

Eukaryota
Entamoeba
DUF590 homologue of Entamoeba nuttalli
*1.A.17.2.5









DUF590 protein of 914 aas

Eukaryota
Fungi
DUF590 protein of Allomyces macrogynus
*1.A.17.2.6









Uncharacterized protein of 569 aas and 8 predicted TMSs.

Eukaryota
Dictyosteliida
UP of Dictyostelium fasciculatum (Slime mold)
*1.A.17.3.1









Uncharacterized protein of 2464 aas and 11 TMSs.  Contains a trypsin-like serine protease domain (residues 100 - 400), a rabaptin (chromosome segregation) domain (residues 900 - 1200), an anoctamin domain (residues 1500 - 2000) and an AAA ATPase-containing von Willebrand factor type A domain (residues 2200 - 2500).

Eukaryota
Bacillariophyta
UP of Thalassiosira pseudonana (Marine diatom) (Cyclotella nana)
*1.A.17.3.2









Uncharacterized protein of 842 aas and 9 TMSs.

Eukaryota
Bacillariophyta
UP of Thalassiosira pseudonana (Marine diatom) (Cyclotella nana)
*1.A.17.3.3









Uncharacterized protein of 835 aas and 9 TMSs.

Eukaryota
Peronosporales
UP of Phytophthora parasitica (Potato buckeye rot agent)
*1.A.17.3.4









Uncharacterized protein of 1231 aas and 9 TMSs

Eukaryota
Pelagophyceae
UP of Aureococcus anophagefferens (Harmful bloom alga)
*1.A.17.3.5









Uncharacterized protein of 945 aas and 8 TMSs

Eukaryota
Phaeophyceae
UP of Ectocarpus siliculosus (Brown alga)
*1.A.17.3.6









Uncharacterized protein of 1437 aas

Eukaryota
Isochrysidales
UP of Emiliania huxleyi
*1.A.17.3.7









Uncharacterized protein of 1150 aas

Eukaryota
Ichthyosporea
UP of Capsaspora owczarzaki
*1.A.17.3.8









DUF590/putative methyltransferase of 1221 aas and 10 TMSs.

Eukaryota
Intramacronucleata
DUF490 homologue of Oxytricha trifallax
*1.A.17.3.9









DUF590 homologue of 1026 aas and 10 TMSs

Eukaryota
Intramacronucleata
DUF590 homologue of Paramecium tetraurelia (ciliate)
*1.A.17.3.10









Uncharacterized protein of 1080 aas

Eukaryota
Viridiplantae
UP of Ostreococcus lucimarinus
*1.A.17.3.11









Anoctamin homologue of 1265 aas

Eukaryota
Intramacronucleata
Anoctamin homologue of Tetrahymena thermophila
*1.A.17.3.12









Uncharacterized protein of 995 aas and 8 TMSs.

Eukaryota
Intramacronucleata
UP of Tetrahymena thermophila
*1.A.17.3.13









Uncharacterized protein of 10 TMSs in a 3 + 4 +3 arrangement

Eukaryota
Intramacronucleata
UP of Paramecium tetraurelia
*1.A.17.3.14









Uncharacterized protein of 888 aas and 10 TMSs in a 3 + 4 + 3 arrangement

Eukaryota
Intramacronucleata
UP of Paramecium tetraurelia
*1.A.17.3.15









Uncharacterized protein of 958 aas and 11 or 12 TMSs in a 3 or 4 + 5 +3 arrangement.

Eukaryota
Intramacronucleata
UP of Paramecium tetraurelia
*1.A.17.4.1









TMC2, like TMC1, plays a role in hearing and gravity detection (Kawashima et al., 2011).  Required for normal function of cochlear hair cells, possibly as a Ca2+ channel (Kim and Fettiplace 2013).  TMC1 and TMC2 are both components of hair cell transduction channels and contribute to permeation properties (Pan et al. 2013; Kawashima et al. 2014).  Both TMC1 and 2 interact with Protocadherin 15 (Maeda et al. 2014). TMC1 and TMC2 are components of the stereocilia mechanoelectrical transduction channel complex (Kurima et al. 2015).

