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

 PK2L1_MOUSE             Reviewed;         760 AA.
A2A259; Q14B55; Q14B73; Q80ZH4;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
05-DEC-2018, entry version 86.
RecName: Full=Polycystic kidney disease 2-like 1 protein;
AltName: Full=Polycystin-2 homolog;
Name=Pkd2l1; Synonyms=Trpp3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
INTERACTION WITH PKD1L3, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=16891422; DOI=10.1073/pnas.0602702103;
Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M.,
Matsunami H.;
"Transient receptor potential family members PKD1L3 and PKD2L1 form a
candidate sour taste receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
Guo L., Zhou J.;
"Cloning and gene targeting of murine Pkdl gene.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PKD1, TISSUE
SPECIFICITY, AND MUTAGENESIS OF LYS-568 AND ASP-576.
PubMed=15548533; DOI=10.1074/jbc.M411496200;
Murakami M., Ohba T., Xu F., Shida S., Satoh E., Ono K., Miyoshi I.,
Watanabe H., Ito H., Iijima T.;
"Genomic organization and functional analysis of murine PKD2L1.";
J. Biol. Chem. 280:5626-5635(2005).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16929298; DOI=10.1038/nature05084;
Huang A.L., Chen X., Hoon M.A., Chandrashekar J., Guo W., Trankner D.,
Ryba N.J., Zuker C.S.;
"The cells and logic for mammalian sour taste detection.";
Nature 442:934-938(2006).
[7]
TISSUE SPECIFICITY.
PubMed=18156604; DOI=10.1093/chemse/bjm083;
Kataoka S., Yang R., Ishimaru Y., Matsunami H., Sevigny J.,
Kinnamon J.C., Finger T.E.;
"The candidate sour taste receptor, PKD2L1, is expressed by type III
taste cells in the mouse.";
Chem. Senses 33:243-254(2008).
[8]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
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).
[9]
FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND SUBUNIT.
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).
[10]
FUNCTION.
PubMed=19833970; DOI=10.1126/science.1174601;
Chandrashekar J., Yarmolinsky D., von Buchholtz L., Oka Y., Sly W.,
Ryba N.J., Zuker C.S.;
"The taste of carbonation.";
Science 326:443-445(2009).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PKD1L3.
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).
[12]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=20406802; DOI=10.1074/jbc.C110.132944;
Kawaguchi H., Yamanaka A., Uchida K., Shibasaki K., Sokabe T.,
Maruyama Y., Yanagawa Y., Murakami S., Tominaga M.;
"Activation of polycystic kidney disease-2-like 1 (PKD2L1)-PKD1L3
complex by acid in mouse taste cells.";
J. Biol. Chem. 285:17277-17281(2010).
[13]
FUNCTION.
PubMed=21098668; DOI=10.1073/pnas.1013664107;
Chang R.B., Waters H., Liman E.R.;
"A proton current drives action potentials in genetically identified
sour taste cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:22320-22325(2010).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-523; ASP-525
AND ASP-530.
PubMed=21185261; DOI=10.1016/j.bbrc.2010.12.086;
Fujimoto C., Ishimaru Y., Katano Y., Misaka T., Yamasoba T.,
Asakura T., Abe K.;
"The single pore residue Asp523 in PKD2L1 determines Ca2+ permeation
of the PKD1L3/PKD2L1 complex.";
Biochem. Biophys. Res. Commun. 404:946-951(2011).
[15]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=21625513; DOI=10.1371/journal.pone.0020007;
Horio N., Yoshida R., Yasumatsu K., Yanagawa Y., Ishimaru Y.,
Matsunami H., Ninomiya Y.;
"Sour taste responses in mice lacking PKD channels.";
PLoS ONE 6:E20007-E20007(2011).
[16]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
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]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24336288; DOI=10.1038/nature12833;
Delling M., DeCaen P.G., Doerner J.F., Febvay S., Clapham D.E.;
"Primary cilia are specialized calcium signalling organelles.";
Nature 504:311-314(2013).
