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PKD1L3 Membrane Protein Introduction

Introduction of PKD1L3

Polycystic kidney disease-1-like 3 (PKD1L3) is a member of the polycystin-1 (PKD1)-like family consisting of 5 members, including PKD1, PKD1L1, PKD1L2, PKD1L3, and PKDREJ. PKD1L3, as well as PKD1L2, was first identified from human and mouse genomes as a gene homologous to PKD1. Similar to PKD1, PKD1L3 contains an N-terminal C-type lectin domain, a G-protein-coupled receptor proteolytic site (GPS), and a polycystin-1-lipoxygenase-alpha toxin (PLAT)/lipoxygenase homology 2 (LH2) domain

Basic Information of PKD1L3
Protein Name Polycystic kidney disease protein 1-like 3
Gene Name PKD1L3
Aliases PC1-like 3 protein, Polycystin-1L3
Organism Homo sapiens (Human)
UniProt ID Q7Z443
Transmembrane Times 12
Length (aa) 1732
Sequence MFFKGGSWLWLYIRTSIILGSELNSPAPHGQNNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGKKWWIGQNVMPLKKHQDNKYPADVAANGPPKPLSCTYLSRNFIRISSKGDKCLLKYYFICQTGDFLDGDAHYERNGNNSHLYQRHKKTKRGVAIARDKMPPGPGHLPTTCHYPLPAHLSKTLCHPISQFPSVLSSITSQVTSAASEPSSQPLPVITQLTMPVSVTHAGQSLAETTSSPKEEGHPNTFTSYLQVSLQKASGQVIDEIAGNFSRAVHGLQALNKLQEACEFLQKLTALTPRFSKPAQVNLINSLIYLSEELLRIPFQNNNSLGFKVPPTVCPFHSLNNVTKAGEGSWLESKRHTEPVEDILEMSLVEFGNIGEAFLEQNQSPESSVTLTSANATLLLSRQNISTLPLSSYTLGHPAPVRLGFPSALALKELLNKHPGVNVQITGLAFNPFKDLDNRNIVGSIGSVLLSANRKLLQVHDLMEDIEIMLWRNVSLETHPTSLNMSTHQLTITVNVTSLEKSLIVSIDPDSPLLMTLYLGFQYQPNCTHFHLNITLPKDKVWQKDEEYTWVLNPEHLQHGIGTYYITAVLSERQEGAQQTPSLVSVITAVTQCYYWEIHNQTWSSAGCQVGPQSTILRTQCLCNHLTFFASDFFVVPRTVNVEDTIKLFLRVTNNPVGVSLLASLLGFYVITVVWARKKDQADMQKVKVTVLADNDPSAQFHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSWYVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVFIPVSKRELFSFRHLFSSMIVEKFTQDYLWLSIATRHPWNQFTRVQRLSCCMTLLLCNMVINVMFWKINSTTAKRDEQMRPFAVAWSELLVSIHTAVILFPINLVIGRLFPLIEPQETLPLFPPIQASCLSDASVEPLSATMVVEELKETVRFLLRRNTYLLSKCEQPPWSSWDITKLVKLLSSLVSSHLEGQGCHQQGERHWARVVPENHHHFCCYLHRVLQRLKSHLGTLGLTQGHQSCDFLDAASQLQKLQELLETHILPTEQEPSREVTSFAILSSEEGKKPISNGLSKWLTSVCWLLLGFTSLASAFFTALYSLELSKDQATSWMISIILSVLQNIFISQPVKVVFFTFLYSLMMSRMPRLNKENEQQTKRILALLAKCSSSVPGSRDKNNPVYVAPAINSPTKHPERTLKKKKLFKLTGDILVQILFLTLLMTAIYSAKNSNRFYLHQAIWKTFSHQFSEIKLLQDFYPWANHILLPSLYGDYRGKNAVLEPSHCKCGVQLIFQIPRTKTYEKVDEGQLAFCDNGHTCGRPKSLFPGLHLRRFSYICSPRPMVLIPTDELHERLTSKNENGFSYIMRGAFFTSLRLESFTSLQMSKKGCVWSIISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAVKVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSSAVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGKERKSLKKEAALIDTLLQKLSNLLGISWPQKTSSEQAATTAVGSDTEVLDELP

