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Polycystic kidney disease 2-like 1 protein (Polycystin-2 homolog) (Polycystin-2L1) (Polycystin-L) (Polycystin-L1)

 PK2L1_HUMAN             Reviewed;         805 AA.
Q9P0L9; O75972; Q5W039; Q9UP35; Q9UPA2;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=Polycystic kidney disease 2-like 1 protein;
AltName: Full=Polycystin-2 homolog;
AltName: Full=Polycystin-2L1;
AltName: Full=Polycystin-L;
AltName: Full=Polycystin-L1;
Name=PKD2L1; Synonyms=PKD2L, PKDL, TRPP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT ILE-393.
TISSUE=Retina;
PubMed=9748274; DOI=10.1074/jbc.273.40.25967;
Nomura H., Turco A.E., Pei Y., Kalaydjieva L., Schiavello T.,
Weremowicz S., Ji W., Morton C.C., Meisler M., Reeders S.T., Zhou J.;
"Identification of PKDL, a novel polycystic kidney disease 2-like gene
whose murine homologue is deleted in mice with kidney and retinal
defects.";
J. Biol. Chem. 273:25967-25973(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
PubMed=10602992; DOI=10.1007/s003350010009;
Guo L., Chen M., Basora N., Zhou J.;
"The human polycystic kidney disease 2-like (PKDL) gene: exon/intron
structure and evidence for a novel splicing mechanism.";
Mamm. Genome 11:46-50(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 96-805 (ISOFORM 1).
TISSUE=Retina;
PubMed=9878261; DOI=10.1006/geno.1998.5618;
Wu G., Hayashi T., Park J.-H., Dixit M., Reynolds D.M., Li L.,
Maeda Y., Cai Y., Coca-Prados M., Somlo S.;
"Identification of PKD2L, a human PKD2-related gene: tissue-specific
expression and mapping to chromosome 10q25.";
Genomics 54:564-568(1998).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 43-805 (ISOFORMS 1 AND 4), AND TISSUE
SPECIFICITY.
TISSUE=Testis;
PubMed=10602361; DOI=10.1038/sj.ejhg.5200383;
Veldhuisen B., Spruit L., Dauwerse H.G., Breuning M.H., Peters D.J.M.;
"Genes homologous to the autosomal dominant polycystic kidney disease
genes (PKD1 and PKD2).";
Eur. J. Hum. Genet. 7:860-872(1999).
[8]
FUNCTION.
PubMed=10517637; DOI=10.1038/43907;
Chen X.-Z., Vassilev P.M., Basora N., Peng J.-B., Nomura H., Segal Y.,
Brown E.M., Reeders S.T., Hediger M.A., Zhou J.;
"Polycystin-L is a calcium-regulated cation channel permeable to
calcium ions.";
Nature 401:383-386(1999).
[9]
REVIEW.
PubMed=11698076; DOI=10.1016/S0165-6147(00)01832-0;
Stayner C., Zhou J.;
"Polycystin channels and kidney disease.";
Trends Pharmacol. Sci. 22:543-546(2001).
[10]
ALTERNATIVE SPLICING (ISOFORMS 2 AND 5).
PubMed=11959145;
Li Q., Liu Y., Zhao W., Chen X.Z.;
"The calcium-binding EF-hand in polycystin-L is not a domain for
channel activation and ensuing inactivation.";
FEBS Lett. 516:270-278(2002).
[11]
ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=18535624; DOI=10.1038/embor.2008.89;
Inada H., Kawabata F., Ishimaru Y., Fushiki T., Matsunami H.,
Tominaga M.;
"Off-response property of an acid-activated cation channel complex
PKD1L3-PKD2L1.";
EMBO Rep. 9:690-697(2008).
[12]
ENZYME REGULATION.
PubMed=19464260; DOI=10.1016/j.bbrc.2009.05.069;
Ishii S., Misaka T., Kishi M., Kaga T., Ishimaru Y., Abe K.;
"Acetic acid activates PKD1L3-PKD2L1 channel--a candidate sour taste
receptor.";
Biochem. Biophys. Res. Commun. 385:346-350(2009).
[13]
FUNCTION.
PubMed=19812697; DOI=10.1371/journal.pone.0007347;
Huque T., Cowart B.J., Dankulich-Nagrudny L., Pribitkin E.A.,
Bayley D.L., Spielman A.I., Feldman R.S., Mackler S.A., Brand J.G.;
"Sour ageusia in two individuals implicates ion channels of the ASIC
and PKD families in human sour taste perception at the anterior
tongue.";
PLoS ONE 4:E7347-E7347(2009).
