PK2L1_MOUSE
ID PK2L1_MOUSE Reviewed; 760 AA.
AC A2A259; Q14B55; Q14B73; Q80ZH4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Polycystic kidney disease 2-like 1 protein;
DE AltName: Full=Polycystin-2 homolog;
GN Name=Pkd2l1; Synonyms=Trpp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH PKD1L3, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=16891422; DOI=10.1073/pnas.0602702103;
RA Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M., Matsunami H.;
RT "Transient receptor potential family members PKD1L3 and PKD2L1 form a
RT candidate sour taste receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Guo L., Zhou J.;
RT "Cloning and gene targeting of murine Pkdl gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PKD1, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF LYS-568 AND ASP-576.
RX PubMed=15548533; DOI=10.1074/jbc.m411496200;
RA Murakami M., Ohba T., Xu F., Shida S., Satoh E., Ono K., Miyoshi I.,
RA Watanabe H., Ito H., Iijima T.;
RT "Genomic organization and functional analysis of murine PKD2L1.";
RL J. Biol. Chem. 280:5626-5635(2005).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16929298; DOI=10.1038/nature05084;
RA Huang A.L., Chen X., Hoon M.A., Chandrashekar J., Guo W., Trankner D.,
RA Ryba N.J., Zuker C.S.;
RT "The cells and logic for mammalian sour taste detection.";
RL Nature 442:934-938(2006).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=18156604; DOI=10.1093/chemse/bjm083;
RA Kataoka S., Yang R., Ishimaru Y., Matsunami H., Sevigny J., Kinnamon J.C.,
RA Finger T.E.;
RT "The candidate sour taste receptor, PKD2L1, is expressed by type III taste
RT cells in the mouse.";
RL Chem. Senses 33:243-254(2008).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18535624; DOI=10.1038/embor.2008.89;
RA Inada H., Kawabata F., Ishimaru Y., Fushiki T., Matsunami H., Tominaga M.;
RT "Off-response property of an acid-activated cation channel complex PKD1L3-
RT PKD2L1.";
RL EMBO Rep. 9:690-697(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=19464260; DOI=10.1016/j.bbrc.2009.05.069;
RA Ishii S., Misaka T., Kishi M., Kaga T., Ishimaru Y., Abe K.;
RT "Acetic acid activates PKD1L3-PKD2L1 channel--a candidate sour taste
RT receptor.";
RL Biochem. Biophys. Res. Commun. 385:346-350(2009).
RN [10]
RP FUNCTION.
RX PubMed=19833970; DOI=10.1126/science.1174601;
RA Chandrashekar J., Yarmolinsky D., von Buchholtz L., Oka Y., Sly W.,
RA Ryba N.J., Zuker C.S.;
RT "The taste of carbonation.";
RL Science 326:443-445(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PKD1L3.
RX PubMed=20538909; DOI=10.1096/fj.10-162925;
RA Ishimaru Y., Katano Y., Yamamoto K., Akiba M., Misaka T., Roberts R.W.,
RA Asakura T., Matsunami H., Abe K.;
RT "Interaction between PKD1L3 and PKD2L1 through their transmembrane domains
RT is required for localization of PKD2L1 at taste pores in taste cells of
RT circumvallate and foliate papillae.";
RL FASEB J. 24:4058-4067(2010).
RN [12]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20406802; DOI=10.1074/jbc.c110.132944;
RA Kawaguchi H., Yamanaka A., Uchida K., Shibasaki K., Sokabe T., Maruyama Y.,
RA Yanagawa Y., Murakami S., Tominaga M.;
RT "Activation of polycystic kidney disease-2-like 1 (PKD2L1)-PKD1L3 complex
RT by acid in mouse taste cells.";
RL J. Biol. Chem. 285:17277-17281(2010).
RN [13]
RP FUNCTION.
RX PubMed=21098668; DOI=10.1073/pnas.1013664107;
RA Chang R.B., Waters H., Liman E.R.;
RT "A proton current drives action potentials in genetically identified sour
RT taste cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22320-22325(2010).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-523; ASP-525 AND
RP ASP-530.