Function of PKD1L3 Membrane Protein

PKD1L3 is abundantly expressed in taste tissues and testis, and it is also expressed with small amounts in brain tissues. In taste tissues, PKD1L3 may be associated with a taste sensation other than sweetness, bitterness, and umami, that is, sour or salty. Especially, PKD1L3 is expressed in sour-sensing type III taste cells that have synaptic contacts with afferent nerve fibers in circumvallate (CvP) and foliate papillae (FoP) located in the posterior region of the tongue, although not in fungiform papillae (FuP) or the palate. Recently, a study has been conducted to examine the PKD1L3/PKD2L1 channel property in more detail. The results show that the PKD1L3/PKD2L1 channel responds to various acid solutions adjusted at pH 2.5 or 2.6, including H2SO4, phosphoric acid, succinic acid, and tartaric acid, in addition to citric acid, hydrochloric acid, and malic acid. Interestingly, the PKD1L3/PKD2L1 channel has a unique “off-response” property, which suggests that this channel is gated open only after the removal of an acid stimulus, although initial acid exposure is essential.

Schematic drawing illustrating conformational structures of TRPM5, PKD1L3, and PKD2L1. Fig.1 Schematic drawing illustrating conformational structures of TRPM5, PKD1L3, and PKD2L1. (Ishimaru, 2009)

Application of PKD1L3 Membrane Protein in Literature

  1. Chen D., et al. Molecular evolution of candidate sour taste receptor gene PKD1L3 in mammals. Genome. 2011, 54(11):890-897. PubMed ID: 22011139

    Combined with other functional studies, results of the study suggest that rodents may not be the most appropriate model for functional studies of PKD1L3 genes.

  2. Yamamoto K., et al. Genetic tracing of the gustatory neural pathway originating from Pkd1l3-expressing type III taste cells in circumvallate and foliate papillae. Journal of Neurochemistry. 2011, 119(3):497-506. PubMed ID: 21883212

    In this study, authors demonstrate a sour gustatory pathway that originates from taste receptor cells (TRCs) in the posterior region of the tongue using the pkd1l3-wheat germ agglutinin (WGA) transgenic mice.

  3. Nelson T.M., et al. Taste function in mice with a targeted mutation of the Pkd1l3 gene. Chemical Senses. 2010, 35(7):565-77. PubMed ID: 20605874

    This article suggests further studies are required to describe the function of PKD1L3 in taste bud cells because the present results show no significant decrease in taste responsiveness in Pkd1l3 mutant mice in behavioral or electrophysiological tests compared with wild-type controls.

  4. Kawaguchi H., et al. Activation of polycystic kidney disease-2-like 1 (PKD2L1)-PKD1L3 complex by acid in mouse taste cells. Journal of Biological Chemistry. 2010, 285(23):17277-17281. PubMed ID: 20406802

    In this study, PKD2L1-PKD1L3-mediated acid-evoked off responses is observed in HEK293 cells and in native taste cells, which indicates that PKD2L1-PKD1L3 complex is involved in the acid sensing in vivo.

  5. Ishii S., et al. Acetic acid activates PKD1L3-PKD2L1 channel--a candidate sour taste receptor. Biochem Biophys Res Commun. 2009, 385(3):346-350. PubMed ID: 19464260

    This report suggests that PKD1L3-PKD2L1 channel activation by acetic acid is pH-dependent and occurs when the ambient pH is less than 3.1.

PKD1L3 Preparation Options

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Reference

  1. Ishimaru Y and Matsunami H. (2009). Transient receptor potential (TRP) channels and taste sensation. Journal of Dental Research. 88(3): 212-218.

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