[18]
FUNCTION, AND INTERACTION WITH PKD1L1.
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]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=25820328; DOI=10.1038/srep09460;
Zheng W., Hussein S., Yang J., Huang J., Zhang F.,
Hernandez-Anzaldo S., Fernandez-Patron C., Cao Y., Zeng H., Tang J.,
Chen X.Z.;
"A novel PKD2L1 C-terminal domain critical for trimerization and
channel function.";
Sci. Rep. 5:9460-9460(2015).
[20]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF ASN-531 AND ASN-533.
PubMed=28904867; DOI=10.1002/2211-5463.12273;
Shimizu T., Higuchi T., Toba T., Ohno C., Fujii T., Nilius B.,
Sakai H.;
"The asparagine 533 residue in the outer pore loop region of the mouse
PKD2L1 channel is essential for its voltage-dependent inactivation.";
FEBS Open Bio 7:1392-1401(2017).
[21]
FUNCTION.
PubMed=28553944; DOI=10.1038/nn.4575;
Zocchi D., Wennemuth G., Oka Y.;
"The cellular mechanism for water detection in the mammalian taste
system.";
Nat. Neurosci. 20:927-933(2017).
[22] {ECO:0000244|PDB:5Z1W}
STRUCTURE BY ELECTRON MICROSCOPY (3.38 ANGSTROMS) OF 64-629, FUNCTION,
ACTIVITY REGULATION, SUBUNIT, TOPOLOGY, MUTAGENESIS OF GLY-522 AND
ILE-560, GLYCOSYLATION AT ASN-177; ASN-207 AND ASN-241, AND DISULFIDE
BOND.
PubMed=29567962; DOI=10.1038/s41467-018-03606-0;
Su Q., Hu F., Liu Y., Ge X., Mei C., Yu S., Shen A., Zhou Q., Yan C.,
Lei J., Zhang Y., Liu X., Wang T.;
"Cryo-EM structure of the polycystic kidney disease-like channel
PKD2L1.";
Nat. Commun. 9:1192-1192(2018).
-!- FUNCTION: Pore-forming subunit of a heteromeric, non-selective
cation channel that is permeable to Ca(2+) (PubMed:16891422,
PubMed:15548533, PubMed:19464260, PubMed:20538909,
PubMed:21185261, PubMed:22420714, PubMed:25820328,
PubMed:28904867, PubMed:29567962). Pore-forming subunit of a
calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in
primary cilia, where it controls cilium calcium concentration, but
does not affect cytoplasmic calcium concentration
(PubMed:24336288, PubMed:24336289). The channel formed by PKD1L2
and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling
and GLI2 transcription (PubMed:24336288). Pore-forming subunit of
a channel formed by PKD1L2 and PKD1L3 that contributes to sour
taste perception in gustatory cells (PubMed:16891422,
PubMed:16929298, PubMed:20406802, PubMed:21098668,
PubMed:21625513). The heteromeric channel formed by PKD1L2 and
PKD1L3 is activated by low pH, but opens only when the
extracellular pH rises again (PubMed:18535624, PubMed:19464260,
PubMed:20538909, PubMed:20406802, PubMed:22420714,
PubMed:28904867, PubMed:29567962). May play a role in the
perception of carbonation taste (PubMed:19833970). May play a role
in the sensory perception of water, via a mechanism that activates
the channel in response to dilution of salivary bicarbonate and
changes in salivary pH (PubMed:28553944).
{ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18535624,
ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:19833970,
ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909,
ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21185261,
ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:22420714,
ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289,
ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:28553944,
ECO:0000269|PubMed:28904867, ECO:0000269|PubMed:29567962}.
-!- ACTIVITY REGULATION: The ion channel is gated following an off-
response property by acid: gated open after the removal of acid
stimulus, but not during acid application (PubMed:18535624,
PubMed:19464260, PubMed:20406802, PubMed:22420714,
PubMed:28904867, PubMed:29567962). Responses to acid stimulus are
inhibited by capsaicin (PubMed:22420714).
{ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260,
ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:22420714,
ECO:0000269|PubMed:28904867, ECO:0000269|PubMed:29567962}.
-!- SUBUNIT: Homotetramer (PubMed:25820328, PubMed:29567962).
Heterotetramer with either PKD1L1, PKD1L3 or PKD1; the
heterotetrameric complex probably contains 3 PKD1L2 chains plus
one chain from another family member (PubMed:16891422,
PubMed:15548533, PubMed:25820328, PubMed:29567962). Interacts with
PKD1L1, forming a ciliary calcium channel (PubMed:24336289).
Interacts with PKD1L3, forming a cation channel that is activated
by low extracellular pH (PubMed:16891422, PubMed:18535624,
PubMed:19464260, PubMed:20538909, PubMed:20406802,
PubMed:22420714, PubMed:25820328, PubMed:29567962). Interacts with
PKD1 (PubMed:15548533). Interacts with RACK1; inhibits the channel
activity possibly by impairing localization to the cell membrane
(By similarity). {ECO:0000250|UniProtKB:Q9P0L9,
ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260,
ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909,
ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:24336289,
ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:29567962}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15594711, EBI-15594711;
Q2EG98:Pkd1l3; NbExp=2; IntAct=EBI-15594711, EBI-15594779;
-!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
{ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}; Multi-
pass membrane protein {ECO:0000269|PubMed:29567962}. Cell membrane
{ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260,
ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909,
ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:22420714,
ECO:0000269|PubMed:25820328}; Multi-pass membrane protein
{ECO:0000269|PubMed:29567962}. Cytoplasmic vesicle
{ECO:0000305|PubMed:20538909}. Note=Interaction with PKD1 or
PKD1L3 is required for localization to the cell membrane.
{ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}.
-!- TISSUE SPECIFICITY: Detected in kidney, testis and brain,
(PubMed:25820328). Expressed in all 4 taste areas in taste buds.
Detected in the taste pore region of circumvallate papillae,
foliate papillae, fungiform papillae and palate (PubMed:16891422,
PubMed:16929298, PubMed:20538909, PubMed:21625513). Expressed in
cells distinct from those mediating sweet, umami and bitter taste
(at protein level) (PubMed:16891422). Expressed in type III taste
cells (at protein level) (PubMed:18156604). Ubiquitous
(PubMed:15548533). Detected in circumvallate, foliate, fungiform
and palate taste buds, in cells distinct from those mediating
sweet, umami and bitter taste (PubMed:16929298, PubMed:21625513).
Detected in taste tissues and testis (PubMed:16891422).
{ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18156604,
ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21625513,
ECO:0000269|PubMed:25820328}.
-!- DOMAIN: The EF-hand domain probably mediates calcium-binding. It
is not required for channel activation.
{ECO:0000250|UniProtKB:Q9P0L9}.
-!- DOMAIN: Interaction of the cytoplasmic N- and C-terminal domains
is important for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}.
-!- PTM: Palmitoylation is important for expression at the cell
membrane and for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}.
-!- DISRUPTION PHENOTYPE: Intestinal malrotation in 50% of animals,
while other organs do not show major organ laterality defects.
Intestinal malformations are associated with SHH pathway defects
during early development (PubMed:24336288). Partial reduction of
chorda tympani nerve response to sour stimuli, without affecting
sweet, salty, bitter, and umami perception (PubMed:21625513).
{ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:24336288}.
-!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
-!- CAUTION: The active channel complex is an obligate tetramer
(PubMed:29567962). In contrast, the isolated cytoplasmic C-
terminal domain forms homotrimers in vitro (PubMed:25820328).
Likewise, photobleaching experiments suggest formation of
homotrimers in the membrane (By similarity).
{ECO:0000250|UniProtKB:Q9P0L9, ECO:0000269|PubMed:25820328,
ECO:0000269|PubMed:29567962}.