[14]
SUBUNIT, AND CALCIUM-BINDING.
PubMed=20408813; DOI=10.1042/BJ20091843;
Molland K.L., Narayanan A., Burgner J.W., Yernool D.A.;
"Identification of the structural motif responsible for trimeric
assembly of the C-terminal regulatory domains of polycystin channels
PKD2L1 and PKD2.";
Biochem. J. 429:171-183(2010).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH PKD1L1.
PubMed=20538909; DOI=10.1096/fj.10-162925;
Ishimaru Y., Katano Y., Yamamoto K., Akiba M., Misaka T.,
Roberts R.W., Asakura T., Matsunami H., Abe K.;
"Interaction between PKD1L3 and PKD2L1 through their transmembrane
domains is required for localization of PKD2L1 at taste pores in taste
cells of circumvallate and foliate papillae.";
FASEB J. 24:4058-4067(2010).
[16]
ENZYME REGULATION.
PubMed=22420714; DOI=10.1111/j.1742-4658.2012.08566.x;
Ishii S., Kurokawa A., Kishi M., Yamagami K., Okada S., Ishimaru Y.,
Misaka T.;
"The response of PKD1L3/PKD2L1 to acid stimuli is inhibited by
capsaicin and its pungent analogs.";
FEBS J. 279:1857-1870(2012).
[17]
INTERACTION WITH RACK1.
PubMed=22174419; DOI=10.1074/jbc.M111.305854;
Yang J., Wang Q., Zheng W., Tuli J., Li Q., Wu Y., Hussein S.,
Dai X.Q., Shafiei S., Li X.G., Shen P.Y., Tu J.C., Chen X.Z.;
"Receptor for activated C kinase 1 (RACK1) inhibits function of
transient receptor potential (TRP)-type channel Pkd2L1 through
physical interaction.";
J. Biol. Chem. 287:6551-6561(2012).
[18]
FUNCTION, SUBUNIT, INTERACTION WITH PKD1L1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 523-GLU--GLU-525.
PubMed=24336289; DOI=10.1038/nature12832;
DeCaen P.G., Delling M., Vien T.N., Clapham D.E.;
"Direct recording and molecular identification of the calcium channel
of primary cilia.";
Nature 504:315-318(2013).
[19]
X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT,
CALCIUM-BINDING, AND MUTAGENESIS OF LEU-710; VAL-714; LEU-717;
ILE-728; VAL-731 AND LEU-735.
PubMed=22193359; DOI=10.1016/j.bbapap.2011.12.002;
Molland K.L., Paul L.N., Yernool D.A.;
"Crystal structure and characterization of coiled-coil domain of the
transient receptor potential channel PKD2L1.";
Biochim. Biophys. Acta 1824:413-421(2012).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 699-743, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-523 AND ASP-525.
PubMed=23212381; DOI=10.1038/ncomms2257;
Yu Y., Ulbrich M.H., Li M.H., Dobbins S., Zhang W.K., Tong L.,
Isacoff E.Y., Yang J.;
"Molecular mechanism of the assembly of an acid-sensing receptor ion
channel complex.";
Nat. Commun. 3:1252-1252(2012).
-!- FUNCTION: Pore-forming subunit of a ciliary calcium channel that
controls calcium concentration within primary cilia without
affecting cytoplasmic calcium concentration. Forms a heterodimer
with PKD1L1 in primary cilia and forms a calcium-permeant ciliary
channel that regulates sonic hedgehog/SHH signaling and GLI2
transcription. May act as a sour taste receptor by forming a
calcium channel with PKD1L3 in gustatory cells; however, its
contribution to sour taste perception is unclear in vivo and may
be indirect. {ECO:0000269|PubMed:10517637,
ECO:0000269|PubMed:19812697, ECO:0000269|PubMed:23212381,
ECO:0000269|PubMed:24336289}.
-!- ENZYME REGULATION: The calcium channel is gated following an off-
response property by acid: gated open after the removal of acid
stimulus, but not during acid application.
{ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260,
ECO:0000269|PubMed:22420714}.
-!- SUBUNIT: Homotrimer; trimerization is independent of calcium-
binding. Calcium channels are probably composed of 3 subunit of
PKD2L1 and 1 subunit of some PKD1 protein (PKD1, PKD1L1, PKD1L2 or
PKDL3). Interacts with PKD1. Interacts with PKD1L1; to form
ciliary calcium channel. Interacts with PKD1L3, to form putative
sour taste receptor. Interacts with RACK1; inhibits the channel
activity possibly by impairing localization to the cell membrane.
