Polycystic kidney disease 2-like 1 (Predicted)

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• alpha-actinin binding Source: RGDInferred from sequence orthologyⁱ
  • "Direct binding of alpha-actinin enhances TRPP3 channel activity."
    Li Q., Dai X.Q., Shen P.Y., Wu Y., Long W., Chen C.X., Hussain Z., Wang S., Chen X.Z.
    J. Neurochem. 103:2391-2400(2007) [PubMed] [Europe PMC] [Abstract]
• calcium activated cation channel activity Source: RGDInferred from sequence orthologyⁱ
  • "Polycystin-L is a calcium-regulated cation channel permeable to calcium ions."
    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.
    Nature 401:383-386(1999) [PubMed] [Europe PMC] [Abstract]
  • "The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation."
    Li Q., Liu Y., Zhao W., Chen X.Z.
    FEBS Lett. 516:270-278(2002) [PubMed] [Europe PMC] [Abstract]
• calcium-activated potassium channel activity Source: RGDInferred from sequence orthologyⁱ
  • "Polycystin-L is a calcium-regulated cation channel permeable to calcium ions."
    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.
    Nature 401:383-386(1999) [PubMed] [Europe PMC] [Abstract]
• calcium channel activity Source: RGDInferred from sequence orthologyⁱ
  • "Primary cilia are specialized calcium signalling organelles."
    Delling M., DeCaen P.G., Doerner J.F., Febvay S., Clapham D.E.
    Nature 504:311-314(2013) [PubMed] [Europe PMC] [Abstract]
  • "Direct recording and molecular identification of the calcium channel of primary cilia."
    DeCaen P.G., Delling M., Vien T.N., Clapham D.E.
    Nature 504:315-318(2013) [PubMed] [Europe PMC] [Abstract]
• calcium ion binding Source: RGDInferred from sequence orthologyⁱ
  • "Identification of the structural motif responsible for trimeric assembly of the C-terminal regulatory domains of polycystin channels PKD2L1 and PKD2."
    Molland K.L., Narayanan A., Burgner J.W., Yernool D.A.
    Biochem. J. 429:171-183(2010) [PubMed] [Europe PMC] [Abstract]
  • "Crystal structure and characterization of coiled-coil domain of the transient receptor potential channel PKD2L1."
    Molland K.L., Paul L.N., Yernool D.A.
    Biochim. Biophys. Acta 1824:413-421(2012) [PubMed] [Europe PMC] [Abstract]
• cation channel activity Source: RGDInferred from sequence orthologyⁱ
  • "Genomic organization and functional analysis of murine PKD2L1."
    Murakami M., Ohba T., Xu F., Shida S., Satoh E., Ono K., Miyoshi I., Watanabe H., Ito H., Iijima T.
    J. Biol. Chem. 280:5626-5635(2005) [PubMed] [Europe PMC] [Abstract]
  • "Direct binding of alpha-actinin enhances TRPP3 channel activity."
    Li Q., Dai X.Q., Shen P.Y., Wu Y., Long W., Chen C.X., Hussain Z., Wang S., Chen X.Z.
    J. Neurochem. 103:2391-2400(2007) [PubMed] [Europe PMC] [Abstract]
  • "The asparagine 533 residue in the outer pore loop region of the mouse PKD2L1 channel is essential for its voltage-dependent inactivation."
    Shimizu T., Higuchi T., Toba T., Ohno C., Fujii T., Nilius B., Sakai H.
    FEBS Open Bio 7:1392-1401(2017) [PubMed] [Europe PMC] [Abstract]
  • "Cryo-EM structure of the polycystin 2-l1 ion channel."
    Hulse R.E., Li Z., Huang R.K., Zhang J., Clapham D.E.
    Elife 7:0-0(2018) [PubMed] [Europe PMC] [Abstract]
• cytoskeletal protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Troponin I binds polycystin-L and inhibits its calcium-induced channel activation."
    Li Q., Liu Y., Shen P.Y., Dai X.Q., Wang S., Smillie L.B., Sandford R., Chen X.Z.
    Biochemistry 42:7618-7625(2003) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor."
    Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M., Matsunami H.
    Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006) [PubMed] [Europe PMC] [Abstract]
  • "Identification of the structural motif responsible for trimeric assembly of the C-terminal regulatory domains of polycystin channels PKD2L1 and PKD2."
    Molland K.L., Narayanan A., Burgner J.W., Yernool D.A.
    Biochem. J. 429:171-183(2010) [PubMed] [Europe PMC] [Abstract]
• muscle alpha-actinin binding Source: RGDInferred from sequence orthologyⁱ
  • "Direct binding of alpha-actinin enhances TRPP3 channel activity."
    Li Q., Dai X.Q., Shen P.Y., Wu Y., Long W., Chen C.X., Hussain Z., Wang S., Chen X.Z.
    J. Neurochem. 103:2391-2400(2007) [PubMed] [Europe PMC] [Abstract]
• sodium channel activity Source: RGDInferred from sequence orthologyⁱ
  • "Polycystin-L is a calcium-regulated cation channel permeable to calcium ions."
    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.
    Nature 401:383-386(1999) [PubMed] [Europe PMC] [Abstract]
• sour taste receptor activity Source: Ensembl