RX PubMed=21185261; DOI=10.1016/j.bbrc.2010.12.086;
RA Fujimoto C., Ishimaru Y., Katano Y., Misaka T., Yamasoba T., Asakura T.,
RA Abe K.;
RT "The single pore residue Asp523 in PKD2L1 determines Ca2+ permeation of the
RT PKD1L3/PKD2L1 complex.";
RL Biochem. Biophys. Res. Commun. 404:946-951(2011).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21625513; DOI=10.1371/journal.pone.0020007;
RA Horio N., Yoshida R., Yasumatsu K., Yanagawa Y., Ishimaru Y., Matsunami H.,
RA Ninomiya Y.;
RT "Sour taste responses in mice lacking PKD channels.";
RL PLoS ONE 6:E20007-E20007(2011).
RN [16]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=22420714; DOI=10.1111/j.1742-4658.2012.08566.x;
RA Ishii S., Kurokawa A., Kishi M., Yamagami K., Okada S., Ishimaru Y.,
RA Misaka T.;
RT "The response of PKD1L3/PKD2L1 to acid stimuli is inhibited by capsaicin
RT and its pungent analogs.";
RL FEBS J. 279:1857-1870(2012).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24336288; DOI=10.1038/nature12833;
RA Delling M., DeCaen P.G., Doerner J.F., Febvay S., Clapham D.E.;
RT "Primary cilia are specialized calcium signalling organelles.";
RL Nature 504:311-314(2013).
RN [18]
RP FUNCTION, AND INTERACTION WITH PKD1L1.
RX PubMed=24336289; DOI=10.1038/nature12832;
RA DeCaen P.G., Delling M., Vien T.N., Clapham D.E.;
RT "Direct recording and molecular identification of the calcium channel of
RT primary cilia.";
RL Nature 504:315-318(2013).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=25820328; DOI=10.1038/srep09460;
RA Zheng W., Hussein S., Yang J., Huang J., Zhang F., Hernandez-Anzaldo S.,
RA Fernandez-Patron C., Cao Y., Zeng H., Tang J., Chen X.Z.;
RT "A novel PKD2L1 C-terminal domain critical for trimerization and channel
RT function.";
RL Sci. Rep. 5:9460-9460(2015).
RN [20]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASN-531 AND ASN-533.
RX PubMed=28904867; DOI=10.1002/2211-5463.12273;
RA Shimizu T., Higuchi T., Toba T., Ohno C., Fujii T., Nilius B., Sakai H.;
RT "The asparagine 533 residue in the outer pore loop region of the mouse
RT PKD2L1 channel is essential for its voltage-dependent inactivation.";
RL FEBS Open Bio 7:1392-1401(2017).
RN [21]
RP FUNCTION.
RX PubMed=28553944; DOI=10.1038/nn.4575;
RA Zocchi D., Wennemuth G., Oka Y.;
RT "The cellular mechanism for water detection in the mammalian taste
RT system.";
RL Nat. Neurosci. 20:927-933(2017).
RN [22] {ECO:0007744|PDB:5Z1W}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.38 ANGSTROMS) OF 64-629, FUNCTION,
RP ACTIVITY REGULATION, SUBUNIT, TOPOLOGY, MUTAGENESIS OF GLY-522 AND ILE-560,
RP GLYCOSYLATION AT ASN-177; ASN-207 AND ASN-241, AND DISULFIDE BOND.
RX PubMed=29567962; DOI=10.1038/s41467-018-03606-0;
RA Su Q., Hu F., Liu Y., Ge X., Mei C., Yu S., Shen A., Zhou Q., Yan C.,
RA Lei J., Zhang Y., Liu X., Wang T.;
RT "Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1.";
RL Nat. Commun. 9:1192-1192(2018).
CC -!- FUNCTION: Pore-forming subunit of a heteromeric, non-selective cation
CC channel that is permeable to Ca(2+) (PubMed:16891422, PubMed:15548533,
CC PubMed:19464260, PubMed:20538909, PubMed:21185261, PubMed:22420714,
CC PubMed:25820328, PubMed:28904867, PubMed:29567962). Pore-forming
CC subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1
CC in primary cilia, where it controls cilium calcium concentration, but
CC does not affect cytoplasmic calcium concentration (PubMed:24336288,
CC PubMed:24336289). The channel formed by PKD1L2 and PKD1L1 in primary
CC cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription
CC (PubMed:24336288). Pore-forming subunit of a channel formed by PKD1L2
CC and PKD1L3 that contributes to sour taste perception in gustatory cells
CC (PubMed:16891422, PubMed:16929298, PubMed:20406802, PubMed:21098668,
CC PubMed:21625513). The heteromeric channel formed by PKD1L2 and PKD1L3
CC is activated by low pH, but opens only when the extracellular pH rises
CC again (PubMed:18535624, PubMed:19464260, PubMed:20538909,
CC PubMed:20406802, PubMed:22420714, PubMed:28904867, PubMed:29567962).