{ECO:0000269|PubMed:20408813, ECO:0000269|PubMed:20538909,
ECO:0000269|PubMed:22174419, ECO:0000269|PubMed:22193359,
ECO:0000269|PubMed:23212381, ECO:0000269|PubMed:24336289}.
-!- INTERACTION:
Q8N6F1-2:CLDN19; NbExp=3; IntAct=EBI-7956847, EBI-12256978;
-!- SUBCELLULAR LOCATION: Cell projection, cilium membrane; Multi-pass
membrane protein. Cell membrane; Multi-pass membrane protein.
Endoplasmic reticulum {ECO:0000250}. Note=Interaction with PKD1 or
PKD1L3 is required for localization to the cell membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9P0L9-1; Sequence=Displayed;
Name=2; Synonyms=PKDLdel15, PCL-TS, Testis isoform;
IsoId=Q9P0L9-2; Sequence=VSP_004730, VSP_004731;
Name=3; Synonyms=PKDLdel5;
IsoId=Q9P0L9-3; Sequence=VSP_004729;
Name=4; Synonyms=PKDLdel456;
IsoId=Q9P0L9-4; Sequence=VSP_004728;
Note=Unusual intron exon spliced junction.;
Name=5; Synonyms=PCL-LV, Liver isoform;
IsoId=Q9P0L9-5; Sequence=VSP_053718;
-!- TISSUE SPECIFICITY: Expressed in adult heart, skeletal muscle,
brain, spleen, testis, retina and liver. According to
PubMed:9748274, expressed at high levels in fetal tissues,
including kidney and liver, and down-regulated in adult tissues.
According to PubMed:10602361, expressed in fetal brain, but not
expressed in fetal lung, liver or kidney. Isoform 4 appears to be
expressed only in transformed lymphoblasts.
{ECO:0000269|PubMed:10602361, ECO:0000269|PubMed:9748274}.
-!- DOMAIN: The EF-hand domain probably mediates calcium-binding. It
is not required for channel activation (PubMed:11959145).
{ECO:0000269|PubMed:11959145}.
-!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
-!- CAUTION: PKD1L3 and PKD2L1 have been defined as sour taste
receptor in gustatory cells based on a number of indirect
evidences in mouse. Some data confirm this hypothesis in human: in
2 patients with sour ageusia that are unresponsive to sour
stimuli, but show normal responses to bitter, sweet, and salty
stimuli, expression of PKD1L3 and PKD2L1 is absent in the anterior
part of the tongue (PubMed:19812697). However, a number of
experiments have recently shown that the sour taste receptor
activity is probably indirect. {ECO:0000305|PubMed:19812697}.
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EMBL; AF073481; AAD41638.1; -; mRNA.
EMBL; AF153474; AAF28108.1; -; Genomic_DNA.
EMBL; AF153459; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153460; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153461; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153462; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153463; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153464; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153465; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153466; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153467; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153468; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153469; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153470; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153471; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153472; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AF153473; AAF28108.1; JOINED; Genomic_DNA.
EMBL; AL139819; CAH72822.1; -; Genomic_DNA.
EMBL; CH471066; EAW49833.1; -; Genomic_DNA.
EMBL; BC025665; AAH25665.1; -; mRNA.
EMBL; AF094827; AAD08695.1; -; mRNA.
EMBL; AF053316; AAD51859.1; -; mRNA.
CCDS; CCDS7492.1; -. [Q9P0L9-1]
RefSeq; NP_001240766.1; NM_001253837.1.
RefSeq; NP_057196.2; NM_016112.2. [Q9P0L9-1]
UniGene; Hs.159241; -.
PDB; 3TE3; X-ray; 2.69 A; A/B/C/D/E/F=699-737.
PDB; 4GIF; X-ray; 2.80 A; A=699-743.
PDBsum; 3TE3; -.
PDBsum; 4GIF; -.
ProteinModelPortal; Q9P0L9; -.
SMR; Q9P0L9; -.
BioGrid; 114499; 2.
IntAct; Q9P0L9; 2.
MINT; MINT-3973148; -.
STRING; 9606.ENSP00000325296; -.
GuidetoPHARMACOLOGY; 505; -.
TCDB; 1.A.5.1.3; the polycystin cation channel (pcc) family.
iPTMnet; Q9P0L9; -.
PhosphoSitePlus; Q9P0L9; -.
BioMuta; PKD2L1; -.
DMDM; 23821938; -.
PaxDb; Q9P0L9; -.
PeptideAtlas; Q9P0L9; -.
PRIDE; Q9P0L9; -.
DNASU; 9033; -.