Eukaryota
Metazoa
TMC2 of Mus musculus (Q8R4P4)
*1.A.17.4.2









Transmembrane channel-like protein-B, Tmc8 (EVER2).  Occurs in the endoplasmic reticulum where it functions to release Ca2+ and Zn2+ and supresses Cl- currents (Sirianant et al. 2014). 

Eukaryota
Metazoa
Tmc8 of Mus musculus (Q7TN58)
*1.A.17.4.3









Hypothetical protein, HP

Eukaryota
Choanoflagellida
HP of Salpingoeca sp. (F2U2C0)
*1.A.17.4.4









Hypothetical protein, HP

Eukaryota
Ichthyosporea
HP of Capsaspora owczarzaki (E9C7I1)
*1.A.17.4.5









Transmembrane channel-like protein 7, TMC7

Eukaryota
Metazoa
TMC7 of Acromyrmex echinatior (F4X8H9)
*1.A.17.4.6









Transmembrane channel-like protein-1, Tmc1. Also called Transmembrane cochlear-expressed protein-1, Beethoven protein and deafness protein.  Required for normal function of cochlear hair cells, possibly as a Na+/K+/Ca2+ channel (Kim and Fettiplace 2013).  TMC1 and TMC2 are both components of hair cell transduction channels and contribute to permeation properties (Pan et al. 2013; Kawashima et al. 2014).  Channel activity has been demonstrated for the C. elegans orthologue, and the mouse Tmc1.  The C. elegans Tmc1 is probably a Na+-activated Na+-selective mechanosensor. The C. elegans Tmc2 may be a Na+/K+ channel.  The mouse Tmc1 is functional and replaces Tmc2 when expressed in C. elegans (WR Schafer, personal communication).  Ca2+ currents are blocked by the peptide toxin GsMTx-4 (Beurg et al. 2014).  Tmc1 and Tmc2, expressed in cochlear and vestibular hair cells, are required for hair cell mechanoelectric transduction (Nakanishi et al. 2014); mutations disrupt mechanoelectric transduction and are a cause of autosomal dominant and recessive forms of nonsyndromic hearing loss (Gao et al. 2015).  Using the mutant mouse model (Tmc1; Beethoven) for progressive hearing loss in humans (DFNA36) this mutation has been shown to affect the MET channel pore, reducing its Ca2+ permeability and its affinity for the permeant blocker, dihydrostreptomycin (Corns et al. 2016).  Evidence for TMC1 beiing the hair cell mechanosensitive channel has been evaluated (Fettiplace 2016).  The human orthologue (UniProt acc # Q8TDI8) is 96% identical.

Eukaryota
Metazoa
Tmc1 of Mus musculus
*1.A.17.4.7









The sodium sensor/cation conductance channel activated by high extracellular Na+, Tmc-1 (Tmc1) (Chatzigeorgiou et al. 2013).  It functions in salt taste chemosensation and salt avoidance and is an ionotropic sensory receptor.  Wang et al. 2016 showed that C. elegans TMC-1 mediates nociceptor responses to high pH, not sodium, allowing the nematode to avoid strongly alkaline environments in which most animals cannot survive (Spalthoff and Göpfert 2016).

Eukaryota
Metazoa
Tmc-1 of Caenorhabditis elegans
*1.A.17.4.8









Tmc2 channel of 1203 aas and 9 - 11 TMSs; functions in touch neurons as a mechanosensitive touch sensor (Chatzigeorgiou et al. 2013; WR Schafer, personal communication).  May function as a Na+/K+ channel.

Eukaryota
Metazoa
Tmc2 of Caenorhabditis elegans
*1.A.17.4.9









Tmc receptor/channel of 1932 aas. Plays a role in Drosophila proprioception and the sensory control of larval locomotion (Guo et al. 2016).

Eukaryota
Metazoa
Tmc of Drosophila melanogaster
*1.A.17.4.10









Transmembrane channel 6, TMC6/EVER1 of 805 aas.  Mutations give rise to epidermodysplasia verruciformis (EV), a rare genodermatosis, characterized by increased sensitivity to infection by the beta-subtype of human papillomaviruses (beta-HPVs), causing persistent, tinea versicolor-like dermal lesions (Horton and Stokes 2014).