CC May play a role in the perception of carbonation taste
CC (PubMed:19833970). May play a role in the sensory perception of water,
CC via a mechanism that activates the channel in response to dilution of
CC salivary bicarbonate and changes in salivary pH (PubMed:28553944).
CC {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
CC ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18535624,
CC ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:19833970,
CC ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909,
CC ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21185261,
CC ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:22420714,
CC ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289,
CC ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:28553944,
CC ECO:0000269|PubMed:28904867, ECO:0000269|PubMed:29567962}.
CC -!- ACTIVITY REGULATION: The ion channel is gated following an off-response
CC property by acid: gated open after the removal of acid stimulus, but
CC not during acid application (PubMed:18535624, PubMed:19464260,
CC PubMed:20406802, PubMed:22420714, PubMed:28904867, PubMed:29567962).
CC Responses to acid stimulus are inhibited by capsaicin
CC (PubMed:22420714). {ECO:0000269|PubMed:18535624,
CC ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:20406802,
CC ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:28904867,
CC ECO:0000269|PubMed:29567962}.
CC -!- SUBUNIT: Homotetramer (PubMed:25820328, PubMed:29567962).
CC Heterotetramer with either PKD1L1, PKD1L3 or PKD1; the heterotetrameric
CC complex probably contains 3 PKD1L2 chains plus one chain from another
CC family member (PubMed:16891422, PubMed:15548533, PubMed:25820328,
CC PubMed:29567962). Interacts with PKD1L1, forming a ciliary calcium
CC channel (PubMed:24336289). Interacts with PKD1L3, forming a cation
CC channel that is activated by low extracellular pH (PubMed:16891422,
CC PubMed:18535624, PubMed:19464260, PubMed:20538909, PubMed:20406802,
CC PubMed:22420714, PubMed:25820328, PubMed:29567962). Interacts with PKD1
CC (PubMed:15548533). Interacts with RACK1; inhibits the channel activity
CC possibly by impairing localization to the cell membrane (By
CC similarity). {ECO:0000250|UniProtKB:Q9P0L9,
CC ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
CC ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260,
CC ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909,
CC ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:24336289,
CC ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:29567962}.
CC -!- INTERACTION:
CC A2A259; Q2EG98: Pkd1l3; NbExp=2; IntAct=EBI-15594711, EBI-15594779;
CC A2A259; A2A259: Pkd2l1; NbExp=2; IntAct=EBI-15594711, EBI-15594711;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:29567962}. Cell membrane
CC {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
CC ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260,
CC ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909,
CC ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:22420714,
CC ECO:0000269|PubMed:25820328}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29567962}. Cytoplasmic vesicle
CC {ECO:0000305|PubMed:20538909}. Note=Interaction with PKD1 or PKD1L3 is
CC required for localization to the cell membrane.
CC {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
CC ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, testis and brain,
CC (PubMed:25820328). Expressed in all 4 taste areas in taste buds.
CC Detected in the taste pore region of circumvallate papillae, foliate
CC papillae, fungiform papillae and palate (PubMed:16891422,
CC PubMed:16929298, PubMed:20538909, PubMed:21625513). Expressed in cells
CC distinct from those mediating sweet, umami and bitter taste (at protein
CC level) (PubMed:16891422). Expressed in type III taste cells (at protein
CC level) (PubMed:18156604). Ubiquitous (PubMed:15548533). Detected in
CC circumvallate, foliate, fungiform and palate taste buds, in cells
CC distinct from those mediating sweet, umami and bitter taste
CC (PubMed:16929298, PubMed:21625513). Detected in taste tissues and
CC testis (PubMed:16891422). {ECO:0000269|PubMed:15548533,
CC ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298,
CC ECO:0000269|PubMed:18156604, ECO:0000269|PubMed:20538909,
CC ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:25820328}.
CC -!- DOMAIN: The EF-hand domain probably mediates calcium-binding. It is not
CC required for channel activation. {ECO:0000250|UniProtKB:Q9P0L9}.
CC -!- DOMAIN: Interaction of the cytoplasmic N- and C-terminal domains is
CC important for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}.
CC -!- PTM: Palmitoylation is important for expression at the cell membrane
CC and for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}.