GO - Biological processⁱ

• cation transport Source: RGDInferred from sequence orthologyⁱ
  • "Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor."
    Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M., Matsunami H.
    Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006) [PubMed] [Europe PMC] [Abstract]
• cellular response to acidic pH Source: RGDInferred from sequence orthologyⁱ
  • "Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor."
    Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M., Matsunami H.
    Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006) [PubMed] [Europe PMC] [Abstract]
  • "Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1."
    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.
    Nat. Commun. 9:1192-1192(2018) [PubMed] [Europe PMC] [Abstract]
• cellular response to pH Source: RGDInferred from sequence orthologyⁱ
  • "The asparagine 533 residue in the outer pore loop region of the mouse PKD2L1 channel is essential for its voltage-dependent inactivation."
    Shimizu T., Higuchi T., Toba T., Ohno C., Fujii T., Nilius B., Sakai H.
    FEBS Open Bio 7:1392-1401(2017) [PubMed] [Europe PMC] [Abstract]
• detection of chemical stimulus involved in sensory perception of sour taste Source: RGDInferred from sequence orthologyⁱ
  • "Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor."
    Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M., Matsunami H.
    Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006) [PubMed] [Europe PMC] [Abstract]
• detection of chemical stimulus involved in sensory perception of taste Source: RGDInferred from sequence orthologyⁱ
  • "The cellular mechanism for water detection in the mammalian taste system."
    Zocchi D., Wennemuth G., Oka Y.
    Nat. Neurosci. 20:927-933(2017) [PubMed] [Europe PMC] [Abstract]
• detection of mechanical stimulus Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• inorganic cation transmembrane transport Source: RGDInferred from sequence orthologyⁱ
  • "The asparagine 533 residue in the outer pore loop region of the mouse PKD2L1 channel is essential for its voltage-dependent inactivation."
    Shimizu T., Higuchi T., Toba T., Ohno C., Fujii T., Nilius B., Sakai H.
    FEBS Open Bio 7:1392-1401(2017) [PubMed] [Europe PMC] [Abstract]
  • "Cryo-EM structure of the polycystin 2-l1 ion channel."
    Hulse R.E., Li Z., Huang R.K., Zhang J., Clapham D.E.
    Elife 7:0-0(2018) [PubMed] [Europe PMC] [Abstract]
• potassium ion transmembrane transport Source: RGDInferred from sequence orthologyⁱ
  • "Polycystin-L is a calcium-regulated cation channel permeable to calcium ions."
    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.
    Nature 401:383-386(1999) [PubMed] [Europe PMC] [Abstract]
• protein homotetramerization Source: RGDInferred from sequence orthologyⁱ
  • "Cryo-EM structure of the polycystin 2-l1 ion channel."
    Hulse R.E., Li Z., Huang R.K., Zhang J., Clapham D.E.
    Elife 7:0-0(2018) [PubMed] [Europe PMC] [Abstract]
• protein tetramerization Source: RGDInferred from sequence orthologyⁱ
  • "Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1."
    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.
    Nat. Commun. 9:1192-1192(2018) [PubMed] [Europe PMC] [Abstract]
• response to water Source: RGDInferred from sequence orthologyⁱ
  • "The cellular mechanism for water detection in the mammalian taste system."
    Zocchi D., Wennemuth G., Oka Y.
    Nat. Neurosci. 20:927-933(2017) [PubMed] [Europe PMC] [Abstract]
• sensory perception of sour taste Source: RGDInferred from sequence orthologyⁱ
  • "Sour ageusia in two individuals implicates ion channels of the ASIC and PKD families in human sour taste perception at the anterior tongue."
    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.
    PLoS ONE 4:E7347-E7347(2009) [PubMed] [Europe PMC] [Abstract]
• smoothened signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Primary cilia are specialized calcium signalling organelles."
    Delling M., DeCaen P.G., Doerner J.F., Febvay S., Clapham D.E.
    Nature 504:311-314(2013) [PubMed] [Europe PMC] [Abstract]
• sodium ion transmembrane transport Source: RGDInferred from sequence orthologyⁱ
  • "Polycystin-L is a calcium-regulated cation channel permeable to calcium ions."
    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.
    Nature 401:383-386(1999) [PubMed] [Europe PMC] [Abstract]