-!- CAUTION: Pkd1l3 and Pkd2l1 have been defined as sour taste
receptor in gustatory cells based on a number of indirect
evidences: Pkd2l1 is expressed in a subset of taste receptor cells
distinct from those responsible for sweet, bitter and unami taste
and genetic elimination of cells expressing Pkd2l1 reduces
gustatory nerve responses to sour taste stimuli (PubMed:16891422,
PubMed:16929298). However, a number of experiments have recently
shown that the sour taste receptor activity is probably indirect:
mice lacking Pkd2l1 only show partial defects in sour taste
perception (PubMed:21625513). Moreover, the PKD1L3-PKD2L1
heteromer, when expressed in cells does not respond to acid
stimuli used to evoke proton currents in taste cells
(PubMed:21098668). {ECO:0000305|PubMed:16891422,
ECO:0000305|PubMed:16929298, ECO:0000305|PubMed:21098668,
ECO:0000305|PubMed:21625513}.
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EMBL; AB290927; BAF45380.1; -; mRNA.
EMBL; AF271381; AAK58371.1; -; mRNA.
EMBL; AC125101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC116297; AAI16298.1; -; mRNA.
EMBL; BC116323; AAI16324.2; -; mRNA.
CCDS; CCDS29846.1; -.
RefSeq; NP_852087.2; NM_181422.3.
UniGene; Mm.308481; -.
PDB; 5Z1W; EM; 3.38 A; A/B/C/D=64-629.
PDBsum; 5Z1W; -.
ProteinModelPortal; A2A259; -.
SMR; A2A259; -.
BioGrid; 236700; 1.
DIP; DIP-61250N; -.
IntAct; A2A259; 1.
STRING; 10090.ENSMUSP00000045675; -.
TCDB; 1.A.5.2.2; the polycystin cation channel (pcc) family.
PhosphoSitePlus; A2A259; -.
PaxDb; A2A259; -.
PeptideAtlas; A2A259; -.
PRIDE; A2A259; -.
Ensembl; ENSMUST00000042026; ENSMUSP00000045675; ENSMUSG00000037578.
GeneID; 329064; -.
KEGG; mmu:329064; -.
UCSC; uc008hpm.2; mouse.
CTD; 9033; -.
MGI; MGI:1352448; Pkd2l1.
eggNOG; KOG3599; Eukaryota.
eggNOG; ENOG410XTGE; LUCA.
GeneTree; ENSGT00940000157274; -.
HOGENOM; HOG000230858; -.
HOVERGEN; HBG014945; -.
InParanoid; A2A259; -.
KO; K04990; -.
OMA; FSTFVKC; -.
OrthoDB; EOG091G034F; -.
PhylomeDB; A2A259; -.
TreeFam; TF316484; -.
PRO; PR:A2A259; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000037578; Expressed in 31 organ(s), highest expression level in lumbar subsegment of spinal cord.
Genevisible; A2A259; MM.
GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
GO; GO:0034703; C:cation channel complex; IDA:BHF-UCL.
GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0097730; C:non-motile cilium; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IPI:MGI.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
GO; GO:0005227; F:calcium activated cation channel activity; ISO:MGI.
GO; GO:0005262; F:calcium channel activity; IMP:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:MGI.
GO; GO:0005261; F:cation channel activity; IDA:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051371; F:muscle alpha-actinin binding; ISO:MGI.
GO; GO:0005272; F:sodium channel activity; ISO:MGI.
GO; GO:0006812; P:cation transport; IDA:BHF-UCL.
GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB.
GO; GO:0001581; P:detection of chemical stimulus involved in sensory perception of sour taste; IDA:BHF-UCL.
GO; GO:0050912; P:detection of chemical stimulus involved in sensory perception of taste; IMP:UniProtKB.
GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0009415; P:response to water; IMP:UniProtKB.
GO; GO:0050915; P:sensory perception of sour taste; ISO:MGI.
GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR013122; PKD1_2_channel.