CC -!- DISRUPTION PHENOTYPE: Intestinal malrotation in 50% of animals, while
CC other organs do not show major organ laterality defects. Intestinal
CC malformations are associated with SHH pathway defects during early
CC development (PubMed:24336288). Partial reduction of chorda tympani
CC nerve response to sour stimuli, without affecting sweet, salty, bitter,
CC and umami perception (PubMed:21625513). {ECO:0000269|PubMed:21625513,
CC ECO:0000269|PubMed:24336288}.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
CC -!- CAUTION: The active channel complex is an obligate tetramer
CC (PubMed:29567962). In contrast, the isolated cytoplasmic C-terminal
CC domain forms homotrimers in vitro (PubMed:25820328). Likewise,
CC photobleaching experiments suggest formation of homotrimers in the
CC membrane (By similarity). {ECO:0000250|UniProtKB:Q9P0L9,
CC ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:29567962}.
CC -!- CAUTION: Pkd1l3 and Pkd2l1 have been defined as sour taste receptor in
CC gustatory cells based on a number of indirect evidences: Pkd2l1 is
CC expressed in a subset of taste receptor cells distinct from those
CC responsible for sweet, bitter and unami taste and genetic elimination
CC of cells expressing Pkd2l1 reduces gustatory nerve responses to sour
CC taste stimuli (PubMed:16891422, PubMed:16929298). However, a number of
CC experiments have recently shown that the sour taste receptor activity
CC is probably indirect: mice lacking Pkd2l1 only show partial defects in
CC sour taste perception (PubMed:21625513). Moreover, the PKD1L3-PKD2L1
CC heteromer, when expressed in cells does not respond to acid stimuli
CC used to evoke proton currents in taste cells (PubMed:21098668).
CC {ECO:0000305|PubMed:16891422, ECO:0000305|PubMed:16929298,
CC ECO:0000305|PubMed:21098668, ECO:0000305|PubMed:21625513}.
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DR EMBL; AB290927; BAF45380.1; -; mRNA.
DR EMBL; AF271381; AAK58371.1; -; mRNA.
DR EMBL; AC125101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116297; AAI16298.1; -; mRNA.
DR EMBL; BC116323; AAI16324.2; -; mRNA.
DR CCDS; CCDS29846.1; -.
DR RefSeq; NP_852087.2; NM_181422.3.
DR PDB; 5Z1W; EM; 3.38 A; A/B/C/D=64-629.
DR PDB; 7D7E; EM; 3.40 A; B/C/D=64-629.
DR PDB; 7D7F; EM; 3.00 A; B/C/D=64-629.
DR PDBsum; 5Z1W; -.
DR PDBsum; 7D7E; -.
DR PDBsum; 7D7F; -.
DR AlphaFoldDB; A2A259; -.
DR SMR; A2A259; -.
DR BioGRID; 236700; 1.
DR DIP; DIP-61250N; -.
DR IntAct; A2A259; 1.
DR STRING; 10090.ENSMUSP00000045675; -.
DR TCDB; 1.A.5.2.2; the polycystin cation channel (pcc) family.
DR GlyGen; A2A259; 4 sites.
DR iPTMnet; A2A259; -.
DR PhosphoSitePlus; A2A259; -.
DR PaxDb; A2A259; -.
DR PeptideAtlas; A2A259; -.
DR PRIDE; A2A259; -.
DR ProteomicsDB; 289746; -.
DR Antibodypedia; 31169; 140 antibodies from 22 providers.
DR DNASU; 329064; -.
DR Ensembl; ENSMUST00000042026; ENSMUSP00000045675; ENSMUSG00000037578.
DR GeneID; 329064; -.
DR KEGG; mmu:329064; -.
DR UCSC; uc008hpm.2; mouse.
DR CTD; 9033; -.
DR MGI; MGI:1352448; Pkd2l1.
DR VEuPathDB; HostDB:ENSMUSG00000037578; -.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000157274; -.
DR HOGENOM; CLU_012097_0_0_1; -.
DR InParanoid; A2A259; -.
DR OMA; PDPWGVQ; -.
DR OrthoDB; 426073at2759; -.
DR PhylomeDB; A2A259; -.
DR TreeFam; TF316484; -.
DR BioGRID-ORCS; 329064; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Pkd2l1; mouse.
DR PRO; PR:A2A259; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; A2A259; protein.
DR Bgee; ENSMUSG00000037578; Expressed in lumbar subsegment of spinal cord and 27 other tissues.