Eukaryota
Metazoa
TMC6 of Homo sapiens
*1.A.17.4.11









Transmembrane channel 8, TMC8/EVER2/EVIN2 of 726 aas.  Mutations give rise to epidermodysplasia verruciformis (EV), a rare genodermatosis characterized by increased sensitivity to infection by the beta-subtype of human papillomaviruses (beta-HPVs) as well as increased incidence of cancer, causing persistent, tinea versicolor-like dermal lesions (Horton and Stokes 2014).  This is due to release of Zn2+ and Ca2+ from the endoplasmic reticulum (Sirianant et al. 2014).  The channel-like domain has been identified (Miyauchi et al. 2016). It plays a role in several aspects of human pathophysiology, such as ion channel permeability, human papillomavirus infection and skin cancer (Lu et al. 2017).

 

Eukaryota
Metazoa
TMC8 of Homo sapiens
*1.A.17.4.12









Transmembrane channel protein 3, Tmc3 of 1130 aas (Kurima et al. 2003; Beurg et al. 2014).

Eukaryota
Metazoa
Tmc3 of Mus musculus
*1.A.17.4.13









Tmc1/Tmc2a or Tmc2b/protocadherin 15a (Pcdh15a). The complex is part of a mechanotransduction system (Maeda et al. 2014). Its trafficing to the plasma membrane depends on the transmembrane O-methyltransferase (TOMT/LRTOMT; 259 aas, 1 N-terminal TMS) (Erickson et al. 2017).

Eukaryota
Metazoa
Tmc1/Tmc2/Pcdh15 complex of Danio rerio (Zebrafish) (Brachydanio rerio)
*1.A.17.4.14









Tmc4 of 712 aas and 10 TMSs (Mancina et al. 2016).

Eukaryota
Metazoa
TMC4 of Homo sapiens
*1.A.17.5.1









Uncharacterized protein, DUF221, of 703 aas

Eukaryota
Viridiplantae
UP of Zea mays
*1.A.17.5.2









Uncharacterized protein of 816 aas containe a DUF221 domain

Eukaryota
Metazoa
UP of Danio rerio
*1.A.17.5.3









Uncharacterized transmembrane protein 63B of 832 aas with a DUF221 domain.

Eukaryota
Metazoa
UP of Homo sapiens
*1.A.17.5.4









Uncharacterized transmembrane protein 63B of 832 aas with a DUF221 domain.

Eukaryota
Longamoebia
UP of Acanthamoeba castellanii
*1.A.17.5.5









Uncharacterized protein of 853 aas with a DUF221 domain.

Eukaryota
Fungi
UP of Botryotinia fuckeliana
*1.A.17.5.6









Phosphate metabolism protein 7, Phm7

Eukaryota
Fungi
Phm7 of Saccharomyces cerevisiae
*1.A.17.5.7









Sporulation-specific protein 75, Spo75

Eukaryota
Fungi
Spo75 of Saccharomyce cerevisiae
*1.A.17.5.8









RSN-1-like protein of 957 aas

Eukaryota
Fungi
RSN-1-like protein of Saccharomyces kudriavzevii
*1.A.17.5.9









Early response to dehydrate stress protein, ERD4 of 785 aas

Eukaryota
Viridiplantae
ERD4 of Arabidopsis thaliana
*1.A.17.5.10









The non-rectifying, plasma membrane, calcium-permeable, stress-gated, cation channel 1 (CSC1) of 771 aas (Hou et al. 2014).  Activated by hyperosmotic shock.  Permeable to Ca2+, K+ and Na+.  Inactivation or closure is Ca2+-dependent.  The N-terminal region contains 3 TMSs, the first of which may be a cleavable signal peptide., and the C-terminal region contains 6 TMSs corresponding to the DUF221 domain.  Arabidopsis contains at least 15 CSCs ((Hou et al. 2014).  Some plant homologues are transcriptionally upregulated in response to vaious abiotic and biotic stresses involving mechanical perturbation (Kiyosue et al. 1994).