InterPro; IPR003915; PKD_2.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF08016; PKD_channel; 1.
PRINTS; PR01433; POLYCYSTIN2.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS50222; EF_HAND_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Calcium channel; Calcium transport;
Cell membrane; Cell projection; Cilium; Coiled coil;
Complete proteome; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 760 Polycystic kidney disease 2-like 1
protein.
/FTId=PRO_0000425551.
TOPO_DOM 1 103 Cytoplasmic.
{ECO:0000305|PubMed:29567962}.
TRANSMEM 104 124 Helical. {ECO:0000305|PubMed:29567962}.
TOPO_DOM 125 356 Extracellular.
{ECO:0000305|PubMed:29567962}.
TRANSMEM 357 376 Helical. {ECO:0000305|PubMed:29567962}.
TOPO_DOM 377 384 Cytoplasmic.
{ECO:0000305|PubMed:29567962}.
TRANSMEM 385 405 Helical. {ECO:0000305|PubMed:29567962}.
TOPO_DOM 406 433 Extracellular.
{ECO:0000305|PubMed:29567962}.
TRANSMEM 434 454 Helical. {ECO:0000305|PubMed:29567962}.
TOPO_DOM 455 479 Cytoplasmic.
{ECO:0000305|PubMed:29567962}.
TRANSMEM 480 499 Helical. {ECO:0000305|PubMed:29567962}.
TOPO_DOM 500 511 Extracellular.
{ECO:0000305|PubMed:29567962}.
INTRAMEM 512 526 Pore-forming.
{ECO:0000305|PubMed:29567962}.
TOPO_DOM 527 536 Extracellular.
{ECO:0000305|PubMed:29567962}.
TRANSMEM 537 557 Helical. {ECO:0000305|PubMed:29567962}.
TOPO_DOM 558 760 Cytoplasmic.
{ECO:0000305|PubMed:29567962}.
DOMAIN 630 665 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 643 654 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 701 760 Required for homooligomerization.
{ECO:0000250}.
COILED 559 580 {ECO:0000255}.
COILED 650 682 {ECO:0000255}.
LIPID 38 38 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9P0L9}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5Z1W,
ECO:0000269|PubMed:29567962}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5Z1W,
ECO:0000269|PubMed:29567962}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5Z1W,
ECO:0000269|PubMed:29567962}.
CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 210 223 {ECO:0000244|PDB:5Z1W,
ECO:0000269|PubMed:29567962}.
MUTAGEN 522 522 G->L: Loss of channel activity.
{ECO:0000269|PubMed:29567962}.
MUTAGEN 523 523 D->E: Little or no effect on calcium
channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 523 523 D->N: Impaired calcium channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 525 525 D->N: Little or no effect on calcium
channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 530 530 D->N: Little or no effect on calcium
channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 531 531 N->Q: No effect on activation by low pH.
{ECO:0000269|PubMed:28904867}.
MUTAGEN 533 533 N->Q: Loss of activation by low pH.
{ECO:0000269|PubMed:28904867}.
MUTAGEN 560 560 I->F: Loss of channel activity.
{ECO:0000269|PubMed:29567962}.
MUTAGEN 568 568 K->A: Increases localization at the cell
surface when expressed in absence of
PKD1. {ECO:0000269|PubMed:15548533}.
MUTAGEN 576 576 D->A: Induces localization to the
endoplasmic reticulum when expressed in
absence of PKD1.
{ECO:0000269|PubMed:15548533}.
CONFLICT 114 114 I -> V (in Ref. 2; AAK58371 and 4;
AAI16324/AAI16298). {ECO:0000305}.
CONFLICT 202 203 QL -> HV (in Ref. 2; AAK58371).
{ECO:0000305}.
CONFLICT 438 438 Y -> D (in Ref. 2; AAK58371).
{ECO:0000305}.
CONFLICT 482 482 I -> V (in Ref. 2; AAK58371).
{ECO:0000305}.