Ensembl; ENST00000318222; ENSP00000325296; ENSG00000107593. [Q9P0L9-1]
GeneID; 9033; -.
KEGG; hsa:9033; -.
UCSC; uc001kqx.2; human. [Q9P0L9-1]
CTD; 9033; -.
DisGeNET; 9033; -.
EuPathDB; HostDB:ENSG00000107593.16; -.
GeneCards; PKD2L1; -.
HGNC; HGNC:9011; PKD2L1.
HPA; CAB022621; -.
MIM; 604532; gene.
neXtProt; NX_Q9P0L9; -.
OpenTargets; ENSG00000107593; -.
PharmGKB; PA33344; -.
eggNOG; KOG3599; Eukaryota.
eggNOG; ENOG410XTGE; LUCA.
GeneTree; ENSGT00700000104221; -.
HOGENOM; HOG000230858; -.
HOVERGEN; HBG014945; -.
InParanoid; Q9P0L9; -.
KO; K04990; -.
OMA; FSTFVKC; -.
OrthoDB; EOG091G034F; -.
PhylomeDB; Q9P0L9; -.
TreeFam; TF316484; -.
GeneWiki; PKD2L1; -.
GenomeRNAi; 9033; -.
PRO; PR:Q9P0L9; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107593; -.
CleanEx; HS_PKD2L1; -.
ExpressionAtlas; Q9P0L9; baseline and differential.
Genevisible; Q9P0L9; HS.
GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; ISS:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; IPI:BHF-UCL.
GO; GO:0005227; F:calcium activated cation channel activity; IDA:BHF-UCL.
GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:BHF-UCL.
GO; GO:0005261; F:cation channel activity; IDA:BHF-UCL.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
GO; GO:0051371; F:muscle alpha-actinin binding; IPI:BHF-UCL.
GO; GO:0005272; F:sodium channel activity; IDA:BHF-UCL.
GO; GO:0033040; F:sour taste receptor activity; IEA:Ensembl.
GO; GO:0006812; P:cation transport; ISS:BHF-UCL.
GO; GO:0071468; P:cellular response to acidic pH; ISS:BHF-UCL.
GO; GO:0001581; P:detection of chemical stimulus involved in sensory perception of sour taste; ISS:BHF-UCL.
GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
GO; GO:0050915; P:sensory perception of sour taste; IMP:UniProtKB.
GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; IDA:BHF-UCL.
InterPro; IPR013122; PKD1_2_channel.
InterPro; IPR003915; PKD_2.
Pfam; PF08016; PKD_channel; 1.
PRINTS; PR01433; POLYCYSTIN2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Cell membrane; Cell projection; Cilium;
Coiled coil; Complete proteome; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Ion channel; Ion transport; Membrane; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 805 Polycystic kidney disease 2-like 1
protein.
/FTId=PRO_0000164360.
TOPO_DOM 1 103 Cytoplasmic. {ECO:0000255}.
TRANSMEM 104 124 Helical. {ECO:0000255}.
TOPO_DOM 125 313 Extracellular. {ECO:0000255}.
TRANSMEM 314 334 Helical. {ECO:0000255}.
TOPO_DOM 335 347 Cytoplasmic. {ECO:0000255}.
TRANSMEM 348 368 Helical. {ECO:0000255}.
TOPO_DOM 369 384 Extracellular. {ECO:0000255}.
TRANSMEM 385 405 Helical. {ECO:0000255}.
TOPO_DOM 406 476 Cytoplasmic. {ECO:0000255}.
TRANSMEM 477 497 Helical. {ECO:0000255}.
TOPO_DOM 498 511 Extracellular. {ECO:0000255}.
INTRAMEM 512 526 Pore-forming.
{ECO:0000250|UniProtKB:Q13563}.
TOPO_DOM 527 539 Extracellular. {ECO:0000255}.
TRANSMEM 540 560 Helical. {ECO:0000255}.
TOPO_DOM 561 805 Cytoplasmic. {ECO:0000255}.
DOMAIN 633 668 EF-hand.
CA_BIND 646 657 {ECO:0000255}.
REGION 704 763 Required for protein homotrimerization.
COILED 650 686 {ECO:0000255}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 210 223 {ECO:0000250|UniProtKB:Q13563}.
VAR_SEQ 225 344 Missing (in isoform 4).
{ECO:0000303|PubMed:10602361}.
/FTId=VSP_004728.
VAR_SEQ 245 319 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_004729.
VAR_SEQ 638 666 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_053718.
VAR_SEQ 751 760 KEQAIWKHPQ -> RFPIKEKRKP (in isoform 2).
