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 27-MAR-2024, entry version 112. DE RecName: Full=Polycystin-2-like protein 1; DE Short=Polycystin-2L1; DE AltName: 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-30606; -. DR EMDB; EMD-30607; -. DR EMDB; EMD-6877; -. 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 GlyCosmos; A2A259; 4 sites, No reported glycans. DR GlyGen; A2A259; 4 sites. DR iPTMnet; A2A259; -. DR PhosphoSitePlus; A2A259; -. DR PaxDb; 10090-ENSMUSP00000045675; -. DR PeptideAtlas; A2A259; -. DR ProteomicsDB; 289746; -. DR Antibodypedia; 31169; 161 antibodies from 22 providers. DR DNASU; 329064; -. DR Ensembl; ENSMUST00000042026.5; ENSMUSP00000045675.5; ENSMUSG00000037578.5. DR GeneID; 329064; -. DR KEGG; mmu:329064; -. DR UCSC; uc008hpm.2; mouse. DR AGR; MGI:1352448; -. 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; AFSQFDR; -. DR OrthoDB; 56358at2759; -. DR PhylomeDB; A2A259; -. DR TreeFam; TF316484; -. DR BioGRID-ORCS; 329064; 4 hits in 78 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 30 other cell types or tissues. 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: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; IDA:UniProtKB. DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL. DR GO; GO:0051393; F:alpha-actinin binding; 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:0005227; F:calcium-activated cation channel activity; ISO:MGI. DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:MGI. DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005261; F:monoatomic cation channel activity; IDA:UniProtKB. DR GO; GO:0051371; F:muscle alpha-actinin binding; ISO:MGI. DR GO; GO:0005272; F:sodium channel activity; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; IPI: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:0006812; P:monoatomic cation transport; IDA:BHF-UCL. 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; 1.10.287.70; -; 1. DR Gene3D; 1.20.5.340; -; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR046791; Polycystin_dom. DR InterPro; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR10877:SF194; POLYCYSTIC KIDNEY DISEASE 2-LIKE 1 PROTEIN; 1. DR PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 1. DR Pfam; PF18109; Fer4_24; 1. DR Pfam; PF08016; PKD_channel; 1. DR Pfam; PF20519; Polycystin_dom; 1. DR PRINTS; PR01433; POLYCYSTIN2. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR PROSITE; PS50222; EF_HAND_2; 1. DR Genevisible; A2A259; MM. 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="Polycystin-2-like protein 1" 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; FT AAI16324/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 //