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

GO - Molecular functionⁱ

• alpha-actinin binding Source: RGDInferred from sequence orthologyⁱ
  • "Direct binding of alpha-actinin enhances TRPP3 channel activity."
    Li Q., Dai X.Q., Shen P.Y., Wu Y., Long W., Chen C.X., Hussain Z., Wang S., Chen X.Z.
    J. Neurochem. 103:2391-2400(2007) [PubMed] [Europe PMC] [Abstract]
• cytoskeletal protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Troponin I binds polycystin-L and inhibits its calcium-induced channel activation."
    Li Q., Liu Y., Shen P.Y., Dai X.Q., Wang S., Smillie L.B., Sandford R., Chen X.Z.
    Biochemistry 42:7618-7625(2003) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor."
    Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M., Matsunami H.
    Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006) [PubMed] [Europe PMC] [Abstract]
  • "Identification of the structural motif responsible for trimeric assembly of the C-terminal regulatory domains of polycystin channels PKD2L1 and PKD2."
    Molland K.L., Narayanan A., Burgner J.W., Yernool D.A.
    Biochem. J. 429:171-183(2010) [PubMed] [Europe PMC] [Abstract]
• muscle alpha-actinin binding Source: RGDInferred from sequence orthologyⁱ
  • "Direct binding of alpha-actinin enhances TRPP3 channel activity."
    Li Q., Dai X.Q., Shen P.Y., Wu Y., Long W., Chen C.X., Hussain Z., Wang S., Chen X.Z.
    J. Neurochem. 103:2391-2400(2007) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Coiled coil

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MNIMENSKEQ ELQTLGSRVW DNPAYSSPPS PNGTPRICTV SSVALPETQP 
        60         70         80         90        100
KKPEVRRQEK TPRVPVSGCC LLICRGIRGL WGTTLTENTA ENRELYVKTT 
       110        120        130        140        150
LRELVVYIVF LVDVCLLTYG MTSSSAYYYT KVMSELFLHT PSESAVSFQT 
       160        170        180        190        200
ISSMSDFWDG PLLDSLYWTK WYNNQSLGSS SHSFIYYENL LLGVPRLRQL 
       210        220        230        240        250
RVRNDSCVVH EDFREDILNC YDVYSPDKED QLPFGPLNGT AWTYHSQNEL 
       260        270        280        290        300
GGSSHWGRLT SYSGGGYYLD LPGSRQASAE ALQGLQEGLW LDRGTRVVFI 
       310        320        330        340        350
DFSVYNANIN LFCILRLVVE FPATGGAIPS WQIRTVKLIR YVNNWDFFIV 
       360        370        380        390        400
GCEVIFCIFI FYYVVEEILE IRVHRFRYLS SVWNILDLVV ILLSIVAVGF 
       410        420        430        440        450
HVFRTLEVNR LMGELLQQPD TYPDFEFLAF WQTQYNNMNA VNLFFAWIKI 
       460        470        480        490        500
FKYISFNKTM TQLSSTLARC AKDILGFAIM FFIVFFAYAQ LGYLLFGTQV 
       510        520        530        540        550
ESFSTFVKCI FTQFRIILGD FDYNAIDNAN RILGPVYFIT YVFFVFFVLL 
       560        570        580        590        600
NMFLAIINDT YSEVKEELAG QRDQLQLSDL LKQSYSKTLQ RLRLRKERVS 
       610        620        630        640        650
DVQKVLKGGE PEIQFEDFTN TLRELTRRVL QLQRVLEGVV SQVDALSSKL 
       660        670 
KMLERKGELA PSPGMARGAS CLGEPL                           

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