Eukaryota
Viridiplantae
CSC1 of Arabidopsis thaliana
*1.A.17.5.11









Osmotically-gated calcium conductance channel of 782 aas. CSC1 (Hou et al. 2014). Activated under hyperosmotic conditions. There are four paralogues in S. cerevisiae

Eukaryota
Fungi
CSC1 of Saccharomyces cerevisiae
*1.A.17.5.12









The osmosensitive calcium-permeable cation channel, CSC1 of 806 aas.  Activated by hyperosmolarity and Ca2+ (Hou et al. 2014).

Eukaryota
Metazoa
CSC1 of Homo sapiens
*1.A.17.5.13









Uncharacterized protein of 901 aas

Eukaryota
Hexamitidae
UP of Spironucleus salmonicida
*1.A.17.5.14









Uncharacterized protein of 1267 aas and 12 TMSs

Eukaryota
Dictyosteliida
UP of Dictyostelium discoideum (Slime mold)
*1.A.17.5.15









Uncharacterized protein of 1548 aas and 12 TMSs.

Eukaryota
Bacillariophyta
UP of Thalassiosira pseudonana (Marine diatom) (Cyclotella nana)
*1.A.17.5.16









Uncharacterized protein of 1172 aas

Eukaryota
Kinetoplastida
UP of Phytomonas sp. isolate EM1
*1.A.17.5.17









Uncharacterized protein of 1258 aas and 11 TMSs.

Eukaryota
Fungi
UP of Agaricus bisporus (White button mushroom)
*1.A.17.6.1









Uncharacterized protein of 878 aas and 7 putative TMSs.

Eukaryota
Intramacronucleata
UP of Oxytricha trifallax
*1.A.17.6.2









TMC-like protein 8 of 890 aas and 8 TMSs

Eukaryota
Intramacronucleata
TMC homologue of Oxytricha trifallax
*1.A.17.6.3









Uncharacterized protein of 834 aas and 7 TMSs

Eukaryota
Intramacronucleata
UP of Oxytricha trifallax
*1.A.17.6.4









Uncharacterized protein of 912 aas and 10 TMSs

Eukaryota
Peronosporales
UP of Phytophthora parasitica (Potato buckeye rot agent)
*1.A.17.6.5









Uncharacterized protein of 620 aas and 9 TMSs

Eukaryota
Phaeophyceae
UP of Ectocarpus siliculosus (Brown alga)
*1.A.17.6.6









Uncharacterized protein of 865 aas and 10 TMSs

Eukaryota
Cryptophyta
UP of Guillardia theta
*1.A.17.6.7









TMC protein of 890 aas and 10 TMSs

Eukaryota
Intramacronucleata
TMC protein of Tetrahymena thermophila
*1.A.17.6.8









Uncharacterized protein of 1057 aas and 10 TMSs.

Eukaryota
Intramacronucleata
UP of Tetrahymena thermophila
*1.A.17.6.9









Uncharacterized protein of 867 aas and 10 TMSs.

Eukaryota
Oomycetes
UP of Saprolegnia diclina
*1.A.17.6.10









Uncharacterized protein of 707 aas and 10 TMSs

Eukaryota
Plasmodiophoridae
UP of Plasmodiophora brassicae
*1.A.17.7.1









Uncharacterized protein of 836 aas and 12 TMSs.

Eukaryota
Hexamitidae
UP of Giardia intestinalis (Giardia lamblia)
*1.A.17.7.2









Uncharacterized protein of 637 aas and 8 TMSs.

Eukaryota
Hexamitidae
UP of Spironucleus salmonicida
*1.A.17.7.3









Distant Anoctamin homologue of 718 aas and 14 TMSs in a 4 + 1+1+1+2+2+2+1 arramgement.

Eukaryota
Hexamitidae
Anoctamin homologue of Spironucleus salmonicida
*1.A.17.7.4









Uncharacterized Anoctamin homologue of 502 aas and 8 putative TMSs

Eukaryota
Hexamitidae
UP of Spironucleus salmonicida
*1.A.17.7.5









Uncharacterized anoctamin homologue of 823 aas and 8 predicted TMSs in a 3 + 2 + 3 arrangement.

Eukaryota
Hexamitidae
UP of Giardia intestinalis (Giardia lamblia)