CONFLICT 756 756 L -> P (in Ref. 4; AAI16324/AAI16298).
{ECO:0000305}.
HELIX 102 119 {ECO:0000244|PDB:5Z1W}.
HELIX 126 137 {ECO:0000244|PDB:5Z1W}.
HELIX 154 161 {ECO:0000244|PDB:5Z1W}.
HELIX 164 167 {ECO:0000244|PDB:5Z1W}.
TURN 189 191 {ECO:0000244|PDB:5Z1W}.
STRAND 192 205 {ECO:0000244|PDB:5Z1W}.
TURN 214 219 {ECO:0000244|PDB:5Z1W}.
TURN 250 254 {ECO:0000244|PDB:5Z1W}.
STRAND 261 265 {ECO:0000244|PDB:5Z1W}.
STRAND 269 273 {ECO:0000244|PDB:5Z1W}.
HELIX 278 290 {ECO:0000244|PDB:5Z1W}.
STRAND 298 309 {ECO:0000244|PDB:5Z1W}.
TURN 310 313 {ECO:0000244|PDB:5Z1W}.
STRAND 314 323 {ECO:0000244|PDB:5Z1W}.
STRAND 331 339 {ECO:0000244|PDB:5Z1W}.
HELIX 347 371 {ECO:0000244|PDB:5Z1W}.
HELIX 386 420 {ECO:0000244|PDB:5Z1W}.
STRAND 422 424 {ECO:0000244|PDB:5Z1W}.
HELIX 429 451 {ECO:0000244|PDB:5Z1W}.
HELIX 452 456 {ECO:0000244|PDB:5Z1W}.
HELIX 481 498 {ECO:0000244|PDB:5Z1W}.
STRAND 499 502 {ECO:0000244|PDB:5Z1W}.
HELIX 509 520 {ECO:0000244|PDB:5Z1W}.
HELIX 526 532 {ECO:0000244|PDB:5Z1W}.
HELIX 536 561 {ECO:0000244|PDB:5Z1W}.
SEQUENCE 760 AA; 87234 MW; 4C76777051CFC2EF CRC64;
MNSMESPKNQ ELQTLGNRAW DNPAYSDPPS PNRTLRICTV SSVALPETQP KKPEVRCQEK
TQRTLVSSCC LHICRSIRGL WGTTLTENTA ENRELYVKTT LRELVVYIVF LVDICLLTYG
MTSSSAYYYT KVMSELFLHT PSDSGVSFQT ISSMSDFWDF AQGPLLDSLY WTKWYNNQSL
GRGSHSFIYY ENLLLGAPRL RQLRVRNDSC VVHEDFREDI LNCYDVYSPD KEDQLPFGPQ
NGTAWTYHSQ NELGGSSHWG RLTSYSGGGY YLDLPGSRQA SAEALQGLQE GLWLDRGTRV
VFIDFSVYNA NINLFCILRL VVEFPATGGT IPSWQIRTVK LIRYVNNWDF FIVGCEVVFC
VFIFYYVVEE ILEIHLHRLR YLSSVWNILD LVVILLSIVA VGFHIFRTLE VNRLMGKLLQ
QPDTYADFEF LAFWQTQYNN MNAVNLFFAW IKIFKYISFN KTMTQLSSTL ARCAKDILGF
AIMFFIVFFA YAQLGYLLFG TQVENFSTFV KCIFTQFRII LGDFDYNAID NANRILGPVY
FVTYVFFVFF VLLNMFLAII NDTYSEVKEE LAGQKDQLQL SDFLKQSYNK TLLRLRLRKE
RVSDVQKVLK GGEPEIQFED FTSTLRELGH EEHEITAAFT RFDQDGDHIL DEEEQEQMRQ
GLEEERVTLN AEIENLGRSV GHSPPGELGA EAARGQSWVS GEEFDMLTRR VLQLQCVLEG
VVSQIDAVGS KLKMLERKGE LAPSPGMGEP AVWENLYNPS


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