DR Genevisible; A2A259; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0034703; C:cation channel complex; IDA:BHF-UCL.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0097730; C:non-motile cilium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IPI:MGI.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0005227; F:calcium activated cation channel activity; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:MGI.
DR GO; GO:0005261; F:cation channel activity; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051371; F:muscle alpha-actinin binding; ISO:MGI.
DR GO; GO:0005272; F:sodium channel activity; ISO:MGI.
DR GO; GO:0006812; P:cation transport; IDA:BHF-UCL.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB.
DR GO; GO:0001581; P:detection of chemical stimulus involved in sensory perception of sour taste; IDA:BHF-UCL.
DR GO; GO:0050912; P:detection of chemical stimulus involved in sensory perception of taste; IMP:UniProtKB.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0009415; P:response to water; IMP:UniProtKB.
DR GO; GO:0050915; P:sensory perception of sour taste; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08016; PKD_channel; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Cell projection; Cilium; Coiled coil; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..760
FT /note="Polycystic kidney disease 2-like 1 protein"
FT /id="PRO_0000425551"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TOPO_DOM 125..356
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TOPO_DOM 377..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TOPO_DOM 406..433
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TOPO_DOM 455..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TRANSMEM 480..499
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TOPO_DOM 500..511
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29567962"
FT INTRAMEM 512..526
FT /note="Pore-forming"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TOPO_DOM 527..536
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29567962"
FT TOPO_DOM 558..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29567962"
FT DOMAIN 630..665
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..760
FT /note="Required for homooligomerization"
FT /evidence="ECO:0000250"
FT COILED 559..580
FT /evidence="ECO:0000255"
FT COILED 650..682
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 654
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT LIPID 38
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L9"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29567962,
FT ECO:0007744|PDB:5Z1W"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29567962,
FT ECO:0007744|PDB:5Z1W"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29567962,
FT ECO:0007744|PDB:5Z1W"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 210..223
FT /evidence="ECO:0000269|PubMed:29567962,
FT ECO:0007744|PDB:5Z1W"
FT MUTAGEN 522
FT /note="G->L: Loss of channel activity."
FT /evidence="ECO:0000269|PubMed:29567962"
FT MUTAGEN 523
FT /note="D->E: Little or no effect on calcium channel
FT activity."
FT /evidence="ECO:0000269|PubMed:21185261"
FT MUTAGEN 523
FT /note="D->N: Impaired calcium channel activity."
FT /evidence="ECO:0000269|PubMed:21185261"
FT MUTAGEN 525
FT /note="D->N: Little or no effect on calcium channel
FT activity."
FT /evidence="ECO:0000269|PubMed:21185261"
FT MUTAGEN 530
FT /note="D->N: Little or no effect on calcium channel
FT activity."
FT /evidence="ECO:0000269|PubMed:21185261"
FT MUTAGEN 531
FT /note="N->Q: No effect on activation by low pH."
FT /evidence="ECO:0000269|PubMed:28904867"
FT MUTAGEN 533
FT /note="N->Q: Loss of activation by low pH."
FT /evidence="ECO:0000269|PubMed:28904867"
FT MUTAGEN 560
FT /note="I->F: Loss of channel activity."
FT /evidence="ECO:0000269|PubMed:29567962"
FT MUTAGEN 568
FT /note="K->A: Increases localization at the cell surface
FT when expressed in absence of PKD1."
FT /evidence="ECO:0000269|PubMed:15548533"
FT MUTAGEN 576
FT /note="D->A: Induces localization to the endoplasmic
FT reticulum when expressed in absence of PKD1."
FT /evidence="ECO:0000269|PubMed:15548533"
FT CONFLICT 114
FT /note="I -> V (in Ref. 2; AAK58371 and 4; AAI16324/
FT AAI16298)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..203
FT /note="QL -> HV (in Ref. 2; AAK58371)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="Y -> D (in Ref. 2; AAK58371)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="I -> V (in Ref. 2; AAK58371)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="L -> P (in Ref. 4; AAI16324/AAI16298)"
FT /evidence="ECO:0000305"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:5Z1W"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 298..309
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 331..339
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 349..367
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:7D7E"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 386..420
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:5Z1W"
FT HELIX 429..451
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 452..456
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 477..498
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 509..520
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 526..532
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 536..574
FT /evidence="ECO:0007829|PDB:7D7F"
SQ 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