{ECO:0000305}.
/FTId=VSP_004730.
VAR_SEQ 761 805 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_004731.
VARIANT 278 278 R -> Q (in dbSNP:rs17112895).
/FTId=VAR_050555.
VARIANT 378 378 R -> W (in dbSNP:rs7909153).
/FTId=VAR_050556.
VARIANT 393 393 V -> I (in dbSNP:rs2278842).
{ECO:0000269|PubMed:9748274}.
/FTId=VAR_024569.
VARIANT 681 681 R -> L (in dbSNP:rs6584356).
/FTId=VAR_024570.
VARIANT 788 788 A -> D (in dbSNP:rs12782963).
/FTId=VAR_050557.
MUTAGEN 523 525 DFD->AFA: Abolishes ion channel activity.
{ECO:0000269|PubMed:24336289}.
MUTAGEN 523 523 D->Q: Increased permeability of
dimethylamine and trimethylamine and
decreased permeability of magnesium.
{ECO:0000269|PubMed:23212381}.
MUTAGEN 525 525 D->K: Increased permeability of
dimethylamine and trimethylamine and
decreased permeability of magnesium.
{ECO:0000269|PubMed:23212381}.
MUTAGEN 530 530 D->A: Does not affect ion channel
activity.
MUTAGEN 710 710 L->A: Abolishes homotrimer formation;
when associated with A-714; A-717; A-728;
A-731 and A-735.
{ECO:0000269|PubMed:22193359}.
MUTAGEN 714 714 V->A: Abolishes homotrimer formation;
when associated with A-710; A-717; A-728;
A-731 and A-735.
{ECO:0000269|PubMed:22193359}.
MUTAGEN 717 717 L->A: Abolishes homotrimer formation;
when associated with A-710; A-714; A-728;
A-731 and A-735.
{ECO:0000269|PubMed:22193359}.
MUTAGEN 728 728 I->A: Abolishes homotrimer formation;
when associated with A-710; A-714; A-717;
A-731 and A-735.
{ECO:0000269|PubMed:22193359}.
MUTAGEN 731 731 V->A: Abolishes homotrimer formation;
when associated with A-710; A-714; A-717;
A-728 and A-735.
{ECO:0000269|PubMed:22193359}.
MUTAGEN 735 735 L->A: Abolishes homotrimer formation;
when associated with A-710; A-714; A-717;
A-728 and A-731.
{ECO:0000269|PubMed:22193359}.
CONFLICT 13 13 Q -> H (in Ref. 1; AAD41638).
{ECO:0000305}.
HELIX 704 731 {ECO:0000244|PDB:3TE3}.
HELIX 734 741 {ECO:0000244|PDB:4GIF}.
SEQUENCE 805 AA; 91982 MW; 3714C07F4B71F9C6 CRC64;
MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP KKPEDEPQET
AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT LRELLVYIVF LVDICLLTYG
MTSSSAYYYT KVMSELFLHT PSDTGVSFQA ISSMADFWDF AQGPLLDSLY WTKWYNNQSL
GHGSHSFIYY ENMLLGVPRL RQLKVRNDSC VVHEDFREDI LSCYDVYSPD KEEQLPFGPF
NGTAWTYHSQ DELGGFSHWG RLTSYSGGGY YLDLPGSRQG SAEALRALQE GLWLDRGTRV
VFIDFSVYNA NINLFCVLRL VVEFPATGGA IPSWQIRTVK LIRYVSNWDF FIVGCEVIFC
VFIFYYVVEE ILELHIHRLR YLSSIWNILD LVVILLSIVA VGFHIFRTLE VNRLMGKLLQ
QPNTYADFEF LAFWQTQYNN MNAVNLFFAW IKIFKYISFN KTMTQLSSTL ARCAKDILGF
AVMFFIVFFA YAQLGYLLFG TQVENFSTFI KCIFTQFRII LGDFDYNAID NANRILGPAY
FVTYVFFVFF VLLNMFLAII NDTYSEVKEE LAGQKDELQL SDLLKQGYNK TLLRLRLRKE
RVSDVQKVLQ GGEQEIQFED FTNTLRELGH AEHEITELTA TFTKFDRDGN RILDEKEQEK
MRQDLEEERV ALNTEIEKLG RSIVSSPQGK SGPEAARAGG WVSGEEFYML TRRVLQLETV
LEGVVSQIDA VGSKLKMLER KGWLAPSPGV KEQAIWKHPQ PAPAVTPDPW GVQGGQESEV
PYKREEEALE ERRLSRGEIP TLQRS


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